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Conserved domains on  [gi|169293994|gb|EDS76127|]
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ABC transporter, ATP-binding protein [[Clostridium] spiroforme DSM 1552]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438222)

ABC transporter ATP-binding protein, typically containing two ATP-binding domains; with similarity to the cobalt import ATP-binding protein CbiO, which is part of the group-I cobalt energy-coupling factor (ECF) transporter CbiMNQO

CATH:  3.40.50.300
Gene Ontology:  GO:0042626|GO:0140359|GO:0016887|GO:0005524
PubMed:  10529352|25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-479 5.33e-93

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: 292.19  E-value: 5.33e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPK-DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDEE------IENDDTKIG 76
Cdd:COG1123    7 VRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRdllelsEALRGRRIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:COG1123   87 MVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDneikMAVDEMLTKKIFVESLPN 236
Cdd:COG1123  167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED----GPPEEILAAPQALAAVPR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 237 YVRVSSLCDKlclsIKEAREALVNFENfdikimdeidnriLMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKS 316
Cdd:COG1123  243 LGAARGRAAP----AAAAAEPLLEVRN-------------LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 317 SFLRCLAGL-------VDCQGE-ISKVGCVD------RIGYLPQDPTTLF-----VADKV-----IDDLLLVDDVVASVE 372
Cdd:COG1123  306 TLARLLLGLlrptsgsILFDGKdLTKLSRRSlrelrrRVQMVFQDPYSSLnprmtVGDIIaeplrLHGLLSRAERRERVA 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 373 SHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDL 449
Cdd:COG1123  386 ELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDL 465

                        490       500       510
                 ....*....|....*....|....*....|
gi 169293994 450 EFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG1123  466 AVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
 
Name Accession Description Interval E-value
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-479 5.33e-93

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: 292.19  E-value: 5.33e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPK-DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDEE------IENDDTKIG 76
Cdd:COG1123    7 VRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRdllelsEALRGRRIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:COG1123   87 MVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDneikMAVDEMLTKKIFVESLPN 236
Cdd:COG1123  167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED----GPPEEILAAPQALAAVPR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 237 YVRVSSLCDKlclsIKEAREALVNFENfdikimdeidnriLMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKS 316
Cdd:COG1123  243 LGAARGRAAP----AAAAAEPLLEVRN-------------LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 317 SFLRCLAGL-------VDCQGE-ISKVGCVD------RIGYLPQDPTTLF-----VADKV-----IDDLLLVDDVVASVE 372
Cdd:COG1123  306 TLARLLLGLlrptsgsILFDGKdLTKLSRRSlrelrrRVQMVFQDPYSSLnprmtVGDIIaeplrLHGLLSRAERRERVA 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 373 SHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDL 449
Cdd:COG1123  386 ELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDL 465

                        490       500       510
                 ....*....|....*....|....*....|
gi 169293994 450 EFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG1123  466 AVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 3-210 9.02e-77

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: 240.06  E-value: 9.02e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPK-DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFV 78
Cdd:cd03225    1 ELKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVlvDGKDLTKLSLKELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:cd03225   81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 159 ATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGK 210
Cdd:cd03225  161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 3-214 7.97e-67

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: 216.14  E-value: 7.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEE-IENDDTKIGF 77
Cdd:TIGR04520   2 EVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPtSGKVtvDGLDTLDEEnLWEIRKKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   78 VFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLD 157
Cdd:TIGR04520  82 VFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994  158 EATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKIVID 214
Cdd:TIGR04520 162 EATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE 217
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
4-212 1.35e-52

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 179.44  E-value: 1.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKKI-INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK-GDID-GVIILDEEIEND-DTKIGFVF 79
Cdd:PRK13635   8 VEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITvGGMVLSEETVWDvRRQVGMVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:PRK13635  88 QNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 160 TAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 18-161 8.78e-28

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: 108.50  E-value: 8.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFVFQNPEDQLVMnTVWHE 94
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTIllDGQDLTDDERKSLRKEIGYVFQDPQLFPRL-TVREN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994   95 IAFGLKNKGISLKQMKRRIGEIVNYFNLQ----SIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:pfam00005  80 LRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
286-461 3.25e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 85.36  E-value: 3.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 286 GHDdiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDRIGYLPQ-----DPTTLFVADKVI-- 358
Cdd:NF040873   4 GRP--VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPLTVRDLVAmg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 359 ------DDLLLVDDVVASVESHLDNFGIIDLKDAhPFD-LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLAN 431
Cdd:NF040873  82 rwarrgLWRRLTRDDRAAVDDALERVGLADLAGR-QLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169293994 432 LIRGLS-KHMTIVVASHDLEFVAKISDRVAM 461
Cdd:NF040873 161 LLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
104-227 1.07e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.13  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 104 ISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfN 183
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-G 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 169293994 184 VTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEikmaVDEMLTK 227
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK----VDELKTK 234
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-175 1.64e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.44  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  19 NNISFEIKKGD---FLvitGKSGCGKTT-------LLryfKPSlrpkgdiDG-VIILDEEIENDD----TKIGF------ 77
Cdd:NF033858 283 DHVSFRIRRGEifgFL---GSNGCGKSTtmkmltgLL---PAS-------EGeAWLFGQPVDAGDiatrRRVGYmsqafs 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 ------VFQNpedqLVMntvwHEIAFGLKNKGIslkqmKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNP 151
Cdd:NF033858 350 lygeltVRQN----LEL----HARLFHLPAAEI-----AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416

                        170       180
                 ....*....|....*....|....
gi 169293994 152 KVILLDEATAQLDPVNREEFIKIL 175
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLL 440
GguA NF040905
sugar ABC transporter ATP-binding protein;
390-466 1.55e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 390 DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSITVLRDGR 216
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-205 2.18e-03

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: 38.89  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    27 KGDFLVITGKSGCGKTTLLRYFKPSLRPKGDidGVIILDEEienddtkigfvfqnpedqlvmntvwheiafglknkgisl 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGE--------------------------------------- 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   107 kqmkrRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNR-----EEFIKILKHINDD 181
Cdd:smart00382  40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLLLKSE 114

                          170       180
                   ....*....|....*....|....
gi 169293994   182 FNVTVVFVEHQLEGLLDVANRLIV 205
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
GguA NF040905
sugar ABC transporter ATP-binding protein;
4-212 2.48e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.54  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYP--KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpSL--RPKG-DIDGVIILD-EEIEND------ 71
Cdd:NF040905 260 VKNWTVYHPlhPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAM----SVfgRSYGrNISGTVFKDgKEVDVStvsdai 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVfqnPEDQ----LV-MNTVWHEIAF----GLKNKGISLKQMKRRIGEivNYFNLQSI----INKETQSLSNGQK 138
Cdd:NF040905 336 DAGLAYV---TEDRkgygLNlIDDIKRNITLanlgKVSRRGVIDENEEIKVAE--EYRKKMNIktpsVFQKVGNLSGGNQ 410

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 139 QLVALASVMVMNPKVILLDEATAQLDPVNREEFIKIlkhIND--DFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
 
Name Accession Description Interval E-value
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 4-479 5.33e-93

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: 292.19  E-value: 5.33e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPK-DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDEE------IENDDTKIG 76
Cdd:COG1123    7 VRDLSVRYPGgDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRdllelsEALRGRRIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:COG1123   87 MVFQDPMTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIA 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDneikMAVDEMLTKKIFVESLPN 236
Cdd:COG1123  167 DEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVED----GPPEEILAAPQALAAVPR 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 237 YVRVSSLCDKlclsIKEAREALVNFENfdikimdeidnriLMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKS 316
Cdd:COG1123  243 LGAARGRAAP----AAAAAEPLLEVRN-------------LSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKS 305

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 317 SFLRCLAGL-------VDCQGE-ISKVGCVD------RIGYLPQDPTTLF-----VADKV-----IDDLLLVDDVVASVE 372
Cdd:COG1123  306 TLARLLLGLlrptsgsILFDGKdLTKLSRRSlrelrrRVQMVFQDPYSSLnprmtVGDIIaeplrLHGLLSRAERRERVA 385

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 373 SHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDL 449
Cdd:COG1123  386 ELLERVGLPpDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRelGLTYLFISHDL 465

                        490       500       510
                 ....*....|....*....|....*....|
gi 169293994 450 EFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG1123  466 AVVRYIADRVAVMYDGRIVEDGPTEEVFAN 495
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 3-214 1.00e-81

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: 253.41  E-value: 1.00e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDidgVIILDEEIENDD-----TKIG 76
Cdd:COG1122    2 ELENLSFSYPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPtSGE---VLVDGKDITKKNlrelrRKVG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:COG1122   79 LVFQNPDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:COG1122  159 DEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVAD 215
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 3-210 9.02e-77

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: 240.06  E-value: 9.02e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPK-DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFV 78
Cdd:cd03225    1 ELKNLSFSYPDgARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPtSGEVlvDGKDLTKLSLKELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:cd03225   81 FQNPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 159 ATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGK 210
Cdd:cd03225  161 PTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 3-214 7.97e-67

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: 216.14  E-value: 7.97e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEE-IENDDTKIGF 77
Cdd:TIGR04520   2 EVENVSFSYPESEKpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPtSGKVtvDGLDTLDEEnLWEIRKKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   78 VFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLD 157
Cdd:TIGR04520  82 VFQNPDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPDIIILD 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994  158 EATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKIVID 214
Cdd:TIGR04520 162 EATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAE 217
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
4-212 1.35e-52

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 179.44  E-value: 1.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKKI-INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK-GDID-GVIILDEEIEND-DTKIGFVF 79
Cdd:PRK13635   8 VEHISFRYPDAATYaLKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITvGGMVLSEETVWDvRRQVGMVF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:PRK13635  88 QNPDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 160 TAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PRK13635 168 TSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEIL 219
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-211 5.27e-50

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 172.61  E-value: 5.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKD--KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK-GDI--DGVIILDEEIENDDTKI 75
Cdd:PRK13650   4 IIEVKNLTFKYKEDqeKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIiiDGDLLTEENVWDIRHKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK13650  84 GMVFQNPDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEgllDVA--NRLIVMDEGKI 211
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLD---EVAlsDRVLVMKNGQV 218
cbiO PRK13637
energy-coupling factor transporter ATPase;
3-218 1.98e-49

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 171.38  E-value: 1.98e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGD---IDGVIILDEEIENDDT-- 73
Cdd:PRK13637   4 KIENLTHIYmegtPFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGkiiIDGVDITDKKVKLSDIrk 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 KIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL--QSIINKETQSLSNGQKQLVALASVMVMNP 151
Cdd:PRK13637  84 KVGLVFQYPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEP 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 152 KVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIK 218
Cdd:PRK13637 164 KILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPR 230
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 1-212 3.97e-49

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 170.17  E-value: 3.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKG---DIDGVIILDEEIENDDTKIG 76
Cdd:PRK13632   7 MIKVENVSFSYPNSENnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSgeiKIDGITISKENLKEIRKKIG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK13632  87 IIFQNPDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIF 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLdVANRLIVMDEGKIV 212
Cdd:PRK13632 167 DESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLI 221
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-229 8.06e-48

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 166.80  E-value: 8.06e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKK-----IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGD---IDGVIILDEE-IEND 71
Cdd:PRK13633   4 MIKCKNVSYKYESNEEsteklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGkvyVDGLDTSDEEnLWDI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNP 151
Cdd:PRK13633  84 RNKAGMVFQNPDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRP 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 152 KVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKIVID---NEIKMAVDEMltKK 228
Cdd:PRK13633 164 ECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEgtpKEIFKEVEMM--KK 240


                 .
gi 169293994 229 I 229
Cdd:PRK13633 241 I 241
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 3-212 1.60e-44

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: 155.76  E-value: 1.60e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIILDEEIEndDTKIG 76
Cdd:cd03259    2 ELKGLSKTY-GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRliagLERPD---SGEIliDGRDVTGVPPE--RRNIG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPedQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:cd03259   76 MVFQDY--ALFPHlTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03259  154 LDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIV 210
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-212 3.62e-44

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 155.20  E-value: 3.62e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDK---KIINNISFEIKKGDFLVITGKSGCGKTTLLryfkpSL-----RP-KGDidgVIILDEEIE-- 69
Cdd:COG1136    4 LLELRNLTKSYGTGEgevTALRGVSLSIEAGEFVAIVGPSGSGKSTLL-----NIlggldRPtSGE---VLIDGQDISsl 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  70 NDD-------TKIGFVFQNPedQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLV 141
Cdd:COG1136   76 SERelarlrrRHIGFVFQFF--NLLPElTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRV 153

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 142 ALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEgLLDVANRLIVMDEGKIV 212
Cdd:COG1136  154 AIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIV 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 3-211 1.09e-43

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: 153.80  E-value: 1.09e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKK---IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDidgVIILDEEIENDD------ 72
Cdd:cd03255    2 ELKNLSKTYGGGGEkvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPtSGE---VRVDGTDISKLSekelaa 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 ---TKIGFVFQNPedQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:cd03255   79 frrRHIGFVFQSF--NLLPDlTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEgLLDVANRLIVMDEGKI 211
Cdd:cd03255  157 NDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPE-LAEYADRIIELRDGKI 218
cbiO PRK13640
energy-coupling factor transporter ATPase;
4-251 1.80e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 155.34  E-value: 1.80e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDEEIENDDT------KIG 76
Cdd:PRK13640   8 FKHVSFTYPDSKKpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTvwdireKVG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK13640  88 IVFQNPDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGlLDVANRLIVMDEGKIVI-DNEIKMAVDEMLTKKIFVEsLP 235
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDE-ANMADQVLVLDDGKLLAqGSPVEIFSKVEMLKEIGLD-IP 245

                        250
                 ....*....|....*.
gi 169293994 236 NYVRVSSLCDKLCLSI 251
Cdd:PRK13640 246 FVYKLKNKLKEKGISV 261
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 4-212 5.05e-42

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 153.33  E-value: 5.05e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIILDEEIENDDtkIGF 77
Cdd:COG3842    8 LENVSKRY-GDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRmiagFETPD---SGRIllDGRDVTGLPPEKRN--VGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQN----PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:COG3842   82 VFQDyalfPH----L-TVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEH-QLEGLLdVANRLIVMDEGKIV 212
Cdd:COG3842  157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHdQEEALA-LADRIAVMNDGRIE 215
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 3-211 5.98e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 150.67  E-value: 5.98e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKI-INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDTK------I 75
Cdd:PRK13648   9 VFKNVSFQYQSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK---SGEIFYNNQAITDDNFeklrkhI 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK13648  86 GIVFQNPDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVII 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKI 211
Cdd:PRK13648 166 LDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTV 220
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
 11-194 1.01e-41

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 147.57  E-value: 1.01e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   11 YPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD-EEIENDD-------TKIGFVFQNP 82
Cdd:TIGR01166   1 YPGGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQS---GAVLIDgEPLDYSRkgllerrQRVGLVFQDP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   83 EDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:TIGR01166  78 DDQLFAADVDQDVAFGPLNLGLSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAG 157

                         170       180       190
                  ....*....|....*....|....*....|..
gi 169293994  163 LDPVNREEFIKILKHINDDFNvTVVFVEHQLE 194
Cdd:TIGR01166 158 LDPAGREQMLAILRRLRAEGM-TVVISTHDVD 188
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-214 1.65e-41

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 147.89  E-value: 1.65e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEE----IENDDT--- 73
Cdd:COG2884    1 MIRFENVSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPT---SGQVLVNGQdlsrLKRREIpyl 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 --KIGFVFQnpeD-QLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:COG2884   78 rrRIGVVFQ---DfRLLPDrTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVN 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINdDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:COG2884  155 RPELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLELVDRMPKRVLELEDGRLVRD 218
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-216 1.98e-40

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 147.06  E-value: 1.98e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEIENDDTK------ 74
Cdd:PRK13644   1 MIRLENVSYSYPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQK---GKVLVSGIDTGDFSKlqgirk 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 -IGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:PRK13644  78 lVGIVFQNPETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPEC 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGlLDVANRLIVMDEGKIVIDNE 216
Cdd:PRK13644 158 LIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGE 218
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 3-212 4.18e-40

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: 144.69  E-value: 4.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIILDeeIENDDTKIG 76
Cdd:cd03300    2 ELENVSKFY-GGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRliagFETPT---SGEIllDGKDITN--LPPHKRPVN 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQN----PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:cd03300   76 TVFQNyalfPH----L-TVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 153 VILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03300  151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQ 210
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 1-212 8.82e-40

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: 143.88  E-value: 8.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYP---KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpKGDI--DGVIILD---EEI 68
Cdd:cd03258    1 MIELKNVSKVFGdtgGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCIngleRPT---SGSVlvDGTDLTLlsgKEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  69 ENDDTKIGFVFQNpEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:cd03258   78 RKARRRIGMIFQH-FNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03258  157 NNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVV 220
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 3-258 1.91e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 144.11  E-value: 1.91e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKP-SLRPKGDID--GVIILDEEIENDDTKIGFVF 79
Cdd:PRK13647   6 EVEDLHFRYKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQRGRVKvmGREVNAENEKWVRSKVGLVF 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:PRK13647  86 QDPDDQVFSSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEP 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 160 TAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLTK----------KI 229
Cdd:PRK13647 166 MAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEqaglrlplvaQI 244

                        250       260
                 ....*....|....*....|....*....
gi 169293994 230 FvESLPNYVRvsslcDKLCLSIKEAREAL 258
Cdd:PRK13647 245 F-EDLPELGQ-----SKLPLTVKEAVQII 267
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 1-212 2.29e-39

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: 142.64  E-value: 2.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDK---KIINNISFEIKKGDFLVITGKSGCGKTTL----LRYFKPSlrpKGDIdgvIILDEEIENDD- 72
Cdd:cd03257    1 LLEVKNLSVSFPTGGgsvKALDDVSFSIKKGETLGLVGESGSGKSTLaraiLGLLKPT---SGSI---IFDGKDLLKLSr 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 -------TKIGFVFQNPedQLVMN---TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQ---SIINKETQSLSNGQKQ 139
Cdd:cd03257   75 rlrkirrKEIQMVFQDP--MSSLNprmTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVGlpeEVLNRYPHELSGGQRQ 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 140 LVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03257  153 RVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIV 225
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-225 3.37e-39

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 142.12  E-value: 3.37e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDIdgvIILDEEIENDDTK----I 75
Cdd:COG1131    3 VRGLTKRY-GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRmllgLLRPT---SGEV---RVLGEDVARDPAEvrrrI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPE--DQLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:COG1131   76 GYVPQEPAlyPDL---TVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEML 225
Cdd:COG1131  153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 3-210 4.33e-39

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: 140.01  E-value: 4.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVII--LDEEIENDDTKIGF 77
Cdd:cd03229    2 ELKNVSKRY-GQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPdSGSIliDGEDLtdLEDELPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQNPedQLVMN-TVWHEIAFGLknkgislkqmkrrigeivnyfnlqsiinketqslSNGQKQLVALASVMVMNPKVILL 156
Cdd:cd03229   81 VFQDF--ALFPHlTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDVLLL 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGK 210
Cdd:cd03229  125 DEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 3-211 1.14e-38

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: 140.94  E-value: 1.14e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIdgvIILDEEIENDDTK---IGFV 78
Cdd:cd03296    4 EVRNVSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPdSGTI---LFGGEDATDVPVQernVGFV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEDQLVMnTVWHEIAFGLKNKGISLK----QMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:cd03296   80 FQHYALFRHM-TVFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:cd03296  159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRI 215
cbiO PRK13642
energy-coupling factor transporter ATPase;
1-212 2.45e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 141.38  E-value: 2.45e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKI--INNISFEIKKGDFLVITGKSGCGKTTLLRYFK---PSLRPKGDIDGVIILDEEIENDDTKI 75
Cdd:PRK13642   4 ILEVENLVFKYEKESDVnqLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDglfEEFEGKVKIDGELLTAENVWNLRRKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK13642  84 GMVFQNPDNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIII 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PRK13642 164 LDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEII 219
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 3-212 3.56e-38

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: 139.14  E-value: 3.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKD---KKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILD-EEIENDDTK 74
Cdd:cd03293    2 EVRNVSKTYGGGggaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRiiagLERPT-------SGEVLVDgEPVTGPGPD 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPedqLVM--NTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:cd03293   75 RGYVFQQD---ALLpwLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 153 VILLDEATAQLDPVNR----EEFIKILKHinddFNVTVVFVEHQLEGLLDVANRLIVMDE--GKIV 212
Cdd:cd03293  152 VLLLDEPFSALDALTReqlqEELLDIWRE----TGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 4-212 5.40e-38

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 138.16  E-value: 5.40e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDT---KIGFVFQ 80
Cdd:cd03226    2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES---SGSILLNGKPIKAKErrkSIGYVMQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 NPEDQLVMNTVWHEIAFGLKNKGISLKQmkrrIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEAT 160
Cdd:cd03226   79 DVDYQLFTDSVREELLLGLKELDAGNEQ----AETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPT 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 161 AQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03226  155 SGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 1-212 5.56e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 140.21  E-value: 5.56e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILD-EEIENDDT------ 73
Cdd:PRK13639   1 ILETRDLKYSYPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT---SGEVLIKgEPIKYDKKsllevr 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 -KIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:PRK13639  78 kTVGIVFQNPDDQLFAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 153 VILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK13639 158 IIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKII 216
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 3-212 8.35e-38

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: 138.57  E-value: 8.35e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRY----FKPSlrpKGDI--DGVIIL---DEEIENDDT 73
Cdd:COG1127    7 EVRNLTKSF-GDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLiiglLRPD---SGEIlvDGQDITglsEKELYELRR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 KIGFVFQNPE--DQLvmnTVWHEIAFGLK-NKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:COG1127   83 RIGMLFQGGAlfDSL---TVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG1127  160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 3-227 1.00e-37

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: 138.47  E-value: 1.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDidgVIILDEEIENDDTK------- 74
Cdd:cd03256    2 EVENLSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPtSGS---VLIDGTDINKLKGKalrqlrr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 -IGFVFQN---PEDQLVMNTVWHEiAFGLKNKGISL-----KQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALAS 145
Cdd:cd03256   79 qIGMIFQQfnlIERLSVLENVLSG-RLGRRSTWRSLfglfpKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 146 VMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEML 225
Cdd:cd03256  158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAELTDEVL 237


                 ..
gi 169293994 226 TK 227
Cdd:cd03256  238 DE 239
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 1-239 1.86e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 138.78  E-value: 1.86e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIE--NFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGD---IDGVIILDEEIENDDTKI 75
Cdd:PRK13652   1 MHLIEtrDLCYSYSGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGsvlIRGEPITKENIREVRKFV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK13652  81 GLVFQNPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLV 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDN---EIKMAVDEMLTKKIFVE 232
Cdd:PRK13652 161 LDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGtveEIFLQPDLLARVHLDLP 240


                 ....*..
gi 169293994 233 SLPNYVR 239
Cdd:PRK13652 241 SLPKLIR 247
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 4-212 2.45e-37

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 137.91  E-value: 2.45e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK---IINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILD-EEIENDDTKI 75
Cdd:COG1116   10 LRGVSKRFPTGGGgvtALDDVSLTVAAGEFVALVGPSGCGKSTLLRliagLEKPT-------SGEVLVDgKPVTGPGPDR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPedqLVMN--TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:COG1116   83 GVVFQEP---ALLPwlTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQL-EGLLdVANRLIVMDE--GKIV 212
Cdd:COG1116  160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVdEAVF-LADRVVVLSArpGRIV 220
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 20-212 2.65e-37

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: 136.66  E-value: 2.65e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  20 NISFEIKkGDFLVITGKSGCGKTTLLRYFKPSLRPKG---DIDGVIILDEEIEND----DTKIGFVFQNpeDQLVMN-TV 91
Cdd:cd03297   16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGgtiVLNGTVLFDSRKKINlppqQRKIGLVFQQ--YALFPHlNV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  92 WHEIAFGLKNKgiSLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEF 171
Cdd:cd03297   93 RENLAFGLKRK--RNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQL 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169293994 172 IKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03297  171 LPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 280-466 4.17e-37

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: 135.85  E-value: 4.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDDI--VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIS----KVGCVDR---IGYLPQDPT 349
Cdd:cd03226    2 IENISFSYKKGteILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKeSSGSILlngkPIKAKERrksIGYVMQDVD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 350 T-LF---VADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASS 425
Cdd:cd03226   82 YqLFtdsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKN 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169293994 426 KEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03226  162 MERVGELIRELAAQgKAVIVITHDYEFLAKVCDRVLLLANGA 203
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 3-212 4.17e-37

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 139.82  E-value: 4.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILDEEIEND----DTK 74
Cdd:COG3839    5 ELENVSKSY-GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRmiagLEDPT-------SGEILIGGRDVTDlppkDRN 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQN----PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:COG3839   77 IAMVFQSyalyPH----M-TVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVRE 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEH-QLEGLLdVANRLIVMDEGKIV 212
Cdd:COG3839  152 PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHdQVEAMT-LADRIAVMNDGRIQ 213
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 3-212 1.26e-36

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: 135.51  E-value: 1.26e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFVF 79
Cdd:cd03295    2 EFENVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPtSGEIfiDGEDIREQDPVELRRKIGYVI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QN----PEdqlvmNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL--QSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:cd03295   82 QQiglfPH-----MTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03295  157 LLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIV 215
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 3-263 1.46e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 136.52  E-value: 1.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPkgdIDGVIILDEE--------IENDDTK 74
Cdd:PRK13636   7 KVEELNYNYSDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP---SSGRILFDGKpidysrkgLMKLRES 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:PRK13636  84 VGMVFQDPDNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKmavdEMLTKKIFVES- 233
Cdd:PRK13636 164 VLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPK----EVFAEKEMLRKv 239

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 169293994 234 ---LPnyvRVSSLC-----------DKLCLSIKEAREALVNFEN 263
Cdd:PRK13636 240 nlrLP---RIGHLMeilkekdgfvfDELDLTISQARKTLNSWKN 280
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 3-259 3.72e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 135.53  E-value: 3.72e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDID-GVIILDEEIENDD---- 72
Cdd:PRK13634   4 TFQKVEHRYqyktPFERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPtSGTVTiGERVITAGKKNKKlkpl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 -TKIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:PRK13634  84 rKKVGIVFQFPEHQLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAME 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID---NEIKMAVDEMLTK 227
Cdd:PRK13634 164 PEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQgtpREIFADPDELEAI 243

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 169293994 228 KIfveSLPNYVRVSSLC--------DKLCLSIKEAREALV 259
Cdd:PRK13634 244 GL---DLPETVKFKRALeekfgisfPKPCLTLEELAHEVV 280
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-214 4.28e-36

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase domain [Defense mechanisms];


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 142.28  E-value: 4.28e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   2 YKIENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIIldEEIENDD-- 72
Cdd:COG2274  474 IELENVSFRYPGDSPpVLDNISLTIKPGERVAIVGRSGSGKSTLLKlllgLYEPT---SGRIliDGIDL--RQIDPASlr 548

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 TKIGFVFQnpEDQLVMNTVWHEIAFGlkNKGISLKQMKR--RIGEIVNYFN-----LQSIINKETQSLSNGQKQLVALAS 145
Cdd:COG2274  549 RQIGVVLQ--DVFLFSGTIRENITLG--DPDATDEEIIEaaRLAGLHDFIEalpmgYDTVVGEGGSNLSGGQRQRLAIAR 624

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 146 VMVMNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEgLLDVANRLIVMDEGKIVID 214
Cdd:COG2274  625 ALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVED 690
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 279-479 9.71e-36

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: 132.84  E-value: 9.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIsKVGCVD-----------RIGYL 344
Cdd:COG1122    2 ELENLSFSYPGgtPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKpTSGEV-LVDGKDitkknlrelrrKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 PQDPTTLFVADKV-----------------IDdlllvddvvASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA----- 402
Cdd:COG1122   81 FQNPDDQLFAPTVeedvafgpenlglpreeIR---------ERVEEALELVGLEHLADRPPHELSGGQKQRVAIAgvlam 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 403 --KILLtkpqlllLDEPTKGIDASSKEFLANLIRGLSK-HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG1122  152 epEVLV-------LDEPTAGLDPRGRRELLELLKRLNKeGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSD 224
cbiO PRK13641
energy-coupling factor transporter ATPase;
3-212 1.61e-35

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 133.80  E-value: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIDgviILDEEIENDDT---- 73
Cdd:PRK13641   4 KFENVDYIYspgtPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPsSGTIT---IAGYHITPETGnknl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 -----KIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVM 147
Cdd:PRK13641  81 kklrkKVSLVFQFPEAQLFENTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVM 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNvTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK13641 161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLI 224
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 279-466 3.19e-35

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: 130.66  E-value: 3.19e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV-DCQGEI----------SKVGCVDRIGYL 344
Cdd:cd03225    1 ELKNLSFSYPDgarPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLgPTSGEVlvdgkdltklSLKELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 PQDPTTLFVADKVI--------DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDE 416
Cdd:cd03225   81 FQNPDDQFFGPTVEeevafgleNLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDE 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 417 PTKGIDASSKEFLANLIRGLSK-HMTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03225  161 PTAGLDPAGRRELLELLKKLKAeGKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 3-212 4.78e-35

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: 130.92  E-value: 4.78e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIiNNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPslrpkgdIDGVIILDEE-IEN---DDTK 74
Cdd:cd03299    2 KVENLSKDW-KEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLEtiagFIKP-------DSGKILLNGKdITNlppEKRD 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNpeDQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:cd03299   73 ISYVPQN--YALFPHmTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03299  151 LLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLI 209
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 3-212 7.84e-35

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: 128.71  E-value: 7.84e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKdKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDeeienddtkigfvfqnp 82
Cdd:cd03214    1 EVENLSVGYGG-RTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSS---GEILLD----------------- 59

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 edqlvmntvwheiafGLKNKGISLKQMKRRIG---EIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:cd03214   60 ---------------GKDLASLSPKELARKIAyvpQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEP 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 160 TAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03214  125 TSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIV 177
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 4-213 8.70e-35

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: 130.31  E-value: 8.70e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILD---EEIENDDTKIGF 77
Cdd:cd03261    3 LRGLTKSF-GGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPdSGEVliDGEDISGlseAELYRLRRRMGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQNPE--DQLvmnTVWHEIAFGLKNKGI-SLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:cd03261   82 LFQSGAlfDSL---TVFENVAFPLREHTRlSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVI 213
Cdd:cd03261  159 LYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVA 217
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 3-210 1.22e-34

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: 127.36  E-value: 1.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFVF 79
Cdd:cd00267    1 EIENLSFRYG-GRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPtSGEIliDGKDIAKLPLEELRRRIGYVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QnpedqlvmntvwheiafglknkgislkqmkrrigeivnyfnlqsiinketqsLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:cd00267   80 Q----------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEP 107

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 160 TAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGK 210
Cdd:cd00267  108 TSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 3-210 1.34e-34

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: 127.88  E-value: 1.34e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYP-KDKKIINNISFEIKKGDFLVITGKSGCGKTTL----LRYFKPSlrpkgdiDGVIILD-EEIENDDT--- 73
Cdd:cd03228    2 EFKNVSFSYPgRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLlkllLRLYDPT-------SGEILIDgVDLRDLDLesl 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 --KIGFVFQNPedQLVMNTVWHEIafglknkgislkqmkrrigeivnyfnlqsiinketqsLSNGQKQLVALASVMVMNP 151
Cdd:cd03228   75 rkNIAYVPQDP--FLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 152 KVILLDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDvANRLIVMDEGK 210
Cdd:cd03228  116 PILILDEATSALDPETEALILEALRALAKG--KTVIVIAHRLSTIRD-ADRIIVLDDGR 171
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 1-226 1.74e-34

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: 130.16  E-value: 1.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD-EEIENDDTK----- 74
Cdd:COG1120    1 MLEAENLSVGYG-GRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSS---GEVLLDgRDLASLSRRelarr 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPEDQLVMnTVWHEIAFG----LKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:COG1120   77 IAYVPQEPPAPFGL-TVRELVALGryphLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQE 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDneikMAVDEMLT 226
Cdd:COG1120  156 PPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQ----GPPEEVLT 227
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 1-236 1.90e-34

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: 129.59  E-value: 1.90e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KG--DIDGVIILDEEIENDdTKIGF 77
Cdd:COG4555    1 MIEVENLSKKY-GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPdSGsiLIDGEDVRKEPREAR-RQIGV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQNPE--DQLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:COG4555   79 LPDERGlyDRL---TVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLL 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLT---KKIFVE 232
Cdd:COG4555  156 LDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELREEIGEenlEDAFVA 234


                 ....
gi 169293994 233 SLPN 236
Cdd:COG4555  235 LIGS 238
cbiO PRK13646
energy-coupling factor transporter ATPase;
3-212 4.14e-34

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 129.90  E-value: 4.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP---KGDIDGVIIL----DEEIEND 71
Cdd:PRK13646   4 RFDNVSYTYqkgtPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPttgTVTVDDITIThktkDKYIRPV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:PRK13646  84 RKRIGMVFQFPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFsRDVMSQSPFQMSGGQMRKIAIVSILAMN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK13646 164 PDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIV 225
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 4-212 5.32e-34

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 131.42  E-value: 5.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpslrpkgdI-------D-GVIILDEEienD---- 71
Cdd:COG1118    5 VRNISKRFG-SFTLLDDVSLEIASGELVALLGPSGSGKTTLLR-----------IiagletpDsGRIVLNGR---Dlftn 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 ----DTKIGFVFQN----PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIIN-KETQsLSNGQKQLVA 142
Cdd:COG1118   70 lpprERRVGFVFQHyalfPH----M-TVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADrYPSQ-LSGGQRQRVA 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 143 LASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG1118  144 LARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIE 213
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 3-212 6.79e-34

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: 127.37  E-value: 6.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKdKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpkgdiDGVIILDEEIEND----DTK 74
Cdd:cd03301    2 ELENVTKRFGN-VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIagleEPT-------SGRIYIGGRDVTDlppkDRD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQN----PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:cd03301   74 IAMVFQNyalyPH----M-TVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVRE 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEH-QLEGlLDVANRLIVMDEGKIV 212
Cdd:cd03301  149 PKVFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHdQVEA-MTMADRIAVMNDGQIQ 210
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 3-216 3.45e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 125.20  E-value: 3.45e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDTK---- 74
Cdd:PRK13651   4 KVKNIVKIFnkklPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPD---TGTIEWIFKDEKNKKKtkek 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 --------------------------IGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIIN 127
Cdd:PRK13651  81 ekvleklviqktrfkkikkikeirrrVGVVFQFAEYQLFEQTIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQ 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 128 KETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMD 207
Cdd:PRK13651 161 RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFK 239


                 ....*....
gi 169293994 208 EGKIVIDNE 216
Cdd:PRK13651 240 DGKIIKDGD 248
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 4-212 3.57e-32

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: 123.06  E-value: 3.57e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFtYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF------KPSLRPKGDI--DGVII--LDEEIENDDT 73
Cdd:cd03260    3 LRDLNV-YYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLnrlndlIPGAPDEGEVllDGKDIydLDVDVLELRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 KIGFVFQNPeDQLVMnTVWHEIAFGLKNKGISLKqmkRRIGEIV----------NYFNLQSIINketqSLSNGQKQLVAL 143
Cdd:cd03260   82 RVGMVFQKP-NPFPG-SIYDNVAYGLRLHGIKLK---EELDERVeealrkaalwDEVKDRLHAL----GLSGGQQQRLCL 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 144 ASVMVMNPKVILLDEATAQLDPVNR---EEFIKILKHinddfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03260  153 ARALANEPEVLLLDEPTSALDPISTakiEELIAELKK-----EYTIVIVTHNMQQAARVADRTAFLLNGRLV 219
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 3-230 6.86e-32

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 122.51  E-value: 6.86e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDIDgviILDEEIENDDTKIGFV 78
Cdd:COG1121    8 ELENLTVSYG-GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKailgLLPPT---SGTVR---LFGKPPRRARRRIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPED---------QLVMNTVWHEIAFGlknKGISlKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:COG1121   81 PQRAEVdwdfpitvrDVVLMGRYGRRGLF---RRPS-RADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDneikmAVDEMLTKKI 229
Cdd:COG1121  157 DPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAHG-----PPEEVLTPEN 230


                 .
gi 169293994 230 F 230
Cdd:COG1121  231 L 231
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 14-226 7.94e-32

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: 122.50  E-value: 7.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSLRPKgdidgVIILDEEIENDD-----TKIGFV-----F 79
Cdd:COG1119   15 GKTILDDISWTVKPGEHWAILGPNGAGKSTLLSlitgDLPPTYGND-----VRLFGERRGGEDvwelrKRIGLVspalqL 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPEDQLVMNTV----------WHEIAfglknkgislKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:COG1119   90 RFPRDETVLDVVlsgffdsiglYREPT----------DEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVK 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIkmavDEMLT 226
Cdd:COG1119  160 DPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPK----EEVLT 232
cbiO PRK13643
energy-coupling factor transporter ATPase;
1-212 1.33e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 123.31  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDID-GVIIL-----DEEIE 69
Cdd:PRK13643   1 MIKFEKVNYTYqpnsPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPtEGKVTvGDIVVsstskQKEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  70 NDDTKIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMV 148
Cdd:PRK13643  81 PVRKKVGVVFQFPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILA 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK13643 161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHII 223
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 3-211 1.45e-31

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: 119.42  E-value: 1.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDIdgvIILDEEIENDDT----K 74
Cdd:cd03230    2 EVRNLSKRY-GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKiilgLLKPD---SGEI---KVLGKDIKKEPEevkrR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPE--DQLvmnTVWHeiafglknkgislkqmkrrigeivnyfNLQsiinketqsLSNGQKQLVALASVMVMNPK 152
Cdd:cd03230   75 IGYLPEEPSlyENL---TVRE---------------------------NLK---------LSGGMKQRLALAQALLHDPE 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 153 VILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:cd03230  116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
cbiO PRK13649
energy-coupling factor transporter ATPase;
4-260 2.09e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 122.55  E-value: 2.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIdgVIILDEEIENDDT------ 73
Cdd:PRK13649   5 LQNVSYTYqagtPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGS--VRVDDTLITSTSKnkdikq 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 ---KIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:PRK13649  83 irkKVGLVFQFPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILAM 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIK---MAVDEMLT 226
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKdifQDVDFLEE 241

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 169293994 227 KKIFVESLPNYVRvsSLCDK------LCLSIKEAREALVN 260
Cdd:PRK13649 242 KQLGVPKITKFAQ--RLADRgisfssLPITIEEFREVLKH 279
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 278-476 2.88e-31

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: 120.36  E-value: 2.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD----------------- 339
Cdd:cd03260    1 IELRDLNVYYGDKhALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLIPGAPDEGEVLldgkdiydldvdvlelr 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 -RIGYLPQDPTtLF---VADKV-----IDDLLLVDDVVASVESHLDNFGIID-LKD-AHPFDLSSGQKQLVALAKILLTK 408
Cdd:cd03260   81 rRVGMVFQKPN-PFpgsIYDNVayglrLHGIKLKEELDERVEEALRKAALWDeVKDrLHALGLSGGQQQRLCLARALANE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 409 PQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREF 476
Cdd:cd03260  160 PEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-212 4.44e-31

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 122.88  E-value: 4.44e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKII---NNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpkgdiDGVIILD-EEIENDD 72
Cdd:COG1135    1 MIELENLSKTFPTKGGPVtalDDVSLTIEKGEIFGIIGYSGAGKSTLIRCInlleRPT-------SGSVLVDgVDLTALS 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 T--------KIGFVFQNpeDQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVAL 143
Cdd:COG1135   74 ErelraarrKIGMIFQH--FNLLSSrTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 144 ASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG1135  152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIV 220
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
5-212 6.20e-31

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 126.05  E-value: 6.20e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTL----LRYFKPSlrpKGDI--DGVIIldEEIENDD--TKIG 76
Cdd:COG1132  343 ENVSFSYPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLvnllLRFYDPT---SGRIliDGVDI--RDLTLESlrRQIG 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPedQLVMNTVWHEIAFGlkNKGISLKQMKR-----RIGEIVNYFN--LQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:COG1132  418 VVPQDT--FLFSGTIRENIRYG--RPDATDEEVEEaakaaQAHEFIEALPdgYDTVVGERGVNLSGGQRQRIAIARALLK 493

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 150 NPKVILLDEATAQLDPVNrEEfiKILKHINDDF-NVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:COG1132  494 DPPILILDEATSALDTET-EA--LIQEALERLMkGRTTIVIAHRLSTIRN-ADRILVLDDGRIV 553
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 3-211 7.52e-31

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: 118.79  E-value: 7.52e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDIDgviILDEEIENDDTKIGFV 78
Cdd:cd03235    1 EVEDLTVSYG-GHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKailgLLKPT---SGSIR---VFGKPLEKERKRIGYV 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPE---------DQLVMNTVWHEIAFGLKNKgislKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:cd03235   74 PQRRSidrdfpisvRDVVLMGLYGHKGLFRRLS----KADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQ 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:cd03235  150 DPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
14-211 1.44e-30

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 122.36  E-value: 1.44e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILDEEIEND----DTKIGFVFQN---- 81
Cdd:PRK09452  26 GKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRliagFETPD-------SGRIMLDGQDITHvpaeNRHVNTVFQSyalf 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  82 PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:PRK09452  99 PH----M-TVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLS 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 169293994 162 QLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK09452 174 ALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRI 223
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
19-467 1.76e-30

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 123.98  E-value: 1.76e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  19 NNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILD-EEIENDDTK------IGFVFQnpEDQLV 87
Cdd:COG1129   21 DGVSLELRPGEVHALLGENGAGKSTLMKilsgVYQPD-------SGEILLDgEPVRFRSPRdaqaagIAIIHQ--ELNLV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  88 MN-TVWHEIAFG--LKNKG-ISLKQMKRRIGEIVNYFNLQsiINKETQ--SLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:COG1129   92 PNlSVAENIFLGrePRRGGlIDWRAMRRRARELLARLGLD--IDPDTPvgDLSVAQQQLVEIARALSRDARVLILDEPTA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 162 QLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIK-MAVDEMLTKKIfveslpnyvrv 240
Cdd:COG1129  170 SLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAeLTEDELVRLMV----------- 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 241 sslcdklclsikeAREalvnFENFDIKIMDEIDnRILMKVRDLNFGHddiVLKDLEIDILENEILSIVGANGSGKSSFLR 320
Cdd:COG1129  238 -------------GRE----LEDLFPKRAAAPG-EVVLEVEGLSVGG---VVRDVSFSVRAGEILGIAGLVGAGRTELAR 296

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 321 CLAGLVDC-QGEISkvgcVD---------------RIGYLPQDPTT--LF----VADKVIddlllvddvvASVESHLDNF 378
Cdd:COG1129  297 ALFGADPAdSGEIR----LDgkpvrirsprdairaGIAYVPEDRKGegLVldlsIRENIT----------LASLDRLSRG 362

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 379 GIIDLKD----------------AHPFD----LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK 438
Cdd:COG1129  363 GLLDRRReralaeeyikrlriktPSPEQpvgnLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAA 442

                        490       500       510
                 ....*....|....*....|....*....|
gi 169293994 439 H-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:COG1129  443 EgKAVIVISSELPELLGLSDRILVMREGRI 472
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-468 2.42e-30

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 124.02  E-value: 2.42e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpslrpkgdidgviILDEEIEND--------DTKI 75
Cdd:COG0488    1 LENLSKSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLK----------------ILAGELEPDsgevsipkGLRI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNP---EDQlvmnTVWHEIAFGLKNKGISLKQMKR-------------RIGEIVNYF------NLQSII------- 126
Cdd:COG0488   64 GYLPQEPpldDDL----TVLDTVLDGDAELRALEAELEEleaklaepdedleRLAELQEEFealggwEAEARAeeilsgl 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 127 -------NKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDpVNR----EEFIKilkhindDFNVTVVFVEHQLEg 195
Cdd:COG0488  140 gfpeedlDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LESiewlEEFLK-------NYPGTVLVVSHDRY- 210

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 196 LLD-VANRLIVMDEGKIVI--------------DNEIKMAVDEMLTKKI-----FVESLP--------NYVRVSSLcDKL 247
Cdd:COG0488  211 FLDrVATRILELDRGKLTLypgnysayleqraeRLEQEAAAYAKQQKKIakeeeFIRRFRakarkakqAQSRIKAL-EKL 289

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 248 CLSIKEAREALVNFEnfdIKIMDEIDNRILMkVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-L 325
Cdd:COG0488  290 EREEPPRRDKTVEIR---FPPPERLGKKVLE-LEGLSKSYGDkTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGeL 365

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 326 VDCQGEIsKVGCVDRIGYLPQDPTTLFVADKVID--DLLLVDDVVASVESHLDNFGiidlkdahpF----------DLSS 393
Cdd:COG0488  366 EPDSGTV-KLGETVKIGYFDQHQEELDPDKTVLDelRDGAPGGTEQEVRGYLGRFL---------FsgddafkpvgVLSG 435

                        490       500       510       520       530       540       550
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 394 GQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIR---GlskhmTIVVASHDLEFVAKISDRVAMIFNGQME 468
Cdd:COG0488  436 GEKARLALAKLLLSPPNVLLLDEPTNHLDIETLEALEEALDdfpG-----TVLLVSHDRYFLDRVATRILEFEDGGVR 508
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 3-211 2.67e-30

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: 117.25  E-value: 2.67e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpKGDI--DGVIILD--EEIENDDTK 74
Cdd:cd03262    2 EIKNLHKSF-GDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCInlleEPD---SGTIiiDGLKLTDdkKNINELRQK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNpedqlvMN-----TVWHEIAFGL-KNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:cd03262   78 VGMVFQQ------FNlfphlTVLENITLAPiKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:cd03262  152 MNPKVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
cbiO PRK13645
energy-coupling factor transporter ATPase;
4-232 6.39e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 118.57  E-value: 6.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTY----PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK------GD--IDGVIILDEEIEND 71
Cdd:PRK13645   9 LDNVSYTYakktPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivGDyaIPANLKKIKEVKRL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:PRK13645  89 RKEIGLVFQFPEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMD 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV-IDNEIKMAVDEMLTKKI 229
Cdd:PRK13645 169 GNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVIsIGSPFEIFSNQELLTKI 248


                 ...
gi 169293994 230 FVE 232
Cdd:PRK13645 249 EID 251
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 279-479 8.11e-30

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 117.11  E-value: 8.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVG-----CVDRIGYLPQD---- 347
Cdd:COG1121    8 ELENLTVSYGGrPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPpTSGTVRLFGkpprrARRRIGYVPQRaevd 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 ---PTTlfVAD--------KVIDDLLLVDDVVASVESHLDNFGIIDLKDaHPF-DLSSGQKQLVALAK---------ILl 406
Cdd:COG1121   88 wdfPIT--VRDvvlmgrygRRGLFRRPSRADREAVDEALERVGLEDLAD-RPIgELSGGQQQRVLLARalaqdpdllLL- 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 407 tkpqllllDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIfNGQMESVDSTREFFSH 479
Cdd:COG1121  164 --------DEPFAGVDAATEEALYELLRELRREgKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTP 228
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
16-211 1.02e-29

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 119.42  E-value: 1.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLR-------YFKPSLRPKG-DIDGViildeeiENDDTKIGFVFQNPEDQLV 87
Cdd:PRK10851  16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRiiaglehQTSGHIRFHGtDVSRL-------HARDRKVGFVFQHYALFRH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  88 MnTVWHEIAFGLK----NKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQL 163
Cdd:PRK10851  89 M-TVFDNIAFGLTvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGAL 167

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 169293994 164 DPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK10851 168 DAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNI 215
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 18-212 1.50e-29

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: 116.97  E-value: 1.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlRPKGDIDGVIIL----DEEIENDDTKIGFVFQN----PEdq 85
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCInrliEPT-SGKVLIDGQDIAamsrKELRELRRKKISMVFQSfallPH-- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  86 lvmNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDP 165
Cdd:cd03294  117 ---RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDP 193

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 166 VNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03294  194 LIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLV 240
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 5-212 4.13e-29

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: 114.63  E-value: 4.13e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpKGD--IDGVIILDEEIENDDTKIGFV 78
Cdd:cd03253    4 ENVTFAYDPGRPVLKDVSFTIPAGKKVAIVGPSGSGKSTilrlLFRFYDVS---SGSilIDGQDIREVTLDSLRRAIGVV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 fqnPEDQLVMN-TVWHEIAFGlkNKGISLKQMKR-----RIGEIVNYFN--LQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:cd03253   81 ---PQDTVLFNdTIGYNIRYG--RPDATDEEVIEaakaaQIHDKIMRFPdgYDTIVGERGLKLSGGEKQRVAIARAILKN 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 151 PKVILLDEATAQLDPVNREEfikILKHINDDF-NVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03253  156 PPILLLDEATSALDTHTERE---IQAALRDVSkGRTTIVIAHRLSTIVN-ADKIIVLKDGRIV 214
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 4-212 7.96e-29

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: 119.86  E-value: 7.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpKGDI--DGVIILDEEIENDDTKIGF 77
Cdd:COG4988  339 LEDVSFSYPGGRPALDGLSLTIPPGERVALVGPSGAGKSTllnlLLGFLPPY---SGSIliNGVDLSDLDPASWRRQIAW 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQNPedQLVMNTVWHEIAFGlkNKGISLKQMKR-----RIGEIVNYFN--LQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:COG4988  416 VPQNP--YLFAGTIRENLRLG--RPDASDEELEAaleaaGLDEFVAALPdgLDTPLGEGGRGLSGGQAQRLALARALLRD 491

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEgLLDVANRLIVMDEGKIV 212
Cdd:COG4988  492 APLLLLDEPTAHLDAETEAEILQALRRLAKG--RTVILITHRLA-LLAQADRILVLDDGRIV 550
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 3-212 1.13e-28

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: 113.47  E-value: 1.13e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpKGDI--DGVIILDEEIENDDTKIG 76
Cdd:cd03254    4 EFENVNFSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTlinlLMRFYDPQ---KGQIliDGIDIRDISRKSLRSMIG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQnpEDQLVMNTVWHEIAFG------------LKNKGISLKQMKRRIGeivnyfnLQSIINKETQSLSNGQKQLVALA 144
Cdd:cd03254   81 VVLQ--DTFLFSGTIMENIRLGrpnatdeevieaAKEAGAHDFIMKLPNG-------YDTVLGENGGNLSQGERQLLAIA 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 145 SVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03254  152 RAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKII 216
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 16-212 1.63e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 115.33  E-value: 1.63e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK-GDI--------DGVIILDEEIENDDTKI----------G 76
Cdd:PRK13631  40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKyGTIqvgdiyigDKKNNHELITNPYSKKIknfkelrrrvS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQ-SIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK13631 120 MVFQFPEYQLFKDTIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDdSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKIL 255
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 1-212 3.07e-28

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 114.90  E-value: 3.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKIIN---NISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpKGDI--DGVIIL---DEEI 68
Cdd:PRK11153   1 MIELKNISKVFPQGGRTIHalnNVSLHIPAGEIFGVIGASGAGKSTLIRCInlleRPT---SGRVlvDGQDLTalsEKEL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  69 ENDDTKIGFVFQ--NpedQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASV 146
Cdd:PRK11153  78 RKARRQIGMIFQhfN---LLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 147 MVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11153 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLV 220
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 279-467 3.65e-28

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: 110.22  E-value: 3.65e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV-DCQGEIsKVGCVD-----------RIGYLP 345
Cdd:cd03214    1 EVENLSVGYGGrTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLkPSSGEI-LLDGKDlaslspkelarKIAYVP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QdpttlfvadkviddlllvddvvAsveshLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASS 425
Cdd:cd03214   80 Q----------------------A-----LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAH 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 426 KEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03214  133 QIELLELLRRLARErgKTVVMVLHDLNLAARYADRVILLKDGRI 176
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 277-475 4.53e-28

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: 112.44  E-value: 4.53e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIskvgCVD--------------R 340
Cdd:COG1120    1 MLEAENLSVGYGGrPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSsGEV----LLDgrdlaslsrrelarR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 341 IGYLPQDPTTLF---VADKVI--------DDLLLVDDVVASVESHLDNFGIIDLKDaHPFD-LSSGQKQLVALAK----- 403
Cdd:COG1120   77 IAYVPQEPPAPFgltVRELVAlgryphlgLFGRPSAEDREAVEEALERTGLEHLAD-RPVDeLSGGERQRVLIARalaqe 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 404 ----IlltkpqlllLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:COG1120  156 ppllL---------LDEPTSHLDLAHQLEVLELLRRLARErgRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEE 224
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-212 4.76e-28

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 112.65  E-value: 4.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKD---KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD-EEIENDDTKIG 76
Cdd:COG4525    3 MLTVRHVSVRYPGGgqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSS---GEITLDgVPVTGPGADRG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNpeDQLV--MNtVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:COG4525   80 VVFQK--DALLpwLN-VLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFL 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMD--EGKIV 212
Cdd:COG4525  157 LMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSpgPGRIV 216
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 16-212 6.28e-28

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: 111.37  E-value: 6.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEienDDTK----------IGFVFQNP--- 82
Cdd:cd03219   14 VALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTS---GSVLFDGE---DITGlppheiarlgIGRTFQIPrlf 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 ------EDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:cd03219   88 peltvlENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLL 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 157 DEATAQLDPVNREEFIKILKHINdDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03219  168 DEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVI 222
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 279-462 6.33e-28

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: 110.70  E-value: 6.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVG-----CVDRIGYLPQD---- 347
Cdd:cd03235    1 EVEDLTVSYGGhPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKpTSGSIRVFGkplekERKRIGYVPQRrsid 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 ---PTTL--FVA----DKVIDDLLLVDDVVASVESHLDNFGIIDLKDaHPFD-LSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:cd03235   81 rdfPISVrdVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELAD-RQIGeLSGGQQQRVLLARALVQDPDLLLLDEP 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 418 TKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMI 462
Cdd:cd03235  160 FAGVDPKTQEDIYELLRELRREgMTILVVTHDLGLVLEYFDRVLLL 205
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 18-161 8.78e-28

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: 108.50  E-value: 8.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFVFQNPEDQLVMnTVWHE 94
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPtEGTIllDGQDLTDDERKSLRKEIGYVFQDPQLFPRL-TVREN 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994   95 IAFGLKNKGISLKQMKRRIGEIVNYFNLQ----SIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:pfam00005  80 LRLGLLLKGLSKREKDARAEEALEKLGLGdladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 2-214 1.03e-27

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: 110.37  E-value: 1.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   2 YKIENFSFTYPKDK-KIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILD----EEIENDDTK-- 74
Cdd:cd03245    3 IEFRNVSFSYPNQEiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDgtdiRQLDPADLRrn 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPedQLVMNTVWHEIAFGlknKGISLKQMKRRIGEIV----------NYFNLQsiINKETQSLSNGQKQLVALA 144
Cdd:cd03245   80 IGYVPQDV--TLFYGTLRDNITLG---APLADDERILRAAELAgvtdfvnkhpNGLDLQ--IGERGRGLSGGQRQAVALA 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 145 SVMVMNPKVILLDEATAQLDPVNREEFIKILKH-INDDfnvTVVFVEHQLEgLLDVANRLIVMDEGKIVID 214
Cdd:cd03245  153 RALLNDPPILLLDEPTSAMDMNSEERLKERLRQlLGDK---TLIIITHRPS-LLDLVDRIIVMDSGRIVAD 219
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-217 1.14e-27

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 110.61  E-value: 1.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKiinNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIILDEEIenDDTK 74
Cdd:COG3840    1 MLRLDDLTYRYGDFPL---RFDLTIAAGERVAILGPSGAGKSTLLNliagFLPPD---SGRIlwNGQDLTALPP--AERP 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQnpEDQLVMN-TVWHEIAFGLKNkgiSLK---QMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:COG3840   73 VSMLFQ--ENNLFPHlTVAQNIGLGLRP---GLKltaEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRK 147

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEI 217
Cdd:COG3840  148 RPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPT 214
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 279-466 1.52e-27

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: 108.10  E-value: 1.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISkvgcvdrigYLPQDPTTLFVadk 356
Cdd:cd00267    1 EIENLSFRYGGrTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKpTSGEIL---------IDGKDIAKLPL--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 viddlllvddvvasvESHLDNFGIIdlkdahpFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL 436
Cdd:cd00267   69 ---------------EELRRRIGYV-------PQLSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLREL 126

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169293994 437 SKH-MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd00267  127 AEEgRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 3-212 1.56e-27

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: 109.59  E-value: 1.56e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKdKKIINNISFEIKKGdFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVI-ILDEEIENDDTK----IGF 77
Cdd:cd03264    2 QLENLTKRYGK-KRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSS---GTIrIDGQDVLKQPQKlrrrIGY 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQ--NPEDQLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:cd03264   77 LPQefGVYPNF---TVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILI 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03264  154 VDEPTAGLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLV 208
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 17-212 2.05e-27

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: 109.45  E-value: 2.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  17 IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD-EEIENDDT------KIGFVfqnPEDQLV-- 87
Cdd:cd03224   15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRS---GSIRFDgRDITGLPPheraraGIGYV---PEGRRIfp 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  88 -MnTVWHEIAFGLKNKGISLKqmKRRIGEIVNYF-NLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDP 165
Cdd:cd03224   89 eL-TVEENLLLGAYARRRAKR--KARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 166 VNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03224  166 KIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVV 211
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
17-212 3.68e-27

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 112.12  E-value: 3.68e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  17 IINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpKGDI--DGVIILDEEIENDDtkIGFVFQN----PEDQL 86
Cdd:PRK11432  21 VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVagleKPT---EGQIfiDGEDVTHRSIQQRD--ICMVFQSyalfPHMSL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  87 VMNtvwheIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPV 166
Cdd:PRK11432  96 GEN-----VGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDAN 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 167 NREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11432 171 LRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIM 216
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 16-212 4.37e-27

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: 109.74  E-value: 4.37e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILD-EEIEN----DDTKIGFV--FQNPed 84
Cdd:COG0411   18 VAVDDVSLEVERGEIVGLIGPNGAGKTTLFNlitgFYRPT-------SGRILFDgRDITGlpphRIARLGIArtFQNP-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  85 QLVMN-TV---------------WHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:COG0411   89 RLFPElTVlenvlvaaharlgrgLLAALLRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG0411  169 TEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVI 232
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
1-212 4.49e-27

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 110.10  E-value: 4.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI-----------DGVIILDEEI 68
Cdd:PRK13638   1 MLATSDLWFRY-QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPqKGAVlwqgkpldyskRGLLALRQQV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  69 ENddtkigfVFQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:PRK13638  80 AT-------VFQDPEQQIFYTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALV 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDFNvTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK13638 153 LQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQIL 215
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 3-212 1.39e-26

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: 109.76  E-value: 1.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDK---KIINNISFEIKKGDFLVITGKSGCGKTTL----LRYFKPSLRPKGDI--DGVIIL---DEEIEN 70
Cdd:COG0444    3 EVRNLKVYFPTRRgvvKAVDGVSFDVRRGETLGLVGESGSGKSTLaraiLGLLPPPGITSGEIlfDGEDLLklsEKELRK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  71 -DDTKIGFVFQNPEDQL--VMnTVWHEIAFGLK-NKGISLKQMKRRIGEIVNYFNL---QSIINK---EtqsLSNGQKQL 140
Cdd:COG0444   83 iRGREIQMIFQDPMTSLnpVM-TVGDQIAEPLRiHGGLSKAEARERAIELLERVGLpdpERRLDRyphE---LSGGMRQR 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 141 VALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG0444  159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIV 230
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 5-211 1.78e-26

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: 106.72  E-value: 1.78e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEIEND---------DTKI 75
Cdd:cd03292    4 INVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTS---GTIRVNGQDVSDlrgraipylRRKI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQnpEDQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:cd03292   81 GVVFQ--DFRLLPDrNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTIL 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:cd03292  159 IADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-214 1.96e-26

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 107.86  E-value: 1.96e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKD----KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdIDGVIILDE---EIENDD- 72
Cdd:COG1101    1 MLELKNLSKTFNPGtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNA----------IAGSLPPDSgsiLIDGKDv 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 TK---------IGFVFQNPedqlVMNTvwheiAFGL-------------KNKGISLKQMKRRIGEIVNYF-----NLQSI 125
Cdd:COG1101   71 TKlpeykrakyIGRVFQDP----MMGT-----APSMtieenlalayrrgKRRGLRRGLTKKRRELFRELLatlglGLENR 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 126 INKETQSLSNGQKQLVALasVM-VMN-PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRL 203
Cdd:COG1101  142 LDTKVGLLSGGQRQALSL--LMaTLTkPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRL 219

                        250
                 ....*....|.
gi 169293994 204 IVMDEGKIVID 214
Cdd:COG1101  220 IMMHEGRIILD 230
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 3-475 2.88e-26

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: 111.82  E-value: 2.88e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFK--PSLRPkgdIDGVII----------------- 63
Cdd:TIGR03269   2 EVKNLTKKF-DGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRgmDQYEP---TSGRIIyhvalcekcgyverpsk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   64 ---------------------LDEEIENDDTK-IGFVFQNP----EDQLVMNTVWHeiafGLKNKGISLKQMKRRIGEIV 117
Cdd:TIGR03269  78 vgepcpvcggtlepeevdfwnLSDKLRRRIRKrIAIMLQRTfalyGDDTVLDNVLE----ALEEIGYEGKEAVGRAVDLI 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  118 NYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLL 197
Cdd:TIGR03269 154 EMVQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIE 233

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  198 DVANRLIVMDEGKIVIDNEikmaVDEMLTKkiFVESLPnyvrvsslcdklclsikeareALVNFENFDIKimDEIdnril 277
Cdd:TIGR03269 234 DLSDKAIWLENGEIKEEGT----PDEVVAV--FMEGVS---------------------EVEKECEVEVG--EPI----- 279

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  278 MKVRDLN---FGHDDIVLK---DLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI-----------SKVGCVD 339
Cdd:TIGR03269 280 IKVRNVSkryISVDRGVVKavdNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEpTSGEVnvrvgdewvdmTKPGPDG 359

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  340 R------IGYLPQDpTTLFVADKVIDDLLLvddvvaSVESHL-DNFG----IIDLK-------------DAHPFDLSSGQ 395
Cdd:TIGR03269 360 RgrakryIGILHQE-YDLYPHRTVLDNLTE------AIGLELpDELArmkaVITLKmvgfdeekaeeilDKYPDELSEGE 432

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  396 KQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDST 473
Cdd:TIGR03269 433 RHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMeqTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDP 512


                  ..
gi 169293994  474 RE 475
Cdd:TIGR03269 513 EE 514
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
14-214 1.08e-25

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 105.17  E-value: 1.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRP--KGD--IDGVIILDEEIenDDTKI----GFVFQ--NPE 83
Cdd:PRK09493  13 PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCIN-KLEEitSGDliVDGLKVNDPKV--DERLIrqeaGMVFQqfYLF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 DQLvmnTVWHEIAFG-LKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:PRK09493  90 PHL---TALENVMFGpLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 163 LDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAED 217
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 18-212 1.33e-25

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: 104.37  E-value: 1.33e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP---KGDIDGVIILDEEIENDDtKIGFVFQNP--EDQLV--MNT 90
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPtsgRATVAGHDVVREPREVRR-RIGIVFQDLsvDDELTgwENL 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEIAFGLKNKgislkQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREE 170
Cdd:cd03265   95 YIHARLYGVPGA-----ERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAH 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169293994 171 FIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03265  170 VWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRII 211
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 3-230 2.72e-25

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 104.73  E-value: 2.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFK------PSLRPKGDI--DGVIILDEEIENDD-- 72
Cdd:COG1117   13 EVRNLNVYY-GDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrmndliPGARVEGEIllDGEDIYDPDVDVVElr 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  73 TKIGFVFQNPedqlvmN----TVWHEIAFGLKNKGISlkqMKRRIGEIVNyfnlQSI------------INKETQSLSNG 136
Cdd:COG1117   92 RRVGMVFQKP------NpfpkSIYDNVAYGLRLHGIK---SKSELDEIVE----ESLrkaalwdevkdrLKKSALGLSGG 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 137 QKQLVALASVMVMNPKVILLDEATAQLDPVNR---EEFIKILKHinddfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVI 213
Cdd:COG1117  159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTakiEELILELKK-----DYTIVIVTHNMQQAARVSDYTAFFYLGELVE 233

                        250
                 ....*....|....*..
gi 169293994 214 DNEikmavdemlTKKIF 230
Cdd:COG1117  234 FGP---------TEQIF 241
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 4-211 6.56e-25

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: 101.14  E-value: 6.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGD--IDGVII--LDEEIENDdtKIGF 77
Cdd:cd03246    3 VENVSFRYPGAEPpVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPtSGRvrLDGADIsqWDPNELGD--HVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQnpEDQLVMNTVWHEIafglknkgislkqmkrrigeivnyfnlqsiinketqsLSNGQKQLVALASVMVMNPKVILLD 157
Cdd:cd03246   81 LPQ--DDELFSGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLD 121

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169293994 158 EATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEgLLDVANRLIVMDEGKI 211
Cdd:cd03246  122 EPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPE-TLASADRILVLEDGRV 173
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 279-467 8.34e-25

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: 100.94  E-value: 8.34e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DcQGEIsKVGCVD----------RIGYL 344
Cdd:cd03230    2 EVRNLSkrYG-KKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLkpD-SGEI-KVLGKDikkepeevkrRIGYL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 PQDPTtLFvadkviddlllvddVVASVESHLDnfgiidlkdahpfdLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS 424
Cdd:cd03230   79 PEEPS-LY--------------ENLTVRENLK--------------LSGGMKQRLALAQALLHDPELLILDEPTSGLDPE 129

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 425 SKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03230  130 SRREFWELLRELKKEgKTILLSSHILEEAERLCDRVAILNNGRI 173
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
18-212 1.27e-24

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 105.30  E-value: 1.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILD----EEIENDDTKIGFVFQNPEDQLVMnTVWH 93
Cdd:PRK11607  35 VDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT---AGQIMLDgvdlSHVPPYQRPINMMFQSYALFPHM-TVEQ 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  94 EIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNRE---- 169
Cdd:PRK11607 111 NIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKLRDrmql 190

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 170 EFIKILKHInddfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11607 191 EVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFV 229
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 4-212 1.40e-24

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: 101.92  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLL----RYFKPSlrpKGDI--DGVIILDEEIENDDTKIG 76
Cdd:cd03251    3 FKNVTFRYPGDGPpVLRDISLDIPAGETVALVGPSGSGKSTLVnlipRFYDVD---SGRIliDGHDVRDYTLASLRRQIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPedQLVMNTVWHEIAFGlkNKGISLKQMkRRIGEIVNYFN--------LQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:cd03251   80 LVSQDV--FLFNDTVAENIAYG--RPGATREEV-EEAARAANAHEfimelpegYDTVIGERGVKLSGGQRQRIAIARALL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03251  155 KDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIV 215
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 18-477 1.86e-24

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 106.86  E-value: 1.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKT----TLLRYFKPS----------LRPKGDidGVIILDEEIEND-----DTKIGFV 78
Cdd:PRK10261  32 VRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLEQAgglvqcdkmlLRRRSR--QVIELSEQSAAQmrhvrGADMAMI 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEDQL-VMNTVWHEIAFGLK-NKGIS----LKQMKRRIgEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:PRK10261 110 FQEPMTSLnPVFTVGEQIAESIRlHQGASreeaMVEAKRML-DQVRIPEAQTILSRYPHQLSGGMRQRVMIAMALSCRPA 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 153 VILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKM------------- 219
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQifhapqhpytral 268

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 220 --AVDEM-------LTKKIFVESLPNYVRVSSLCDKLCL----SIKEAREALVNFenfdiKIMDEIDNRILMKVRdlnfg 286
Cdd:PRK10261 269 laAVPQLgamkgldYPRRFPLISLEHPAKQEPPIEQDTVvdgePILQVRNLVTRF-----PLRSGLLNRVTREVH----- 338

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 287 hddiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI------------SKVGCVDR-IGYLPQDPTT-- 350
Cdd:PRK10261 339 ----AVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQgGEIifngqridtlspGKLQALRRdIQFIFQDPYAsl 414

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 ---LFVADKV-----IDDLLLVDDVVASVESHLDNFGiidLKDAH----PFDLSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:PRK10261 415 dprQTVGDSImeplrVHGLLPGKAAAARVAWLLERVG---LLPEHawryPHEFSGGQRQRICIARALALNPKVIIADEAV 491

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 419 KGIDASSKEFLANLIRGLSKHMTI--VVASHDLEFVAKISDRVAMIFNGQMESVDSTREFF 477
Cdd:PRK10261 492 SALDVSIRGQIINLLLDLQRDFGIayLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVF 552
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 280-479 3.36e-24

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: 101.04  E-value: 3.36e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIsKVGCVD--------------RIGY 343
Cdd:cd03261    3 LRGLTKSFGGrTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDsGEV-LIDGEDisglseaelyrlrrRMGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 344 LPQDP---TTLFVADKVI-----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLD 415
Cdd:cd03261   82 LFQSGalfDSLTVFENVAfplreHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLLYD 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 416 EPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:cd03261  162 EPTAGLDPIASGVIDDLIRSLKKElgLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRAS 227
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
10-211 3.38e-24

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 103.77  E-value: 3.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  10 TYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdI-------DGVIILDEEIEND----DTKIGFV 78
Cdd:PRK11650  12 SYDGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRM----------VagleritSGEIWIGGRVVNElepaDRDIAMV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQN----PEdqlvMnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:PRK11650  82 FQNyalyPH----M-SVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVF 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 155 LLDEATAQLDP---VN-REEfikiLKHINDDFNVTVVFVEH-QLEGlLDVANRLIVMDEGKI 211
Cdd:PRK11650 157 LFDEPLSNLDAklrVQmRLE----IQRLHRRLKTTSLYVTHdQVEA-MTLADRVVVMNGGVA 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 13-218 4.78e-24

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 100.98  E-value: 4.78e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  13 KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKG--------DIDGVIILDEE---IENDDTKIGFVFQN 81
Cdd:PRK11264  14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAgtirvgdiTIDTARSLSQQkglIRQLRQHVGFVFQN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  82 pedqlvMNTVWHEIAfgLKN--------KGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:PRK11264  94 ------FNLFPHRTV--LENiiegpvivKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEV 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIK 218
Cdd:PRK11264 166 ILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAK 229
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
280-476 5.79e-24

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 100.14  E-value: 5.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISkVGCVD----------RIGYLPQ 346
Cdd:COG1131    3 VRGLTkrYG-DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTsGEVR-VLGEDvardpaevrrRIGYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 347 DPTT----------LFVADkviDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAK---------Illt 407
Cdd:COG1131   81 EPALypdltvrenlRFFAR---LYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALallhdpellI--- 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 408 kpqlllLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREF 476
Cdd:COG1131  155 ------LDEPTSGLDPEARRELWELLRELAAEgKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 4-212 1.13e-23

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: 99.54  E-value: 1.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYP--KDKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPslrpkgdIDGVIILDeeieNDDTK--- 74
Cdd:cd03249    3 FKNVSFRYPsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTvvslLERFYDP-------TSGEILLD----GVDIRdln 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 -------IGFVFQNPedQLVMNTVWHEIAFGlKNKGISLKQMkrrigEIVNYFNLQSIINK-----ETQ------SLSNG 136
Cdd:cd03249   72 lrwlrsqIGLVSQEP--VLFDGTIAENIRYG-KPDATDEEVE-----EAAKKANIHDFIMSlpdgyDTLvgergsQLSGG 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 137 QKQLVALASVMVMNPKVILLDEATAQLDpvNREEfiKILKHINDDF--NVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03249  144 QKQRIAIARALLRNPKILLLDEATSALD--AESE--KLVQEALDRAmkGRTTIVIAHRLSTIRN-ADLIAVLQNGQVV 216
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 277-467 1.15e-23

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: 99.12  E-value: 1.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLN--FGHDDI---VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQG-EISKVGCVDR--- 340
Cdd:cd03257    1 LLEVKNLSvsFPTGGGsvkALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLlkptsgsIIFDGkDLLKLSRRLRkir 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 341 ---IGYLPQDPTTLF---------VADKVIDDLLLVDDVVASVESHLDNFGIIDLK---DAHPFDLSSGQKQLVALAKIL 405
Cdd:cd03257   81 rkeIQMVFQDPMSSLnprmtigeqIAEPLRIHGKLSKKEARKEAVLLLLVGVGLPEevlNRYPHELSGGQRQRVAIARAL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 406 LTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03257  161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElgLTLLFITHDLGVVAKIADRVAVMYAGKI 224
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 14-191 1.17e-23

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 99.02  E-value: 1.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFVFQNPedQLVMNT 90
Cdd:PRK10247  19 DAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPtSGTLlfEGEDISTLKPEIYRQQVSYCAQTP--TLFGDT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEIAFGLKNKGISlKQMKRRIGEIVnYFNL-QSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNRE 169
Cdd:PRK10247  97 VYDNLIFPWQIRNQQ-PDPAIFLDDLE-RFALpDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174

                        170       180
                 ....*....|....*....|..
gi 169293994 170 EFIKILKHINDDFNVTVVFVEH 191
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTH 196
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 3-213 2.00e-23

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the subfamily A transporters involved in drug resistance, nodulation, lipid transport, and bacteriocin and lantibiotic immunity. In eubacteria and archaea, the typical organization consists of one ABC and one or two integral membranes. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 98.12  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDT--KIGFVfq 80
Cdd:cd03269    2 EVENVTKRF-GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPLDIAArnRIGYL-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 nPEDQ-LVMNTVWHEIAFGLKN-KGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:cd03269   76 -PEERgLYPKMKVIDQLVYLAQlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 159 ATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVI 213
Cdd:cd03269  155 PFSGLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVL 208
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 1-212 3.12e-23

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: 97.82  E-value: 3.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKII---NNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKG---DIDGVIILDEEIENDdTK 74
Cdd:cd03266    1 MITADALTKRFRDVKKTVqavDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAgfaTVDGFDVVKEPAEAR-RR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPE--DQLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:cd03266   80 LGFVSDSTGlyDRL---TARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 153 VILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03266  157 VLLLDEPTTGLDVMATRALREFIRQLRAL-GKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
14-211 5.45e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 100.49  E-value: 5.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpslrpkG--DI-DGVIILDEEIEND----DTKIGFVFQN----P 82
Cdd:PRK11000  15 DVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIA------GleDItSGDLFIGEKRMNDvppaERGVGMVFQSyalyP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 EdqlvMNtVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:PRK11000  89 H----LS-VAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSN 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 163 LDPVNREEF-IKILKhINDDFNVTVVFVEH-QLEGlLDVANRLIVMDEGKI 211
Cdd:PRK11000 164 LDAALRVQMrIEISR-LHKRLGRTMIYVTHdQVEA-MTLADKIVVLDAGRV 212
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
279-467 6.31e-23

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 96.42  E-value: 6.31e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI----SKVGCVD------RIGYLPQ 346
Cdd:COG4619    2 ELEGLSFRVGGkPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPpTSGEIyldgKPLSAMPppewrrQVAYVPQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 347 DPTtLF---VAD--KVIDDLLLVDDVVASVESHLDNFGI--IDL-KDAHpfDLSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:COG4619   82 EPA-LWggtVRDnlPFPFQLRERKFDRERALELLERLGLppDILdKPVE--RLSGGERQRLALIRALLLQPDVLLLDEPT 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 419 KGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:COG4619  159 SALDPENTRRVEELLREYLAEegRAVLWVSHDPEQIERVADRVLTLEAGRL 209
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 3-212 9.16e-23

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: 96.42  E-value: 9.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKI-INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIdgvIILDEEIENDDTK----IG 76
Cdd:cd03263    2 QIRNLTKTYKKGTKPaVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPtSGTA---YINGYSIRTDRKAarqsLG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNpeDQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:cd03263   79 YCPQF--DALFDElTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03263  157 LDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLR 211
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 5-212 1.45e-22

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: 96.40  E-value: 1.45e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTT---LLRYFKPSLRPKGDIDGVIILDEEIENDDTKIGFVFQ 80
Cdd:cd03252    4 EHVRFRYKPDGPvILDNISLRIKPGEVVGIVGRSGSGKSTltkLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 npEDQLVMNTVWHEIAfgLKNKGISLkqmkRRIGEIVNY-----FNLQ------SIINKETQSLSNGQKQLVALASVMVM 149
Cdd:cd03252   84 --ENVLFNRSIRDNIA--LADPGMSM----ERVIEAAKLagahdFISElpegydTIVGEQGAGLSGGQRQRIAIARALIH 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03252  156 NPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIV 215
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 279-490 1.96e-22

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: 96.08  E-value: 1.96e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCV---------DRIGYLPQD 347
Cdd:COG4555    3 EVENLSKKYGKVpALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDsGSILIDGEDvrkeprearRQIGVLPDE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 P-----TTL-----FVADkviDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:COG4555   83 RglydrLTVrenirYFAE---LYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 418 TKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQ---MESVDSTREFFSHNLFYTTTINKI 490
Cdd:COG4555  160 TNGLDVMARRLLREILRALKKEgKTVLFSSHIMQEVEALCDRVVILHKGKvvaQGSLDELREEIGEENLEDAFVALI 236
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 278-466 2.50e-22

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: 93.79  E-value: 2.50e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFG-HDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCV------------DRIGY 343
Cdd:cd03229    1 LELKNVSKRyGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEpDSGSILIDGEDltdledelpplrRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 344 LPQDPtTLFvadkviddlllvddvvasveSHLDNFGIIdlkdAHPfdLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDA 423
Cdd:cd03229   81 VFQDF-ALF--------------------PHLTVLENI----ALG--LSGGQQQRVALARALAMDPDVLLLDEPTSALDP 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 169293994 424 SSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03229  134 ITRREVRALLKSLQAQlgITVVLVTHDLDEAARLADRVVVLRDGK 178
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-214 2.65e-22

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 95.42  E-value: 2.65e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpkdKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEienDDTK------ 74
Cdd:PRK10771   1 MLKLTDITWLY---HHLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPAS---GSLTLNGQ---DHTTtppsrr 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 -IGFVFQnpEDQLVMN-TVWHEIAFGLkNKGISLK-QMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNP 151
Cdd:PRK10771  72 pVSMLFQ--ENNLFSHlTVAQNIGLGL-NPGLKLNaAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQ 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 152 KVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:PRK10771 149 PILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWD 211
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 20-212 2.72e-22

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: 98.25  E-value: 2.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  20 NISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDTK----------IGFVFQNPE--DQLv 87
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD---SGRIRLGGEVLQDSARgiflpphrrrIGYVFQEARlfPHL- 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  88 mnTVWHEIAFGLKNKGISlkQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVN 167
Cdd:COG4148   93 --SVRGNLLYGRKRAPRA--ERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 169293994 168 REEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG4148  169 KAEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVV 213
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1-212 5.04e-22

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 95.15  E-value: 5.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEE-IENDDTKIGFVF 79
Cdd:PRK11248   1 MLQISHLYADYG-GKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQH---GSITLDGKpVEGPGAERGVVF 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNpEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:PRK11248  77 QN-EGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEP 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 160 TAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVM--DEGKIV 212
Cdd:PRK11248 156 FGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLspGPGRVV 210
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 278-471 7.06e-22

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: 93.74  E-value: 7.06e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDL--NFGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISkVGCVD---------RIGYLP 345
Cdd:cd03259    1 LELKGLskTYG-SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERpDSGEIL-IDGRDvtgvpperrNIGMVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTtLF----VADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:cd03259   79 QDYA-LFphltVAENIAfglkLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 418 TKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVD 471
Cdd:cd03259  158 LSALDAKLREELREELKELQRelGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 277-453 7.09e-22

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: 93.31  E-value: 7.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGEISKVGCVD---RIGYLP 345
Cdd:COG4133    2 MLEAENLSCRRGErLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLlppsageVLWNGEPIRDAREDyrrRLAYLG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDP---TTLFVAD--KVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKG 420
Cdd:COG4133   82 HADglkPELTVREnlRFWAALYGLRADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTA 161

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169293994 421 IDASSKEFLANLIRGLSKH-MTIVVASHDLEFVA 453
Cdd:COG4133  162 LDAAGVALLAELIAAHLARgGAVLLTTHQPLELA 195
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 14-481 7.39e-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: 98.36  E-value: 7.39e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRPKGDIDGVIILD-EEIE----NDDTKIGFVFQNPEDQLVM 88
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILS-GVYPHGTWDGEIYWSgSPLKasniRDTERAGIVIIHQELTLVP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   89 N-TVWHEIAFG----LKNKGISLKQMKRRIGEIVNYFNLQSI-INKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:TIGR02633  92 ElSVAENIFLGneitLPGGRMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSSS 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  163 LDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIK-MAVDEMLTKKIFVEslpnyvrVS 241
Cdd:TIGR02633 172 LTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHVATKDMStMSEDDIITMMVGRE-------IT 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  242 SLCDKLCLSIKEAREALVNFENFDikimdeIDNRILMKVRDLNFghddivlkdleiDILENEILSIVGANGSGKSSFLRC 321
Cdd:TIGR02633 244 SLYPHEPHEIGDVILEARNLTCWD------VINPHRKRVDDVSF------------SLRRGEILGVAGLVGAGRTELVQA 305

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  322 LAGLVD--CQGEISKVG-------CVDRI--------------GYLPQ----DPTTLFVADKVidDLLLVDDVVASVESH 374
Cdd:TIGR02633 306 LFGAYPgkFEGNVFINGkpvdirnPAQAIragiamvpedrkrhGIVPIlgvgKNITLSVLKSF--CFKMRIDAAAELQII 383

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  375 LDNFGIIDLKDAHPF----DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDL 449
Cdd:TIGR02633 384 GSAIQRLKVKTASPFlpigRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEgVAIIVVSSEL 463

                         490       500       510
                  ....*....|....*....|....*....|..
gi 169293994  450 EFVAKISDRVAMIFNGQMESvdstrEFFSHNL 481
Cdd:TIGR02633 464 AEVLGLSDRVLVIGEGKLKG-----DFVNHAL 490
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-233 1.50e-21

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 94.79  E-value: 1.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPkgdiDG--VIILDEEIENDDT-KIGF 77
Cdd:COG4152    1 MLELKGLTKRF-GDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAP----DSgeVLWDGEPLDPEDRrRIGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VfqnPE-----------DQLVmntvwheiAFG-LKnkGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALAS 145
Cdd:COG4152   76 L---PEerglypkmkvgEQLV--------YLArLK--GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIA 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 146 VMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID---NEIKmavD 222
Cdd:COG4152  143 ALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSgsvDEIR---R 218

                        250
                 ....*....|.
gi 169293994 223 EMLTKKIFVES 233
Cdd:COG4152  219 QFGRNTLRLEA 229
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 4-214 4.98e-21

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 90.45  E-value: 4.98e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYP-KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEienddtkigfvfqnp 82
Cdd:cd03247    3 INNVSFSYPeQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQ---QGEITLDGV--------------- 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 EDQLVMNTVWHEIAFglknkgislkqmkrrIGEIVNYFNlQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:cd03247   65 PVSDLEKALSSLISV---------------LNQRPYLFD-TTLRNNLGRRFSGGERQRLALARILLQDAPIVLLDEPTVG 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 163 LDPVNREEFIK-ILKHINDDfnvTVVFVEHQLEGlLDVANRLIVMDEGKIVID 214
Cdd:cd03247  129 LDPITERQLLSlIFEVLKDK---TLIWITHHLTG-IEHMDKILFLENGKIIMQ 177
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 8-212 5.17e-21

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: 90.69  E-value: 5.17e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   8 SFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF---KPSLRPKGD--IDGVIILDEEIENddtKIGFVFQnp 82
Cdd:cd03213   15 SSPSKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALagrRTGLGVSGEvlINGRPLDKRSFRK---IIGYVPQ-- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 EDQLVMN-TVWHEIAFGLKNKGISLKQMKRrigeivnyfnlqsiinketqslsngqkqlVALASVMVMNPKVILLDEATA 161
Cdd:cd03213   90 DDILHPTlTVRETLMFAAKLRGLSGGERKR-----------------------------VSIALELVSNPSLLFLDEPTS 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 162 QLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLL-DVANRLIVMDEGKIV 212
Cdd:cd03213  141 GLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIfELFDKLLLLSQGRVI 191
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 3-212 1.08e-20

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 91.23  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKkIINNISFEIKKGDFLVITGKSGCGKTTLLR------------------YFKPSLRPKgdidgviil 64
Cdd:PRK11124   4 QLNGINCFYGAHQ-ALFDITLDCPQGETLVLLGPSGAGKSSLLRvlnllemprsgtlniagnHFDFSKTPS--------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  65 DEEIENDDTKIGFVFQN----PEDQLVMNTvwheIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQL 140
Cdd:PRK11124  74 DKAIRELRRNVGMVFQQynlwPHLTVQQNL----IEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQR 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 141 VALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11124 150 VAIARALMMEPQVLLFDEPTAALDPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIV 220
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 3-212 1.16e-20

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: 90.63  E-value: 1.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpKGDI--DGVIILDEEIENDDTKI 75
Cdd:cd03244    4 EFKNVSLRYRPNLPpVLKNISFSIKPGEKVGIVGRTGSGKSSlllaLFRLVELS---SGSIliDGVDISKIGLHDLRSRI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPedQLVMNTVWHEIA-FGLKNKG-----ISLKQMKRRIGEIVNyfNLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:cd03244   81 SIIPQDP--VLFSGTIRSNLDpFGEYSDEelwqaLERVGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLR 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 150 NPKVILLDEATAQLDPvnrEEFIKILKHINDDF-NVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03244  157 KSKILVLDEATASVDP---ETDALIQKTIREAFkDCTVLTIAHRLDTIID-SDRILVLDKGRVV 216
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 13-212 1.17e-20

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


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 90.41  E-value: 1.17e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  13 KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILD-EEIENDDTK--IGFVFQNpeDQLVMN 89
Cdd:cd03234   18 KYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNgQPRKPDQFQkcVAYVRQD--DILLPG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  90 -TVWHEIAFGLKNKG--ISLKQMKRRIGEIV--NYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLD 164
Cdd:cd03234   96 lTVRETLTYTAILRLprKSSDAIRKKRVEDVllRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169293994 165 PVNREEFIKILKHINDDfNVTVVFVEHQ-LEGLLDVANRLIVMDEGKIV 212
Cdd:cd03234  176 SFTALNLVSTLSQLARR-NRIVILTIHQpRSDLFRLFDRILLLSSGEIV 223
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 3-211 1.35e-20

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 90.61  E-value: 1.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPK--DKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpkgdiDGVIILDEEIEND----- 71
Cdd:cd03248   13 KFQNVTFAYPTrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTvvalLENFYQPQ-------GGQVLLDGKPISQyehky 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 -DTKIGFVFQNPedQLVMNTVWHEIAFGLKNKGISlkqmkrRIGEIVNYFNLQSIINKETQS-----------LSNGQKQ 139
Cdd:cd03248   86 lHSKVSLVGQEP--VLFARSLQDNIAYGLQSCSFE------CVKEAAQKAHAHSFISELASGydtevgekgsqLSGGQKQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 140 LVALASVMVMNPKVILLDEATAQLDpVNREEFIKILkHINDDFNVTVVFVEHQLEgLLDVANRLIVMDEGKI 211
Cdd:cd03248  158 RVAIARALIRNPQVLILDEATSALD-AESEQQVQQA-LYDWPERRTVLVIAHRLS-TVERADQILVLDGGRI 226
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 21-467 1.37e-20

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 94.73  E-value: 1.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  21 ISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdIDGVIILDE-EIENDDT-----------KIGFVFQNPEDQLVM 88
Cdd:PRK15439  30 IDFTLHAGEVHALLGGNGAGKSTLMKI----------IAGIVPPDSgTLEIGGNpcarltpakahQLGIYLVPQEPLLFP 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  89 N-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSiinkETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVN 167
Cdd:PRK15439 100 NlSVKENILFGLPKRQASMQKMKQLLAALGCQLDLDS----SAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAE 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 168 REEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIkmavdEMLTKKIFVESLPNYVRVSSLCD-- 245
Cdd:PRK15439 176 TERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKT-----ADLSTDDIIQAITPAAREKSLSAsq 249

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 246 KLCLSIKEARealvnfenfdikiMDEIDNRILMKVRDLN---FghddivlKDLEIDILENEILSIVGANGSGKSSFLRCL 322
Cdd:PRK15439 250 KLWLELPGNR-------------RQQAAGAPVLTVEDLTgegF-------RNISLEVRAGEILGLAGVVGAGRTELAETL 309

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 323 AGL--------VDCQGEISKVGCVDRIG----YLPQD----------PTTLFVADKVIDDL---LLVDDVVASVESHLDN 377
Cdd:PRK15439 310 YGLrparggriMLNGKEINALSTAQRLArglvYLPEDrqssglyldaPLAWNVCALTHNRRgfwIKPARENAVLERYRRA 389

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 378 FGIidlKDAHPFD----LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK-HMTIVVASHDLEFV 452
Cdd:PRK15439 390 LNI---KFNHAEQaartLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAqNVAVLFISSDLEEI 466

                        490
                 ....*....|....*
gi 169293994 453 AKISDRVAMIFNGQM 467
Cdd:PRK15439 467 EQMADRVLVMHQGEI 481
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 290-475 1.40e-20

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: 90.26  E-value: 1.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 290 IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI---------SKVGCVDRIGYLPQD---PTTLFVADK 356
Cdd:cd03263   16 PAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRpTSGTAyingysirtDRKAARQSLGYCPQFdalFDELTVREH 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 VIDDL----LLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:cd03263   96 LRFYArlkgLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPASRRAIWDL 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 433 IRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:cd03263  176 ILEVRKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 4-484 1.60e-20

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 94.39  E-value: 1.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPK---DKKIINNISFEIKKGDFLVITGKSGCGKT----TLLRYF--KPSLRPKGDI----DGVIILDEE--- 67
Cdd:PRK15134   8 IENLSVAFRQqqtVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLpsPPVVYPSGDIrfhgESLLHASEQtlr 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  68 -IENDdtKIGFVFQNP----------EDQLVMNTVWH----------EIAFGLKNKGIslKQMKRRIGEivnyFNLQsii 126
Cdd:PRK15134  88 gVRGN--KIAMIFQEPmvslnplhtlEKQLYEVLSLHrgmrreaargEILNCLDRVGI--RQAAKRLTD----YPHQ--- 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 127 nketqsLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVM 206
Cdd:PRK15134 157 ------LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVM 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 207 DEGKIVIDNEikmavdemlTKKIFVESLPNYVR--VSSLCDKLCLSIKEAREALVNFENFDIKImdEIDNRILMKVRDLN 284
Cdd:PRK15134 231 QNGRCVEQNR---------AATLFSAPTHPYTQklLNSEPSGDPVPLPEPASPLLDVEQLQVAF--PIRKGILKRTVDHN 299

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 285 fghddIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEI----SKVGCVDRIGYLP---------QDPTT- 350
Cdd:PRK15134 300 -----VVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQGEIwfdgQPLHNLNRRQLLPvrhriqvvfQDPNSs 374

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 ----LFVAD------KVIDDLLLVDDVVASVESHLDNFGI-IDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTK 419
Cdd:PRK15134 375 lnprLNVLQiieeglRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 420 GIDASSKEFLANLIRGL-SKH-MTIVVASHDLEFVAKISDRVAMIFNGQ-MESVDSTREFFSHNLFYT 484
Cdd:PRK15134 455 SLDKTVQAQILALLKSLqQKHqLAYLFISHDLHVVRALCHQVIVLRQGEvVEQGDCERVFAAPQQEYT 522
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 25-214 1.65e-20

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: 89.86  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  25 IKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEE----IENDDTKIGFVFQnpEDQLVMN-TVWHEIAFGL 99
Cdd:cd03298   21 FAQGEITAIVGPSGSGKSTLLNLIAGFETPQS---GRVLINGVdvtaAPPADRPVSMLFQ--ENNLFAHlTVEQNVGLGL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 100 kNKGISLKQMKR-RIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHI 178
Cdd:cd03298   96 -SPGLKLTAEDRqAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDL 174

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 169293994 179 NDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:cd03298  175 HAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 1-210 1.75e-20

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: 89.46  E-value: 1.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIIlDEEIENDDTK 74
Cdd:COG4133    2 MLEAENLSCRRG-ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRilagLLPPS---AGEVlwNGEPI-RDAREDYRRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQNPE--DQLvmnTVWHEIAFGLKNKGISLKQMkrRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:COG4133   77 LAYLGHADGlkPEL---TVRENLRFWAALYGLRADRE--AIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 153 VILLDEATAQLDPVNREEFIKILK-HINDDfnVTVVFVEHQLEGLLDVanRLIVMDEGK 210
Cdd:COG4133  152 LWLLDEPFTALDAAGVALLAELIAaHLARG--GAVLLTTHQPLELAAA--RVLDLGDFK 206
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 3-232 3.96e-20

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 89.83  E-value: 3.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKdKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFK--PSLRPKGDIDGVIILDEE---IENDDT---- 73
Cdd:PRK14239   7 QVSDLSVYYNK-KKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINrmNDLNPEVTITGSIVYNGHniySPRTDTvdlr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 -KIGFVFQNPeDQLVMnTVWHEIAFGLKNKGISLKQmkrRIGEIVNYFNLQSIINKETQ--------SLSNGQKQLVALA 144
Cdd:PRK14239  86 kEIGMVFQQP-NPFPM-SIYENVVYGLRLKGIKDKQ---VLDEAVEKSLKGASIWDEVKdrlhdsalGLSGGQQQRVCIA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 145 SVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFnvTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEikmavdem 224
Cdd:PRK14239 161 RVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYND-------- 230


                 ....*...
gi 169293994 225 lTKKIFVE 232
Cdd:PRK14239 231 -TKQMFMN 237
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 273-480 4.74e-20

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: 89.27  E-value: 4.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 273 DNRILMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DcQGEIsKVGCVD---------- 339
Cdd:COG1127    1 MSEPMIEVRNLTKSFGDrVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLrpD-SGEI-LVDGQDitglsekely 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 ----RIGYLPQDPTtLF--------VA----------DKVIDDLllvddvvasVESHLDNFGIIDLKDAHPFDLSSGQKQ 397
Cdd:COG1127   79 elrrRIGMLFQGGA-LFdsltvfenVAfplrehtdlsEAEIREL---------VLEKLELVGLPGAADKMPSELSGGMRK 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 398 LVALA-------KILLtkpqlllLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQME 468
Cdd:COG1127  149 RVALAralaldpEILL-------YDEPTAGLDPITSAVIDELIRELRDelGLTSVVVTHDLDSAFAIADRVAVLADGKII 221

                        250
                 ....*....|..
gi 169293994 469 SVDSTREFFSHN 480
Cdd:COG1127  222 AEGTPEELLASD 233
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 4-206 7.38e-20

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: 92.35  E-value: 7.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    4 IENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD----EEIENDD--TKIGF 77
Cdd:TIGR02857 324 FSGVSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTE---GSIAVNgvplADADADSwrDQIAW 400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   78 VFQNPedQLVMNTVWHEIAFGLKN-KGISLKQMKRRIG--EIVNYF--NLQSIINKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:TIGR02857 401 VPQHP--FLFAGTIAENIRLARPDaSDAEIREALERAGldEFVAALpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAP 478

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 169293994  153 VILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEgLLDVANRLIVM 206
Cdd:TIGR02857 479 LLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLA-LAALADRIVVL 529
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 16-491 7.57e-20

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 92.30  E-value: 7.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRPKGDIDGVIILD-EEIE----NDDTKIGFVFQNPEDQLVMN- 89
Cdd:PRK13549  19 KALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLS-GVYPHGTYEGEIIFEgEELQasniRDTERAGIAIIHQELALVKEl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  90 TVWHEIAFG---LKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDpv 166
Cdd:PRK13549  98 SVLENIFLGneiTPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTASLT-- 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 167 nrEEFIKILKHINDDF---NVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIK-MAVDEMLTKKIfveslpnyvrvss 242
Cdd:PRK13549 176 --ESETAVLLDIIRDLkahGIACIYISHKLNEVKAISDTICVIRDGRHIGTRPAAgMTEDDIITMMV------------- 240

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 243 lcdklclsikeARE--ALVNFENFDIKimDEIdnrilMKVRDLNFGHDDI----VLKDLEIDILENEILSIVGANGSGKS 316
Cdd:PRK13549 241 -----------GREltALYPREPHTIG--EVI-----LEVRNLTAWDPVNphikRVDDVSFSLRRGEILGIAGLVGAGRT 302

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 317 SFLRCLAGLVD--CQGEISKVG-------CVDR----IGYLPQDPTtlfvADKVIDDLLLVDDVVASVESHLDNFGIID- 382
Cdd:PRK13549 303 ELVQCLFGAYPgrWEGEIFIDGkpvkirnPQQAiaqgIAMVPEDRK----RDGIVPVMGVGKNITLAALDRFTGGSRIDd 378

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 383 ---------------LKDAHPF----DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK-HMTI 442
Cdd:PRK13549 379 aaelktilesiqrlkVKTASPElaiaRLSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQqGVAI 458

                        490       500       510       520
                 ....*....|....*....|....*....|....*....|....*....
gi 169293994 443 VVASHDLEFVAKISDRVAMIFNGQMESvdstrEFFSHNLfyttTINKIM 491
Cdd:PRK13549 459 IVISSELPEVLGLSDRVLVMHEGKLKG-----DLINHNL----TQEQVM 498
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 1-212 8.94e-20

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 88.75  E-value: 8.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSF-TYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKP--SLRPKGDIDG-VIILDEEIENDDT--- 73
Cdd:PRK14267   2 KFAIETVNLrVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRllELNEEARVEGeVRLFGRNIYSPDVdpi 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 ----KIGFVFQ--NPEDQLvmnTVWHEIAFGLKNKGisLKQMKRRIGEIVNYF--------NLQSIINKETQSLSNGQKQ 139
Cdd:PRK14267  82 evrrEVGMVFQypNPFPHL---TIYDNVAIGVKLNG--LVKSKKELDERVEWAlkkaalwdEVKDRLNDYPSNLSGGQRQ 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 140 LVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFnvTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLI 227
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-242 9.11e-20

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 90.15  E-value: 9.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   7 FSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDdTKIGFVFQNPE 83
Cdd:COG4586   28 FRREY-REVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPtSGEVrvLGYVPFKRRKEFA-RRIGVVFGQRS 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 dQLvmntvWHEIA----FGLkNK---GISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:COG4586  106 -QL-----WWDLPaidsFRL-LKaiyRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLTKKIFV----- 231
Cdd:COG4586  179 DEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRIIYDGSLEELKERFGPYKTIVlelae 258

                        250
                 ....*....|....*
gi 169293994 232 ----ESLPNYVRVSS 242
Cdd:COG4586  259 pvppLELPRGGEVIE 273
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
18-212 9.15e-20

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 91.25  E-value: 9.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGD--IDGVIIL---DEEI-ENDDTKIGFVFQNPEDQLVMnT 90
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPtRGQvlIDGVDIAkisDAELrEVRRKKIAMVFQSFALMPHM-T 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREE 170
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169293994 171 FIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVV 244
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 5-212 9.61e-20

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 88.41  E-value: 9.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLrYFKPSLRPKgDIDGVIILDEEI------ENDDTKIGFV 78
Cdd:PRK10895   7 KNLAKAY-KGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTF-YMVVGIVPR-DAGNIIIDDEDIsllplhARARRGIGYL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:PRK10895  84 PQEASIFRRLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDE 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169293994 159 ATAQLDPVNREEFIKILKHINdDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK10895 164 PFAGVDPISVIDIKRIIEHLR-DSGLGVLITDHNVRETLAVCERAYIVSQGHLI 216
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 16-212 1.03e-19

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: 85.94  E-value: 1.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDIdgvIILDEEIENDDTK------IGFVFQnpedq 85
Cdd:cd03216   14 KALDGVSLSVRRGEVHALLGENGAGKSTLMKilsgLYKPD---SGEI---LVDGKEVSFASPRdarragIAMVYQ----- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  86 lvmntvwheiafglknkgislkqmkrrigeivnyfnlqsiinketqsLSNGQKQLVALASVMVMNPKVILLDEATAQLDP 165
Cdd:cd03216   83 -----------------------------------------------LSVGERQMVEIARALARNARLLILDEPTAALTP 115

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 166 VNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:cd03216  116 AEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
cbiO PRK13650
energy-coupling factor transporter ATPase;
277-478 1.26e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 89.02  E-value: 1.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD----IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCV----------DRI 341
Cdd:PRK13650   4 IIEVKNLTFKYKEdqekYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAEsGQIIIDGDLlteenvwdirHKI 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 342 GYLPQDPTTLFVADKVIDDL--------LLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLL 413
Cdd:PRK13650  84 GMVFQNPDNQFVGATVEDDVafglenkgIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIII 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAkISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13650 164 LDEATSMLDPEGRLELIKTIKGIRDdyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 19-467 1.66e-19

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 91.24  E-value: 1.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  19 NNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpkgdiDGVIILD-EEIENDDTK------IGFVFQNPedQLV 87
Cdd:COG3845   22 DDVSLTVRPGEIHALLGENGAGKSTLMKilygLYQPD-------SGEILIDgKPVRIRSPRdaialgIGMVHQHF--MLV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  88 MN-TVWHEIAFGLKNKG---ISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQL 163
Cdd:COG3845   93 PNlTVAENIVLGLEPTKggrLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 164 DPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLTKKIFVESLPNYVRvssl 243
Cdd:COG3845  173 TPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELAELMVGREVLLRVE---- 247

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 244 cdklclsiKEAREAlvnfenfdikimdeidNRILMKVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRC 321
Cdd:COG3845  248 --------KAPAEP----------------GEVVLEVENLSVRDDRgvPALKDVSLEVRAGEILGIAGVAGNGQSELAEA 303

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 322 LAGLVDCQG--------EISKVGCVDR----IGYLPQDP------TTLFVADKVIDDLLLvddvvasvESHLDNFGIIDL 383
Cdd:COG3845  304 LAGLRPPASgsirldgeDITGLSPRERrrlgVAYIPEDRlgrglvPDMSVAENLILGRYR--------RPPFSRGGFLDR 375

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 384 KDAHP--------FD------------LSSG--QKQLVA----------LAkilltkpqllllDEPTKGIDASSKEFLAN 431
Cdd:COG3845  376 KAIRAfaeelieeFDvrtpgpdtparsLSGGnqQKVILArelsrdpkllIA------------AQPTRGLDVGAIEFIHQ 443

                        490       500       510
                 ....*....|....*....|....*....|....*..
gi 169293994 432 LIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:COG3845  444 RLLELRDAgAAVLLISEDLDEILALSDRIAVMYEGRI 480
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 3-214 2.69e-19

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: 86.12  E-value: 2.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEIENDDTK----IGFV 78
Cdd:cd03268    2 KTNDLTKTY-GKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDS---GEITFDGKSYQKNIEalrrIGAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEdqLVMNTVWHEiafGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:cd03268   78 IEAPG--FYPNLTARE---NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 159 ATAQLDPVNREEFIKILKHINdDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:cd03268  153 PTNGLDPDGIKELRELILSLR-DQGITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
286-461 3.25e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 85.36  E-value: 3.25e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 286 GHDdiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDRIGYLPQ-----DPTTLFVADKVI-- 358
Cdd:NF040873   4 GRP--VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGARVAYVPQrsevpDSLPLTVRDLVAmg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 359 ------DDLLLVDDVVASVESHLDNFGIIDLKDAhPFD-LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLAN 431
Cdd:NF040873  82 rwarrgLWRRLTRDDRAAVDDALERVGLADLAGR-QLGeLSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIA 160

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169293994 432 LIRGLS-KHMTIVVASHDLEFVAKISDRVAM 461
Cdd:NF040873 161 LLAEEHaRGATVVVVTHDLELVRRADPCVLL 191
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 280-479 3.27e-19

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 89.05  E-value: 3.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLN--FGHDDiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DcQGEISKVGCV--------DR-IGYLPQ 346
Cdd:COG1118    5 VRNISkrFGSFT-LLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLEtpD-SGRIVLNGRDlftnlpprERrVGFVFQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 347 DPTtLF----VADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA-------KILltkpql 411
Cdd:COG1118   83 HYA-LFphmtVAENIAfglrVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALAralavepEVL------ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 412 lLLDEPTKGIDASSKEFL-ANLIRGLSK-HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG1118  156 -LLDEPFGALDAKVRKELrRWLRRLHDElGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDR 224
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
15-212 7.44e-19

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 86.28  E-value: 7.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  15 KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDidgVIILDEEIENDDTK--------IGFVFQ----- 80
Cdd:PRK10419  25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPsQGN---VSWRGEPLAKLNRAqrkafrrdIQMVFQdsisa 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 -NPEdqlvmNTVWHEIAFGLKNKgISLKQMKR--RIGEIVNYFNLQ-SIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK10419 102 vNPR-----KTVREIIREPLRHL-LSLDKAERlaRASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIV 231
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 13-214 8.16e-19

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 85.46  E-value: 8.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  13 KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDID-GVIILDEEIENDDTKIGFVFQNpedqlvMNT 90
Cdd:cd03267   32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPtSGEVRvAGLVPWKRRKKFLRRIGVVFGQ------KTQ 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEI----AFGLKNK--GISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLD 164
Cdd:cd03267  106 LWWDLpvidSFYLLAAiyDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLD 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 169293994 165 PVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:cd03267  186 VVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYD 235
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 3-210 8.94e-19

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: 82.88  E-value: 8.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpslrpkgdidgviILDEEIENDdtkigfvfqnp 82
Cdd:cd03221    2 ELENLSKTY-GGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLK----------------LIAGELEPD----------- 53

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 edqlvmntvwheiafglknKGISLKQMKRRIGeivnYFnlqsiinkeTQsLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:cd03221   54 -------------------EGIVTWGSTVKIG----YF---------EQ-LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169293994 163 LDPVNREEFIKILKhindDFNVTVVFVEHQLEgLLD-VANRLIVMDEGK 210
Cdd:cd03221  101 LDLESIEALEEALK----EYPGTVILVSHDRY-FLDqVATKIIELEDGK 144
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-222 9.15e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 85.88  E-value: 9.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpKGDI-DGVIILDEEIenDDTKIgfV 78
Cdd:PRK11247  15 LNAVSKRY-GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLagleTPS---AGELlAGTAPLAEAR--EDTRL--M 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEdQLVMNTVWHEIAFGLKNKgisLKQMKRRIGEIVNyfnLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:PRK11247  87 FQDAR-LLPWKKVIDNVGLGLKGQ---WRDAALQALAAVG---LADRANEWPAALSGGQKQRVALARALIHRPGLLLLDE 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 159 ATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDneikMAVD 222
Cdd:PRK11247 160 PLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKIGLD----LTVD 219
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 278-466 9.48e-19

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: 83.59  E-value: 9.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIsKVGCVD-----------RIG 342
Cdd:cd03228    1 IEFKNVSFSYPGrpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTsGEI-LIDGVDlrdldleslrkNIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 343 YLPQDPTtLFvadkviddlllvddvVASVEshlDNFgiidlkdahpfdLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:cd03228   80 YVPQDPF-LF---------------SGTIR---ENI------------LSGGQRQRIAIARALLRDPPILILDEATSALD 128

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 423 ASSKEFLANLIRGLSKHMTIVVASHDLEfVAKISDRVAMIFNGQ 466
Cdd:cd03228  129 PETEALILEALRALAKGKTVIVIAHRLS-TIRDADRIIVLDDGR 171
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 279-479 2.53e-18

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 84.28  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISkvgcVD---------------- 339
Cdd:COG1126    3 EIENLHksFG-DLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIT----VDgedltdskkdinklrr 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 RIGYLPQDPtTLF----VADKVIddlllvddvVASV--------------ESHLDNFGIIDLKDAHPFDLSSGQKQLVAL 401
Cdd:COG1126   78 KVGMVFQQF-NLFphltVLENVT---------LAPIkvkkmskaeaeeraMELLERVGLADKADAYPAQLSGGQQQRVAI 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 402 A-------KIlltkpqlLLLDEPTkgidaSS------KEFLaNLIRGLSK-HMTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:COG1126  148 AralamepKV-------MLFDEPT-----SAldpelvGEVL-DVMRDLAKeGMTMVVVTHEMGFAREVADRVVFMDGGRI 214

                        250
                 ....*....|..
gi 169293994 468 ESVDSTREFFSH 479
Cdd:COG1126  215 VEEGPPEEFFEN 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 273-479 2.55e-18

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 84.70  E-value: 2.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 273 DNRILMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD------CQGEI---------SKVG 336
Cdd:COG1117    7 TLEPKIEVRNLNVYYGDkQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMNDlipgarVEGEIlldgediydPDVD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 337 CVD---RIGYLPQDPTtLF---VADKV-----IDDLLLVDDVVASVESHLDNFGIID-LKD---AHPFDLSSGQKQ-LV- 399
Cdd:COG1117   87 VVElrrRVGMVFQKPN-PFpksIYDNVayglrLHGIKSKSELDEIVEESLRKAALWDeVKDrlkKSALGLSGGQQQrLCi 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 400 --ALA---KILLTkpqllllDEPTKGID--ASSK-EflaNLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVD 471
Cdd:COG1117  166 arALAvepEVLLM-------DEPTSALDpiSTAKiE---ELILELKKDYTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235


                 ....*...
gi 169293994 472 STREFFSH 479
Cdd:COG1117  236 PTEQIFTN 243
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 3-212 2.66e-18

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: 83.23  E-value: 2.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTY-PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP---KGDIDGVIILDEEIENDDTKIGFV 78
Cdd:cd03369    8 EVENLSVRYaPDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAeegKIEIDGIDISTIPLEDLRSSLTII 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPedQLVMNTVwheiafgLKNKGISLKQMKRRIGEIVNyfnlqsiINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:cd03369   88 PQDP--TLFSGTI-------RSNLDPFDEYSDEEIYGALR-------VSEGGLNLSQGQRQLLCLARALLKRPRVLVLDE 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 159 ATAQLDpvnREEFIKILKHINDDF-NVTVVFVEHQLEGLLDVAnRLIVMDEGKIV 212
Cdd:cd03369  152 ATASID---YATDALIQKTIREEFtNSTILTIAHRLRTIIDYD-KILVMDAGEVK 202
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 274-461 2.77e-18

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 84.37  E-value: 2.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDLN--FGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISkvgcVD-------- 339
Cdd:COG1116    4 AAPALELRGVSkrFPTGGggvTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPtSGEVL----VDgkpvtgpg 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 -RIGYLPQDPtTLF----VADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA-------K 403
Cdd:COG1116   80 pDRGVVFQEP-ALLpwltVLDNVAlgleLRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIAralandpE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 404 IlltkpqlLLLDEPTKGIDASSKEFLANLIRGL--SKHMTIVVASHDLEFVAKISDRVAM 461
Cdd:COG1116  159 V-------LLMDEPFGALDALTRERLQDELLRLwqETGKTVLFVTHDVDEAVFLADRVVV 211
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 278-462 3.27e-18

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: 83.29  E-value: 3.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLN--FGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIS-----KVGCVDRIGYLPQ 346
Cdd:cd03293    1 LEVRNVSktYGGGGgavTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTsGEVLvdgepVTGPGPDRGYVFQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 347 DPTtLF----VADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:cd03293   81 QDA-LLpwltVLDNVAlgleLQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 419 KGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMI 462
Cdd:cd03293  160 SALDALTREQLQEELLDIWREtgKTVLLVTHDIDEAVFLADRVVVL 205
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 294-471 3.60e-18

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: 83.11  E-value: 3.60e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 294 DLEIDI-LENEILSIVGANGSGKSSFLRCLAGL--VDcQGEISKVGCV--------------DRIGYLPQDpTTLF---- 352
Cdd:cd03297   14 TLKIDFdLNEEVTGIFGASGAGKSTLLRCIAGLekPD-GGTIVLNGTVlfdsrkkinlppqqRKIGLVFQQ-YALFphln 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKVI--DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLA 430
Cdd:cd03297   92 VRENLAfgLKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLL 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 431 NLIRGLSKHMTIVV--ASHDLEFVAKISDRVAMIFNGQMESVD 471
Cdd:cd03297  172 PELKQIKKNLNIPVifVTHDLSEAEYLADRIVVMEDGRLQYIG 214
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 4-332 3.65e-18

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: 87.43  E-value: 3.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK---IINNISFEIKKGDFLVITGKSGCGKT-T------LLRYfkPSLRPKGDI--DG--VIILDE--- 66
Cdd:COG4172    9 VEDLSVAFGQGGGtveAVKGVSFDIAAGETLALVGESGSGKSvTalsilrLLPD--PAAHPSGSIlfDGqdLLGLSErel 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  67 -EIENDDtkIGFVFQ------NP----EDQLVMNTVWHeiafglknKGISLKQMKRRIGEI---VNYFNLQSIINKETQS 132
Cdd:COG4172   87 rRIRGNR--IAMIFQepmtslNPlhtiGKQIAEVLRLH--------RGLSGAAARARALELlerVGIPDPERRLDAYPHQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 133 LSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLeGLL-DVANRLIVMDEGKI 211
Cdd:COG4172  157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL-GVVrRFADRVAVMRQGEI 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 212 VIDNEikmavdemlTKKIFveSLPN--YVRvsslcdKLCLSIKEAREALVnfenfdikimdEIDNRILMKVRDLN----- 284
Cdd:COG4172  236 VEQGP---------TAELF--AAPQhpYTR------KLLAAEPRGDPRPV-----------PPDAPPLLEARDLKvwfpi 287

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 285 ----FGHDDIVLK---DLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEI 332
Cdd:COG4172  288 krglFRRTVGHVKavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIPSEGEI 342
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 14-212 4.03e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 83.81  E-value: 4.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKP--SLRPKGDIDGVIILD-EEIENDDT-----KIGFVFQ--NPE 83
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRliELYPEARVSGEVYLDgQDIFKMDVielrrRVQMVFQipNPI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 DQLvmnTVWHEIAFGLKNKGI--SLKQMKRRIGEIVNYFNL----QSIINKETQSLSNGQKQLVALASVMVMNPKVILLD 157
Cdd:PRK14247  95 PNL---SIFENVALGLKLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 158 EATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK14247 172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIV 224
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
277-469 4.05e-18

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 83.17  E-value: 4.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLN--FGHDDI---VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISkVGCVD----------- 339
Cdd:COG1136    4 LLELRNLTksYGTGEGevtALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPtSGEVL-IDGQDisslserelar 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 ----RIGYLPQDPT---TLFVADKV----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA------ 402
Cdd:COG1136   83 lrrrHIGFVFQFFNllpELTALENValplLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIAralvnr 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 403 -KILLtkpqlllLDEPTKGID-ASSKEFLaNLIRGLSK--HMTIVVASHDLEfVAKISDRVAMIFNGQMES 469
Cdd:COG1136  163 pKLIL-------ADEPTGNLDsKTGEEVL-ELLRELNRelGTTIVMVTHDPE-LAARADRVIRLRDGRIVS 224
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 279-466 6.21e-18

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: 82.58  E-value: 6.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI------------------SKVGC 337
Cdd:cd03262    2 EIKNLHksFG-DFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDsGTIiidglkltddkkninelrQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 338 V----------DRIGYLPQDPTTLFVADKviddlllvDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLT 407
Cdd:cd03262   81 VfqqfnlfphlTVLENITLAPIKVKGMSK--------AEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAM 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 408 KPQLLLLDEPTKGIDAS-SKEFLaNLIRGLSK-HMTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03262  153 NPKVMLFDEPTSALDPElVGEVL-DVMKDLAEeGMTMVVVTHEMGFAREVADRVIFMDDGR 212
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 291-466 7.28e-18

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: 82.15  E-value: 7.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL--VDcQGEISKVGCV--------------DRIGYLPQDPT---TL 351
Cdd:cd03255   19 ALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLdrPT-SGEVRVDGTDisklsekelaafrrRHIGFVFQSFNllpDL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADKV----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDA-SSK 426
Cdd:cd03255   98 TALENVelplLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNLDSeTGK 177

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169293994 427 EFLaNLIRGLSK--HMTIVVASHDLEfVAKISDRVAMIFNGQ 466
Cdd:cd03255  178 EVM-ELLRELNKeaGTTIVVVTHDPE-LAEYADRIIELRDGK 217
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
5-230 8.59e-18

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 83.11  E-value: 8.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKdKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPkgdIDGVIILD-EEIENDDTK-----IGFV 78
Cdd:PRK10253  11 EQLTLGYGK-YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTP---AHGHVWLDgEHIQHYASKevarrIGLL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQN---PEDQLVMNTVW-----HEIAFGLKNKgislkQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:PRK10253  87 AQNattPGDITVQELVArgrypHQPLFTRWRK-----EDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLTKKIF 230
Cdd:PRK10253 162 TAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIY 241
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
277-480 9.06e-18

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 83.53  E-value: 9.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNF---GHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCV----------DRIG 342
Cdd:PRK13635   5 IIRVEHISFrypDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEaGTITVGGMVlseetvwdvrRQVG 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 343 YLPQDPTTLFV----ADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLL 414
Cdd:PRK13635  85 MVFQNPDNQFVgatvQDDVAfgleNIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 415 DEPTKGIDASSKEFLANLIRGLSKHMTIVVAS--HDLEFVAKiSDRVAMIFNGQMESVDSTREFFSHN 480
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSitHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKSG 231
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 279-466 1.10e-17

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: 81.71  E-value: 1.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI-------SKVGCVDR----IGYLP 345
Cdd:cd03224    2 EVENLNAGYGKSqILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPpRSGSIrfdgrdiTGLPPHERaragIGYVP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDP---TTLFVAD--KVIDDLLLVDDVVASVESHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTK 419
Cdd:cd03224   82 EGRrifPELTVEEnlLLGAYARRRAKRKARLERVYELFPRLkERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSE 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 169293994 420 GIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03224  162 GLAPKIVEEIFEAIRELRDEgVTILLVEQNARFALEIADRAYVLERGR 209
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 9-231 1.86e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 82.02  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   9 FTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLR---PKGDIDG-VIILDEEIENDDT-----KIGFVF 79
Cdd:PRK14246  17 YLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGkVLYFGKDIFQIDAiklrkEVGMVF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPeDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGE-----IVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:PRK14246  97 QQP-NPFPHLSIYDNIAYPLKSHGIKEKREIKKIVEeclrkVGLWKEVYDRLNSPASQLSGGQQQRLTIARALALKPKVL 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDVANRLIVMDEGKIV---IDNEIKMAVDEMLTKKIFV 231
Cdd:PRK14246 176 LMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVewgSSNEIFTSPKNELTEKYVI 253
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 3-212 2.05e-17

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 85.28  E-value: 2.05e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRY---FKP---SLRpkgdIDGVIILDEEIENDDTKIG 76
Cdd:PRK11174 351 EAEDLEILSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNAllgFLPyqgSLK----INGIELRELDPESWRKHLS 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPedQLVMNTVWHEIAFGlkNKGISLKQ-----MKRRIGEIVNYFN--LQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:PRK11174 427 WVGQNP--QLPHGTLRDNVLLG--NPDASDEQlqqalENAWVSEFLPLLPqgLDTPIGDQAAGLSVGQAQRLALARALLQ 502

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDVaNRLIVMDEGKIV 212
Cdd:PRK11174 503 PCQLLLLDEPTASLDAHSEQLVMQALNAASRR--QTTLMVTHQLEDLAQW-DQIWVMQDGQIV 562
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 3-194 2.41e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 81.75  E-value: 2.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIiNNISFEIKKGDFLVITGKSGCGKTTLLRYFK------PSLRPKGDI--DGVIILDEEIENDDTK 74
Cdd:PRK14243  12 RTENLNVYYGSFLAV-KNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlndliPGFRVEGKVtfHGKNLYAPDVDPVEVR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 --IGFVFQNPEDqlVMNTVWHEIAFGLKNKGislkqMKRRIGEIVNYFNLQSIINKET--------QSLSNGQKQLVALA 144
Cdd:PRK14243  91 rrIGMVFQKPNP--FPKSIYDNIAYGARING-----YKGDMDELVERSLRQAALWDEVkdklkqsgLSLSGGQQQRLCIA 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 145 SVMVMNPKVILLDEATAQLDPVNR---EEFIKILKHinddfNVTVVFVEHQLE 194
Cdd:PRK14243 164 RAIAVQPEVILMDEPCSALDPISTlriEELMHELKE-----QYTIIIVTHNMQ 211
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
4-212 3.36e-17

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 84.38  E-value: 3.36e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTL----LRYFKPSlrpKGDI--DG--VIILDEEIENDDtkI 75
Cdd:PRK10790 343 IDNVSFAYRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLasllMGYYPLT---EGEIrlDGrpLSSLSHSVLRQG--V 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPedqLVM-NTVWHEIAFGlknKGISLKQMKR-----RIGEIVNYF--NLQSIINKETQSLSNGQKQLVALASVM 147
Cdd:PRK10790 418 AMVQQDP---VVLaDTFLANVTLG---RDISEEQVWQaletvQLAELARSLpdGLYTPLGEQGNNLSVGQKQLLALARVL 491

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PRK10790 492 VQTPQILILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTIVE-ADTILVLHRGQAV 553
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 291-467 3.45e-17

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: 80.02  E-value: 3.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGEISKVGCVDRIGYLPQDpTTLFVADKVIDDLL- 362
Cdd:cd03269   15 ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIilpdsgeVLFDGKPLDIAARNRIGYLPEE-RGLYPKMKVIDQLVy 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 363 -------LVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRG 435
Cdd:cd03269   94 laqlkglKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNVELLKDVIRE 173

                        170       180       190
                 ....*....|....*....|....*....|...
gi 169293994 436 L-SKHMTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03269  174 LaRAGKTVILSTHQMELVEELCDRVLLLNKGRA 206
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 2-212 3.75e-17

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 82.32  E-value: 3.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   2 YKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPS---LRpkgdIDGVIILD---EEIEND 71
Cdd:PRK11308  15 YPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLtmieTPTggeLY----YQGQDLLKadpEAQKLL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVFQNP--------------EDQLVMNTvwheiafglknkGISLKQMKRRIGEIVNYFNLQS-IINKETQSLSNG 136
Cdd:PRK11308  91 RQKIQIVFQNPygslnprkkvgqilEEPLLINT------------SLSAAERREKALAMMAKVGLRPeHYDRYPHMFSGG 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 137 QKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11308 159 QRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCV 234
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 279-479 3.96e-17

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: 81.32  E-value: 3.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  279 KVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEISkvgcVD--------------- 339
Cdd:TIGR04520   2 EVENVSFSYPEsekPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLlLPTSGKVT----VDgldtldeenlweirk 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  340 RIGYLPQDPTTLFVAdkviddlllvddvvASVESH----LDNFGI------------------IDLKDAHPFDLSSGQKQ 397
Cdd:TIGR04520  78 KVGMVFQNPDNQFVG--------------ATVEDDvafgLENLGVpreemrkrvdealklvgmEDFRDREPHLLSGGQKQ 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  398 LVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTRE 475
Cdd:TIGR04520 144 RVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKeeGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPRE 222


                  ....
gi 169293994  476 FFSH 479
Cdd:TIGR04520 223 IFSQ 226
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 291-478 4.41e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 81.30  E-value: 4.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCV-----------------DRIGYLPQ--DPTTL 351
Cdd:PRK14271  36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVllggrsifnyrdvlefrRRVGMLFQrpNPFPM 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADKVIDDLLLVDDV-----VASVESHLDNFGIID-LKDA---HPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:PRK14271 116 SIMDNVLAGVRAHKLVprkefRGVAQARLTEVGLWDaVKDRlsdSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALD 195

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 423 ASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK14271 196 PTTTEKIEEFIRSLADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFS 251
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 280-482 7.55e-17

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 81.68  E-value: 7.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISkVGCVD---------RIGYLPQDP 348
Cdd:COG3842    8 LENVSKRYGDvTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPdSGRIL-LDGRDvtglppekrNVGMVFQDY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 349 TtLF----VADKV-------------IDdlllvddvvASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA-------KI 404
Cdd:COG3842   87 A-LFphltVAENVafglrmrgvpkaeIR---------ARVAELLELVGLEGLADRYPHQLSGGQQQRVALAralapepRV 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 405 LltkpqllLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLE--FVakISDRVAMIFNGQMESVDSTREFFSH- 479
Cdd:COG3842  157 L-------LLDEPLSALDAKLREEMREELRRLQRElgITFIYVTHDQEeaLA--LADRIAVMNDGRIEQVGTPEEIYERp 227


                 ....
gi 169293994 480 -NLF 482
Cdd:COG3842  228 aTRF 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 3-230 7.81e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 80.47  E-value: 7.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpSLRPKGDIDGVIILDEEIE--NDDT------- 73
Cdd:PRK14258   9 KVNNLSFYY-DTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLK----CLNRMNELESEVRVEGRVEffNQNIyerrvnl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 -----KIGFVFqnPEDQLVMNTVWHEIAFGLKNKGIslkQMKRRIGEIVN--------YFNLQSIINKETQSLSNGQKQL 140
Cdd:PRK14258  84 nrlrrQVSMVH--PKPNLFPMSVYDNVAYGVKIVGW---RPKLEIDDIVEsalkdadlWDEIKHKIHKSALDLSGGQQQR 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 141 VALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGkiviDNEIKMA 220
Cdd:PRK14258 159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGN----ENRIGQL 234

                        250
                 ....*....|
gi 169293994 221 VDEMLTKKIF 230
Cdd:PRK14258 235 VEFGLTKKIF 244
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 277-477 8.79e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 79.82  E-value: 8.79e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLN-FGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD---------------- 339
Cdd:PRK14239   5 ILQVSDLSvYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNPEVTITGSIVynghniysprtdtvdl 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 --RIGYLPQDPTT--LFVADKV-----IDDLLLVDDVVASVESHLDNFGIID-LKD---AHPFDLSSGQKQLVALAKILL 406
Cdd:PRK14239  85 rkEIGMVFQQPNPfpMSIYENVvyglrLKGIKDKQVLDEAVEKSLKGASIWDeVKDrlhDSALGLSGGQQQRVCIARVLA 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 407 TKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFF 477
Cdd:PRK14239 165 TSPKIILLDEPTSALDPISAGKIEETLLGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMF 235
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 3-212 8.98e-17

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 83.23  E-value: 8.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIE--NFSFTYPK--DKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpKGD--IDGVIILDEEIENDD 72
Cdd:TIGR00958 478 LIEfqDVSFSYPNrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTvaalLQNLYQPT---GGQvlLDGVPLVQYDHHYLH 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   73 TKIGFVFQNPedQLVMNTVWHEIAFGLKNKGISLKQMKRR-------IGEIVNYFNlqSIINKETQSLSNGQKQLVALAS 145
Cdd:TIGR00958 555 RQVALVGQEP--VLFSGSVRENIAYGLTDTPDEEIMAAAKaanahdfIMEFPNGYD--TEVGEKGSQLSGGQKQRIAIAR 630

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994  146 VMVMNPKVILLDEATAQLDpVNREEFIKILKHINDdfnVTVVFVEHQLEgLLDVANRLIVMDEGKIV 212
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALD-AECEQLLQESRSRAS---RTVLLIAHRLS-TVERADQILVLKKGSVV 692
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 4-209 1.00e-16

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 82.93  E-value: 1.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpS---LRPKGDidGVIILdeeieNDDTKIGFVFQ 80
Cdd:COG4178  365 LEDLTLRTPDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLR----AiagLWPYGS--GRIAR-----PAGARVLFLPQ 433

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 NP-------EDQLvmntvwheiAFGLKNKGISLKQMKrrigEIVNYFNLQSIINK---ET---QSLSNGQKQLVALASVM 147
Cdd:COG4178  434 RPylplgtlREAL---------LYPATAEAFSDAELR----EALEAVGLGHLAERldeEAdwdQVLSLGEQQRLAFARLL 500

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQlEGLLDVANRLIVMDEG 209
Cdd:COG4178  501 LHKPDWLFLDEATSALDEENEAALYQLLREELPG--TTVISVGHR-STLAAFHDRVLELTGD 559
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 290-479 1.02e-16

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: 79.55  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 290 IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQG-EISKVGCVD------RIGYLPQDpTTLF--- 352
Cdd:cd03258   19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLerptsgsVLVDGtDLTLLSGKElrkarrRIGMIFQH-FNLLssr 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 -VADKVIDDLLLVDDVVASVES---HLDNF-GIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKE 427
Cdd:cd03258   98 tVFENVALPLEIAGVPKAEIEErvlELLELvGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDPETTQ 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169293994 428 FLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:cd03258  178 SILALLRDINRElgLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 279-459 1.20e-16

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: 76.72  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEISKVGCVdRIGYLPQdpttlfvadk 356
Cdd:cd03221    2 ELENLSKTYGGkLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGeLEPDEGIVTWGSTV-KIGYFEQ---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 viddlllvddvvasveshldnfgiidlkdahpfdLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL 436
Cdd:cd03221   71 ----------------------------------LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLESIEALEEALKEY 116

                        170       180
                 ....*....|....*....|...
gi 169293994 437 SKhmTIVVASHDLEFVAKISDRV 459
Cdd:cd03221  117 PG--TVILVSHDRYFLDQVATKI 137
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 12-212 1.53e-16

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: 82.04  E-value: 1.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  12 PKDKKIINNISFEIKKGDFLVITGKSGCGKTTL----LRYfkpsLRPKGDIdgvIILDEEIENDDTK--------IGFVF 79
Cdd:COG4172  296 VGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRL----IPSEGEI---RFDGQDLDGLSRRalrplrrrMQVVF 368

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPEDQLvmN---TVWHEIAFGLK--NKGISLKQMKRRIGEIvnyfnLQSI-INKETQS-----LSNGQKQLVALASVMV 148
Cdd:COG4172  369 QDPFGSL--SprmTVGQIIAEGLRvhGPGLSAAERRARVAEA-----LEEVgLDPAARHrypheFSGGQRQRIAIARALI 441

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 149 MNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG4172  442 LEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVV 505
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 4-234 1.58e-16

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: 82.48  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    4 IENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDI--DGVIILDEEIENDDTKIGF 77
Cdd:TIGR01193 476 INDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKllvgFFQAR---SGEIllNGFSLKDIDRHTLRQFINY 552

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   78 VFQNPedQLVMNTVWHEIAFGLKnKGISLKQMKR--RIGEIVNYFN-----LQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:TIGR01193 553 LPQEP--YIFSGSILENLLLGAK-ENVSQDEIWAacEIAEIKDDIEnmplgYQTELSEEGSSISGGQKQRIALARALLTD 629

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  151 PKVILLDEATAQLDPVNREEFIKILKHINDDfnvTVVFVEHQLEgLLDVANRLIVMDEGKIVIDNEikmaVDEMLTKKIF 230
Cdd:TIGR01193 630 SKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLS-VAKQSDKIIVLDHGKIIEQGS----HDELLDRNGF 701


                  ....
gi 169293994  231 VESL 234
Cdd:TIGR01193 702 YASL 705
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 269-467 1.60e-16

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: 82.57  E-value: 1.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 269 MDEIDNRIlmKVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIsKVGCVD----- 339
Cdd:COG2274  467 LPRLKGDI--ELENVSFRYPGdspPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEpTSGRI-LIDGIDlrqid 543

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 ------RIGYLPQDPTtLF---VADKVIDDLLLVDDvvASVESHLDNFGIIDLKDAHP--FD---------LSSGQKQLV 399
Cdd:COG2274  544 paslrrQIGVVLQDVF-LFsgtIRENITLGDPDATD--EEIIEAARLAGLHDFIEALPmgYDtvvgeggsnLSGGQRQRL 620

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 400 ALA-------KILLtkpqlllLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVaKISDRVAMIFNGQM 467
Cdd:COG2274  621 AIArallrnpRILI-------LDEATSALDAETEAIILENLRRLLKGRTVIIIAHRLSTI-RLADRIIVLDKGRI 687
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-212 2.24e-16

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 77.99  E-value: 2.24e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK-GDI-----DGVIILDEEIENDDTK 74
Cdd:PRK10908   1 MIRFEHVSKAYLGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSaGKIwfsghDITRLKNREVPFLRRQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQnpEDQLVMN-TVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:PRK10908  81 IGMIFQ--DHHLLMDrTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAV 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 154 ILLDEATAQLDPVNREEFIKILKHINdDFNVTVVFVEHQLeGLLDVAN-RLIVMDEGKIV 212
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDI-GLISRRSyRMLTLSDGHLH 216
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 3-214 2.43e-16

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: 78.35  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEeieNDDTK-------- 74
Cdd:cd03218    2 RAENLSKRY-GKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDS---GKILLDG---QDITKlpmhkrar 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 --IGFVFQNPE--DQLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:cd03218   75 lgIGYLPQEASifRKL---TVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATN 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINdDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:cd03218  152 PKFLLLDEPFAGVDPIAVQDIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAE 214
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 288-447 2.81e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 77.61  E-value: 2.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD--------CQGEISKVGCVDRIGYL-PQDP--TTLFVADK 356
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPpaagtiklDGGDIDDPDVAEACHYLgHRNAmkPALTVAEN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 VIDDLLLVDDVVASVESHLDNFGIIDLkdAH-PF-DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIR 434
Cdd:PRK13539  94 LEFWAAFLGGEELDIAAALEAVGLAPL--AHlPFgYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAELIR 171

                        170
                 ....*....|....
gi 169293994 435 G-LSKHMTIVVASH 447
Cdd:PRK13539 172 AhLAQGGIVIAATH 185
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 3-210 3.91e-16

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: 77.12  E-value: 3.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKD----KKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpSL-----RPKGDIDGViildeeienddT 73
Cdd:cd03250    2 SVEDASFTWDSGeqetSFTLKDINLEVPKGELVAIVGPVGSGKSSLLS----ALlgeleKLSGSVSVP-----------G 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  74 KIGFVFQNPedqLVMN-TVWHEIAFGLK------NKGIS-------LKQMKR----RIGEivnyfnlQSIinketqSLSN 135
Cdd:cd03250   67 SIAYVSQEP---WIQNgTIRENILFGKPfdeeryEKVIKacalepdLEILPDgdltEIGE-------KGI------NLSG 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 136 GQKQLVALASVMVMNPKVILLDEATAQLDP-VNREEFIK-ILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGK 210
Cdd:cd03250  131 GQKQRISLARAVYSDADIYLLDDPLSAVDAhVGRHIFENcILGLLLN--NKTRILVTHQLQLLPH-ADQIVVLDNGR 204
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 272-465 4.03e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 78.62  E-value: 4.03e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 272 IDNRIlmKVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEISKVGCV---------- 338
Cdd:PRK13647   1 MDNII--EVEDLHFRYKDgtKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIyLPQRGRVKVMGREvnaenekwvr 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 339 DRIGYLPQDP------TTLF--VADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQ 410
Cdd:PRK13647  79 SKVGLVFQDPddqvfsSTVWddVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 411 LLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK13647 159 VIVLDEPMAYLDPRGQETLMEILDRLHNQgKTVIVATHDVDLAAEWADQVIVLKEG 214
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 292-479 4.40e-16

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: 77.76  E-value: 4.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGE-ISKVGCVDR-IGYLPQDpTTLF----VADKV- 357
Cdd:cd03296   18 LDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLerpdsgtILFGGEdATDVPVQERnVGFVFQH-YALFrhmtVFDNVa 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 -------IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLA 430
Cdd:cd03296   97 fglrvkpRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELR 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 431 NLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:cd03296  177 RWLRRLHDelHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDH 227
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-230 4.55e-16

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 78.13  E-value: 4.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDT------K 74
Cdd:PRK11231   2 TLRTENLTVGY-GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQ---SGTVFLGDKPISMLSsrqlarR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVFQN---PEDQlvmnTVWHEIAFGlKNKGISL-----KQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASV 146
Cdd:PRK11231  78 LALLPQHhltPEGI----TVRELVAYG-RSPWLSLwgrlsAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMV 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 147 MVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLT 226
Cdd:PRK11231 153 LAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLL 231


                 ....
gi 169293994 227 KKIF 230
Cdd:PRK11231 232 RTVF 235
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 274-467 5.13e-16

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: 75.93  E-value: 5.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDLNFGHddiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCVDR-----------I 341
Cdd:cd03215    1 GEPVLEVRGLSVKG---AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPpASGEITLDGKPVTrrsprdairagI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 342 GYLPQDP-TTLFVADkviddlllvddvvASVEshlDNFGIIDLkdahpfdLSSGQKQLVALAKILLTKPQLLLLDEPTKG 420
Cdd:cd03215   78 AYVPEDRkREGLVLD-------------LSVA---ENIALSSL-------LSGGNQQKVVLARWLARDPRVLILDEPTRG 134

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 169293994 421 IDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03215  135 VDVGAKAEIYRLIRELADAgKAVLLISSELDELLGLCDRILVMYEGRI 182
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 9-207 5.50e-16

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: 77.45  E-value: 5.50e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   9 FTYPKDKKIINNISFEIKKGDF-----LVITGKSGCGKTTLLRYFKPSLRPKGdidgviildEEIENDDTKIGFVFQ--N 81
Cdd:cd03237    1 YTYPTMKKTLGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDE---------GDIEIELDTVSYKPQyiK 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  82 PEDQLVMNTVWHEIafgLKNKGISlKQMKRrigEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:cd03237   72 ADYEGTVRDLLSSI---TKDFYTH-PYFKT---EIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSA 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 162 QLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMD 207
Cdd:cd03237  145 YLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 299-466 6.53e-16

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: 76.46  E-value: 6.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 299 ILENEILSIVGANGSGKSSFLRCLAGL------------VDCQGEISKVgcVDRIGYLPQDPTTL-------FVADKVID 359
Cdd:cd03264   22 TLGPGMYGLLGPNGAGKTTLMRILATLtppssgtiridgQDVLKQPQKL--RRRIGYLPQEFGVYpnftvreFLDYIAWL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 360 DLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH 439
Cdd:cd03264  100 KGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIRFRNLLSELGED 179

                        170       180
                 ....*....|....*....|....*..
gi 169293994 440 MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03264  180 RIVILSTHIVEDVESLCNQVAVLNKGK 206
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 278-479 6.55e-16

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: 76.99  E-value: 6.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGcVD---------RIGYLPQD 347
Cdd:cd03299    1 LKVENLSKDWKEFKLKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPdSGKILLNG-KDitnlppekrDISYVPQN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 pTTLF----VADKVIDDLLLVDDVVASVESHLDN----FGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTK 419
Cdd:cd03299   80 -YALFphmtVYKNIAYGLKKRKVDKKEIERKVLEiaemLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFS 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 420 GIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:cd03299  159 ALDVRTKEKLREELKKIRKEfgVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKK 220
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
3-212 7.81e-16

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 80.06  E-value: 7.81e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYP-KDKKIINNISFEIKKGDFLVITGKSGCGKTT----LLRYFKPSlrpKGDI--DGVIILDEEIENDDTKI 75
Cdd:PRK11176 343 EFRNVTFTYPgKEVPALRNINFKIPAGKTVALVGRSGSGKSTianlLTRFYDID---EGEIllDGHDLRDYTLASLRNQV 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPedQLVMNTVWHEIAFGLKNKgISLKQMKR--RIGEIVNYFN-----LQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:PRK11176 420 ALVSQNV--HLFNDTIANNIAYARTEQ-YSREQIEEaaRMAYAMDFINkmdngLDTVIGENGVLLSGGQRQRIAIARALL 496

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 149 MNPKVILLDEATAQLDPvnrEEFIKILKHIND-DFNVTVVFVEHQLEgLLDVANRLIVMDEGKIV 212
Cdd:PRK11176 497 RDSPILILDEATSALDT---ESERAIQAALDElQKNRTSLVIAHRLS-TIEKADEILVVEDGEIV 557
cbiO PRK13637
energy-coupling factor transporter ATPase;
292-477 1.10e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 77.40  E-value: 1.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI---------SKVGCVD---RIGYLPQDPT-TLF----- 352
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKpTSGKIiidgvditdKKVKLSDirkKVGLVFQYPEyQLFeetie 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 --VADKVIDDLLLVDDVVASVESHLDNFGII--DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEF 428
Cdd:PRK13637 103 kdIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 429 LANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFF 477
Cdd:PRK13637 183 ILNKIKELHKeyNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 3-207 1.48e-15

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 74.11  E-value: 1.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRPKGdiDGVIILDEeiendDTKIGFVFQNP 82
Cdd:cd03223    2 ELENLSLATPDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALA-GLWPWG--SGRIGMPE-----GEDLLFLPQRP 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 -------EDQLVMntVWHEIafglknkgislkqmkrrigeivnyfnlqsiinketqsLSNGQKQLVALASVMVMNPKVIL 155
Cdd:cd03223   74 ylplgtlREQLIY--PWDDV-------------------------------------LSGGEQQRLAFARLLLHKPKFVF 114

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 156 LDEATAQLDPvnrEEFIKILKHINDDFnVTVVFVEHQlEGLLDVANRLIVMD 207
Cdd:cd03223  115 LDEATSALDE---ESEDRLYQLLKELG-ITVISVGHR-PSLWKFHDRVLDLD 161
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 292-418 1.51e-15

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: 73.84  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCVD----------RIGYLPQDPT---TLFVADKV 357
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTeGTILLDGQDLtdderkslrkEIGYVFQDPQlfpRLTVRENL 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994  358 IDDLLLVDDVVASVESH----LDNFGIIDLKD----AHPFDLSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:pfam00005  81 RLGLLLKGLSKREKDARaeeaLEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 279-467 1.67e-15

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: 75.94  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDL--NFGhdDIV-LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG----------------EISKVG--- 336
Cdd:cd03219    2 EVRGLtkRFG--GLVaLDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSgsvlfdgeditglpphEIARLGigr 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 337 ---------------CVdRIGYLPQDPTTLFVAdkviDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVAL 401
Cdd:cd03219   80 tfqiprlfpeltvleNV-MVAAQARTGSGLLLA----RARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 402 AKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03219  155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERgITVLLVEHDMDVVMSLADRVTVLDQGRV 221
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
18-497 2.08e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 78.67  E-value: 2.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIdgvIILDEEIENDDTK------IGFVFQNPE--DQLvm 88
Cdd:PRK09700  21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPtKGTI---TINNINYNKLDHKlaaqlgIGIIYQELSviDEL-- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  89 nTVWHEIAFGL----KNKGISL---KQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:PRK09700  96 -TVLENLYIGRhltkKVCGVNIidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 162 QLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEMLTKKIFVESLPNyvRVS 241
Cdd:PRK09700 175 SLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIVRLMVGRELQN--RFN 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 242 SLCDKLclsikearealvnfenfdikimDEIDNRILMKVRDLNfGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRC 321
Cdd:PRK09700 252 AMKENV----------------------SNLAHETVFEVRNVT-SRDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNC 308

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 322 LAGlVD--CQGEI----------SKVGCVDR-IGYLPQD-PTTLFVADKVIDDLLlvddvvaSVESHLDN------FGII 381
Cdd:PRK09700 309 LFG-VDkrAGGEIrlngkdisprSPLDAVKKgMAYITESrRDNGFFPNFSIAQNM-------AISRSLKDggykgaMGLF 380

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 382 DLKDAHPF--------------------DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-M 440
Cdd:PRK09700 381 HEVDEQRTaenqrellalkchsvnqnitELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADDgK 460

                        490       500       510       520       530
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 441 TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREffshnlfyTTTINKIMRENNPE 497
Cdd:PRK09700 461 VILMVSSELPEIITVCDRIAVFCEGRLTQILTNRD--------DMSEEEIMAWALPQ 509
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 279-466 2.57e-15

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: 78.65  E-value: 2.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISkVGCVD-----------RIGY 343
Cdd:COG4987  335 ELEDVSFRYPGagrPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQsGSIT-LGGVDlrdldeddlrrRIAV 413

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 344 LPQDP----TT----LFVADKviddlllvddvVAS---VESHLDNFGIIDLKDAHP--FD---------LSSGQKQLVAL 401
Cdd:COG4987  414 VPQRPhlfdTTlrenLRLARP-----------DATdeeLWAALERVGLGDWLAALPdgLDtwlgeggrrLSGGERRRLAL 482

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 402 AKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKIsDRVAMIFNGQ 466
Cdd:COG4987  483 ARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTVLLITHRLAGLERM-DRILVLEDGR 546
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
16-211 2.61e-15

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 75.78  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPS----------LRPKGDIDGVI-ILD-EEIENDDTKIGFVF 79
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCInfleKPSegsivvngqtINLVRDKDGQLkVADkNQLRLLRTRLTMVF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNPEDQLVMNTVWHEIAFGLKNKGISLKQMKRRIgeiVNYFNLQSIINKETQS----LSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK10619  99 QHFNLWSHMTVLENVMEAPIQVLGLSKQEARERA---VKYLAKVGIDERAQGKypvhLSGGQQQRVSIARALAMEPEVLL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK10619 176 FDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKI 230
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 12-214 2.81e-15

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: 74.88  E-value: 2.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  12 PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdIDGVIILDE---EIENDDTKI-----GFvfqNPE 83
Cdd:cd03220   32 VGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRL----------LAGIYPPDSgtvTVRGRVSSLlglggGF---NPE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 ----DQLVMNTVWHeiafglknkGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:cd03220   99 ltgrENIYLNGRLL---------GLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEV 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 160 TAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:cd03220  170 LAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFD 223
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 280-467 3.32e-15

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: 73.40  E-value: 3.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEIsKVGCVD-----------RIGYL 344
Cdd:cd03246    3 VENVSFRYPGaepPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLlRPTSGRV-RLDGADisqwdpnelgdHVGYL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 PQDpTTLF---VADKViddlllvddvvasveshldnfgiidlkdahpfdLSSGQKQLVALAKILLTKPQLLLLDEPTKGI 421
Cdd:cd03246   82 PQD-DELFsgsIAENI---------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHL 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 422 DASSKEFLANLIRGLSKH-MTIVVASHDLEfVAKISDRVAMIFNGQM 467
Cdd:cd03246  128 DVEGERALNQAIAALKAAgATRIVIAHRPE-TLASADRILVLEDGRV 173
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
18-212 3.34e-15

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 75.60  E-value: 3.34e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPK-GDIdgvIILDEEIENDD-----TKIGFVFQNPEDQL-VMNT 90
Cdd:PRK15112  29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTsGEL---LIDDHPLHFGDysyrsQRIRMIFQDPSTSLnPRQR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEIAFGLK-NKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNR 168
Cdd:PRK15112 106 ISQILDFPLRlNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 169 EEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVV 229
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 10-223 3.54e-15

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 75.12  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  10 TYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdIDGVIILDE-EIEND-------DTKIGFvfqN 81
Cdd:COG1134   34 TRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKL----------IAGILEPTSgRVEVNgrvsallELGAGF---H 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  82 PEdqLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:COG1134  101 PE--L---TGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLA 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 162 QLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDE 223
Cdd:COG1134  176 VGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 18-210 4.05e-15

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 75.03  E-value: 4.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD-EEIEN-DDTKI---GFV--FQNP-------- 82
Cdd:PRK11300  21 VNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTG---GTILLRgQHIEGlPGHQIarmGVVrtFQHVrlfremtv 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 -EDQLV-----MNTVWheIAFGLKNKGISLKQMK--RRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:PRK11300  98 iENLLVaqhqqLKTGL--FSGLLKTPAFRRAESEalDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGK 210
Cdd:PRK11300 176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGT 231
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 17-223 4.23e-15

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: 75.66  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  17 IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDI--DGVIILDEEIENDDTKIGFVfqnPEDQLVMNTVWHe 94
Cdd:cd03289   19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIqiDGVSWNSVPLQKWRKAFGVI---PQKVFIFSGTFR- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  95 iafglKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSL-----------SNGQKQLVALASVMVMNPKVILLDEATAQL 163
Cdd:cd03289   95 -----KNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEPSAHL 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 164 DPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDvANRLIVMDEGKIVIDNEIKMAVDE 223
Cdd:cd03289  170 DPITYQVIRKTLKQAFAD--CTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNE 226
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 277-479 5.55e-15

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: 75.86  E-value: 5.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLN--FGHDDIVLK---DLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISkvGCV------------- 338
Cdd:COG0444    1 LLEVRNLKvyFPTRRGVVKavdGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITS--GEIlfdgedllklsek 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 339 -------DRIGYLPQDPTTLF-----VADKV-----IDDLLLVDDVVASVESHLDNFGIID---LKDAHPFDLSSGQKQ- 397
Cdd:COG0444   79 elrkirgREIQMIFQDPMTSLnpvmtVGDQIaeplrIHGGLSKAEARERAIELLERVGLPDperRLDRYPHELSGGMRQr 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 398 -------------LVAlakilltkpqllllDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMI 462
Cdd:COG0444  159 vmiaralalepklLIA--------------DEPTTALDVTIQAQILNLLKDLQRelGLAILFITHDLGVVAEIADRVAVM 224

                        250
                 ....*....|....*...
gi 169293994 463 FNGQ-MESVDsTREFFSH 479
Cdd:COG0444  225 YAGRiVEEGP-VEELFEN 241
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 279-467 6.05e-15

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: 73.79  E-value: 6.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDL--NFGHDDiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL---------VDCQGEISKVGCVDRIGYLPQD 347
Cdd:cd03268    2 KTNDLtkTYGKKR-VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLikpdsgeitFDGKSYQKNIEALRRIGALIEA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 PT---TLFVADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS 424
Cdd:cd03268   81 PGfypNLTARENLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPD 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 425 SKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03268  161 GIKELRELILSLRDQgITVLISSHLLSEIQKVADRIGIINKGKL 204
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
3-214 6.79e-15

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 74.66  E-value: 6.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIiNNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLR----PKGDID--GVII-----LDEEIEND 71
Cdd:PRK09984   6 RVEKLAKTFNQHQAL-HAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIEllGRTVqregrLARDIRKS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVFQ--NPEDQLvmnTVWHEIAFGLKNKGISLK--------QMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLV 141
Cdd:PRK09984  85 RANTGYIFQqfNLVNRL---SVLENVLIGALGSTPFWRtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 142 ALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVID 214
Cdd:PRK09984 162 AIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYD 234
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 278-493 7.17e-15

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 74.69  E-value: 7.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHD-DIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD-----------RIGYLP 345
Cdd:PRK14258   8 IKVNNLSFYYDtQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESEVRVEGRVEffnqniyerrvNLNRLR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTTLF---------VADKV-----IDDLLLVDDVVASVESHLDNFGIID-LKDA---HPFDLSSGQKQLVALAKILLT 407
Cdd:PRK14258  88 RQVSMVHpkpnlfpmsVYDNVaygvkIVGWRPKLEIDDIVESALKDADLWDeIKHKihkSALDLSGGQQQRLCIARALAV 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 408 KPQLLLLDEPTKGIDASSKEFLANLIRG--LSKHMTIVVASHDLEFVAKISDRVAMiFNGQMESVDSTREFFSHNLFYTT 485
Cdd:PRK14258 168 KPKVLLMDEPCFGLDPIASMKVESLIQSlrLRSELTMVIVSHNLHQVSRLSDFTAF-FKGNENRIGQLVEFGLTKKIFNS 246


                 ....*...
gi 169293994 486 TINKIMRE 493
Cdd:PRK14258 247 PHDSRTRE 254
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 277-478 8.43e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 74.88  E-value: 8.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI---------SKVGCVD---RI 341
Cdd:PRK13636   5 ILKVEELNYNYSDgtHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKpSSGRIlfdgkpidySRKGLMKlreSV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 342 GYLPQDP-TTLFVAD-------KVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLL 413
Cdd:PRK13636  85 GMVFQDPdNQLFSASvyqdvsfGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLV 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13636 165 LDEPTAGLDPMGVSEIMKLLVEMQKELglTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 280-467 9.40e-15

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: 73.39  E-value: 9.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG--------EISKVGCVD---RIGYLP 345
Cdd:cd03245    5 FRNVSFSYPNqeiPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSgsvlldgtDIRQLDPADlrrNIGYVP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTTLFVADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHP-----------FDLSSGQKQLVALAKILLTKPQLLLL 414
Cdd:cd03245   85 QDVTLFYGTLRDNITLGAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLL 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 415 DEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAkISDRVAMIFNGQM 467
Cdd:cd03245  165 DEPTSAMDMNSEERLKERLRQLLGDKTLIIITHRPSLLD-LVDRIIVMDSGRI 216
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 4-212 9.86e-15

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: 76.71  E-value: 9.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDE-EIEN-DDTK----IG 76
Cdd:COG4618  333 VENLTVVPPGSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA---GSVRLDGaDLSQwDREElgrhIG 409

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPEdqLVMNTVWHEIAfglknkgislkqmkrRIGEIvnyfNLQSIINK-----------------ETQ------SL 133
Cdd:COG4618  410 YLPQDVE--LFDGTIAENIA---------------RFGDA----DPEKVVAAaklagvhemilrlpdgyDTRigeggaRL 468

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 134 SNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLeGLLDVANRLIVMDEGKIV 212
Cdd:COG4618  469 SGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRP-SLLAAVDKLLVLRDGRVQ 545
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 3-193 1.37e-14

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: 76.25  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRY---FKPSLRPKGDIDGVIILDEEIENDDTKIGFVF 79
Cdd:TIGR02868 336 ELRDLSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATlagLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVCA 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   80 QNPedQLVMNTVWHEIAFGLKN-KGISLKQMKRRIGeIVNYF-----NLQSIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:TIGR02868 416 QDA--HLFDTTVRENLRLARPDaTDEELWAALERVG-LADWLralpdGLDTVLGEGGARLSGGERQRLALARALLADAPI 492

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 169293994  154 ILLDEATAQLDPVNREEFIKILKHINDDFnvTVVFVEHQL 193
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHHL 530
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 15-212 2.63e-14

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 75.47  E-value: 2.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   15 KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRPKG-DIDGVIILD-EEIENDDTKI--GFVFQnpEDQLV-MN 89
Cdd:TIGR00955  38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALA-FRSPKGvKGSGSVLLNgMPIDAKEMRAisAYVQQ--DDLFIpTL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   90 TVWHEIAFG----LKNKgISLKQMKRRIGEIVNYFNLQS----IINKETQ--SLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:TIGR00955 115 TVREHLMFQahlrMPRR-VTKKEKRERVDEVLQALGLRKcantRIGVPGRvkGLSGGERKRLAFASELLTDPPLLFCDEP 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994  160 TAQLDPVNREEFIKILKHINDDfNVTVVFVEHQ----LEGLLDvanRLIVMDEGKIV 212
Cdd:TIGR00955 194 TSGLDSFMAYSVVQVLKGLAQK-GKTIICTIHQpsseLFELFD---KIILMAEGRVA 246
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
277-478 2.64e-14

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 73.12  E-value: 2.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGH-DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI---------SKVGCV---DRIG 342
Cdd:PRK13638   1 MLATSDLWFRYqDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQkGAVlwqgkpldySKRGLLalrQQVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 343 YLPQDP-TTLFVADkviddlllvddVVASVESHLDNFGI------------IDLKDAHPFD------LSSGQKQLVALAK 403
Cdd:PRK13638  81 TVFQDPeQQIFYTD-----------IDSDIAFSLRNLGVpeaeitrrvdeaLTLVDAQHFRhqpiqcLSHGQKKRVAIAG 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 404 ILLTKPQLLLLDEPTKGID-ASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13638 150 ALVLQARYLLLDEPTAGLDpAGRTQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 283-469 3.91e-14

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 74.72  E-value: 3.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 283 LNFGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGCVdRIGYLPQDPT---------TLF 352
Cdd:COG0488    6 KSFG-GRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPdSGEVSIPKGL-RIGYLPQEPPldddltvldTVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKVID--------------DLLLVDDVVASVESHLDNFGIIDLK------------DAHPFD-----LSSGQKQLVAL 401
Cdd:COG0488   84 DGDAELRaleaeleeleaklaEPDEDLERLAELQEEFEALGGWEAEaraeeilsglgfPEEDLDrpvseLSGGWRRRVAL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 402 AKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKhmTIVVASHDLEFVAKISDRVAMIFNGQMES 469
Cdd:COG0488  164 ARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYPG--TVLVVSHDRYFLDRVATRILELDRGKLTL 229
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 291-466 6.63e-14

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 70.99  E-value: 6.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG--------EISKVGCVD---RIGYLPQDPTtLFvadkvid 359
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSgsilidgvDISKIGLHDlrsRISIIPQDPV-LF------- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 360 dlllvddvVASVESHLDNFGIID-------LKDAHPFD-------------------LSSGQKQLVALAKILLTKPQLLL 413
Cdd:cd03244   91 --------SGTIRSNLDPFGEYSdeelwqaLERVGLKEfveslpggldtvveeggenLSVGQRQLLCLARALLRKSKILV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQ 466
Cdd:cd03244  163 LDEATASVDPETDALIQKTIREAFKDCTVLTIAHRLDTIID-SDRILVLDKGR 214
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 287-479 7.56e-14

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 71.32  E-value: 7.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 287 HDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD-------------------RIGYLPQD 347
Cdd:PRK11264  14 HGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITidtarslsqqkglirqlrqHVGFVFQN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 pTTLF---------VADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:PRK11264  94 -FNLFphrtvleniIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 419 KGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQEkRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFAD 234
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 15-257 7.95e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 71.67  E-value: 7.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  15 KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFK------PSLRPKGDI--DGVIILD-EEIENDDTKIGFVFQNPE-- 83
Cdd:PRK14271  34 KTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNrmndkvSGYRYSGDVllGGRSIFNyRDVLEFRRRVGMLFQRPNpf 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 -----DQLVMNTVWHEIAFGLKNKGISlkqmKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:PRK14271 114 pmsimDNVLAGVRAHKLVPRKEFRGVA----QARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDE 189

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 159 ATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDVANRLIVMDEGKIvidneikmaVDEMLTKKIFveSLPNYV 238
Cdd:PRK14271 190 PTSALDPTTTEKIEEFIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRL---------VEEGPTEQLF--SSPKHA 256

                        250
                 ....*....|....*....
gi 169293994 239 RVSSLCDKLCLSIKEAREA 257
Cdd:PRK14271 257 ETARYVAGLSGDVKDAKRG 275
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 288-478 8.13e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 71.23  E-value: 8.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG-----------------EISKVGCVDRIGYLPQDPTT 350
Cdd:PRK14246  22 DKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDskikvdgkvlyfgkdifQIDAIKLRKEVGMVFQQPNP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 ---LFVADKVIDDLLLVDDVVAS-----VESHLDNFG----IIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:PRK14246 102 fphLSIYDNIAYPLKSHGIKEKReikkiVEECLRKVGlwkeVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 419 KGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFT 241
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
33-212 8.83e-14

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 72.60  E-value: 8.83e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  33 ITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDTK----------IGFVFQnpEDQLVMN-TVWHEIAFGLKN 101
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQ---KGRIVLNGRVLFDAEKgiclppekrrIGYVFQ--DARLFPHyKVRGNLRYGMAK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 102 KgislkqMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDD 181
Cdd:PRK11144 104 S------MVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLARE 177

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169293994 182 FNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11144 178 INIPILYVSHSLDEILRLADRVVVLEQGKVK 208
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 3-212 9.05e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 73.59  E-value: 9.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKI----------INNISFEIKKGDFLVITGKSGCGKTT----LLRYfkpsLRPKGDI--DGviildE 66
Cdd:PRK15134 277 DVEQLQVAFPIRKGIlkrtvdhnvvVKNISFTLRPGETLGLVGESGSGKSTtglaLLRL----INSQGEIwfDG-----Q 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  67 EIENDDTK--------IGFVFQNPEDQLvmN---TVWHEIAFGLK--NKGISLKQMKRRIGEIVNYFNLqsiiNKETQ-- 131
Cdd:PRK15134 348 PLHNLNRRqllpvrhrIQVVFQDPNSSL--NprlNVLQIIEEGLRvhQPTLSAAQREQQVIAVMEEVGL----DPETRhr 421

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 132 ---SLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDE 208
Cdd:PRK15134 422 ypaEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQ 501


                 ....
gi 169293994 209 GKIV 212
Cdd:PRK15134 502 GEVV 505
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
283-471 1.18e-13

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 70.08  E-value: 1.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 283 LNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISkVGCVD--------------RIGYLPQD 347
Cdd:COG2884    9 KRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPtSGQVL-VNGQDlsrlkrreipylrrRIGVVFQD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 PTTLF---VADKV----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA-------KIlltkpqlLL 413
Cdd:COG2884   88 FRLLPdrtVYENValplRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIAralvnrpEL-------LL 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQMESVD 471
Cdd:COG2884  161 ADEPTGNLDPETSWEIMELLEEINRRgTTVLIATHDLELVDRMPKRVLELEDGRLVRDE 219
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
285-475 1.71e-13

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 71.65  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 285 FGHDDiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQG-EISKVGCVDR-IGYLPQDpTTLF--- 352
Cdd:PRK10851  12 FGRTQ-VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLehqtsghIRFHGtDVSRLHARDRkVGFVFQH-YALFrhm 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 -VADKVI--------DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDA 423
Cdd:PRK10851  90 tVFDNIAfgltvlprRERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFGALDA 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169293994 424 SSKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:PRK10851 170 QVRKELRRWLRQLHEELkfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQ 223
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 291-472 2.43e-13

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 68.98  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG--------EISKVGCVD---RIGYLPQDPTtLFvadkvid 359
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEgkieidgiDISTIPLEDlrsSLTIIPQDPT-LF------- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 360 dlllvddvVASVESHLDNFGIIDlkDAHPF----------DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFL 429
Cdd:cd03369   95 --------SGTIRSNLDPFDEYS--DEEIYgalrvsegglNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 430 ANLIRGLSKHMTIVVASHDLEFVAKIsDRVAMIFNGQMESVDS 472
Cdd:cd03369  165 QKTIREEFTNSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDH 206
cbiO PRK13640
energy-coupling factor transporter ATPase;
280-478 3.20e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 70.21  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDDI---VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV----DCQGEISKVGCV----------DRIG 342
Cdd:PRK13640   8 FKHVSFTYPDSkkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpddNPNSKITVDGITltaktvwdirEKVG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 343 YLPQDPTTLFVADKVIDDLLLVDDVVAS--------VESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLL 414
Cdd:PRK13640  88 IVFQNPDNQFVGATVGDDVAFGLENRAVprpemikiVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIIL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 415 DEPTKGIDASSKEFLANLIRGL--SKHMTIVVASHDLEfVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13640 168 DESTSMLDPAGKEQILKLIRKLkkKNNLTVISITHDID-EANMADQVLVLDDGKLLAQGSPVEIFS 232
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 291-479 3.56e-13

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: 71.70  E-value: 3.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGeiskvGCV----------DR------IGYLPQDPTtLFva 354
Cdd:COG4618  347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTA-----GSVrldgadlsqwDReelgrhIGYLPQDVE-LF-- 418

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 355 dkviddlllvddvVASVEshlDN---FGIID---------LKDAH------P--FD---------LSSGQKQLVALA--- 402
Cdd:COG4618  419 -------------DGTIA---ENiarFGDADpekvvaaakLAGVHemilrlPdgYDtrigeggarLSGGQRQRIGLAral 482

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 403 ----KIlltkpqlLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAkISDRVAMIFNGQMESVDSTREFF 477
Cdd:COG4618  483 ygdpRL-------VVLDEPNSNLDDEGEAALAAAIRALKARgATVVVITHRPSLLA-AVDKLLVLRDGRVQAFGPRDEVL 554


                 ..
gi 169293994 478 SH 479
Cdd:COG4618  555 AR 556
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 298-466 3.63e-13

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: 69.36  E-value: 3.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 298 DILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVgcVDRIGYLPQ--DPTTLFVADKVIDDLLLVDDVVASVESH 374
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKpDEGDIEIE--LDTVSYKPQyiKADYEGTVRDLLSSITKDFYTHPYFKTE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 375 LDN-FGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEF 451
Cdd:cd03237   99 IAKpLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFAENneKTAFVVEHDIIM 178

                        170
                 ....*....|....*
gi 169293994 452 VAKISDRVaMIFNGQ 466
Cdd:cd03237  179 IDYLADRL-IVFEGE 192
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 277-478 5.10e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 69.34  E-value: 5.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSF-------LRCLAGLVDCQGEISK------VGCVDRI 341
Cdd:PRK13639   1 ILETRDLKYSYPDgtEALKGINFKAEKGEMVALLGPNGAGKSTLflhfngiLKPTSGEVLIKGEPIKydkkslLEVRKTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 342 GYLPQDPTTLFVADKV--------IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLL 413
Cdd:PRK13639  81 GIVFQNPDDQLFAPTVeedvafgpLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13639 161 LDEPTSGLDPMGASQIMKLLYDLNKEgITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 280-468 5.14e-13

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: 67.34  E-value: 5.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEI-------SKVGCVDR--IGYLPQ 346
Cdd:cd03247    3 INNVSFSYPEqeqQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGdLKPQQGEItldgvpvSDLEKALSslISVLNQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 347 DP----TTLfvadkviddlllvddvvasveshLDNFGIidlkdahpfDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:cd03247   83 RPylfdTTL-----------------------RNNLGR---------RFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 423 ASSKEFLANLIRGLSKHMTIVVASHDLEFVAKIsDRVAMIFNGQME 468
Cdd:cd03247  131 PITERQLLSLIFEVLKDKTLIWITHHLTGIEHM-DKILFLENGKII 175
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
17-211 5.80e-13

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 68.30  E-value: 5.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  17 IINNISFEIKKGDFLVITGKSGCGKTTLLRYFkpslrpkGDID----GVIILDEEIEND----------DTKIGFVFQNp 82
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLL-------GGLDtptsGDVIFNGQPMSKlssaakaelrNQKLGFIYQF- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 EDQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:PRK11629  96 HHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGN 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169293994 163 LDPVNREEFIKILKHINDDFNVTVVFVEHQLEgLLDVANRLIVMDEGKI 211
Cdd:PRK11629 176 LDARNADSIFQLLGELNRLQGTAFLVVTHDLQ-LAKRMSRQLEMRDGRL 223
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 15-212 5.90e-13

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: 67.67  E-value: 5.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  15 KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDeEIENDDTKIGF----VFQNPEDQLVMN- 89
Cdd:cd03233   20 IPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHYN-GIPYKEFAEKYpgeiIYVSEEDVHFPTl 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  90 TVWHEIAFGLKNKGislKQMKRRIgeivnyfnlqsiinketqslSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNRE 169
Cdd:cd03233   99 TVRETLDFALRCKG---NEFVRGI--------------------SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTAL 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 170 EFIKILKHINDDFNVTVVFVEHQL-EGLLDVANRLIVMDEGKIV 212
Cdd:cd03233  156 EILKCIRTMADVLKTTTFVSLYQAsDEIYDLFDKVLVLYEGRQI 199
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 282-471 7.00e-13

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: 68.36  E-value: 7.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 282 DLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCV-------------DRIGYLPQD 347
Cdd:cd03256    7 SKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEpTSGSVLIDGTDinklkgkalrqlrRQIGMIFQQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 PT-----------------------TLF----VADKVIDDlllvddvvasveSHLDNFGIIDLKDAHPFDLSSGQKQLVA 400
Cdd:cd03256   87 FNlierlsvlenvlsgrlgrrstwrSLFglfpKEEKQRAL------------AALERVGLLDKAYQRADQLSGGQQQRVA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 401 LAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDR-VAM-----IFNGQMESVD 471
Cdd:cd03256  155 IARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREegITVIVSLHQVDLAREYADRiVGLkdgriVFDGPPAELT 233
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 4-205 7.51e-13

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: 71.48  E-value: 7.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994     4 IENFSFTYPKD-KKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDI--DGVIILDEEIENDDTKIG---- 76
Cdd:TIGR01271 1220 VQGLTAKYTEAgRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIqiDGVSWNSVTLQTWRKAFGvipq 1299

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    77 --FVFQ-------NPEDQLVMNTVWhEIAfglknKGISLKQMKRRIGEIVNYfnlqsIINKETQSLSNGQKQLVALASVM 147
Cdd:TIGR01271 1300 kvFIFSgtfrknlDPYEQWSDEEIW-KVA-----EEVGLKSVIEQFPDKLDF-----VLVDGGYVLSNGHKQLMCLARSI 1368

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994   148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDVANRLIV 205
Cdd:TIGR01271 1369 LSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLECQQFLVI 1424
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 1-177 7.59e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 67.28  E-value: 7.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIdgvIILDEEIEND----DTKI 75
Cdd:PRK13540   1 MLDVIELDFDY-HDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPeKGEI---LFERQSIKKDlctyQKQL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQ----NPEDQLVMNTVWhEIAFGLKNKGISlkqmkrrigEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNP 151
Cdd:PRK13540  77 CFVGHrsgiNPYLTLRENCLY-DIHFSPGAVGIT---------ELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKA 146

                        170       180
                 ....*....|....*....|....*..
gi 169293994 152 KVILLDEATAQLDPVNREEFI-KILKH 177
Cdd:PRK13540 147 KLWLLDEPLVALDELSLLTIItKIQEH 173
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
5-212 8.61e-13

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 70.76  E-value: 8.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLL----RYFKPSLrpkGD--IDGVIILDEEIENDDTKIGFV 78
Cdd:PRK13657 338 DDVSFSYDNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLInllqRVFDPQS---GRilIDGTDIRTVTRASLRRNIAVV 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPedqLVMNTVWHE-IAFGLKN-------KGISLKQ----MKRRIGeivnyfNLQSIINKETQSLSNGQKQLVALASV 146
Cdd:PRK13657 415 FQDA---GLFNRSIEDnIRVGRPDatdeemrAAAERAQahdfIERKPD------GYDTVVGERGRQLSGGERQRLAIARA 485

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 147 MVMNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PRK13657 486 LLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVV 548
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 288-447 9.36e-13

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: 66.02  E-value: 9.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGCvDRIGYLPQDPTtlfvadkviddlllvdd 366
Cdd:cd03223   13 GRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWgSGRIGMPEG-EDLLFLPQRPY----------------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 367 vvasveshldnFGIIDLKDA--HPFD--LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSkhMTI 442
Cdd:cd03223   75 -----------LPLGTLREQliYPWDdvLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLYQLLKELG--ITV 141


                 ....*
gi 169293994 443 VVASH 447
Cdd:cd03223  142 ISVGH 146
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 274-479 9.68e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 68.02  E-value: 9.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDLNFGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD------CQGE-------ISKVGCVD- 339
Cdd:PRK14247   2 NKIEIRDLKVSFG-QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElypearVSGEvyldgqdIFKMDVIEl 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 --RIGYLPQDPT---TLFVADKVID------DLLLVDDVVASVESHLDNFGIID-LKD---AHPFDLSSGQKQLVALAKI 404
Cdd:PRK14247  81 rrRVQMVFQIPNpipNLSIFENVALglklnrLVKSKKELQERVRWALEKAQLWDeVKDrldAPAGKLSGGQQQRLCIARA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 405 LLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK14247 161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTN 235
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 289-462 1.17e-12

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: 70.01  E-value: 1.17e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  289 DIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCV-----------DRIGYLPQDPTtLF---VA 354
Cdd:TIGR02857 335 RPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVpladadadswrDQIAWVPQHPF-LFagtIA 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  355 DKVidDLLLVDDVVASVESHLDNFGIIDLKDA-----------HPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDA 423
Cdd:TIGR02857 414 ENI--RLARPDASDAEIREALERAGLDEFVAAlpqgldtpigeGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLDA 491

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 169293994  424 SSKEFLANLIRGLSKHMTIVVASHDLEfVAKISDRVAMI 462
Cdd:TIGR02857 492 ETEAEVLEALRALAQGRTVLLVTHRLA-LAALADRIVVL 529
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
279-480 1.21e-12

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 67.47  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDDIVLK-DLEIDilENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGcVDRIGYLP---------QD 347
Cdd:COG3840    3 RLDDLTYRYGDFPLRfDLTIA--AGERVAILGPSGAGKSTLLNLIAGFLPPdSGRILWNG-QDLTALPPaerpvsmlfQE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 pTTLF--------------------VADKviddlllvddvvASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLT 407
Cdd:COG3840   80 -NNLFphltvaqniglglrpglkltAEQR------------AQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVR 146

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 408 KPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSHN 480
Cdd:COG3840  147 KRPILLLDEPFSALDPALRQEMLDLVDELCRerGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 285-479 1.41e-12

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: 67.33  E-value: 1.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 285 FGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIsKVGCVD-----------RIGYLPQDpTTLF 352
Cdd:cd03295   10 YGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEpTSGEI-FIDGEDireqdpvelrrKIGYVIQQ-IGLF 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 ----VADKVIDDLLLVDDVVASVES------HLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:cd03295   88 phmtVEENIALVPKLLKWPKEKIREradellALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLLLMDEPFGALD 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 423 ASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:cd03295  168 PITRDQLQEEFKRLQQelGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRS 226
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
115-466 1.44e-12

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 69.84  E-value: 1.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 115 EIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLe 194
Cdd:PRK13409 195 EVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLDIRQRLNVARLIRELAE--GKYVLVVEHDL- 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 195 GLLDVANRLIVMDEGKividneikmavdemltkkifveslPN-YVRVSSlcdklclsIKEAREALVNF-------ENfdI 266
Cdd:PRK13409 272 AVLDYLADNVHIAYGE------------------------PGaYGVVSK--------PKGVRVGINEYlkgylpeEN--M 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 267 KIMDE------------IDNRILMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEIS 333
Cdd:PRK13409 318 RIRPEpiefeerpprdeSERETLVEYPDLTKKLGDFSLEVEGGEIYEGEVIGIVGPNGIGKTTFAKLLAGvLKPDEGEVD 397

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 334 -KVgcvdRIGYLPQdpttlFVADKViddLLLVDDVVASVESHLDN----------FGIIDLKDAHPFDLSSGQKQLVALA 402
Cdd:PRK13409 398 pEL----KISYKPQ-----YIKPDY---DGTVEDLLRSITDDLGSsyykseiikpLQLERLLDKNVKDLSGGELQRVAIA 465

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 403 KILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL--SKHMTIVVASHDLEFVAKISDRVaMIFNGQ 466
Cdd:PRK13409 466 ACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIaeEREATALVVDHDIYMIDYISDRL-MVFEGE 530
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 4-212 1.45e-12

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 69.85  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDK-KIINNISFEIKKGDFLVITGKSGCGKTTLL----RYFKPSlrpKGDI--DGVIILDEEIENDDTKIG 76
Cdd:PRK11160 341 LNNVSFTYPDQPqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLqlltRAWDPQ---QGEIllNGQPIADYSEAALRQAIS 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 FVFQNPedQLVMNTVWHEIAFGLKNKGIS-LKQMKRRIGeivnyfnLQSIINKET----------QSLSNGQKQLVALAS 145
Cdd:PRK11160 418 VVSQRV--HLFSATLRDNLLLAAPNASDEaLIEVLQQVG-------LEKLLEDDKglnawlgeggRQLSGGEQRRLGIAR 488

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 146 VMVMNPKVILLDEATAQLDPVN-REEFIKILKHINDDfnvTVVFVEHQLEGlLDVANRLIVMDEGKIV 212
Cdd:PRK11160 489 ALLHDAPLLLLDEPTEGLDAETeRQILELLAEHAQNK---TVLMITHRLTG-LEQFDRICVMDNGQII 552
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 258-488 1.96e-12

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: 69.77  E-value: 1.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  258 LVNFENFDIKIMDEIDN---RILMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIS 333
Cdd:TIGR01193 453 LVDSEFINKKKRTELNNlngDIVINDVSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARsGEIL 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  334 KVGC----VDR------IGYLPQDPttLFVADKVIDDLLLVDDVVASVESHLDNFGIIDLKD--------------AHPF 389
Cdd:TIGR01193 533 LNGFslkdIDRhtlrqfINYLPQEP--YIFSGSILENLLLGAKENVSQDEIWAACEIAEIKDdienmplgyqtelsEEGS 610

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  390 DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDA-SSKEFLANLIRglSKHMTIVVASHDLEfVAKISDRVAMIFNGQME 468
Cdd:TIGR01193 611 SISGGQKQRIALARALLTDSKVLILDESTSNLDTiTEKKIVNNLLN--LQDKTIIFVAHRLS-VAKQSDKIIVLDHGKII 687

                         250       260
                  ....*....|....*....|
gi 169293994  469 SVDSTREFFSHNLFYTTTIN 488
Cdd:TIGR01193 688 EQGSHDELLDRNGFYASLIH 707
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 14-212 2.46e-12

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: 66.01  E-value: 2.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF--KPSLRP-KGDI--DGVIILDEEIENDDTK-IGFVFQNPEdqlv 87
Cdd:cd03217   12 GKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVtEGEIlfKGEDITDLPPEERARLgIFLAFQYPP---- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  88 mntvwhEIAfglknkGISLKQMKRRIGEivnyfnlqsiinketqSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVN 167
Cdd:cd03217   88 ------EIP------GVKNADFLRYVNE----------------GFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDA 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 168 REEFIKILKHINDDfNVTVVFVEHQLEgLLD--VANRLIVMDEGKIV 212
Cdd:cd03217  140 LRLVAEVINKLREE-GKSVLIITHYQR-LLDyiKPDRVHVLYDGRIV 184
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 18-209 2.94e-12

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 65.04  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRyfkpslrpkgdiDGVIILDEEIENDDTKIGFvfqnpedqlvmntvwheiaf 97
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN------------EGLYASGKARLISFLPKFS-------------------- 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  98 glKNKGISLKQMKRRIGEIVNYFNLqsiiNKETQSLSNGQKQLVALASVMVMNPK--VILLDEATAQLDPVNREEFIKIL 175
Cdd:cd03238   59 --RNKLIFIDQLQFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169293994 176 KHINDDfNVTVVFVEHQLEgLLDVANRLIVMDEG 209
Cdd:cd03238  133 KGLIDL-GNTVILIEHNLD-VLSSADWIIDFGPG 164
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
4-215 3.25e-12

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 68.98  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYP---KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPS---LRPKG------DIDGVIILDEE 67
Cdd:PRK10535   7 LKDIRRSYPsgeEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILgcldKPTsgtYRVAGqdvatlDADALAQLRRE 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  68 ienddtKIGFVFQNPEdQLVMNTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVM 147
Cdd:PRK10535  87 ------HFGFIFQRYH-LLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARAL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNvTVVFVEHQLEgLLDVANRLIVMDEGKIVIDN 215
Cdd:PRK10535 160 MNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQ-VAAQAERVIEIRDGEIVRNP 225
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 4-194 3.60e-12

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 65.75  E-value: 3.60e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDEEIENDDTKIgfvfqnp 82
Cdd:COG2401   31 LEAFGVELRVVERyVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLI------- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 eDQLVMNTVWHEIAFGLKNKGISLKQ-MKRRIGEivnyfnlqsiinketqsLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:COG2401  104 -DAIGRKGDFKDAVELLNAVGLSDAVlWLRRFKE-----------------LSTGQKFRFRLALLLAERPKLLVIDEFCS 165

                        170       180       190
                 ....*....|....*....|....*....|...
gi 169293994 162 QLDPVNREEFIKILKHINDDFNVTVVFVEHQLE 194
Cdd:COG2401  166 HLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 14-164 3.95e-12

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 65.28  E-value: 3.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEiENDDTKIGFVF-----QNP-EDQLv 87
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAA---GTIKLDGG-DIDDPDVAEAChylghRNAmKPAL- 88

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994  88 mnTVWHEIAFGLKNKGislkQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLD 164
Cdd:PRK13539  89 --TVAENLEFWAAFLG----GEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALD 159
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 274-466 4.73e-12

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: 66.22  E-value: 4.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDL--NFG--HddiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV------------DCQG----EIS 333
Cdd:COG0411    1 SDPLLEVRGLtkRFGglV---AVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYrptsgrilfdgrDITGlpphRIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 334 KVG---------------CVD--RIGYLPQDPTTLFVAD-KVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQ 395
Cdd:COG0411   78 RLGiartfqnprlfpeltVLEnvLVAAHARLGRGLLAALlRLPRARREEREARERAEELLERVGLADRADEPAGNLSYGQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 396 KQLV----ALA---KILltkpqllLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:COG0411  158 QRRLeiarALAtepKLL-------LLDEPAAGLNPEETEELAELIRRLRDErgITILLIEHDMDLVMGLADRIVVLDFGR 230
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 276-467 4.86e-12

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: 65.12  E-value: 4.86e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 276 ILMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIsKVGCVD-------RIGYLPQD 347
Cdd:cd03292    1 IEFINVTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELpTSGTI-RVNGQDvsdlrgrAIPYLRRK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 PTTLF----------VADKVIDDLLLVD----DVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLL 413
Cdd:cd03292   80 IGVVFqdfrllpdrnVYENVAFALEVTGvpprEIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03292  160 ADEPTGNLDPDTTWEIMNLLKKINKAgTTVVVATHAKELVDTTRHRVIALERGKL 214
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 20-211 5.47e-12

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 67.77  E-value: 5.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  20 NISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRPKgdIDGVIILD-EEIENDDTKI----GFVFQnPEDQ--------- 85
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLY-GLRPA--RGGRIMLNgKEINALSTAQrlarGLVYL-PEDRqssglylda 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  86 -LVMNT---VWHEIAFGLKNKGIS--LKQMKRRIGEIVNYfnlqsiINKETQSLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:PRK15439 357 pLAWNVcalTHNRRGFWIKPARENavLERYRRALNIKFNH------AEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEP 430

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 160 TAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK15439 431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
284-465 5.53e-12

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 65.50  E-value: 5.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 284 NFGHDDiVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG------------------EISK-VGCVDRIGYL 344
Cdd:PRK09493  10 HFGPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSgdlivdglkvndpkvderLIRQeAGMVFQQFYL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 PQDPTTL----FVADKVIDDLLLVDDVVAsvESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKG 420
Cdd:PRK09493  89 FPHLTALenvmFGPLRVRGASKEEAEKQA--RELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 421 IDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK09493 167 LDPELRHEVLKVMQDLAEEgMTMVIVTHEIGFAEKVASRLIFIDKG 212
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 115-466 5.74e-12

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 67.89  E-value: 5.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 115 EIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNReefIKILKHIND--DFNVTVVFVEHQ 192
Cdd:COG1245  195 ELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDIYQR---LNVARLIRElaEEGKYVLVVEHD 271

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 193 LeGLLDVANRLIVMDEGKividneikmavdemltkkifveslPN-YVRVSSlcdklclsIKEAREALVNF-------EN- 263
Cdd:COG1245  272 L-AILDYLADYVHILYGE------------------------PGvYGVVSK--------PKSVRVGINQYldgylpeENv 318

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 264 --------FDIK-IMDEIDNRILMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEIS 333
Cdd:COG1245  319 rirdepieFEVHaPRREKEEETLVEYPDLTKSYGGFSLEVEGGEIREGEVLGIVGPNGIGKTTFAKILAGvLKPDEGEVD 398

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 334 KVgcvDRIGYLPQ------DPTTLFVADKVIDDLLLVDDVVASVeshLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLT 407
Cdd:COG1245  399 ED---LKISYKPQyispdyDGTVEEFLRSANTDDFGSSYYKTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSR 472

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 408 KPQLLLLDEPTKGIDASSKEFLANLIRGL--SKHMTIVVASHDLEFVAKISDRVaMIFNGQ 466
Cdd:COG1245  473 DADLYLLDEPSAHLDVEQRLAVAKAIRRFaeNRGKTAMVVDHDIYLIDYISDRL-MVFEGE 532
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
4-212 7.44e-12

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 65.56  E-value: 7.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVII---LDEEIENDDTKIGF 77
Cdd:PRK11831  10 MRGVSFTR-GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPdHGEIlfDGENIpamSRSRLYTVRKRMSM 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQNPEDQLVMNtVWHEIAFGLKNKGI-------SLKQMKRrigEIVNyfnLQSIINKETQSLSNGQKQLVALASVMVMN 150
Cdd:PRK11831  89 LFQSGALFTDMN-VFDNVAYPLREHTQlpapllhSTVMMKL---EAVG---LRGAAKLMPSELSGGMARRAALARAIALE 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 151 PKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11831 162 PDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIV 223
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 291-467 9.69e-12

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: 63.22  E-value: 9.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DcQGEISkvgcVDRIGYLPQDPttlfvadkviddlllvddvv 368
Cdd:cd03216   15 ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYkpD-SGEIL----VDGKEVSFASP-------------------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 369 asveSHLDNFGIidlkdAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL-SKHMTIVVASH 447
Cdd:cd03216   70 ----RDARRAGI-----AMVYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLrAQGVAVIFISH 140

                        170       180
                 ....*....|....*....|
gi 169293994 448 DLEFVAKISDRVAMIFNGQM 467
Cdd:cd03216  141 RLDEVFEIADRVTVLRDGRV 160
cbiO PRK13645
energy-coupling factor transporter ATPase;
292-479 1.09e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 65.41  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ------------GEISKVGCVDR----IGYLPQDPTTLFVAD 355
Cdd:PRK13645  27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISEtgqtivgdyaipANLKKIKEVKRlrkeIGLVFQFPEYQLFQE 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 356 KV--------IDDLLLVDDVVASVESHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSK 426
Cdd:PRK13645 107 TIekdiafgpVNLGENKQEAYKKVPELLKLVQLPeDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGE 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 427 EFLANLIRGLSKHMT--IVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK13645 187 EDFINLFERLNKEYKkrIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 278-449 1.13e-11

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: 67.00  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  278 MKVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVG----------CVDRIGYL 344
Cdd:TIGR02868 335 LELRDLSAGYPGapPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPlQGEVTLDGvpvssldqdeVRRRVSVC 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  345 PQDPTtLFvaDKVIDDLLLVDDVVAS---VESHLDNFGIIDLKDAHPFDL-----------SSGQKQLVALAKILLTKPQ 410
Cdd:TIGR02868 415 AQDAH-LF--DTTVRENLRLARPDATdeeLWAALERVGLADWLRALPDGLdtvlgeggarlSGGERQRLALARALLADAP 491

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 169293994  411 LLLLDEPTKGIDA-SSKEFLANLIRGLSKhMTIVVASHDL 449
Cdd:TIGR02868 492 ILLLDEPTEHLDAeTADELLEDLLAALSG-RTVVLITHHL 530
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 287-466 1.35e-11

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 64.70  E-value: 1.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 287 HDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEIskvgcvdRIGYLP----QDPTTLFVAD------ 355
Cdd:PRK11247  23 GERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLeTPSAGEL-------LAGTAPlaeaREDTRLMFQDarllpw 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 356 -KVIDDLLLVDDVVASVESH--LDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:PRK11247  96 kKVIDNVGLGLKGQWRDAALqaLAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRIEMQDL 175

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169293994 433 IRGL--SKHMTIVVASHDL-EFVAkISDRVAMIFNGQ 466
Cdd:PRK11247 176 IESLwqQHGFTVLLVTHDVsEAVA-MADRVLLIEEGK 211
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
278-467 1.65e-11

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 64.65  E-value: 1.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGH-DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVG----------CVDRIGYLP 345
Cdd:PRK11231   3 LRTENLTVGYgTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQsGTVFLGDkpismlssrqLARRLALLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTT-----------------------LFVADKviddlllvddvvASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA 402
Cdd:PRK11231  83 QHHLTpegitvrelvaygrspwlslwgrLSAEDN------------ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 403 KILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLS-KHMTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNtQGKTVVTVLHDLNQASRYCDHLVVLANGHV 216
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 1-214 1.66e-11

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 64.41  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKdKKIINNISFEIKKGDFLVITGKSGCGKTTLLR----YFKPSlrpKGDIDgviILDEEIEndDTK-- 74
Cdd:PRK13548   2 MLEARNLSVRLGG-RTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRalsgELSPD---SGEVR---LNGRPLA--DWSpa 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 --------------IGFVFqnpedqlvmnTVwHEI-AFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQ 139
Cdd:PRK13548  73 elarrravlpqhssLSFPF----------TV-EEVvAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQ 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 140 LVALASVMV------MNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHqlegllDV------ANRLIVMD 207
Cdd:PRK13548 142 RVQLARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLH------DLnlaaryADRIVLLH 215


                 ....*..
gi 169293994 208 EGKIVID 214
Cdd:PRK13548 216 QGRLVAD 222
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 6-211 1.80e-11

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: 66.89  E-value: 1.80e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994     6 NFSFTYPKDKK-IINNISFEIKKGDFLVITGKSGCGKTTL-LRYFKPSLRPKGD--IDGVIILDEEIENDDTKIGFVFQN 81
Cdd:TIGR00957 1289 NYCLRYREDLDlVLRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINESAEGEiiIDGLNIAKIGLHDLRFKITIIPQD 1368

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    82 P---EDQLVMN----------TVWheiafglknKGISLKQMKRRIGEIVNYFNLQSIINKEtqSLSNGQKQLVALASVMV 148
Cdd:TIGR00957 1369 PvlfSGSLRMNldpfsqysdeEVW---------WALELAHLKTFVSALPDKLDHECAEGGE--NLSVGQRQLVCLARALL 1437

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994   149 MNPKVILLDEATAQLDpVNREEFIKilKHINDDF-NVTVVFVEHQLEGLLDVaNRLIVMDEGKI 211
Cdd:TIGR00957 1438 RKTKILVLDEATAAVD-LETDNLIQ--STIRTQFeDCTVLTIAHRLNTIMDY-TRVIVLDKGEV 1497
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 282-479 1.82e-11

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: 65.51  E-value: 1.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 282 DLNFGHD--DIVLkDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISkvgcVD------------------R 340
Cdd:COG4148    4 EVDFRLRrgGFTL-DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERpDSGRIR----LGgevlqdsargiflpphrrR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 341 IGYLPQDPtTLF----VAD------KVIddllLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA-------K 403
Cdd:COG4148   79 IGYVFQEA-RLFphlsVRGnllygrKRA----PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGrallsspR 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 404 IlltkpqlLLLDEPTKGIDASSKE----FLANLIRGLSkhMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG4148  154 L-------LLMDEPLAALDLARKAeilpYLERLRDELD--IPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSR 224
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 14-452 1.88e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 66.51  E-value: 1.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdIDGVIILDE---EIENDdTKIGFVFQNPEDQlVMNT 90
Cdd:PRK11147  15 DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKI----------LNGEVLLDDgriIYEQD-LIVARLQQDPPRN-VEGT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEIAFGLKNKGISLKQMKR------------------RIGEIVNYFN---LQSIIN-----------KETQSLSNGQK 138
Cdd:PRK11147  83 VYDFVAEGIEEQAEYLKRYHDishlvetdpseknlnelaKLQEQLDHHNlwqLENRINevlaqlgldpdAALSSLSGGWL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 139 QLVALASVMVMNPKVILLDEATAQLDpVNR----EEFIKilkhindDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVid 214
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLD-IETiewlEGFLK-------TFQGSIIFISHDRSFIRNMATRIVDLDRGKLV-- 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 215 neikmavdemltkkifveSLP-NYvrvsslcDKLCLSIKEA-R-EALVNFEnFDIKIMDE-------IDNR--------- 275
Cdd:PRK11147 233 ------------------SYPgNY-------DQYLLEKEEAlRvEELQNAE-FDRKLAQEevwirqgIKARrtrnegrvr 286

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 276 -------------------------------ILMKVRDLNFGHDDIVL-KDLEIDILENEILSIVGANGSGKSSFLRCLA 323
Cdd:PRK11147 287 alkalrrerserrevmgtakmqveeasrsgkIVFEMENVNYQIDGKQLvKDFSAQVQRGDKIALIGPNGCGKTTLLKLML 366

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 324 GLVDCQ-GEIsKVGCVDRIGYLPQ-----DPTTLfVADKVIDDLLLVDDVVAS--VESHLDNFGIidlkdaHPFD----- 390
Cdd:PRK11147 367 GQLQADsGRI-HCGTKLEVAYFDQhraelDPEKT-VMDNLAEGKQEVMVNGRPrhVLGYLQDFLF------HPKRamtpv 438

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 391 --LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKhmTIVVASHDLEFV 452
Cdd:PRK11147 439 kaLSGGERNRLLLARLFLKPSNLLILDEPTNDLDVETLELLEELLDSYQG--TVLLVSHDRQFV 500
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 2-480 1.90e-11

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: 66.11  E-value: 1.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    2 YKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpslrpkG---DIDGVIILDEEIenddtKIGFV 78
Cdd:TIGR03719   5 YTMNRVSKVVPPKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMA------GvdkDFNGEARPQPGI-----KVGYL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   79 FQNPedQLVMN-TVWHEIAFGLKnkgiSLKQMKRRIGEIVNYFN---------------LQSII------NKETQ----- 131
Cdd:TIGR03719  74 PQEP--QLDPTkTVRENVEEGVA----EIKDALDRFNEISAKYAepdadfdklaaeqaeLQEIIdaadawDLDSQleiam 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  132 -------------SLSNGQKQLVALASVMVMNPKVILLDEATAQLDPvnreEFIKILKHINDDFNVTVVFVEHQLEGLLD 198
Cdd:TIGR03719 148 dalrcppwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDA----ESVAWLERHLQEYPGTVVAVTHDRYFLDN 223

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  199 VANRLIVMDEGKIV----------------IDNEIKMAVDEMLTKKIFVEslpnYVRVSSlcdklclsikEAREA----- 257
Cdd:TIGR03719 224 VAGWILELDRGRGIpwegnysswleqkqkrLEQEEKEESARQKTLKRELE----WVRQSP----------KGRQAkskar 289

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  258 LVNFENFDIKIMDEIDNR-------------ILMKVRDLNFGHDDIVL-KDLEIDILENEILSIVGANGSGKSSFLRCLA 323
Cdd:TIGR03719 290 LARYEELLSQEFQKRNETaeiyippgprlgdKVIEAENLTKAFGDKLLiDDLSFKLPPGGIVGVIGPNGAGKSTLFRMIT 369

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  324 GLV-DCQGEIsKVGCVDRIGYLPQ-----DPT-TLF--VAD--KVIDDLLLVDDVVASVESHldNFGIIDlKDAHPFDLS 392
Cdd:TIGR03719 370 GQEqPDSGTI-EIGETVKLAYVDQsrdalDPNkTVWeeISGglDIIKLGKREIPSRAYVGRF--NFKGSD-QQKKVGQLS 445

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  393 SGQKQLVALAKILLTKPQLLLLDEPTKGIDAsskEFLANLIRGLSKHM-TIVVASHDLEFVakisDRVA---MIFNGqme 468
Cdd:TIGR03719 446 GGERNRVHLAKTLKSGGNVLLLDEPTNDLDV---ETLRALEEALLNFAgCAVVISHDRWFL----DRIAthiLAFEG--- 515

                         570
                  ....*....|..
gi 169293994  469 svDSTREFFSHN 480
Cdd:TIGR03719 516 --DSHVEWFEGN 525
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 3-212 2.01e-11

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 65.15  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDK---KIINNISFEIKKGDFLVITGKSGCGKTTllryfkPSLRPKGDID--GVIILDE-EIENDDTK-- 74
Cdd:PRK11022   5 NVDKLSVHFGDESapfRAVDRISYSVKQGEVVGIVGESGSGKSV------SSLAIMGLIDypGRVMAEKlEFNGQDLQri 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 ------------IGFVFQNPEDQLvmN---TVWHEIAFGLK-NKGISLKQMKRRIGEIVNYFNL---QSIINKETQSLSN 135
Cdd:PRK11022  79 sekerrnlvgaeVAMIFQDPMTSL--NpcyTVGFQIMEAIKvHQGGNKKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 136 GQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK11022 157 GMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVV 233
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-215 2.21e-11

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 63.74  E-value: 2.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYPKdKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFkpSLRPKGDIDGVIILDEEIENDDTK------ 74
Cdd:PRK11614   5 MLSFDKVSAHYGK-IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTL--CGDPRATSGRIVFDGKDITDWQTAkimrea 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 IGFVfqnPEDQLVMN--TVWHEIAFGlknkGI--SLKQMKRRIGEIVNYF-NLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:PRK11614  82 VAIV---PEGRRVFSrmTVEENLAMG----GFfaERDQFQERIKWVYELFpRLHERRIQRAGTMSGGEQQMLAIGRALMS 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDN 215
Cdd:PRK11614 155 QPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLED 219
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 285-482 2.36e-11

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 65.09  E-value: 2.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 285 FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEI-------SKVGCVDR-IGYLPQDPTtLF--- 352
Cdd:COG3839   13 YG-GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPtSGEIliggrdvTDLPPKDRnIAMVFQSYA-LYphm 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 -VAD---------KV----IDdlllvddvvASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALA-------KILltkpql 411
Cdd:COG3839   91 tVYEniafplklrKVpkaeID---------RRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGralvrepKVF------ 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 412 lLLDEPTKGIDASSKE----FLANLIRGLSkhMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH--NLF 482
Cdd:COG3839  156 -LLDEPLSNLDAKLRVemraEIKRLHRRLG--TTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRpaNLF 229
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 303-447 2.43e-11

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: 62.90  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 303 EILSIVGANGSGKSSFLRCLAGL--------------VDCQGEISKVGCVdRIGYLPQDPTTLFVADKVidDLLLVDDVV 368
Cdd:cd03231   27 EALQVTGPNGSGKTTLLRILAGLspplagrvllnggpLDFQRDSIARGLL-YLGHAPGIKTTLSVLENL--RFWHADHSD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 369 ASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRG-LSKHMTIVVASH 447
Cdd:cd03231  104 EQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMAGhCARGGMVVLTTH 183
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
291-479 2.48e-11

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 63.83  E-value: 2.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGcvDRIGYLPQDPTTLFVADK------------- 356
Cdd:PRK10619  20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKpSEGSIVVNG--QTINLVRDKDGQLKVADKnqlrllrtrltmv 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 --------------------VIDDLLLVDDVVASVESHLDNFGIID-LKDAHPFDLSSGQKQLVALAKILLTKPQLLLLD 415
Cdd:PRK10619  98 fqhfnlwshmtvlenvmeapIQVLGLSKQEARERAVKYLAKVGIDErAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 416 EPTKGIDAsskEFLANLIRGLSK----HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK10619 178 EPTSALDP---ELVGEVLRIMQQlaeeGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGN 242
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
286-481 2.52e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 64.13  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 286 GHddIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCVDR-------IGYLPQDPTT-----LF 352
Cdd:PRK15056  19 GH--TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRlASGKISILGQPTRqalqknlVAYVPQSEEVdwsfpVL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKVID--------DLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS 424
Cdd:PRK15056  97 VEDVVMMgryghmgwLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVK 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 425 SKEFLANLIRGL-SKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSHNL 481
Cdd:PRK15056 177 TEARIISLLRELrDEGKTMLVSTHNLGSVTEFCDYTVMVKGTVLASGPTETTFTAENL 234
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 278-477 2.55e-11

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 64.09  E-value: 2.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGH-DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD------CQGEISKVGC------VD----- 339
Cdd:PRK14267   5 IETVNLRVYYgSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLElneearVEGEVRLFGRniyspdVDpievr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 -RIGYLPQDPTT---LFVADKVIDDLLLVDDVVAS------VESHLDNFGIID-----LKDaHPFDLSSGQKQLVALAKI 404
Cdd:PRK14267  85 rEVGMVFQYPNPfphLTIYDNVAIGVKLNGLVKSKkelderVEWALKKAALWDevkdrLND-YPSNLSGGQRQRLVIARA 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 405 LLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFF 477
Cdd:PRK14267 164 LAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVF 236
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-212 2.66e-11

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 65.81  E-value: 2.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSftypkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpSL---RPKgdIDGVIILD-EEIENDDTK---- 74
Cdd:COG1129  258 EVEGLS-----VGGVVRDVSFSVRAGEILGIAGLVGAGRTELAR----ALfgaDPA--DSGEIRLDgKPVRIRSPRdair 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 --IGFVfqnPEDQ----LVMN-TVWHEIAFG----LKNKG-ISLKQMKRRIGEIVNYFNLQ-SIINKETQSLSNGQKQLV 141
Cdd:COG1129  327 agIAYV---PEDRkgegLVLDlSIRENITLAsldrLSRGGlLDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKV 403

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 142 ALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG1129  404 VLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIV 473
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 291-465 2.73e-11

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: 63.16  E-value: 2.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD----------RIGYLPqDPTTLF---VADKV 357
Cdd:cd03266   20 AVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDvvkepaearrRLGFVS-DSTGLYdrlTAREN 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 IDDL-----LLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:cd03266   99 LEYFaglygLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREF 178

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169293994 433 IRGL-SKHMTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:cd03266  179 IRQLrALGKCILFSTHIMQEVERLCDRVVVLHRG 212
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 9-225 3.01e-11

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 64.73  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   9 FTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYF----KPSlrpkgdiDG-VIILDEEIENDDTK--------I 75
Cdd:PRK15079  28 WQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIiglvKAT-------DGeVAWLGKDLLGMKDDewravrsdI 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPEDQLvmN---TVWHEIAFGLK--NKGISLKQMKRRIGEIVNYFNL-QSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:PRK15079 101 QMIFQDPLASL--NprmTIGEIIAEPLRtyHPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALIL 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGkividNEIKMAVDEML 225
Cdd:PRK15079 179 EPKLIICDEPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLG-----HAVELGTYDEV 249
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
291-479 3.44e-11

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 64.33  E-value: 3.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL--VDcQGEIsKVGCVD--------------RIGYLPQDpttlF-- 352
Cdd:COG1135   20 ALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLerPT-SGSV-LVDGVDltalserelraarrKIGMIFQH----Fnl 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 -----VADKV-------------IDdlllvddvvASVESHLDNFGIIDLKDAHPFDLSSGQKQLV----ALA---KILLt 407
Cdd:COG1135   94 lssrtVAENValpleiagvpkaeIR---------KRVAELLELVGLSDKADAYPSQLSGGQKQRVgiarALAnnpKVLL- 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 408 kpqlllLDEPTKGID-ASSKEFLAnLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG1135  164 ------CDEATSALDpETTRSILD-LLKDINRELglTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFAN 231
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 283-459 3.59e-11

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 63.59  E-value: 3.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 283 LNFGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCVdRIGYLPQ----DPTTLFVADKV 357
Cdd:PRK09544  12 VSFG-QRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVApDEGVIKRNGKL-RIGYVPQklylDTTLPLTVNRF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 IddLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLS 437
Cdd:PRK09544  90 L--RLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLR 167

                        170       180
                 ....*....|....*....|....
gi 169293994 438 K--HMTIVVASHDLEFVAKISDRV 459
Cdd:PRK09544 168 RelDCAVLMVSHDLHLVMAKTDEV 191
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 288-482 3.78e-11

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: 63.02  E-value: 3.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISkVGCVDRIGYLP---------QDpTTLF----V 353
Cdd:cd03300   12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETpTSGEIL-LDGKDITNLPPhkrpvntvfQN-YALFphltV 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 354 ADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFL 429
Cdd:cd03300   90 FENIAfglrLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDLKLRKDM 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 430 ANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH--NLF 482
Cdd:cd03300  170 QLELKRLQKElgITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEpaNRF 226
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
14-224 3.86e-11

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 64.06  E-value: 3.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPkgDIDGVIILDEEI----ENDDTKIGFVFQ----NPEDQ 85
Cdd:PRK13537  19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHP--DAGSISLCGEPVpsraRHARQRVGVVPQfdnlDPDFT 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  86 LVMNTVWHEIAFGLknkgiSLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDP 165
Cdd:PRK13537  97 VRENLLVFGRYFGL-----SAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDP 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 166 VNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEG-KI-------VIDNEIKMAVDEM 224
Cdd:PRK13537 172 QARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGrKIaegaphaLIESEIGCDVIEI 237
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 289-447 4.43e-11

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: 61.99  E-value: 4.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  289 DIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGEISKVGCVDR------IGYLPQDPTTLFVAD 355
Cdd:TIGR01189  13 RMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLlrpdsgeVRWNGTPLAEQRDEPhenilyLGHLPGLKPELSALE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  356 KVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRG 435
Cdd:TIGR01189  93 NLHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKAGVALLAGLLRA 172

                         170
                  ....*....|...
gi 169293994  436 -LSKHMTIVVASH 447
Cdd:TIGR01189 173 hLARGGIVLLTTH 185
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
8-212 5.62e-11

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 64.73  E-value: 5.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   8 SFTYPK-DKKIINNISFEIKKGDFLVITGKSGCGKTTLL----RYFKPSlrpKGDI--DGVIILDEEIENDDTKIGFVFQ 80
Cdd:PRK10789 320 QFTYPQtDHPALENVNFTLKPGQMLGICGPTGSGKSTLLsliqRHFDVS---EGDIrfHDIPLTKLQLDSWRSRLAVVSQ 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 NPedQLVMNTVWHEIAFGLKNKgislkqMKRRIGEIVNYFNLQSIINKETQS-----------LSNGQKQLVALASVMVM 149
Cdd:PRK10789 397 TP--FLFSDTVANNIALGRPDA------TQQEIEHVARLASVHDDILRLPQGydtevgergvmLSGGQKQRISIARALLL 468

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDdfNVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PRK10789 469 NAEILILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIA 528
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 277-478 5.94e-11

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 63.28  E-value: 5.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGH--DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGE-ISK--VGCVDR-IGY 343
Cdd:PRK13652   3 LIETRDLCYSYsgSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGIlkptsgsVLIRGEpITKenIREVRKfVGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 344 LPQDPTTLFVADKV--------IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLD 415
Cdd:PRK13652  83 VFQNPDDQIFSPTVeqdiafgpINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 416 EPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13652 163 EPTAGLDPQGVKELIDFLNDLPETygMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFL 227
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 278-457 6.55e-11

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 62.28  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDL--NFG--HDDI---VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDRIgyLPQDPTt 350
Cdd:COG2401   25 ERVAIVleAFGveLRVVeryVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQ--FGREAS- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 lfvadkVIDDLLLVDDVVASVEShLDNFGIID--LKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEF 428
Cdd:COG2401  102 ------LIDAIGRKGDFKDAVEL-LNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKR 174

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169293994 429 LANLIRGLSKH--MTIVVASHDLEFVAKISD 457
Cdd:COG2401  175 VARNLQKLARRagITLVVATHHYDVIDDLQP 205
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 279-483 7.39e-11

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 63.20  E-value: 7.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEIS------KVGCVDRIGYLPQDP- 348
Cdd:COG4152    3 ELKGLTkrFG-DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPdSGEVLwdgeplDPEDRRRIGYLPEERg 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 349 ---------TTLFVA-----DKviddlllvDDVVASVESHLDNFGIIDLKDAHPFDLSSG--QK-QLVA----------L 401
Cdd:COG4152   82 lypkmkvgeQLVYLArlkglSK--------AEAKRRADEWLERLGLGDRANKKVEELSKGnqQKvQLIAallhdpelliL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 402 akilltkpqllllDEPTKGIDASSKEFLANLIRGL-SKHMTIVVASHDLEFVAKISDRVAMIFNGQME---SVDSTREFF 477
Cdd:COG4152  154 -------------DEPFSGLDPVNVELLKDVIRELaAKGTTVIFSSHQMELVEELCDRIVIINKGRKVlsgSVDEIRRQF 220


                 ....*.
gi 169293994 478 SHNLFY 483
Cdd:COG4152  221 GRNTLR 226
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 278-466 7.44e-11

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: 61.72  E-value: 7.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHDD------IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGcvdRIGYLPQDP-- 348
Cdd:cd03250    1 ISVEDASFTWDSgeqetsFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKlSGSVSVPG---SIAYVSQEPwi 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 349 --TT-----LFVA-------DKVIDDlllvddvvASVESHLDNF-----------GIidlkdahpfDLSSGQKQLVALAK 403
Cdd:cd03250   78 qnGTireniLFGKpfdeeryEKVIKA--------CALEPDLEILpdgdlteigekGI---------NLSGGQKQRISLAR 140

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 404 ILLTKPQLLLLDEPTKGIDAS-SKEFLANLIRG-LSKHMTIVVASHDLEFVAKiSDRVAMIFNGQ 466
Cdd:cd03250  141 AVYSDADIYLLDDPLSAVDAHvGRHIFENCILGlLLNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 291-471 8.96e-11

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: 61.50  E-value: 8.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI-------SKVGCVDR-IGYLPQD----P-TTLF--VA 354
Cdd:cd03301   15 ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEpTSGRIyiggrdvTDLPPKDRdIAMVFQNyalyPhMTVYdnIA 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 355 DKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIR 434
Cdd:cd03301   95 FGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRVQMRAELK 174

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 169293994 435 GLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVD 471
Cdd:cd03301  175 RLQQRLgtTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
cbiO PRK13644
energy-coupling factor transporter ATPase;
292-506 8.97e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 62.70  E-value: 8.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-----------GEISKVGCVDRI-GYLPQDPTTLFVADKVID 359
Cdd:PRK13644  18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQkgkvlvsgidtGDFSKLQGIRKLvGIVFQNPETQFVGRTVEE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 360 DLLLV--------DDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLAN 431
Cdd:PRK13644  98 DLAFGpenlclppIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLE 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 432 LIRGL-SKHMTIVVASHDLEFVaKISDRVAMIFNGqmesvdstreffshnlfytttinKIMRENNPEVIL----LEDLGL 506
Cdd:PRK13644 178 RIKKLhEKGKTIVYITHNLEEL-HDADRIIVMDRG-----------------------KIVLEGEPENVLsdvsLQTLGL 233
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 292-475 1.11e-10

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: 61.23  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD----------RIGYLPQDPT---------TLF 352
Cdd:cd03265   16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDvvreprevrrRIGIVFQDLSvddeltgweNLY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKVIDDLLLVDDVvaSVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:cd03265   96 IHARLYGVPGAERRE--RIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 169293994 433 IRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:cd03265  174 IEKLKEEfgMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 2-206 1.43e-10

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 63.89  E-value: 1.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    2 YKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIdgvIILDEEIEND------DTK 74
Cdd:PTZ00265  385 FKNVRFHYDTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPtEGDI---IINDSHNLKDinlkwwRSK 461

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   75 IGFVFQNPedQLVMNTVWHEIAFGL-----------------------KNKGIS--------------------LKQMKR 111
Cdd:PTZ00265  462 IGVVSQDP--LLFSNSIKNNIKYSLyslkdlealsnyynedgndsqenKNKRNScrakcagdlndmsnttdsneLIEMRK 539

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  112 RI-----GEIVNYFN--------------LQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDpvNREEFI 172
Cdd:PTZ00265  540 NYqtikdSEVVDVSKkvlihdfvsalpdkYETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD--NKSEYL 617

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 169293994  173 --KILKHINDDFNVTVVFVEHQLEgLLDVANRLIVM 206
Cdd:PTZ00265  618 vqKTINNLKGNENRITIIIAHRLS-TIRYANTIFVL 652
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 17-165 1.48e-10

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: 60.45  E-value: 1.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   17 IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEEIENDdtkigfvfQNPEDQLVMNTVWHeiA 96
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDS---GEVRWNGTPLAE--------QRDEPHENILYLGH--L 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994   97 FGLKNKGISLKQM----------KRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDP 165
Cdd:TIGR01189  82 PGLKPELSALENLhfwaaihggaQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 273-467 1.49e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 61.93  E-value: 1.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 273 DNRILMKVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCV---------- 338
Cdd:PRK13632   3 NKSVMIKVENVSFSYPNsenNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQsGEIKIDGITiskenlkeir 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 339 DRIGYLPQDPTTLFVADKVID--------DLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQ 410
Cdd:PRK13632  83 KKIGIIFQNPDNQFIGATVEDdiafglenKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 411 LLLLDEPTKGIDASSKEFLANLIRGLSKHM--TIVVASHDLEFVAKiSDRVAMIFNGQM 467
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRkkTLISITHDMDEAIL-ADKVIVFSEGKL 220
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 5-211 1.52e-10

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 63.45  E-value: 1.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDI--DGVIILDEEIENDDTKIGFVF-- 79
Cdd:PRK10522 326 RNVTFAYQDNGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPqSGEIllDGKPVTAEQPEDYRKLFSAVFtd 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 ------------QNPEDQLVMNtvWHEIaFGLKNKgISLKQmkrriGEIVNYfnlqsiinketqSLSNGQKQLVALASVM 147
Cdd:PRK10522 406 fhlfdqllgpegKPANPALVEK--WLER-LKMAHK-LELED-----GRISNL------------KLSKGQKKRLALLLAL 464

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQlEGLLDVANRLIVMDEGKI 211
Cdd:PRK10522 465 AEERDILLLDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHD-DHYFIHADRLLEMRNGQL 527
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 279-465 1.64e-10

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: 61.09  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 279 KVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG-----------EISKVGCVDRIGYLP 345
Cdd:cd03254    4 EFENVNFSYDEkkPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKgqilidgidirDISRKSLRSMIGVVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTtLF---VADKVI---DDLLLVDDVVASVESHLDNFgIIDLKDAHPF-------DLSSGQKQLVALAKILLTKPQLL 412
Cdd:cd03254   84 QDTF-LFsgtIMENIRlgrPNATDEEVIEAAKEAGAHDF-IMKLPNGYDTvlgenggNLSQGERQLLAIARAMLRDPKIL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 413 LLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVaKISDRVAMIFNG 465
Cdd:cd03254  162 ILDEATSNIDTETEKLIQEALEKLMKGRTSIIIAHRLSTI-KNADKILVLDDG 213
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 269-479 1.73e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 61.69  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 269 MDEIDNRILMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI-SKVGCVD------ 339
Cdd:PRK13648   1 MEDKNSIIVFKNVSFQYQSDAsFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKsGEIfYNNQAITddnfek 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 ---RIGYLPQDPTTLFVADKVIDDLLLVDDVVA--------SVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTK 408
Cdd:PRK13648  81 lrkHIGIVFQNPDNQFVGSIVKYDVAFGLENHAvpydemhrRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALN 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 409 PQLLLLDEPTKGIDASSKEFLANLIRGL--SKHMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK13648 161 PSVIILDEATSMLDPDARQNLLDLVRKVksEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
280-466 2.01e-10

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 63.26  E-value: 2.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIsKVGCVD-----------RIGYLP 345
Cdd:COG1132  342 FENVSFSYPGdrPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTsGRI-LIDGVDirdltleslrrQIGVVP 420

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTtLF---VAD------------KVIDdlllvddvvASVESHLDNFgIIDLKDAhpFD---------LSSGQKQLVAL 401
Cdd:COG1132  421 QDTF-LFsgtIREnirygrpdatdeEVEE---------AAKAAQAHEF-IEALPDG--YDtvvgergvnLSGGQRQRIAI 487

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 402 AK---------IlltkpqlllLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQ 466
Cdd:COG1132  488 ARallkdppilI---------LDEATSALDTETEALIQEALERLMKGRTTIVIAHRLSTIRN-ADRILVLDDGR 551
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 13-211 2.27e-10

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 60.81  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  13 KDKKIINNISFEIKKGDFLVITGKSGCGKTTLlryF-------KPSlrpkgdiDGVIILDEEienDDTK----------I 75
Cdd:COG1137   14 GKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTT---FymivglvKPD-------SGRIFLDGE---DITHlpmhkrarlgI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GF------VFQNpedqLvmnTVWHEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVM 149
Cdd:COG1137   81 GYlpqeasIFRK----L---TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALAT 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 150 NPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:COG1137  154 NPKFILLDEPFAGVDPIAVADIQKIIRHLKER-GIGVLITDHNVRETLGICDRAYIISEGKV 214
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 279-468 2.43e-10

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


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 60.42  E-value: 2.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  279 KVRDLN--FGHDDI---VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ--------------GEISKVGCVD 339
Cdd:TIGR02982   3 SIRNLNhyYGHGSLrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQegslkvlgqelhgaSKKQLVQLRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  340 RIGYLPQDP---TTLFVADKV-----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQL 411
Cdd:TIGR02982  83 RIGYIFQAHnllGFLTARQNVqmaleLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPKL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994  412 LLLDEPTKGIDASSKEFLANLIRGLSKHM--TIVVASHDlEFVAKISDRVAmifngQME 468
Cdd:TIGR02982 163 VLADEPTAALDSKSGRDVVELMQKLAKEQgcTILMVTHD-NRILDVADRIL-----QME 215
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
16-459 2.50e-10

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 62.62  E-value: 2.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILD-EEIENDDTK------IGFVFQnpEDQLVM 88
Cdd:PRK11288  18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDA---GSILIDgQEMRFASTTaalaagVAIIYQ--ELHLVP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  89 N-TVWHEIAFG-LKNKG--ISLKQMKRRIGEIvnyfnLQSI---INKETQ--SLSNGQKQLVALASVMVMNPKVILLDEA 159
Cdd:PRK11288  93 EmTVAENLYLGqLPHKGgiVNRRLLNYEAREQ-----LEHLgvdIDPDTPlkYLSIGQRQMVEIAKALARNARVIAFDEP 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 160 TAQLDPVNREEFIKILKHINDDFNVtVVFVEHQLEGLLDVANRLIVMDEGKividneikmavdemltkkiFVESLPNYVR 239
Cdd:PRK11288 168 TSSLSAREIEQLFRVIRELRAEGRV-ILYVSHRMEEIFALCDAITVFKDGR-------------------YVATFDDMAQ 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 240 VSslcdklclsikeaREALVnfenfdiKIM--DEIDNRILMKVRDLnfGHDDIVLKDLE---------IDILENEILSIV 308
Cdd:PRK11288 228 VD-------------RDQLV-------QAMvgREIGDIYGYRPRPL--GEVRLRLDGLKgpglrepisFSVRAGEIVGLF 285

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 309 GANGSGKSSFLRCLAGLVDCQG----------EISKVGCVDRIGYL--PQDPTtlfvADKVIDDlllvddvvASVE---- 372
Cdd:PRK11288 286 GLVGAGRSELMKLLYGATRRTAgqvyldgkpiDIRSPRDAIRAGIMlcPEDRK----AEGIIPV--------HSVAdnin 353

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 373 -----SHLDNFGIID----------------LKDAHP----FDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKE 427
Cdd:PRK11288 354 isarrHHLRAGCLINnrweaenadrfirslnIKTPSReqliMNLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKH 433

                        490       500       510
                 ....*....|....*....|....*....|...
gi 169293994 428 FLANLIRGLSKH-MTIVVASHDLEFVAKISDRV 459
Cdd:PRK11288 434 EIYNVIYELAAQgVAVLFVSSDLPEVLGVADRI 466
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 3-209 2.65e-10

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: 60.42  E-value: 2.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIDGVIILDEEIENDDTK------I 75
Cdd:cd03290    2 QVTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTlEGKVHWSNKNESEPSFEATRsrnrysV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPedQLVMNTVWHEIAFGLKNKgislkqmKRRIGEIVNYFNLQSIIN-----KETQ------SLSNGQKQLVALA 144
Cdd:cd03290   82 AYAAQKP--WLLNATVEENITFGSPFN-------KQRYKAVTDACSLQPDIDllpfgDQTEigergiNLSGGQRQRICVA 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 145 SVMVMNPKVILLDEATAQLDPVNREEFIK--ILKHINDDfNVTVVFVEHQLEGLLDvANRLIVMDEG 209
Cdd:cd03290  153 RALYQNTNIVFLDDPFSALDIHLSDHLMQegILKFLQDD-KRTLVLVTHKLQYLPH-ADWIIAMKDG 217
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 291-467 3.30e-10

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: 62.37  E-value: 3.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGC----VDR------IGYLPQDpTTLF---VADK 356
Cdd:TIGR01842 333 TLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPtSGSVRLDGAdlkqWDRetfgkhIGYLPQD-VELFpgtVAEN 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  357 ViddlllvddvvASVESHLDNFGIID---LKDAHP--------FD---------LSSGQKQLVALAKILLTKPQLLLLDE 416
Cdd:TIGR01842 412 I-----------ARFGENADPEKIIEaakLAGVHElilrlpdgYDtvigpggatLSGGQRQRIALARALYGDPKLVVLDE 480

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169293994  417 PTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKIsDRVAMIFNGQM 467
Cdd:TIGR01842 481 PNSNLDEEGEQALANAIKALKARgITVVVITHRPSLLGCV-DKILVLQDGRI 531
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
13-235 4.17e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 62.11  E-value: 4.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  13 KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR-YFKPSLRPKGDIdgvIILDEEIEN----DDTK--IGFVFQNPEDq 85
Cdd:PRK09700 274 RDRKKVRDISFSVCRGEILGFAGLVGSGRTELMNcLFGVDKRAGGEI---RLNGKDISPrsplDAVKkgMAYITESRRD- 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  86 lvmNTVWHE--------IAFGLKNK------GISLKQMKRRIGEivNYFNLQSI----INKETQSLSNGQKQLVALASVM 147
Cdd:PRK09700 350 ---NGFFPNfsiaqnmaISRSLKDGgykgamGLFHEVDEQRTAE--NQRELLALkchsVNQNITELSGGNQQKVLISKWL 424

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 148 VMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIvidNEIKMAVDEMLTK 227
Cdd:PRK09700 425 CCCPEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRL---TQILTNRDDMSEE 500


                 ....*...
gi 169293994 228 KIFVESLP 235
Cdd:PRK09700 501 EIMAWALP 508
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 14-211 4.85e-10

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 61.40  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPkgDIDGVIILDEEIEN--------------DDTKIGFVF 79
Cdd:PRK09536  15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTP--TAGTVLVAGDDVEAlsaraasrrvasvpQDTSLSFEF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 QNpeDQLV-MNTVWHEIAFGLKNKG--ISLKQMKRRIGeiVNYFNLQSIinketQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK09536  93 DV--RQVVeMGRTPHRSRFDTWTETdrAAVERAMERTG--VAQFADRPV-----TSLSGGERQRVLLARALAQATPVLLL 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 157 DEATAQLDpVNREefIKILKHIND--DFNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK09536 164 DEPTASLD-INHQ--VRTLELVRRlvDDGKTAVAAIHDLDLAARYCDELVLLADGRV 217
cbiO PRK13642
energy-coupling factor transporter ATPase;
292-503 4.93e-10

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 60.49  E-value: 4.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKV-----------GCVDRIGYLPQDPTTLFVADKVIDD 360
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIdgelltaenvwNLRRKIGMVFQNPDNQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 361 LLLVDDVVA--------SVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:PRK13642 103 VAFGMENQGipreemikRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIMRV 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 433 IRGLSK--HMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTREFFSH---------NLFYTTTINKIMRENN---PEV 498
Cdd:PRK13642 183 IHEIKEkyQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATsedmveiglDVPFSSNLMKDLRKNGfdlPEK 261


                 ....*
gi 169293994 499 ILLED 503
Cdd:PRK13642 262 YLSED 266
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 277-332 5.21e-10

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: 59.61  E-value: 5.21e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 277 LMKVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEI 332
Cdd:COG0410    3 MLEVENLHAGYGGIhVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPrSGSI 60
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 292-479 5.39e-10

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 60.97  E-value: 5.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGL---------VDCQgEISKVGCVD------RIGYLPQDpttlF---- 352
Cdd:PRK11153  21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLerptsgrvlVDGQ-DLTALSEKElrkarrQIGMIFQH----Fnlls 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 ---VADKVI----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID--- 422
Cdd:PRK11153  96 srtVFDNVAlpleLAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSALDpat 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 423 -ASSKEFLANLIRGLskHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK11153 176 tRSILELLKDINREL--GLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSH 231
PLN03073 PLN03073
ABC transporter F family; Provisional
 3-467 5.84e-10

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 61.80  E-value: 5.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLrpkgdIDG------VIILDEEIENDDTKig 76
Cdd:PLN03073 179 HMENFSISV-GGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHA-----IDGipkncqILHVEQEVVGDDTT-- 250

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  77 fVFQ-------------NPEDQLV--MNTVWHEIAFGL----KNKGISLKQMKRRIGEIVNYFNL----------QSII- 126
Cdd:PLN03073 251 -ALQcvlntdiertqllEEEAQLVaqQRELEFETETGKgkgaNKDGVDKDAVSQRLEEIYKRLELidaytaearaASILa 329

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 127 ---------NKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDpvnrEEFIKILKHINDDFNVTVVFVEHQLEGLL 197
Cdd:PLN03073 330 glsftpemqVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD----LHAVLWLETYLLKWPKTFIVVSHAREFLN 405

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 198 DVANRLIVMDEGKIVI---DNEI-KMAVDEMLT--KKIFVESLPNYVRVSSLCDKLCLSIKEAR---------------E 256
Cdd:PLN03073 406 TVVTDILHLHGQKLVTykgDYDTfERTREEQLKnqQKAFESNERSRSHMQAFIDKFRYNAKRASlvqsrikaldrlghvD 485

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 257 ALVNFEN--FDIKIMDEIDNRILMKVRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGE 331
Cdd:PLN03073 486 AVVNDPDykFEFPTPDDRPGPPIISFSDASFGYPGgpLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGeLQPSSGT 565

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 332 ISKVGCVdRIGYLPQ---DPTTLFVADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHP-FDLSSGQKQLVALAKILLT 407
Cdd:PLN03073 566 VFRSAKV-RMAVFSQhhvDGLDLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPmYTLSGGQKSRVAFAKITFK 644

                        490       500       510       520       530       540
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 408 KPQLLLLDEPTKGIDASSKEflaNLIRGLSKHM-TIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PLN03073 645 KPHILLLDEPSNHLDLDAVE---ALIQGLVLFQgGVLMVSHDEHLISGSVDELWVVSEGKV 702
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 277-479 6.79e-10

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: 61.24  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLN--FGHDDI---VLKDLEIDILENEILSIVGANGSGKS----SFLRCLA-GLVDCQGEIS------------- 333
Cdd:COG4172    6 LLSVEDLSvaFGQGGGtveAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPdPAAHPSGSILfdgqdllglsere 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 334 --KV-GcvDRIGYLPQDPTT----LF-VADKVIddlllvddvvASVESH---------------LDNFGIIDLK---DAH 387
Cdd:COG4172   86 lrRIrG--NRIAMIFQEPMTslnpLHtIGKQIA----------EVLRLHrglsgaaararalelLERVGIPDPErrlDAY 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 388 PFDLSSGQKQLV----ALAK-----IlltkpqlllLDEPTKGIDAS-SKEFLAnLIRGLSK--HMTIVVASHDLEFVAKI 455
Cdd:COG4172  154 PHQLSGGQRQRVmiamALANepdllI---------ADEPTTALDVTvQAQILD-LLKDLQRelGMALLLITHDLGVVRRF 223

                        250       260
                 ....*....|....*....|....
gi 169293994 456 SDRVAMIFNGQMESVDSTREFFSH 479
Cdd:COG4172  224 ADRVAVMRQGEIVEQGPTAELFAA 247
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 294-467 6.81e-10

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: 59.04  E-value: 6.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 294 DLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDRIGYLPQD-PTT-------LF--------VADKV 357
Cdd:cd03298   16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADrPVSmlfqennLFahltveqnVGLGL 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLS 437
Cdd:cd03298   96 SPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLH 175

                        170       180       190
                 ....*....|....*....|....*....|..
gi 169293994 438 KH--MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:cd03298  176 AEtkMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 289-484 7.23e-10

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: 61.89  E-value: 7.23e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   289 DIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI-------SKVGCVD---RIGYLPQDPTtLFvadkv 357
Cdd:TIGR00957 1299 DLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINEsAEGEIiidglniAKIGLHDlrfKITIIPQDPV-LF----- 1372

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   358 iddlllvddvVASVESHLDNFG---------IIDLKDAHPF-----------------DLSSGQKQLVALAKILLTKPQL 411
Cdd:TIGR00957 1373 ----------SGSLRMNLDPFSqysdeevwwALELAHLKTFvsalpdkldhecaeggeNLSVGQRQLVCLARALLRKTKI 1442

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994   412 LLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISdRVAMIFNGQMESVDSTREFFSH-NLFYT 484
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQrGIFYS 1515
PLN03232 PLN03232
ABC transporter C family member; Provisional
 291-497 7.63e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 61.92  E-value: 7.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGC-VDRIGY---------LPQDPTtLFVADKVID 359
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEkGRIMIDDCdVAKFGLtdlrrvlsiIPQSPV-LFSGTVRFN 1329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  360 DLLLVDDVVASVESHLDNFGIIDLKDAHPFDL-----------SSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEF 428
Cdd:PLN03232 1330 IDPFSEHNDADLWEALERAHIKDVIDRNPFGLdaevseggenfSVGQRQLLSLARALLRRSKILVLDEATASVDVRTDSL 1409

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994  429 LANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTREFFSHNlfyTTTINKIMRENNPE 497
Cdd:PLN03232 1410 IQRTIREEFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD---TSAFFRMVHSTGPA 1474
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
14-225 7.67e-10

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 60.23  E-value: 7.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPkgDIDGVIILDEEIEND----DTKIGFVFQNpeDQLVMN 89
Cdd:PRK13536  53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSP--DAGKITVLGVPVPARarlaRARIGVVPQF--DNLDLE 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  90 TVWHE--IAFGlKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVN 167
Cdd:PRK13536 129 FTVREnlLVFG-RYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHA 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 168 R----EEFIKILKHinddfNVTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEML 225
Cdd:PRK13536 208 RhliwERLRSLLAR-----GKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHI 264
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
104-227 1.07e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.13  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 104 ISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfN 183
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-G 194

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 169293994 184 VTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEikmaVDEMLTK 227
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDRGRVIADGK----VDELKTK 234
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 291-465 1.14e-09

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: 58.88  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCV---DRIGYLPQ------DPTTLF----VADK 356
Cdd:cd03267   36 ALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQpTSGEVRVAGLVpwkRRKKFLRRigvvfgQKTQLWwdlpVIDS 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 VIDDLLLVDDVVASVESHLDnfGIIDLKDAHPF------DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLA 430
Cdd:cd03267  116 FYLLAAIYDLPPARFKKRLD--ELSELLDLEELldtpvrQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169293994 431 NLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:cd03267  194 NFLKEYNRErgTTVLLTSHYMKDIEALARRVLVIDKG 230
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
290-478 1.85e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 58.56  E-value: 1.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 290 IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD------------RIGYLPQDPTTLFVADKV 357
Cdd:PRK13633  24 LALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDtsdeenlwdirnKAGMVFQNPDNQIVATIV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 IDDL--------LLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFL 429
Cdd:PRK13633 104 EEDVafgpenlgIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGRREV 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 430 ANLIRGLSK--HMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13633 184 VNTIKELNKkyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
PLN03130 PLN03130
ABC transporter C family member; Provisional
 3-212 2.09e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 60.52  E-value: 2.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFSFTY-PKDKKIINNISFEIKKGDFLVITGKSGCGKT----TLLRYFKPSlRPKGDIDGVIILDEEIENDDTKIGF 77
Cdd:PLN03130 1239 KFEDVVLRYrPELPPVLHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIVELE-RGRILIDGCDISKFGLMDLRKVLGI 1317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   78 VFQNPedQLVMNTVWHEI-AFGLKNKG--------ISLKQMKRRigeivNYFNLQSIINKETQSLSNGQKQLVALASVMV 148
Cdd:PLN03130 1318 IPQAP--VLFSGTVRFNLdPFNEHNDAdlweslerAHLKDVIRR-----NSLGLDAEVSEAGENFSVGQRQLLSLARALL 1390

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994  149 MNPKVILLDEATAQLDpVNREEFIKilKHINDDF-NVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PLN03130 1391 RRSKILVLDEATAAVD-VRTDALIQ--KTIREEFkSCTMLIIAHRLNTIID-CDRILVLDAGRVV 1451
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 5-209 2.22e-09

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: 56.87  E-value: 2.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   5 ENFSFTYP---KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFkpSLRPK-GDIDGVIILDeEIENDDT---KIGF 77
Cdd:cd03232    7 KNLNYTVPvkgGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVL--AGRKTaGVITGEILIN-GRPLDKNfqrSTGY 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 VFQNP--EDQLvmnTVWHEIAFGLKNKGISLKQMKRrigeivnyfnlqsiinketqsLSNGqkqlVALASvmvmNPKVIL 155
Cdd:cd03232   84 VEQQDvhSPNL---TVREALRFSALLRGLSVEQRKR---------------------LTIG----VELAA----KPSILF 131

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 156 LDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEG-LLDVANRLIVMDEG 209
Cdd:cd03232  132 LDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSAsIFEKFDRLLLLKRG 185
PLN03232 PLN03232
ABC transporter C family member; Provisional
 3-212 2.53e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 59.99  E-value: 2.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFSFTY-PKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR-YFKPSLRPKGDI--DGVIILDEEIENDDTKIGFV 78
Cdd:PLN03232 1236 KFEDVHLRYrPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNaLFRIVELEKGRImiDDCDVAKFGLTDLRRVLSII 1315

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   79 FQNPedQLVMNTVWHEI-AFGLKNKGISLKQMKR-RIGEIV--NYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:PLN03232 1316 PQSP--VLFSGTVRFNIdPFSEHNDADLWEALERaHIKDVIdrNPFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKIL 1393

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994  155 LLDEATAQLDpVNREEFIKilKHINDDF-NVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:PLN03232 1394 VLDEATASVD-VRTDSLIQ--RTIREEFkSCTMLVIAHRLNTIID-CDKILVLSSGQVL 1448
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-193 2.57e-09

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 57.82  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIenddtKIGFVFQ 80
Cdd:PRK09544   4 LVSLENVSVSF-GQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVIKRNGKL-----RIGYVPQ 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 NPE-DQLVMNTV--WHEIAFGLKNKGIsLKQMKRrigeivnyFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLD 157
Cdd:PRK09544  75 KLYlDTTLPLTVnrFLRLRPGTKKEDI-LPALKR--------VQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLD 145

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 169293994 158 EATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQL 193
Cdd:PRK09544 146 EPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDL 181
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 288-466 2.79e-09

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: 57.55  E-value: 2.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISkVGCVD-----------RIGYLPQDPTtLF--- 352
Cdd:cd03249   15 DVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDpTSGEIL-LDGVDirdlnlrwlrsQIGLVSQEPV-LFdgt 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKV---IDDLLLVDDVVASVESHLDNFgIIDLKD-------AHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:cd03249   93 IAENIrygKPDATDEEVEEAAKKANIHDF-IMSLPDgydtlvgERGSQLSGGQKQRIAIARALLRNPKILLLDEATSALD 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 169293994 423 ASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQ 466
Cdd:cd03249  172 AESEKLVQEALDRAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQ 214
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 282-465 3.25e-09

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 58.70  E-value: 3.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 282 DLNFGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD-----------RIGYLPQDpTT 350
Cdd:PRK09536  10 SVEFG-DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDvealsaraasrRVASVPQD-TS 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 L---FVADKVIDD---------LLLVDDVVASVESHLDNFGIIDLKDaHPFD-LSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:PRK09536  88 LsfeFDVRQVVEMgrtphrsrfDTWTETDRAAVERAMERTGVAQFAD-RPVTsLSGGERQRVLLARALAQATPVLLLDEP 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 169293994 418 TKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK09536 167 TASLDINHQVRTLELVRRLVDDgKTAVAAIHDLDLAARYCDELVLLADG 215
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 273-479 3.26e-09

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 58.56  E-value: 3.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 273 DNRILMKVRDLNFgHDDI------------VLK---DLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEIS--- 333
Cdd:PRK15079   4 GKKVLLEVADLKV-HFDIkdgkqwfwqppkTLKavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAtDGEVAwlg 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 334 ----KVGCVDR------IGYLPQDPTT-----LFVAD------KVIDDLLLVDDVVASVESHLDNFGII-DLKDAHPFDL 391
Cdd:PRK15079  83 kdllGMKDDEWravrsdIQMIFQDPLAslnprMTIGEiiaeplRTYHPKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 392 SSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMES 469
Cdd:PRK15079 163 SGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLQREMglSLIFIAHDLAVVKHISDRVLVMYLGHAVE 242

                        250
                 ....*....|
gi 169293994 470 VDSTREFFSH 479
Cdd:PRK15079 243 LGTYDEVYHN 252
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 3-212 3.65e-09

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: 57.61  E-value: 3.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKD-KKIINNISFEIKKGDFLVITGKSGCGKTTL-LRYFK--PSLRPKGDIDGVIILDEEIENDDTKIGFV 78
Cdd:cd03288   21 KIHDLCVRYENNlKPVLKHVKAYIKPGQKVGICGRTGSGKSSLsLAFFRmvDIFDGKIVIDGIDISKLPLHTLRSRLSII 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNP-------------EDQLVMNTVWH--EIAfGLKNKGISLKQmkrrigeivnyfNLQSIINKETQSLSNGQKQLVAL 143
Cdd:cd03288  101 LQDPilfsgsirfnldpECKCTDDRLWEalEIA-QLKNMVKSLPG------------GLDAVVTEGGENFSVGQRQLFCL 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 144 ASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfnVTVVFVEHQLEGLLDvANRLIVMDEGKIV 212
Cdd:cd03288  168 ARAFVRKSSILIMDEATASIDMATENILQKVVMTAFAD--RTVVTIAHRVSTILD-ADLVLVLSRGILV 233
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 295-490 3.88e-09

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: 59.64  E-value: 3.88e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   295 LEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD----------RIGYLPQDpTTLF----VADKVIDD 360
Cdd:TIGR01257  949 LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDietnldavrqSLGMCPQH-NILFhhltVAEHILFY 1027

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   361 LLLV----DDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL 436
Cdd:TIGR01257 1028 AQLKgrswEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKY 1107

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994   437 SKHMTIVVASHDLEFVAKISDRVAMIFNGQMESvdSTREFFSHNLF----YTTTINKI 490
Cdd:TIGR01257 1108 RSGRTIIMSTHHMDEADLLGDRIAIISQGRLYC--SGTPLFLKNCFgtgfYLTLVRKM 1163
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
291-476 4.00e-09

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 58.88  E-value: 4.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DcQGEIS---------------KVGcvdrIGYLPQDPT---T 350
Cdd:COG1129   19 ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYqpD-SGEILldgepvrfrsprdaqAAG----IAIIHQELNlvpN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 LFVAD-------KVIDDLLLVDDVVASVESHLDNFGI-IDLkDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:COG1129   94 LSVAEniflgrePRRGGLIDWRAMRRRARELLARLGLdIDP-DTPVGDLSVAQQQLVEIARALSRDARVLILDEPTASLT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 423 ASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREF 476
Cdd:COG1129  173 EREVERLFRIIRRLKAQgVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 292-479 4.42e-09

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 57.72  E-value: 4.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIS--------------------KVGCVDrigylpQDP-T 349
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQpTSGTVTigervitagkknkklkplrkKVGIVF------QFPeH 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 350 TLFvadkviddlllvddvVASVESHL----DNFGII-------------------DLKDAHPFDLSSGQKQLVALAKILL 406
Cdd:PRK13634  97 QLF---------------EETVEKDIcfgpMNFGVSeedakqkaremielvglpeELLARSPFELSGGQMRRVAIAGVLA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 407 TKPQLLLLDEPTKGIDASSK----EFLANLIRglSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK13634 162 MEPEVLVLDEPTAGLDPKGRkemmEMFYKLHK--EKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFAD 236
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 270-477 4.74e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 58.71  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 270 DEIDNRILMKVRDLN--FGHDDI---VLKDLEIDILENEILSIVGANGSGKS----SFLRCL---AGLVDC--------- 328
Cdd:PRK10261   5 DELDARDVLAVENLNiaFMQEQQkiaAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqaGGLVQCdkmllrrrs 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 329 ----------QGEISKVGCVDrIGYLPQDPTT----LFVADKVIDDL------LLVDDVVASVESHLDNFGIIDLKDA-- 386
Cdd:PRK10261  85 rqvielseqsAAQMRHVRGAD-MAMIFQEPMTslnpVFTVGEQIAESirlhqgASREEAMVEAKRMLDQVRIPEAQTIls 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 387 -HPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMT--IVVASHDLEFVAKISDRVAMIF 463
Cdd:PRK10261 164 rYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSmgVIFITHDMGVVAEIADRVLVMY 243

                        250
                 ....*....|....
gi 169293994 464 NGQMESVDSTREFF 477
Cdd:PRK10261 244 QGEAVETGSVEQIF 257
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 291-450 6.96e-09

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: 56.63  E-value: 6.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL--------VDCQGEisKVGCVD------RIGY----LPQD-PTTL 351
Cdd:COG1119   18 ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDlpptygndVRLFGE--RRGGEDvwelrkRIGLvspaLQLRfPRDE 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADKVI--------DDLLLVDDVVASVESHLDNFGIIDLKDaHPF-DLSSGQKQLV----ALAK-----Illtkpqlll 413
Cdd:COG1119   96 TVLDVVLsgffdsigLYREPTDEQRERARELLELLGLAHLAD-RPFgTLSQGEQRRVliarALVKdpellI--------- 165

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLE 450
Cdd:COG1119  166 LDEPTAGLDLGARELLLALLDKLAAEgaPTLVLVTHHVE 204
cbiO PRK13649
energy-coupling factor transporter ATPase;
292-467 7.29e-09

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 57.06  E-value: 7.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEIsKVGCVD---------------RIGYLPQDPTTLFVAD 355
Cdd:PRK13649  23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLhVPTQGSV-RVDDTLitstsknkdikqirkKVGLVFQFPESQLFEE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 356 KVIDDL--------LLVDDVVASVESHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSK 426
Cdd:PRK13649 102 TVLKDVafgpqnfgVSQEEAEALAREKLALVGISeSLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGR 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169293994 427 EFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK13649 182 KELMTLFKKLHQSgMTIVLVTHLMDDVANYADFVYVLEKGKL 223
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 303-475 7.58e-09

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 56.48  E-value: 7.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 303 EILSIVGANGSGKSSFLRCLAGLVDCQGEI----------SKVGCVDRIGYLPQDPTTLFVAD--KVIDDLLLVDDVVAS 370
Cdd:PRK03695  23 EILHLVGPNGAGKSTLLARMAGLLPGSGSIqfagqpleawSAAELARHRAYLSQQQTPPFAMPvfQYLTLHQPDKTRTEA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 371 VESHLDN----FGIIDLKDAHPFDLSSGQKQLVALAKI-------LLTKPQLLLLDEPTKGIDASSKEFLANLIRGL-SK 438
Cdd:PRK03695 103 VASALNEvaeaLGLDDKLGRSVNQLSGGEWQRVRLAAVvlqvwpdINPAGQLLLLDEPMNSLDVAQQAALDRLLSELcQQ 182

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169293994 439 HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:PRK03695 183 GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
277-482 8.01e-09

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 57.26  E-value: 8.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVG-CVDRIGYLPQDPTTLF- 352
Cdd:PRK09452  14 LVELRGISKSFDGkEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPdSGRIMLDGqDITHVPAENRHVNTVFq 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 ---------VADKVIDDLLLVDDVVASVES---------HLDNFGiidlkDAHPFDLSSGQKQLVALAKILLTKPQLLLL 414
Cdd:PRK09452  94 syalfphmtVFENVAFGLRMQKTPAAEITPrvmealrmvQLEEFA-----QRKPHQLSGGQQQRVAIARAVVNKPKVLLL 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 415 DEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH--NLF 482
Cdd:PRK09452 169 DESLSALDYKLRKQMQNELKALQRKlgITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEpkNLF 240
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 1-192 8.32e-09

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: 58.22  E-value: 8.32e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    1 MYKIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFkpslrpkGDI----DGVIILDEeiendDTKIG 76
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRIL-------GELwpvyGGRLTKPA-----KGKLF 518

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   77 FVFQNP-------EDQLvmntVWHEIAFGLKNKGISLKQMKrrigEIVNYFNLQSIINKE---------TQSLSNGQKQL 140
Cdd:TIGR00954 519 YVPQRPymtlgtlRDQI----IYPDSSEDMKRRGLSDKDLE----QILDNVQLTHILEREggwsavqdwMDVLSGGEKQR 590

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 169293994  141 VALASVMVMNPKVILLDEATAQLDPVNREEFIKILKhindDFNVTVVFVEHQ 192
Cdd:TIGR00954 591 IAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLCR----EFGITLFSVSHR 638
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 1-211 8.47e-09

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: 57.91  E-value: 8.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    1 MYKIENFSFTYPKDKKI--INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLrpKGDIDGVIILDEEIENDDT----- 73
Cdd:TIGR02633 257 ILEARNLTCWDVINPHRkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAY--PGKFEGNVFINGKPVDIRNpaqai 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   74 --KIGFVfqnPEDQLVMNTVwHEIAFGlknKGISLKQMKR--RIGEIVNYFNLQSIINKETQ-------------SLSNG 136
Cdd:TIGR02633 335 raGIAMV---PEDRKRHGIV-PILGVG---KNITLSVLKSfcFKMRIDAAAELQIIGSAIQRlkvktaspflpigRLSGG 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994  137 QKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:TIGR02633 408 NQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
hmuV PRK13547
heme ABC transporter ATP-binding protein;
290-467 9.20e-09

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 56.37  E-value: 9.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 290 IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL---------VDCQGEISKVG----CVD------RIGYLPQ--DP 348
Cdd:PRK13547  15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDltgggaprgARVTGDVTLNGeplaAIDaprlarLRAVLPQaaQP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 349 TTLFVADKVIDDLLLVDDVVASVESHLDNfGIID----LKDAHPFD------LSSGQKQLVALAKI---------LLTKP 409
Cdd:PRK13547  95 AFAFSAREIVLLGRYPHARRAGALTHRDG-EIAWqalaLAGATALVgrdvttLSGGELARVQFARVlaqlwpphdAAQPP 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 410 QLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK13547 174 RYLLLDEPTAALDLAHQHRLLDTVRRLARdwNLGVLAIVHDPNLAARHADRIAMLADGAI 233
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 58-193 9.79e-09

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 58.12  E-value: 9.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   58 IDGVIILDEEIENDDTKIGFVFQNPedQLVMNTVWHEIAFGLKNKgiSLKQMKR--RIGEIVNYfnLQSIINKET----- 130
Cdd:PTZ00265 1281 LDGVDICDYNLKDLRNLFSIVSQEP--MLFNMSIYENIKFGKEDA--TREDVKRacKFAAIDEF--IESLPNKYDtnvgp 1354

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994  131 --QSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPvNREEFI-KILKHINDDFNVTVVFVEHQL 193
Cdd:PTZ00265 1355 ygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDS-NSEKLIeKTIVDIKDKADKTIITIAHRI 1419
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 292-479 1.09e-08

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: 56.11  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEIS--------------------KVGCV-DRIGYLPQdpt 349
Cdd:cd03294   40 VNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEpTSGKVLidgqdiaamsrkelrelrrkKISMVfQSFALLPH--- 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 350 tLFVADKV-----IDDLLLVDDVVASVEShLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS 424
Cdd:cd03294  117 -RTVLENVafgleVQGVPRAEREERAAEA-LELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPL 194

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 425 SKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:cd03294  195 IRREMQDELLRLQAELqkTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTN 251
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 291-467 1.12e-08

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 55.93  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEISKVGC----------VDRIGYLPQDPTTLF---VADK 356
Cdd:PRK13548  17 LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGeLSPDSGEVRLNGRpladwspaelARRRAVLPQHSSLSFpftVEEV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 V----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLL------DEPTKGIDASSK 426
Cdd:PRK13548  97 VamgrAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEPDGPprwlllDEPTSALDLAHQ 176

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 427 EFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK13548 177 HHVLRLARQLAHErgLAVIVVLHDLNLAARYADRIVLLHQGRL 219
cbiO PRK13643
energy-coupling factor transporter ATPase;
292-477 1.15e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 56.28  E-value: 1.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCV---------------DRIGYLPQDPTTLFVADK 356
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIvvsstskqkeikpvrKKVGVVFQFPESQLFEET 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 VIDDLLLVDDVVASVESHLDNFGIIDLK---------DAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKE 427
Cdd:PRK13643 102 VLKDVAFGPQNFGIPKEKAEKIAAEKLEmvgladefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 428 FLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFF 477
Cdd:PRK13643 182 EMMQLFESIHQSgQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 277-478 1.16e-08

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 57.41  E-value: 1.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNF-----GHDDIVLKDLEIDILENEILSIVGANGSGKS----SFLRCLAG--LVDCQGEISKVGCV------- 338
Cdd:PRK15134   5 LLAIENLSVafrqqQTVRTVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSppVVYPSGDIRFHGESllhaseq 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 339 -------DRIGYLPQDPTT----LFVADK----VIDDLLLVDDVVASVE--SHLDNFGIID----LKDaHPFDLSSGQKQ 397
Cdd:PRK15134  85 tlrgvrgNKIAMIFQEPMVslnpLHTLEKqlyeVLSLHRGMRREAARGEilNCLDRVGIRQaakrLTD-YPHQLSGGERQ 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 398 LVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:PRK15134 164 RVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQelNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAAT 243


                 ...
gi 169293994 476 FFS 478
Cdd:PRK15134 244 LFS 246
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-212 1.34e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 57.21  E-value: 1.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGdidGVIILDEeiendDTKIGFVFQN-- 81
Cdd:PRK15064 322 VENLTKGFD-NGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDS---GTVKWSE-----NANIGYYAQDha 392

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  82 ---PEDQLVMN--TVWheiafglkNKGISLKQMKRRI-GEIVnyFNlQSIINKETQSLSNGQKQLVALASVMVMNPKVIL 155
Cdd:PRK15064 393 ydfENDLTLFDwmSQW--------RQEGDDEQAVRGTlGRLL--FS-QDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLV 461

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 156 LDEATAQLDpvnrEEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK15064 462 MDEPTNHMD----MESIESLNMALEKYEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 281-466 1.43e-08

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: 55.31  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 281 RDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVD-----------RIGYLPQD 347
Cdd:cd03253    4 ENVTFAYDPgrPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDirevtldslrrAIGVVPQD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 pTTLFvaDKVIDDLLLVDDVVASVE--------SHLDNFgIIDLKDAhpFD---------LSSGQKQLVALAKILLTKPQ 410
Cdd:cd03253   84 -TVLF--NDTIGYNIRYGRPDATDEevieaakaAQIHDK-IMRFPDG--YDtivgerglkLSGGEKQRVAIARAILKNPP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 411 LLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQ 466
Cdd:cd03253  158 ILLLDEATSALDTHTEREIQAALRDVSKGRTTIVIAHRLSTIVN-ADKIIVLKDGR 212
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 385-486 1.56e-08

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 56.40  E-value: 1.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 385 DAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIF 463
Cdd:PRK13631 171 ERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANnKTVFVITHTMEHVLEVADEVIVMD 250

                         90       100
                 ....*....|....*....|...
gi 169293994 464 NGQMESVDSTREFFSHNLFYTTT 486
Cdd:PRK13631 251 KGKILKTGTPYEIFTDQHIINST 273
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-175 1.64e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.44  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  19 NNISFEIKKGD---FLvitGKSGCGKTT-------LLryfKPSlrpkgdiDG-VIILDEEIENDD----TKIGF------ 77
Cdd:NF033858 283 DHVSFRIRRGEifgFL---GSNGCGKSTtmkmltgLL---PAS-------EGeAWLFGQPVDAGDiatrRRVGYmsqafs 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  78 ------VFQNpedqLVMntvwHEIAFGLKNKGIslkqmKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNP 151
Cdd:NF033858 350 lygeltVRQN----LEL----HARLFHLPAAEI-----AARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKP 416

                        170       180
                 ....*....|....*....|....
gi 169293994 152 KVILLDEATAQLDPVNREEFIKIL 175
Cdd:NF033858 417 ELLILDEPTSGVDPVARDMFWRLL 440
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 291-459 1.65e-08

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: 55.13  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAG--LVDcQGEI---SKVGCVD---------------RIGY------- 343
Cdd:COG4778   26 VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnyLPD-SGSIlvrHDGGWVDlaqaspreilalrrrTIGYvsqflrv 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 344 LPQDPTTLFVADKVIDDLLLVDDVVASVESHLDNFGIID-LKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID 422
Cdd:COG4778  105 IPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLD 184

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169293994 423 ASSKEFLANLIRGLSKHMTIVVA-SHDLEFVAKISDRV 459
Cdd:COG4778  185 AANRAVVVELIEEAKARGTAIIGiFHDEEVREAVADRV 222
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 15-211 1.88e-08

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 56.86  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  15 KKIINNISFEIKKGDFLVITGKSGCGKTTLLR-----YfkpslrpKGDIDGVIILD----------EEIENddtKIGFVf 79
Cdd:PRK13549 275 IKRVDDVSFSLRRGEILGIAGLVGAGRTELVQclfgaY-------PGRWEGEIFIDgkpvkirnpqQAIAQ---GIAMV- 343

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  80 qnPEDQ------LVMNtVWHEIAFGlknkgiSLKQMKRriGEIVNYFNLQSIINKETQ--------------SLSNGQKQ 139
Cdd:PRK13549 344 --PEDRkrdgivPVMG-VGKNITLA------ALDRFTG--GSRIDDAAELKTILESIQrlkvktaspelaiaRLSGGNQQ 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 169293994 140 LVALASVMVMNPKVILLDEATAQLDPVNREEfikILKHIND--DFNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK13549 413 KAVLAKCLLLNPKILILDEPTRGIDVGAKYE---IYKLINQlvQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 276-464 1.98e-08

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 55.56  E-value: 1.98e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 276 ILMKVRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD------CQGEI---------SKVGCV 338
Cdd:PRK14243   9 TVLRTENLNvyYG-SFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDlipgfrVEGKVtfhgknlyaPDVDPV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 339 D---RIGYLPQDPTTLfvaDKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFD------------LSSGQKQLVALAK 403
Cdd:PRK14243  88 EvrrRIGMVFQKPNPF---PKSIYDNIAYGARINGYKGDMDELVERSLRQAALWDevkdklkqsglsLSGGQQQRLCIAR 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 169293994 404 ILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRVAMiFN 464
Cdd:PRK14243 165 AIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIIIVTHNMQQAARVSDMTAF-FN 224
cbiO PRK13646
energy-coupling factor transporter ATPase;
382-478 2.05e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 55.56  E-value: 2.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 382 DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLS--KHMTIVVASHDLEFVAKISDRV 459
Cdd:PRK13646 137 DVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQtdENKTIILVSHDMNEVARYADEV 216

                         90
                 ....*....|....*....
gi 169293994 460 AMIFNGQMESVDSTREFFS 478
Cdd:PRK13646 217 IVMKEGSIVSQTSPKELFK 235
cbiO PRK13641
energy-coupling factor transporter ATPase;
292-478 2.67e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 55.22  E-value: 2.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVG--------------CVDRIGYLPQDPTTLFVADK 356
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKpSSGTITIAGyhitpetgnknlkkLRKKVSLVFQFPEAQLFENT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 VIDdlllvddvvaSVESHLDNFGII-------------------DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:PRK13641 103 VLK----------DVEFGPKNFGFSedeakekalkwlkkvglseDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEP 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169293994 418 TKGIDASSKEFLANLIRGLSK--HmTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK13641 173 AAGLDPEGRKEMMQLFKDYQKagH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
277-506 3.47e-08

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 55.61  E-value: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEISKVGcVDrIGYLP--QDPTT-- 350
Cdd:PRK11607  19 LLEIRNLTKSFDGQhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFeQPTAGQIMLDG-VD-LSHVPpyQRPINmm 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 -----LF--------VADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:PRK11607  97 fqsyaLFphmtveqnIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEP 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 418 TKGIDASSKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH-------------NLF 482
Cdd:PRK11607 177 MGALDKKLRDRMQLEVVDILERVgvTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHpttrysaefigsvNVF 256

                        250       260
                 ....*....|....*....|....
gi 169293994 483 ytttiNKIMRENNPEVILLEDLGL 506
Cdd:PRK11607 257 -----EGVLKERQEDGLVIDSPGL 275
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
24-207 3.62e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.97  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  24 EIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIDGVIILD---EEIEND-DTKIGFVFQNPEDQLVMNTVWHEIAFG 98
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPdEGEVDPELKISykpQYIKPDyDGTVEDLLRSITDDLGSSYYKSEIIKP 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  99 LknkgislkqmkrrigeivnyfNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHI 178
Cdd:PRK13409 441 L---------------------QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRI 499

                        170       180       190
                 ....*....|....*....|....*....|
gi 169293994 179 NDDFNVTVVFVEHQLEgLLD-VANRLIVMD 207
Cdd:PRK13409 500 AEEREATALVVDHDIY-MIDyISDRLMVFE 528
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 14-194 4.11e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 55.41  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLryfkpSL----RPKGDIDGVIILD------EEIENDDTKIGFVFQNPE 83
Cdd:PRK10938 272 DRPILHNLSWQVNPGEHWQIVGPNGAGKSTLL-----SLitgdHPQGYSNDLTLFGrrrgsgETIWDIKKHIGYVSSSLH 346

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 -DQLVMNTVWHEIAFGLKN-----KGISLKQMKRrIGEIVNYFNLQSII-NKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK10938 347 lDYRVSTSVRNVILSGFFDsigiyQAVSDRQQKL-AQQWLDILGIDKRTaDAPFHSLSWGQQRLALIVRALVKHPTLLIL 425

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169293994 157 DEATAQLDPVNRE---EFIKILkhINDDfNVTVVFVEHQLE 194
Cdd:PRK10938 426 DEPLQGLDPLNRQlvrRFVDVL--ISEG-ETQLLFVSHHAE 463
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 17-204 4.44e-08

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 54.01  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  17 IINNISFEIKKGDFLVITGKSGCGKTTLLRYFKpslrpkGDIDG----VIILDEEIENDDTK---------IGFVFQNPE 83
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILA------GLDDGssgeVSLVGQPLHQMDEEaraklrakhVGFVFQSFM 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 DQLVMNTvwheiafgLKN-------KGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK10584  99 LIPTLNA--------LENvelpallRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFA 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 169293994 157 DEATAQLDPVNREEFIKILKHINDDFNVTVVFVEH--QLEGLLDVANRLI 204
Cdd:PRK10584 171 DEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHdlQLAARCDRRLRLV 220
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
288-465 4.51e-08

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 54.84  E-value: 4.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVG---------CVDRIGYLPQ----DPT---- 349
Cdd:PRK13536  53 DKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPdAGKITVLGvpvpararlARARIGVVPQfdnlDLEftvr 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 350 -TLFVADKVIDDLLLVDDvvASVESHLDnFGIIDLK-DAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKE 427
Cdd:PRK13536 133 eNLLVFGRYFGMSTREIE--AVIPSLLE-FARLESKaDARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARH 209

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 169293994 428 FLANLIRG-LSKHMTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK13536 210 LIWERLRSlLARGKTILLTTHFMEEAERLCDRLCVLEAG 248
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 298-466 4.66e-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: 52.96  E-value: 4.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 298 DILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVdRIGYLPQDpttlfvadkviddlllvddvvasveshldn 377
Cdd:cd03222   21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGI-TPVYKPQY------------------------------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 378 fgiidlkdahpFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKI 455
Cdd:cd03222   70 -----------IDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEgkKTALVVEHDLAVLDYL 138

                        170
                 ....*....|.
gi 169293994 456 SDRVaMIFNGQ 466
Cdd:cd03222  139 SDRI-HVFEGE 148
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 277-467 5.69e-08

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: 53.63  E-value: 5.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGH----DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI----------------SKV 335
Cdd:cd03248   11 IVKFQNVTFAYptrpDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQgGQVlldgkpisqyehkylhSKV 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 336 GCVDrigylpQDPTtLF---VADKV---IDDLLLVDDVVASVESHLDNFgIIDLKDAHPFD-------LSSGQKQLVALA 402
Cdd:cd03248   91 SLVG------QEPV-LFarsLQDNIaygLQSCSFECVKEAAQKAHAHSF-ISELASGYDTEvgekgsqLSGGQKQRVAIA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 403 KILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQM 467
Cdd:cd03248  163 RALIRNPQVLILDEATSALDAESEQQVQQALYDWPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 136-462 5.89e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 55.28  E-value: 5.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 136 GQKQLVALASVMVMNPKVILLDEATAQLDpVNReefIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIVI-- 213
Cdd:PRK15064 159 GWKLRVLLAQALFSNPDILLLDEPTNNLD-INT---IRWLEDVLNERNSTMIIISHDRHFLNSVCTHMADLDYGELRVyp 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 214 ---DNEIK---MAVDEMLT----KKIFVESLPNYV-RVSSLCDKlclsikeAREALVNFENFD-IKImDEID-------- 273
Cdd:PRK15064 235 gnyDEYMTaatQARERLLAdnakKKAQIAELQSFVsRFSANASK-------AKQATSRAKQIDkIKL-EEVKpssrqnpf 306

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 ---------NRILMKVRDLNFGHDDIVL-KDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEIsKVGCVDRIG 342
Cdd:PRK15064 307 irfeqdkklHRNALEVENLTKGFDNGPLfKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGeLEPDSGTV-KWSENANIG 385

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 343 YLPQDPTTLFVADKV----IDDLLLVDDVVASVESHLDN--FGIIDLKDAhPFDLSSGQKQLVALAKILLTKPQLLLLDE 416
Cdd:PRK15064 386 YYAQDHAYDFENDLTlfdwMSQWRQEGDDEQAVRGTLGRllFSQDDIKKS-VKVLSGGEKGRMLFGKLMMQKPNVLVMDE 464

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 417 PTKGIDASSKEFLANlirGLSKHM-TIVVASHDLEFVAKISDRVAMI 462
Cdd:PRK15064 465 PTNHMDMESIESLNM---ALEKYEgTLIFVSHDREFVSSLATRIIEI 508
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
273-449 6.03e-08

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 55.11  E-value: 6.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 273 DNRILMK----VRDLNF--GHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI----------SKV 335
Cdd:PRK10790 332 DDRPLQSgridIDNVSFayRDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTeGEIrldgrplsslSHS 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 336 GCVDRIGYLPQDPTTLfvADKVIDDLLL-VDDVVASVESHLDNFGIIDLKDAHP-----------FDLSSGQKQLVALAK 403
Cdd:PRK10790 412 VLRQGVAMVQQDPVVL--ADTFLANVTLgRDISEEQVWQALETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALAR 489

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 169293994 404 ILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDL 449
Cdd:PRK10790 490 VLVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLVVIAHRL 535
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 291-483 6.59e-08

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: 53.64  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEI----SKVGCVD------RIGYLPQDpTTLF---VADK 356
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFyVPENGRVlvdgHDLALADpawlrrQVGVVLQE-NVLFnrsIRDN 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 ViddlllvddvvASVESHLDNFGIID---LKDAHPF-----------------DLSSGQKQLVALAKILLTKPQLLLLDE 416
Cdd:cd03252   96 I-----------ALADPGMSMERVIEaakLAGAHDFiselpegydtivgeqgaGLSGGQRQRIAIARALIHNPRILIFDE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 417 PTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVaKISDRVAMIFNGQMESVDSTREFFSHNLFY 483
Cdd:cd03252  165 ATSALDYESEHAIMRNMHDICAGRTVIIIAHRLSTV-KNADRIIVMEKGRIVEQGSHDELLAENGLY 230
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 278-467 7.92e-08

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: 54.81  E-value: 7.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  278 MKVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ---GEI----------------SKVG- 336
Cdd:TIGR03269   1 IEVKNLTKKFDGKeVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQYEptsGRIiyhvalcekcgyverpSKVGe 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  337 ----C--------VD--------------RIGYLPQDPTTLFVADKVIDDLLLVDDVVA-----SVESHLDNFGIIDLkd 385
Cdd:TIGR03269  81 pcpvCggtlepeeVDfwnlsdklrrrirkRIAIMLQRTFALYGDDTVLDNVLEALEEIGyegkeAVGRAVDLIEMVQL-- 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  386 AHPF-----DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDR 458
Cdd:TIGR03269 159 SHRIthiarDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKAsgISMVLTSHWPEVIEDLSDK 238


                  ....*....
gi 169293994  459 VAMIFNGQM 467
Cdd:TIGR03269 239 AIWLENGEI 247
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 18-225 8.54e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 54.62  E-value: 8.54e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLrPKGDidGVIILD-EEIEN----DDTKIGFVFQNPE---DQLVMN 89
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGAL-PRTS--GYVTLDgHEVVTrspqDGLANGIVYISEDrkrDGLVLG 344

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  90 TVWHE----IAFG-LKNKGISLKQMKRRI--GEIVNYFNL------QSIINketqsLSNGQKQLVALASVMVMNPKVILL 156
Cdd:PRK10762 345 MSVKEnmslTALRyFSRAGGSLKHADEQQavSDFIRLFNIktpsmeQAIGL-----LSGGNQQKVAIARGLMTRPKVLIL 419

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 157 DEATAQLDPVNREEfikILKHINdDFN---VTVVFVEHQLEGLLDVANRLIVMDEGKIVIDNEIKMAVDEML 225
Cdd:PRK10762 420 DEPTRGVDVGAKKE---IYQLIN-QFKaegLSIILVSSEMPEVLGMSDRILVMHEGRISGEFTREQATQEKL 487
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 303-475 8.89e-08

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 53.31  E-value: 8.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 303 EILSIVGANGSGKSSFLRCLAGLVDCQGEI----------SKVGCVDRIGYLPQDPTTLFVAD--KVIDDLLLVDDVVAS 370
Cdd:COG4138   23 ELIHLIGPNGAGKSTLLARMAGLLPGQGEIllngrplsdwSAAELARHRAYLSQQQSPPFAMPvfQYLALHQPAGASSEA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 371 VESHL----DNFGIIDLKDAHPFDLSSGQKQLVALAKI-------LLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH 439
Cdd:COG4138  103 VEQLLaqlaEALGLEDKLSRPLTQLSGGEWQRVRLAAVllqvwptINPEGQLLLLDEPMNSLDVAQQAALDRLLRELCQQ 182

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169293994 440 -MTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:COG4138  183 gITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAE 219
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 388-495 1.04e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 53.55  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 388 PFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGID-ASSKEFLaNLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK13651 163 PFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDpQGVKEIL-EIFDNLNKQgKTIILVTHDLDNVLEWTKRTIFFKDG 241

                         90       100       110
                 ....*....|....*....|....*....|
gi 169293994 466 QMESVDSTREFFSHNLFytttinkiMRENN 495
Cdd:PRK13651 242 KIIKDGDTYDILSDNKF--------LIENN 263
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
303-467 1.11e-07

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 52.57  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 303 EILSIVGANGSGKSSFLRCLAGLV-DCQGEI------------SKVGCVDR-IGYLPQDPTTLF-------VADKVIDDL 361
Cdd:PRK10908  29 EMAFLTGHSGAGKSTLLKLICGIErPSAGKIwfsghditrlknREVPFLRRqIGMIFQDHHLLMdrtvydnVAIPLIIAG 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 362 LLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK-HM 440
Cdd:PRK10908 109 ASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRvGV 188

                        170       180
                 ....*....|....*....|....*..
gi 169293994 441 TIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK10908 189 TVLMATHDIGLISRRSYRMLTLSDGHL 215
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 277-479 1.20e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 53.57  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLN--FG-HDDIV--LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISkvGCV------------- 338
Cdd:PRK09473  12 LLDVKDLRvtFStPDGDVtaVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIG--GSAtfngreilnlpek 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 339 -------DRIGYLPQDPTT-----LFVADK---VIDDLLLVDDVVASVES--HLDNFGIIDLK---DAHPFDLSSGQKQL 398
Cdd:PRK09473  90 elnklraEQISMIFQDPMTslnpyMRVGEQlmeVLMLHKGMSKAEAFEESvrMLDAVKMPEARkrmKMYPHEFSGGMRQR 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 399 VALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREF 476
Cdd:PRK09473 170 VMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFntAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDV 249


                 ...
gi 169293994 477 FSH 479
Cdd:PRK09473 250 FYQ 252
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 20-206 1.31e-07

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 52.26  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  20 NISFEIKKGDFLVITGKSGCGKTTL----------LRY---FKPSLR------PKGDIDGVIILDEEIENDDTKIGfvfQ 80
Cdd:cd03270   13 NVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYvesLSAYARqflgqmDKPDVDSIEGLSPAIAIDQKTTS---R 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  81 NPEDQLVMNTvwhEIAFGLK----NKGIslkqmKRRIGEIVN----YFNLqsiiNKETQSLSNGQKQLVALASVMVMNPK 152
Cdd:cd03270   90 NPRSTVGTVT---EIYDYLRllfaRVGI-----RERLGFLVDvglgYLTL----SRSAPTLSGGEAQRIRLATQIGSGLT 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 153 VIL--LDEATAQLDPVNREEFIKILKHINDDFNvTVVFVEHQlEGLLDVANRLIVM 206
Cdd:cd03270  158 GVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGN-TVLVVEHD-EDTIRAADHVIDI 211
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 24-205 1.41e-07

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 51.42  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  24 EIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDidgviildeeienddtkigfvfqnpedqlvmNTVWHEIAFGLKNKG 103
Cdd:cd03222   21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------------------------------NDEWDGITPVYKPQY 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 104 ISLkqmkrrigeivnyfnlqsiinketqslSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFN 183
Cdd:cd03222   70 IDL---------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGK 122

                        170       180
                 ....*....|....*....|..
gi 169293994 184 VTVVFVEHQLEGLLDVANRLIV 205
Cdd:cd03222  123 KTALVVEHDLAVLDYLSDRIHV 144
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 278-465 1.43e-07

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 52.32  E-value: 1.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGH-DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLvdcqgEISKVGCVDRIGY---LPQDPTT--- 350
Cdd:PRK11124   3 IQLNGINCFYgAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLL-----EMPRSGTLNIAGNhfdFSKTPSDkai 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 -------------------LFVADKVI-----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILL 406
Cdd:PRK11124  78 relrrnvgmvfqqynlwphLTVQQNLIeapcrVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 407 TKPQLLLLDEPTKGIDASSKEFLANLIRGLSK-HMTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAEtGITQVIVTHEVEVARKTASRVVYMENG 217
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
292-479 1.67e-07

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 53.50  E-value: 1.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGE-------ISKVGCVD-------RIGYLPQD----PTTLF 352
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEpTRGQvlidgvdIAKISDAElrevrrkKIAMVFQSfalmPHMTV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKVIDDLLLVDDVVASVESHLD---NFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSK-EF 428
Cdd:PRK10070 124 LDNTAFGMELAGINAEERREKALDalrQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRtEM 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 429 LANLIRGLSKHM-TIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSH 479
Cdd:PRK10070 204 QDELVKLQAKHQrTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNN 255
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
291-461 1.82e-07

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 52.13  E-value: 1.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEI--------------------SKVGCVDRIGYLPQDPT 349
Cdd:PRK11629  24 VLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLdTPTSGDVifngqpmsklssaakaelrnQKLGFIYQFHHLLPDFT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 350 TL-FVADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEF 428
Cdd:PRK11629 104 ALeNVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADS 183

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 169293994 429 LANLIRGLSKHM--TIVVASHDLEFVAKISDRVAM 461
Cdd:PRK11629 184 IFQLLGELNRLQgtAFLVVTHDLQLAKRMSRQLEM 218
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 20-211 1.96e-07

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: 54.25  E-value: 1.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    20 NISF-EIKKGDFLvitGKSGCGKTTLLRYFKPSLRPKGDIdgVIILDEEIEnddTKIGFVFQN----PEDQLVMN--TVW 92
Cdd:TIGR01257  950 NITFyENQITAFL---GHNGAGKTTTLSILTGLLPPTSGT--VLVGGKDIE---TNLDAVRQSlgmcPQHNILFHhlTVA 1021

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    93 HEIAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFI 172
Cdd:TIGR01257 1022 EHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 169293994   173 KILKHINDdfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:TIGR01257 1102 DLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 7-212 2.01e-07

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 53.96  E-value: 2.01e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994     7 FSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIDGVIILD----EEIENDdtKIGFVFQN 81
Cdd:TIGR00956   66 KKFRDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGfHIGVEGVITYDgitpEEIKKH--YRGDVVYN 143

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    82 PEDQL---VMnTVWHEIAF-------GLKNKGISLKQMKRRIGEIV-NYFNLQsiINKET-------QSLSNGQKQLVAL 143
Cdd:TIGR00956  144 AETDVhfpHL-TVGETLDFaarcktpQNRPDGVSREEYAKHIADVYmATYGLS--HTRNTkvgndfvRGVSGGERKRVSI 220

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   144 ASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQL-EGLLDVANRLIVMDEGKIV 212
Cdd:TIGR00956  221 AEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCsQDAYELFDKVIVLYEGYQI 290
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 291-466 2.28e-07

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: 51.77  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DcQGEISKVGC------VDR-----IGYLPQDPTT---LFVA 354
Cdd:cd03218   15 VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVkpD-SGKILLDGQditklpMHKrarlgIGYLPQEASIfrkLTVE 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 355 DKVIDDLLLVDDVVAS----VESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLA 430
Cdd:cd03218   94 ENILAVLEIRGLSKKEreekLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGVDPIAVQDIQ 173

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 169293994 431 NLIRGLS-KHMTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:cd03218  174 KIIKILKdRGIGVLITDHNVRETLSITDRAYIIYEGK 210
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
290-481 2.33e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 52.30  E-value: 2.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 290 IVLKDLEIDILENEILSIVGANGSGKSSFLRCLA-------GLVDCQGE-ISKVGCVD---RIGYLPQDPTT---LFVAD 355
Cdd:PRK10253  21 TVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrlmtpahGHVWLDGEhIQHYASKEvarRIGLLAQNATTpgdITVQE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 356 KVI--------DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSK- 426
Cdd:PRK10253 101 LVArgryphqpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQi 180

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 427 ---EFLANLIRglSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSHNL 481
Cdd:PRK10253 181 dllELLSELNR--EKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAEL 236
PLN03211 PLN03211
ABC transporter G-25; Provisional
 13-164 3.22e-07

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 52.96  E-value: 3.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  13 KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILDEEIENDDTK-IGFVFQnpEDQLVMN-T 90
Cdd:PLN03211  79 QERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNFTGTILANNRKPTKQILKrTGFVTQ--DDILYPHlT 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  91 VWHEIAF-GLKNKGISL-KQMKRRIGE-IVNYFNL----QSII-NKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQ 162
Cdd:PLN03211 157 VRETLVFcSLLRLPKSLtKQEKILVAEsVISELGLtkceNTIIgNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSG 236


                 ..
gi 169293994 163 LD 164
Cdd:PLN03211 237 LD 238
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 24-207 3.50e-07

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: 52.86  E-value: 3.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  24 EIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIDGVIILDE-----EIENDDTKIGFVFQNPEDQLvmNTVWHEiaf 97
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPdEGEVDEDLKISYkpqyiSPDYDGTVEEFLRSANTDDF--GSSYYK--- 436

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  98 glknkgislkqmkrriGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKH 177
Cdd:COG1245  437 ----------------TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 500

                        170       180       190
                 ....*....|....*....|....*....|.
gi 169293994 178 INDDFNVTVVFVEHQLEgLLD-VANRLIVMD 207
Cdd:COG1245  501 FAENRGKTAMVVDHDIY-LIDyISDRLMVFE 530
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
292-475 3.76e-07

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 51.71  E-value: 3.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISkvgcVD--------------RIGYLPQDPTTLFVADK 356
Cdd:PRK15112  29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEpTSGELL----IDdhplhfgdysyrsqRIRMIFQDPSTSLNPRQ 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 357 VI----------DDLLLVDDVVASVESHLDNFGII-DLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASS 425
Cdd:PRK15112 105 RIsqildfplrlNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSM 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 426 KEFLANLIRGL-SKH--MTIVVASHdLEFVAKISDRVAMIFNGQMESVDSTRE 475
Cdd:PRK15112 185 RSQLINLMLELqEKQgiSYIYVTQH-LGMMKHISDQVLVMHQGEVVERGSTAD 236
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 303-478 4.96e-07

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 50.85  E-value: 4.96e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 303 EILSIVGANGSGKSsfLRCLA-------GLVDCQGEISkvgcVDRIGYLP------------QDPTTLF-----VADKVI 358
Cdd:PRK10418  30 RVLALVGGSGSGKS--LTCAAalgilpaGVRQTAGRVL----LDGKPVAPcalrgrkiatimQNPRSAFnplhtMHTHAR 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 359 DDLLL--VDDVVASVESHLDNFGIIDLK---DAHPFDLSSG--QKQLVALAKIllTKPQLLLLDEPTKGIDASSK----E 427
Cdd:PRK10418 104 ETCLAlgKPADDATLTAALEAVGLENAArvlKLYPFEMSGGmlQRMMIALALL--CEAPFIIADEPTTDLDVVAQarilD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 428 FLANLIRGLSKHMTIVvaSHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK10418 182 LLESIVQKRALGMLLV--THDMGVVARLADDVAVMSHGRIVEQGDVETLFN 230
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
291-469 4.99e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 52.42  E-value: 4.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDrIGYLPQDP-------------------TTL 351
Cdd:PRK10535  23 VLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQD-VATLDADAlaqlrrehfgfifqryhllSHL 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADKV----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDA-SSK 426
Cdd:PRK10535 102 TAAQNVevpaVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDShSGE 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 427 EFLANLIRGLSKHMTIVVASHDLEfVAKISDRVAMIFNGQMES 469
Cdd:PRK10535 182 EVMAILHQLRDRGHTVIIVTHDPQ-VAAQAERVIEIRDGEIVR 223
PLN03232 PLN03232
ABC transporter C family member; Provisional
 6-211 5.69e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 52.67  E-value: 5.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    6 NFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIildeeienddtkIGFVFQNPEDQ 85
Cdd:PLN03232  621 YFSWDSKTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSSVVI------------RGSVAYVPQVS 688

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   86 LVMN-TVWHEIAFGLKNKgislkqmKRRIGEIVNYFNLQ-----------SIINKETQSLSNGQKQLVALASVMVMNPKV 153
Cdd:PLN03232  689 WIFNaTVRENILFGSDFE-------SERYWRAIDVTALQhdldllpgrdlTEIGERGVNISGGQKQRVSMARAVYSNSDI 761

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994  154 ILLDEATAQLDP-VNREEFIKILKHinDDFNVTVVFVEHQLEgLLDVANRLIVMDEGKI 211
Cdd:PLN03232  762 YIFDDPLSALDAhVAHQVFDSCMKD--ELKGKTRVLVTNQLH-FLPLMDRIILVSEGMI 817
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 285-447 7.06e-07

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: 49.86  E-value: 7.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 285 FGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC---QGEI---------SKVGCvdRIGYLPQDpttlf 352
Cdd:cd03213   18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgvSGEVlingrpldkRSFRK--IIGYVPQD----- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 vaDKVIDDLllvddvvaSVESHLDNfgiidlkDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:cd03213   91 --DILHPTL--------TVRETLMF-------AAKLRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSL 153

                        170
                 ....*....|....*.
gi 169293994 433 IRGLSK-HMTIVVASH 447
Cdd:cd03213  154 LRRLADtGRTIICSIH 169
COG4674 COG4674
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 274-459 7.78e-07

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


Pssm-ID: 443710 [Multi-domain]  Cd Length: 250  Bit Score: 50.50  E-value: 7.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFL-------RCLAGLVDCQG---------EISKVG 336
Cdd:COG4674    7 HGPILYVEDLTVSFDGfKALNDLSLYVDPGELRVIIGPNGAGKTTLMdvitgktRPDSGSVLFGGtdltgldehEIARLG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 337 cvdrIGYLPQDPT-----------------------TLFvadkviddLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSS 393
Cdd:COG4674   87 ----IGRKFQKPTvfeeltvfenlelalkgdrgvfaSLF--------ARLTAEERDRIEEVLETIGLTDKADRLAGLLSH 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 394 GQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKISDRV 459
Cdd:COG4674  155 GQKQWLEIGMLLAQDPKLLLLDEPVAGMTDAETERTAELLKSLAGKHSVVVVEHDMEFVRQIARKV 220
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 291-468 9.18e-07

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: 49.84  E-value: 9.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL--VDCqGEISKVGCVDRI-----GYLPQdpttLFVADKVIDDLLL 363
Cdd:cd03220   37 ALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIypPDS-GTVTVRGRVSSLlglggGFNPE----LTGRENIYLNGRL 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 364 VDDVVASVESHLDNfgIID---LKDAhpFDL-----SSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRG 435
Cdd:cd03220  112 LGLSRKEIDEKIDE--IIEfseLGDF--IDLpvktySSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRE 187

                        170       180       190
                 ....*....|....*....|....*....|....
gi 169293994 436 LSKH-MTIVVASHDLEFVAKISDRVAMIFNGQME 468
Cdd:cd03220  188 LLKQgKTVILVSHDPSSIKRLCDRALVLEKGKIR 221
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 18-210 9.74e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 50.88  E-value: 9.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKGDIDGVIILD-EEIENDDTK---------IGFVFQNP----- 82
Cdd:PRK09473  32 VNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNgREILNLPEKelnklraeqISMIFQDPmtsln 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  83 -----EDQLVMNTVWHeiafglknKGISLKQM---KRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVI 154
Cdd:PRK09473 112 pymrvGEQLMEVLMLH--------KGMSKAEAfeeSVRMLDAVKMPEARKRMKMYPHEFSGGMRQRVMIAMALLCRPKLL 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 155 LLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGK 210
Cdd:PRK09473 184 IADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGR 239
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
379-469 1.29e-06

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 50.29  E-value: 1.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 379 GIIDLKD---AHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKeflANLIRGLSK-----HMTIVVASHDLE 450
Cdd:COG4170  144 GIKDHKDimnSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNAMESTTQ---AQIFRLLARlnqlqGTSILLISHDLE 220

                         90       100
                 ....*....|....*....|
gi 169293994 451 FVAKISDRVAMIFNGQ-MES 469
Cdd:COG4170  221 SISQWADTITVLYCGQtVES 240
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 291-467 1.37e-06

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 49.39  E-value: 1.37e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGC--------------VDRIGYLPQD----PTtL 351
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDgSSGEVSLVGQplhqmdeearaklrAKHVGFVFQSfmliPT-L 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADKV----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKE 427
Cdd:PRK10584 104 NALENVelpaLLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGD 183

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 169293994 428 FLANLIRGLSKHM--TIVVASHDLEFVAKISDRVAMIfNGQM 467
Cdd:PRK10584 184 KIADLLFSLNREHgtTLILVTHDLQLAARCDRRLRLV-NGQL 224
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
2-212 1.49e-06

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 49.79  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   2 YKIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLL----RYFKPSlrpkgdiDGVIILDEE-IENDDTK-- 74
Cdd:PRK10575  12 FALRNVSFRVP-GRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLkmlgRHQPPS-------EGEILLDAQpLESWSSKaf 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 ---IGFVFQN---PEDQLVMNTV------WHEI--AFGLKNKgislkqmkRRIGEIVNYFNLQSIINKETQSLSNGQKQL 140
Cdd:PRK10575  84 arkVAYLPQQlpaAEGMTVRELVaigrypWHGAlgRFGAADR--------EKVEEAISLVGLKPLAHRLVDSLSGGERQR 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 141 VALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK10575 156 AWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMI 227
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 277-468 1.62e-06

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 50.88  E-value: 1.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  277 LMKVRDLNFGH----DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCL-------AGLVDCQGE-ISKVGCV---DRI 341
Cdd:TIGR00958 478 LIEFQDVSFSYpnrpDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLqnlyqptGGQVLLDGVpLVQYDHHylhRQV 557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  342 GYLPQDPTtLF---VADKV---IDDLLLVDDVVASVESHLDNF------GIIDLKDAHPFDLSSGQKQLVALAKILLTKP 409
Cdd:TIGR00958 558 ALVGQEPV-LFsgsVRENIaygLTDTPDEEIMAAAKAANAHDFimefpnGYDTEVGEKGSQLSGGQKQRIAIARALVRKP 636

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994  410 QLLLLDEPTKGIDASSKEFLANLIRglSKHMTIVVASHDLEFVAKiSDRVAMIFNGQME 468
Cdd:TIGR00958 637 RVLILDEATSALDAECEQLLQESRS--RASRTVLLIAHRLSTVER-ADQILVLKKGSVV 692
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 8-212 1.78e-06

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: 50.57  E-value: 1.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   8 SFTYPKDKK----IINNISFEIKKGDFLVITGKSGCGKTTLLR-----YfkpslRP-KGDI--DGVIILDEEIENDDTKI 75
Cdd:COG4615  334 TYRYPGEDGdegfTLGPIDLTIRRGELVFIVGGNGSGKSTLAKlltglY-----RPeSGEIllDGQPVTADNREAYRQLF 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  76 GFVFQNPE--DQLVmntvwheiafglknkGISLKQMKRRIGEIVNYFNLQ---SIINKE--TQSLSNGQKQLVALASVMV 148
Cdd:COG4615  409 SAVFSDFHlfDRLL---------------GLDGEADPARARELLERLELDhkvSVEDGRfsTTDLSQGQRKRLALLVALL 473

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 149 MNPKVILLDEATAQLDPVNR----EEFIKILKHInddfNVTVVFVEHQlEGLLDVANRLIVMDEGKIV 212
Cdd:COG4615  474 EDRPILVFDEWAADQDPEFRrvfyTELLPELKAR----GKTVIAISHD-DRYFDLADRVLKMDYGKLV 536
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 291-469 2.31e-06

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: 48.58  E-value: 2.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEISKVGcvDRIGYLPQDPTTLFVADKV------------ 357
Cdd:COG4181   27 ILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLdRPTSGTVRLAG--QDLFALDEDARARLRARHVgfvfqsfqllpt 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 -----------IDDLLLVDDVVASVEshLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSK 426
Cdd:COG4181  105 ltalenvmlplELAGRRDARARARAL--LERVGLGHRLDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATG 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 169293994 427 EFLANLIRGLSK--HMTIVVASHDLEfVAKISDRVAMIFNGQMES 469
Cdd:COG4181  183 EQIIDLLFELNRerGTTLVLVTHDPA-LAARCDRVLRLRAGRLVE 226
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
288-466 2.49e-06

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 49.42  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 288 DDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVG---------CVDRIGYLPQ----DPTtLFV 353
Cdd:PRK13537  19 DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDaGSISLCGepvpsrarhARQRVGVVPQfdnlDPD-FTV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 354 ADKVIDDLLLVDDVVASVESH---LDNFGIIDLK-DAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFL 429
Cdd:PRK13537  98 RENLLVFGRYFGLSAAAARALvppLLEFAKLENKaDAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARHLM 177

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169293994 430 ANLIRGL-SKHMTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:PRK13537 178 WERLRSLlARGKTILLTTHFMEEAERLCDRLCVIEEGR 215
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 297-453 2.76e-06

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 47.35  E-value: 2.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 297 IDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDRIGYlpqdpttlFVADKVIDdlllvddvvasveshld 376
Cdd:cd03227   16 VTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVKAGC--------IVAAVSAE----------------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 377 nFGIIDLKdahpfdLSSGQKQLVALAKILLTKPQLLLL----DEPTKGIDASSKEFLANLIRGLSKHMTIV-VASHDLEF 451
Cdd:cd03227   71 -LIFTRLQ------LSGGEKELSALALILALASLKPRPlyilDEIDRGLDPRDGQALAEAILEHLVKGAQViVITHLPEL 143


                 ..
gi 169293994 452 VA 453
Cdd:cd03227  144 AE 145
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
294-482 2.85e-06

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 49.49  E-value: 2.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 294 DLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCV--D------------RIGYLPQDpTTLFVADKVi 358
Cdd:PRK11144  16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQkGRIVLNGRVlfDaekgiclppekrRIGYVFQD-ARLFPHYKV- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 359 dDLLLVDDVVASVESHLDN----FGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSK-EFLANLI 433
Cdd:PRK11144  94 -RGNLRYGMAKSMVAQFDKivalLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKrELLPYLE 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 434 RgLSKHMT--IVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFSHNLF 482
Cdd:PRK11144 173 R-LAREINipILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAM 222
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
375-466 2.88e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 49.42  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 375 LDNFGIIDLKDA---HPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKeflANLIRGLSK-----HMTIVVAS 446
Cdd:PRK15093 140 LHRVGIKDHKDAmrsFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQ---AQIFRLLTRlnqnnNTTILLIS 216

                         90       100
                 ....*....|....*....|
gi 169293994 447 HDLEFVAKISDRVAMIFNGQ 466
Cdd:PRK15093 217 HDLQMLSQWADKINVLYCGQ 236
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 280-447 4.73e-06

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 49.04  E-value: 4.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 280 VRDLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-VDCQGEISkVGCVDRIGYLPQDP----TTLf 352
Cdd:COG4178  365 LEDLTLRTPDgrPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLwPYGSGRIA-RPAGARVLFLPQRPylplGTL- 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 vADKVIDDLLLVDDVVASVESHLDNFGIIDLKDAhpFD--------LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS 424
Cdd:COG4178  443 -REALLYPATAEAFSDAELREALEAVGLGHLAER--LDeeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEE 519

                        170       180
                 ....*....|....*....|...
gi 169293994 425 SKEFLANLIRGLSKHMTIVVASH 447
Cdd:COG4178  520 NEAALYQLLREELPGTTVISVGH 542
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 277-447 5.53e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 47.25  E-value: 5.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFG-HDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEISKVGCV---DRIGYLPQdptTL 351
Cdd:PRK13540   1 MLDVIELDFDyHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEkGEILFERQSikkDLCTYQKQ---LC 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADKVIDDLLLVDDVVASVESHLD--NFGIIDL----KDAHPFD-----LSSGQKQLVALAKILLTKPQLLLLDEPTKG 420
Cdd:PRK13540  78 FVGHRSGINPYLTLRENCLYDIHFSpgAVGITELcrlfSLEHLIDypcglLSSGQKRQVALLRLWMSKAKLWLLDEPLVA 157

                        170       180
                 ....*....|....*....|....*...
gi 169293994 421 IDASSKEFLANLIRG-LSKHMTIVVASH 447
Cdd:PRK13540 158 LDELSLLTIITKIQEhRAKGGAVLLTSH 185
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 18-193 5.69e-06

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 48.73  E-value: 5.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDID-----GVIILDEEIENDDTKIgfvfQNPEDQLVMntv 91
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPnKGTVDikgsaALIAISSGLNGQLTGI----ENIELKGLM--- 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  92 wheiafglknKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAqldpVNREEF 171
Cdd:PRK13545 113 ----------MGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALS----VGDQTF 178

                        170       180
                 ....*....|....*....|....*
gi 169293994 172 I-KILKHIND--DFNVTVVFVEHQL 193
Cdd:PRK13545 179 TkKCLDKMNEfkEQGKTIFFISHSL 203
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 26-193 5.98e-06

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: 47.75  E-value: 5.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  26 KKGDFLVITGKSGCGKTTLLRYFKPSLRP-------KGDIDGVI---------ILDEEIENDDTKigfVFQNPedQLVmn 89
Cdd:cd03236   24 REGQVLGLVGPNGIGKSTALKILAGKLKPnlgkfddPPDWDEILdefrgselqNYFTKLLEGDVK---VIVKP--QYV-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  90 tvwHEIAFGLKNKGISLKQMKRRIG---EIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPV 166
Cdd:cd03236   97 ---DLIPKAVKGKVGELLKKKDERGkldELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173

                        170       180
                 ....*....|....*....|....*..
gi 169293994 167 NREEFIKILKHINDDFNVTVVfVEHQL 193
Cdd:cd03236  174 QRLNAARLIRELAEDDNYVLV-VEHDL 199
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 1-169 6.95e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.79  E-value: 6.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   1 MYKIENFSFTYpkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRPKgdiDGVIILDEEIENDDTK--IGFV 78
Cdd:PRK13541   1 MLSLHQLQFNI--EQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPS---SGNIYYKNCNINNIAKpyCTYI 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  79 FQNPEDQLVMnTVWHEIAFGLKnkgisLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDE 158
Cdd:PRK13541  76 GHNLGLKLEM-TVFENLKFWSE-----IYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149

                        170
                 ....*....|.
gi 169293994 159 ATAQLDPVNRE 169
Cdd:PRK13541 150 VETNLSKENRD 160
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 301-478 8.60e-06

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 47.81  E-value: 8.60e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 301 ENEILSIVGANGSGKSSFLRCLAGLVDCQGEISK---------------------VGCvdRIGYLPQDPTT--------- 350
Cdd:PRK11022  32 QGEVVGIVGESGSGKSVSSLAIMGLIDYPGRVMAeklefngqdlqrisekerrnlVGA--EVAMIFQDPMTslnpcytvg 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 --LFVADKVIDDLLLVDDVVASVEShLDNFGIIDLK---DAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASS 425
Cdd:PRK11022 110 fqIMEAIKVHQGGNKKTRRQRAIDL-LNQVGIPDPAsrlDVYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTI 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 426 KEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREFFS 478
Cdd:PRK11022 189 QAQIIELLLELQQkeNMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFR 243
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 274-324 1.02e-05

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 46.94  E-value: 1.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169293994 274 NRILMKVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAG 324
Cdd:CHL00131   4 NKPILEIKNLHASVNENeILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG 55
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 277-450 1.07e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 46.40  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV----------DCQ-GEISKVGCVdRIGYLP 345
Cdd:PRK13541   1 MLSLHQLQFNIEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMqpssgniyykNCNiNNIAKPYCT-YIGHNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 346 QDPTTLFVADKvIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASS 425
Cdd:PRK13541  80 GLKLEMTVFEN-LKFWSEIYNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKEN 158

                        170       180
                 ....*....|....*....|....*
gi 169293994 426 KEFLANLIRGLSKHMTIVVASHDLE 450
Cdd:PRK13541 159 RDLLNNLIVMKANSGGIVLLSSHLE 183
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
287-479 1.10e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 46.93  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 287 HDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD----CQGEISKVG-CVDRIGYLPQD-------------- 347
Cdd:PRK09984  15 NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELLGrTVQREGRLARDirksrantgyifqq 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 ---PTTLFVADKVIDDLLLVD------------DVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLL 412
Cdd:PRK09984  95 fnlVNRLSVLENVLIGALGSTpfwrtcfswftrEQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVI 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 413 LLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMI------FNGQMESVDSTRefFSH 479
Cdd:PRK09984 175 LADEPIASLDPESARIVMDTLRDINQNdgITVVVTLHQVDYALRYCERIVALrqghvfYDGSSQQFDNER--FDH 247
PLN03130 PLN03130
ABC transporter C family member; Provisional
 291-478 1.14e-05

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 48.20  E-value: 1.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEI-------SKVGCVD---RIGYLPQDPTtLFvadkvid 359
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELErGRIlidgcdiSKFGLMDlrkVLGIIPQAPV-LF------- 1325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  360 dlllvddvVASVESHLDNFG------------IIDLKDA---HPFDL-----------SSGQKQLVALAKILLTKPQLLL 413
Cdd:PLN03130 1326 --------SGTVRFNLDPFNehndadlwesleRAHLKDVirrNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILV 1397

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994  414 LDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTREFFS 478
Cdd:PLN03130 1398 LDEATAAVDVRTDALIQKTIREEFKSCTMLIIAHRLNTIID-CDRILVLDAGRVVEFDTPENLLS 1461
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
123-212 1.36e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 47.60  E-value: 1.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 123 QSIINketqsLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANR 202
Cdd:PRK11288 392 QLIMN-----LSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADR 465

                         90
                 ....*....|
gi 169293994 203 LIVMDEGKIV 212
Cdd:PRK11288 466 IVVMREGRIA 475
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
277-333 1.41e-05

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 45.95  E-value: 1.41e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 277 LMKVRDLNFGHDDIVL-KDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEIS 333
Cdd:PRK13538   1 MLEARNLACERDERILfSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPdAGEVL 59
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 2-46 1.51e-05

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 47.64  E-value: 1.51e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 169293994   2 YKIENFSFTYPkDKKIINNISFEIKKGDFLVITGKSGCGKTTLLR 46
Cdd:PRK11147 320 FEMENVNYQID-GKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLK 363
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 274-467 1.67e-05

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 47.51  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEISKVGCV----------D 339
Cdd:PRK11160 335 DQVSLTLNNVSFTYPDqpqPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPqQGEILLNGQPiadyseaalrQ 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 340 RIGYLPQDP----TTL-----FVADKVIDDLLLVDDVVASVESHLDnfgiidlkDAHPFD---------LSSGQKQLVAL 401
Cdd:PRK11160 415 AISVVSQRVhlfsATLrdnllLAAPNASDEALIEVLQQVGLEKLLE--------DDKGLNawlgeggrqLSGGEQRRLGI 486

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 402 AKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKIsDRVAMIFNGQM 467
Cdd:PRK11160 487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTVLMITHRLTGLEQF-DRICVMDNGQI 551
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 14-164 1.80e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 47.42  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYfkpslrpkgdIDGVIILDE-EIENDDT-KIGFVFQNPEDQLVMNTV 91
Cdd:PRK11819 336 DRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKM----------ITGQEQPDSgTIKIGETvKLAYVDQSRDALDPNKTV 405

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994  92 WHEIAFGLKNKGISLKQMKRRigEIVNYFNL----QsiiNKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLD 164
Cdd:PRK11819 406 WEEISGGLDIIKVGNREIPSR--AYVGRFNFkggdQ---QKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 291-465 1.97e-05

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: 47.60  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEISKVGcvdRIGYLPQDPTTL--FVADKVIDDLLLVDDV 367
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGeLEPSEGKIKHSG---RISFSPQTSWIMpgTIKDNIIFGLSYDEYR 517

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   368 VASVESHL---DNFGIIDLKDAHPF-----DLSSGQKQLVALAKILLTKPQLLLLDEPTKGID-ASSKEFLANLIRGLSK 438
Cdd:TIGR01271  518 YTSVIKACqleEDIALFPEKDKTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDvVTEKEIFESCLCKLMS 597

                          170       180
                   ....*....|....*....|....*..
gi 169293994   439 HMTIVVASHDLEFVAKiSDRVAMIFNG 465
Cdd:TIGR01271  598 NKTRILVTSKLEHLKK-ADKILLLHEG 623
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-212 2.10e-05

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 46.94  E-value: 2.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   3 KIENFSFTYPKDKKIINNISFEIKKGDFLVITGKSGCGKTTL------LRyfKPSlrpKGDIdgvIILDEEIENDDTK-- 74
Cdd:COG3845  259 EVENLSVRDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELaealagLR--PPA---SGSI---RLDGEDITGLSPRer 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  75 ----IGFVfqnPEDQ----LVMN-TVWHEIAFG------LKNKG-ISLKQMKRRIGEIVNYFNLQSI-INKETQSLSNGQ 137
Cdd:COG3845  331 rrlgVAYI---PEDRlgrgLVPDmSVAENLILGryrrppFSRGGfLDRKAIRAFAEELIEEFDVRTPgPDTPARSLSGGN 407

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 169293994 138 KQLVALASVMVMNPKVILLDEATAQLDpVNREEFI--KILKHINDdfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:COG3845  408 QQKVILARELSRDPKLLIAAQPTRGLD-VGAIEFIhqRLLELRDA--GAAVLLISEDLDEILALSDRIAVMYEGRIV 481
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 291-467 2.14e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 46.04  E-value: 2.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLV--DC------QGEISKVGCVDR----IGYLPQDPTT---LFVAD 355
Cdd:PRK10895  18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVprDAgniiidDEDISLLPLHARarrgIGYLPQEASIfrrLSVYD 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 356 KV-----IDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLA 430
Cdd:PRK10895  98 NLmavlqIRDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVIDIK 177

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169293994 431 NLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK10895 178 RIIEHLRDSgLGVLITDHNVRETLAVCERAYIVSQGHL 215
PLN03211 PLN03211
ABC transporter G-25; Provisional
 303-467 2.47e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.80  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 303 EILSIVGANGSGKSSFLRCLAGLVDCQGEISKV---------GCVDRIGYLPQD----------PTTLFVADKVIDDLLL 363
Cdd:PLN03211  95 EILAVLGPSGSGKSTLLNALAGRIQGNNFTGTIlannrkptkQILKRTGFVTQDdilyphltvrETLVFCSLLRLPKSLT 174

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 364 VDDVVASVESHLDNFGIIDLKD---AHPF--DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLS- 437
Cdd:PLN03211 175 KQEKILVAESVISELGLTKCENtiiGNSFirGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAq 254

                        170       180       190
                 ....*....|....*....|....*....|
gi 169293994 438 KHMTIVVASHdlefvaKISDRVAMIFNGQM 467
Cdd:PLN03211 255 KGKTIVTSMH------QPSSRVYQMFDSVL 278
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 17-209 2.92e-05

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: 46.83  E-value: 2.92e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    17 IINNISFEIKKGDFLVITGKSGCGKTTLLryfkpslrpkgdidgVIILDeEIENDDTKI---GFVFQNPEDQLVM-NTVW 92
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLL---------------MMIMG-ELEPSEGKIkhsGRISFSPQTSWIMpGTIK 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    93 HEIAFGLK------NKGISLKQMKRRIGEIVNYFNlqSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPV 166
Cdd:TIGR01271  505 DNIIFGLSydeyryTSVIKACQLEEDIALFPEKDK--TVLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHLDVV 582

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 169293994   167 NREEFI-----KILKhinddfNVTVVFVEHQLEGlLDVANRLIVMDEG 209
Cdd:TIGR01271  583 TEKEIFesclcKLMS------NKTRILVTSKLEH-LKKADKILLLHEG 623
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
133-212 3.39e-05

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 45.95  E-value: 3.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 133 LSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTV 238
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 286-466 4.37e-05

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: 44.91  E-value: 4.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 286 GHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDC-QGEIskvgCVD--------------RIGYLPQDpTT 350
Cdd:cd03251   12 GDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVdSGRI----LIDghdvrdytlaslrrQIGLVSQD-VF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 351 LF---VADKVI---DDLLLVDDVVASVESHLDNFgIIDLKDAhpFD---------LSSGQKQLVALAKILLTKPQLLLLD 415
Cdd:cd03251   87 LFndtVAENIAygrPGATREEVEEAARAANAHEF-IMELPEG--YDtvigergvkLSGGQRQRIAIARALLKDPPILILD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 169293994 416 EPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQ 466
Cdd:cd03251  164 EATSALDTESERLVQAALERLMKNRTTFVIAHRLSTIEN-ADRIVVLEDGK 213
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 291-333 4.38e-05

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 45.07  E-value: 4.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGEIS 333
Cdd:COG1134   41 ALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGIleptsgrVEVNGRVS 90
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
281-423 4.55e-05

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 45.79  E-value: 4.55e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 281 RDLNFGHDDIVL-KDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEI-------SKVGCVDR-IGYLPQD--- 347
Cdd:PRK11000   7 RNVTKAYGDVVIsKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDiTSGDLfigekrmNDVPPAERgVGMVFQSyal 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 348 -PTtLFVADKVIDDLLLVDDVVASVESHLDNFGIIdLKDAH-----PFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGI 421
Cdd:PRK11000  87 yPH-LSVAENMSFGLKLAGAKKEEINQRVNQVAEV-LQLAHlldrkPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNL 164


                 ..
gi 169293994 422 DA 423
Cdd:PRK11000 165 DA 166
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 290-332 4.59e-05

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 45.08  E-value: 4.59e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 169293994 290 IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG--LVDcQGEI 332
Cdd:COG1101   20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGslPPD-SGSI 63
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 16-228 4.83e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 45.88  E-value: 4.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  16 KIINNISFEIKKGDFLVITGKSGCGKTTLLR-YFKPSLRPKGDIdgvIILDEEIENDDTK------IGFVFQNPEDQL-- 86
Cdd:PRK10982  12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKcLFGIYQKDSGSI---LFQGKEIDFKSSKealengISMVHQELNLVLqr 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  87 -VMNTVWHEiAFGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDP 165
Cdd:PRK10982  89 sVMDNMWLG-RYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTE 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 166 VNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV---------IDNEIKMAVDEMLTKK 228
Cdd:PRK10982 168 KEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIatqplagltMDKIIAMMVGRSLTQR 238
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 133-467 4.96e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 45.76  E-value: 4.96e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 133 LSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:PRK10762 142 LSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQFI 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 213 I---------DNEIKMAVDEMLTKKifveslpnYVRVSSLCDKLCLSIKEAREALVNFENFDIKimdeidnrilmkvrdl 283
Cdd:PRK10762 221 AerevadlteDSLIEMMVGRKLEDQ--------YPRLDKAPGEVRLKVDNLSGPGVNDVSFTLR---------------- 276

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 284 nfghddivlkdleidilENEILSIVGANGSGKSSFLRCLAG-LVDCQGEISKVGCV-------------------DRIG- 342
Cdd:PRK10762 277 -----------------KGEILGVSGLMGAGRTELMKVLYGaLPRTSGYVTLDGHEvvtrspqdglangivyiseDRKRd 339

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 343 ------------------YLPQDPTTLFVADKVIddlllvddvvaSVESHLDNFGI--------IDLkdahpfdLSSGQK 396
Cdd:PRK10762 340 glvlgmsvkenmsltalrYFSRAGGSLKHADEQQ-----------AVSDFIRLFNIktpsmeqaIGL-------LSGGNQ 401

                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 397 QLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEgLSIILVSSEMPEVLGMSDRILVMHEGRI 473
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 278-459 6.42e-05

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 43.47  E-value: 6.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHddivLKDLEIDILENEILSIVGANGSGKSSFlrclaglvdCQGEISKVGCVDRIGYLPqdpttLFVADKV 357
Cdd:cd03238    1 LTVSGANVHN----LQNLDVSIPLNVLVVVTGVSGSGKSTL---------VNEGLYASGKARLISFLP-----KFSRNKL 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 358 IDDLLLvddvvasveSHLDNFGIIDLKDAHPFD-LSSGQKQLVALAKILLTKPQLLL--LDEPTKGIDASSKEFLANLIR 434
Cdd:cd03238   63 IFIDQL---------QFLIDVGLGYLTLGQKLStLSGGELQRVKLASELFSEPPGTLfiLDEPSTGLHQQDINQLLEVIK 133

                        170       180
                 ....*....|....*....|....*.
gi 169293994 435 GL-SKHMTIVVASHDLEFVaKISDRV 459
Cdd:cd03238  134 GLiDLGNTVILIEHNLDVL-SSADWI 158
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 277-471 7.23e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 45.55  E-value: 7.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEISKVGCVdRIGYLPQDPTTLFVA 354
Cdd:PRK10636 312 LLKMEKVSAGYGDrIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGeLAPVSGEIGLAKGI-KLGYFAQHQLEFLRA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 355 DKVI---DDLLLVDDVVASVESHLDNFGIIDLKDAHPFD-LSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLA 430
Cdd:PRK10636 391 DESPlqhLARLAPQELEQKLRDYLGGFGFQGDKVTEETRrFSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALT 470

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 169293994 431 NLIrgLSKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVD 471
Cdd:PRK10636 471 EAL--IDFEGALVVVSHDRHLLRSTTDDLYLVHDGKVEPFD 509
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 106-348 7.28e-05

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: 45.39  E-value: 7.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  106 LKQMKRRIGEIVN----YFNLQSIINketqSLSNGQKQLVALAS------VMVMnpkvILLDEATAQLDPVNREEFIKIL 175
Cdd:TIGR00630 462 LKEIRERLGFLIDvgldYLSLSRAAG----TLSGGEAQRIRLATqigsglTGVL----YVLDEPSIGLHQRDNRRLINTL 533

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  176 KHINDDFNvTVVFVEHQLEGLLdVANRLIVMDE------GKIVIDNEIK--MAVDEMLT-------KKIFVESlpnyVRV 240
Cdd:TIGR00630 534 KRLRDLGN-TLIVVEHDEDTIR-AADYVIDIGPgagehgGEVVASGTPEeiLANPDSLTgqylsgrKKIEVPA----ERR 607

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  241 SSlcDKLCLSIKEAREalvnfenfdikimdeidnrilmkvrdlnfgHDdivLKDLEIDILENEILSIVGANGSGKSSFL- 319
Cdd:TIGR00630 608 PG--NGKFLTLKGARE------------------------------NN---LKNITVSIPLGLFTCITGVSGSGKSTLIn 652

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 169293994  320 ----RCL------AGLVDCQG-EISKVGCVDRIGYLPQDP 348
Cdd:TIGR00630 653 dtlyPALanrlngAKTVPGRYtSIEGLEHLDKVIHIDQSP 692
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 415-467 8.56e-05

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 44.69  E-value: 8.56e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 415 DEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQM 467
Cdd:COG4586  179 DEPTIGLDVVSKEAIREFLKEYNRerGTTILLTSHDMDDIEALCDRVIVIDHGRI 233
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 278-488 9.26e-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: 44.46  E-value: 9.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCV----------DRIGYL 344
Cdd:cd03289    3 MTVKDLTAKYTEggnAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTEGDIQIDGVSwnsvplqkwrKAFGVI 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 PQ--------------------DPTTLFVADKViddlllvddvvaSVESHLDNF-GIID--LKDAHpFDLSSGQKQLVAL 401
Cdd:cd03289   83 PQkvfifsgtfrknldpygkwsDEEIWKVAEEV------------GLKSVIEQFpGQLDfvLVDGG-CVLSHGHKQLMCL 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 402 AKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDSTREFFSHNL 481
Cdd:cd03289  150 ARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQKLLNEKS 228


                 ....*..
gi 169293994 482 FYTTTIN 488
Cdd:cd03289  229 HFKQAIS 235
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 30-113 1.16e-04

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 44.01  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  30 FLVITGKSGCGKTTLLRYFKPSLrpkgdidgviildeeieNDDTKIGFVFqNPedQLVMNTVWHEIA--FGLKNKGISLK 107
Cdd:COG3267   45 FVVLTGEVGTGKTTLLRRLLERL-----------------PDDVKVAYIP-NP--QLSPAELLRAIAdeLGLEPKGASKA 104


                 ....*.
gi 169293994 108 QMKRRI 113
Cdd:COG3267  105 DLLRQL 110
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 285-466 1.23e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 44.45  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 285 FGHDDIVLKD-LEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEIsKVGCVD-----------RIGYLPQDPtTLF 352
Cdd:PRK11174 358 LSPDGKTLAGpLNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPYQGSL-KINGIElreldpeswrkHLSWVGQNP-QLP 435

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 ---VADKVIddLLLVDDVVASVESHLDNFGIIDLKDAHP--FD---------LSSGQKQLVALAKILLTKPQLLLLDEPT 418
Cdd:PRK11174 436 hgtLRDNVL--LGNPDASDEQLQQALENAWVSEFLPLLPqgLDtpigdqaagLSVGQAQRLALARALLQPCQLLLLDEPT 513

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 169293994 419 KGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKIsDRVAMIFNGQ 466
Cdd:PRK11174 514 ASLDAHSEQLVMQALNAASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQ 560
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
14-46 1.34e-04

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 43.25  E-value: 1.34e-04
                         10        20        30
                 ....*....|....*....|....*....|...
gi 169293994  14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLR 46
Cdd:PRK13538  13 ERILFSGLSFTLNAGELVQIEGPNGAGKTSLLR 45
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 299-348 1.39e-04

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 44.34  E-value: 1.39e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 299 ILENEILS--------IVGANGSGKSSFLRCLAGL-VDCQGE------IskvgcvdRIGYLPQDP 348
Cdd:PRK11819  22 ILKDISLSffpgakigVLGLNGAGKSTLLRIMAGVdKEFEGEarpapgI-------KVGYLPQEP 79
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 284-446 1.63e-04

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: 43.03  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 284 NFGHDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG-----------EISKVGCVDRIGYLPQDPTTL- 351
Cdd:cd03234   15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGttsgqilfngqPRKPDQFQKCVAYVRQDDILLp 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 ---------FVADKVIDDLLLVDDVVASVEShldnFGIIDLKD---AHPF--DLSSGQKQLVALAKILLTKPQLLLLDEP 417
Cdd:cd03234   95 gltvretltYTAILRLPRKSSDAIRKKRVED----VLLRDLALtriGGNLvkGISGGERRRVSIAVQLLWDPKVLILDEP 170

                        170       180
                 ....*....|....*....|....*....
gi 169293994 418 TKGIDASSKEFLANLIRGLSKHMTIVVAS 446
Cdd:cd03234  171 TSGLDSFTALNLVSTLSQLARRNRIVILT 199
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 277-466 1.65e-04

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 43.38  E-value: 1.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDL--NFGHDdIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQ-GEIS------------KVGCVDR- 340
Cdd:PRK11701   6 LLSVRGLtkLYGPR-KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDaGEVHyrmrdgqlrdlyALSEAERr 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 341 ------IGYLPQDPttlfvAD----KVIDDLLLVDDVVASVESHLDNfgI------------IDLK--DAHPFDLSSGQK 396
Cdd:PRK11701  85 rllrteWGFVHQHP-----RDglrmQVSAGGNIGERLMAVGARHYGD--IratagdwlerveIDAAriDDLPTTFSGGMQ 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 397 QLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSK--HMTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRelGLAVVIVTHDLAVARLLAHRLLVMKQGR 229
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 292-480 1.70e-04

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: 44.55  E-value: 1.70e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVD-CQGEISKVGCVdriGYLPQDP---------TTLF---VADKVI 358
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDkVEGHVHMKGSV---AYVPQQAwiqndslreNILFgkaLNEKYY 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   359 DDLLLVDDVVASVE-------SHLDNFGIidlkdahpfDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS-SKEFLA 430
Cdd:TIGR00957  731 QQVLEACALLPDLEilpsgdrTEIGEKGV---------NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHvGKHIFE 801

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 169293994   431 NLI--RGLSKHMTIVVASHDLEFVAKIsDRVAMIFNGQMESVDSTREFFSHN 480
Cdd:TIGR00957  802 HVIgpEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQRD 852
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 17-209 2.04e-04

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: 43.31  E-value: 2.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  17 IINNISFEIKKGDFLVITGKSGCGKTTLLryfkpslrpkgdidgVIILDeEIENDDTKI---GFVFQNPEDQLVM-NTVW 92
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLL---------------MLILG-ELEPSEGKIkhsGRISFSSQFSWIMpGTIK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  93 HEIAFGLKNKgislkqmKRRIGEIVNYFNLQSIINKETQ-----------SLSNGQKQLVALASVMVMNPKVILLDEATA 161
Cdd:cd03291  116 ENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEkdntvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFG 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 169293994 162 QLDPVNREEFI-----KILKhinddfNVTVVFVEHQLEGlLDVANRLIVMDEG 209
Cdd:cd03291  189 YLDVFTEKEIFescvcKLMA------NKTRILVTSKMEH-LKKADKILILHEG 234
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 112-204 2.11e-04

ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a tight junction-associated protein expressed in rat epithelial cells which is thought to have an important regulatory role in tight junction barrier function. Barmotin belongs to the SMC protein family. SMC proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 42.45  E-value: 2.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 112 RIGEIVNYFN--LQSIinketQSLSNGQKQLVALA---SVMVMNPKVI-LLDEATAQLDPVNREEFIKILKHINDD--Fn 183
Cdd:cd03278   96 DVSEIIEAPGkkVQRL-----SLLSGGEKALTALAllfAIFRVRPSPFcVLDEVDAALDDANVERFARLLKEFSKEtqF- 169

                         90       100
                 ....*....|....*....|.
gi 169293994 184 vtvVFVEHQlEGLLDVANRLI 204
Cdd:cd03278  170 ---IVITHR-KGTMEAADRLY 186
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 291-499 2.49e-04

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: 42.92  E-value: 2.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEISKVGcvdRIGYLPQD----PTTlfVADKVIDDLLLVD 365
Cdd:cd03291   52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGeLEPSEGKIKHSG---RISFSSQFswimPGT--IKENIIFGVSYDE 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 366 DVVASV------ESHLDNFGiidLKDAHPF-----DLSSGQKQLVALAKILLTKPQLLLLDEPTKGID-ASSKEFLANLI 433
Cdd:cd03291  127 YRYKSVvkacqlEEDITKFP---EKDNTVLgeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDvFTEKEIFESCV 203

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169293994 434 RGLSKHMTIVVASHDLEFVaKISDRVAMI------FNGQMESVDSTREFFSHNLFYTTTINKIMRENNPEVI 499
Cdd:cd03291  204 CKLMANKTRILVTSKMEHL-KKADKILILhegssyFYGTFSELQSLRPDFSSKLMGYDTFDQFSAERRNSIL 274
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 301-459 2.54e-04

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: 42.74  E-value: 2.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 301 ENEILSIVGANGSGKSSFLRCLAG-----LVDCQGEIS-----------------------KVGCVDRIGYLPQDPTTlf 352
Cdd:cd03236   25 EGQVLGLVGPNGIGKSTALKILAGklkpnLGKFDDPPDwdeildefrgselqnyftkllegDVKVIVKPQYVDLIPKA-- 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKVIDDLLLVDDVVAsVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANL 432
Cdd:cd03236  103 VKGKVGELLKKKDERGK-LDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAARL 181

                        170       180
                 ....*....|....*....|....*...
gi 169293994 433 IRGLSKHM-TIVVASHDLEFVAKISDRV 459
Cdd:cd03236  182 IRELAEDDnYVLVVEHDLAVLDYLSDYI 209
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
379-466 3.22e-04

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 42.26  E-value: 3.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 379 GIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL--SKHMTIVVASHDLEFVAKIS 456
Cdd:PRK10771 118 GIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVcqERQLTLLMVSHSLEDAARIA 197

                         90
                 ....*....|
gi 169293994 457 DRVAMIFNGQ 466
Cdd:PRK10771 198 PRSLVVADGR 207
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 133-206 3.35e-04

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 41.19  E-value: 3.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 133 LSNGQKQLVALASVM----VMNPKVILLDEATAQLDPVNREEFIKILKHINDDFNvTVVFVEHQLEgLLDVANRLIVM 206
Cdd:cd03227   78 LSGGEKELSALALILalasLKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGA-QVIVITHLPE-LAELADKLIHI 153
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 274-465 3.79e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 42.28  E-value: 3.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 274 NRILMKVRDLN--FGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCL-------AGLVDCQGE---------ISKV 335
Cdd:PRK11300   2 SQPLLSVSGLMmrFG-GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLtgfykptGGTILLRGQhieglpghqIARM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 336 GCVDRIGY--LPQDPTT---LFVAD-------------KVIDDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQ 397
Cdd:PRK11300  81 GVVRTFQHvrLFREMTVienLLVAQhqqlktglfsgllKTPAFRRAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 398 LVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRVAMIFNG 465
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhnVTVLLIEHDMKLVMGISDRIYVVNQG 230
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
277-422 4.43e-04

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 41.76  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGL-------VDCQGEISKVGCVDR----IGYL 344
Cdd:PRK13543  11 LLAAHALAFSRNEEpVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLlhvesgqIQIDGKTATRGDRSRfmayLGHL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 345 P---QDPTTLFVADKVIDDLLLVDDVVASveSHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGI 421
Cdd:PRK13543  91 PglkADLSTLENLHFLCGLHGRRAKQMPG--SALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANL 168


                 .
gi 169293994 422 D 422
Cdd:PRK13543 169 D 169
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 283-459 5.47e-04

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 42.63  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 283 LNFGhDDIVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG---LVDCQGEISKVGCVDRigyLPQDPT-----TLF-- 352
Cdd:PRK11147  11 LSFS-DAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGevlLDDGRIIYEQDLIVAR---LQQDPPrnvegTVYdf 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 353 VADKV------------------IDDLLLVDDVVASVESHLDNFGIIDLK--------------DAHPFDLSSGQKQLVA 400
Cdd:PRK11147  87 VAEGIeeqaeylkryhdishlveTDPSEKNLNELAKLQEQLDHHNLWQLEnrinevlaqlgldpDAALSSLSGGWLRKAA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 169293994 401 LAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKhmTIVVASHDLEFVAKISDRV 459
Cdd:PRK11147 167 LGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQG--SIIFISHDRSFIRNMATRI 223
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
278-323 5.61e-04

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 41.91  E-value: 5.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 169293994 278 MKVRDL---NFGHddivLKDLEIDILENE-ILSIVGANGSGKSSFLRCLA 323
Cdd:COG3950    1 MRIKSLtieNFRG----FEDLEIDFDNPPrLTVLVGENGSGKTTLLEAIA 46
PLN03232 PLN03232
ABC transporter C family member; Provisional
 292-494 5.84e-04

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 42.66  E-value: 5.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  292 LKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDcQGEISKVGCVDRIGYLPQDP--------TTLFVADKVIDDLLL 363
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELS-HAETSSVVIRGSVAYVPQVSwifnatvrENILFGSDFESERYW 711

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  364 VDDVVASVESHLDNFGIIDLKD--AHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDAS-SKEFLANLIRGLSKHM 440
Cdd:PLN03232  712 RAIDVTALQHDLDLLPGRDLTEigERGVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHvAHQVFDSCMKDELKGK 791

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 169293994  441 TIVVASHDLEFVAKIsDRVAMIFNGQMESVDSTREffshnLFYTTTINKIMREN 494
Cdd:PLN03232  792 TRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAE-----LSKSGSLFKKLMEN 839
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
18-211 6.38e-04

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 41.73  E-value: 6.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKPSLRP-KGDIDgviildeeiENDDTKIGFVFQNPEDQLvmnTVWHEIA 96
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPtVGKVD---------RNGEVSVIAISAGLSGQL---TGIENIE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  97 FGLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAqldpVNREEFI-KIL 175
Cdd:PRK13546 108 FKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALS----VGDQTFAqKCL 183

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 169293994 176 KHIND--DFNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK13546 184 DKIYEfkEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKL 221
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
277-466 1.09e-03

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 40.90  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 277 LMKVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEI------------SKVGCV-DRI 341
Cdd:PRK11831   7 LVDMRGVSFTRGNrCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGqIAPDHGEIlfdgenipamsrSRLYTVrKRM 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 342 GYLPQDP---TTLFVADKVI-----DDLLLVDDVVASVESHLDNFGIIDLKDAHPFDLSSGQKQLVALAKILLTKPQLLL 413
Cdd:PRK11831  87 SMLFQSGalfTDMNVFDNVAyplreHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 169293994 414 LDEPTKGIDASSKEFLANLIRGLSKH--MTIVVASHDLEFVAKISDRvAMIFNGQ 466
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSAlgVTCVVVSHDVPEVLSIADH-AYIVADK 220
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 278-503 1.30e-03

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: 41.82  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   278 MKVRDLNFGHDD---IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCV----------DRIGYL 344
Cdd:TIGR01271 1218 MDVQGLTAKYTEagrAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTEGEIQIDGVSwnsvtlqtwrKAFGVI 1297

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   345 PQ-------------DPTTLFvADKVIDDLLLVDDVVASVESHLD--NFGIIDlkdaHPFDLSSGQKQLVALAKILLTKP 409
Cdd:TIGR01271 1298 PQkvfifsgtfrknlDPYEQW-SDEEIWKVAEEVGLKSVIEQFPDklDFVLVD----GGYVLSNGHKQLMCLARSILSKA 1372

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   410 QLLLLDEPTKGIDASSKEFLANLIRGLSKHMTIVVASHDLEFVAKiSDRVAMIFNGQMESVDST----------REFFSH 479
Cdd:TIGR01271 1373 KILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTVILSEHRVEALLE-CQQFLVIEGSSVKQYDSIqkllnetslfKQAMSA 1451

                          250       260
                   ....*....|....*....|....*...
gi 169293994   480 ----NLFYTTTINKIMRENNPEVILLED 503
Cdd:TIGR01271 1452 adrlKLFPLHRRNSSKRKPQPKITALRE 1479
AAA_22 pfam13401
AAA domain;
30-197 1.30e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 38.86  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   30 FLVITGKSGCGKTTLLRYFkpslrpkgdidgviiLDEEIENDDTKIGFVFQNPEDQlvmNTVWHEIAFGL---KNKGISL 106
Cdd:pfam13401   7 ILVLTGESGTGKTTLLRRL---------------LEQLPEVRDSVVFVDLPSGTSP---KDLLRALLRALglpLSGRLSK 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  107 KQMKRRIgeivnyfnlqsiinketqslsngQKQLVALASvmvmnPKVILLDEatAQLDPVNREEFIKILkHINDDFNVTV 186
Cdd:pfam13401  69 EELLAAL-----------------------QQLLLALAV-----AVVLIIDE--AQHLSLEALEELRDL-LNLSSKLLQL 117

                         170
                  ....*....|..
gi 169293994  187 VFV-EHQLEGLL 197
Cdd:pfam13401 118 ILVgTPELRELL 129
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 14-164 1.45e-03

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 41.63  E-value: 1.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    14 DKKIINNISFEIKKGDFLVITGKSGCGKTTLLRYFkpSLRPKGdidGVIILDEEIEN----DDT---KIGFVFQNpEDQL 86
Cdd:TIGR00956  775 KRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVL--AERVTT---GVITGGDRLVNgrplDSSfqrSIGYVQQQ-DLHL 848

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    87 VMNTVWHEI---AFGLKNKGISLKQMKRRIGEIVNYFNLQS----IINKETQSLSNGQKQLVALASVMVMNPKVIL-LDE 158
Cdd:TIGR00956  849 PTSTVRESLrfsAYLRQPKSVSKSEKMEYVEEVIKLLEMESyadaVVGVPGEGLNVEQRKRLTIGVELVAKPKLLLfLDE 928


                   ....*.
gi 169293994   159 ATAQLD 164
Cdd:TIGR00956  929 PTSGLD 934
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 296-443 1.51e-03

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 41.15  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 296 EIDILENEILSIVGANGSGKSSFLRCLAG-LVDCQGEisKVGCVDRIGYL-----------------------PQDPTTL 351
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGeLPLLSGE--RQSQFSHITRLsfeqlqklvsdewqrnntdmlspGEDDTGR 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 352 FVADkVIDdlllvddvvasvESHLDN---------FGIIDLKDaHPFD-LSSGQKQLVALAKILLTKPQLLLLDEPTKGI 421
Cdd:PRK10938 101 TTAE-IIQ------------DEVKDParceqlaqqFGITALLD-RRFKyLSTGETRKTLLCQALMSEPDLLILDEPFDGL 166

                        170       180
                 ....*....|....*....|...
gi 169293994 422 DASSKEFLANLIRGLSKH-MTIV 443
Cdd:PRK10938 167 DVASRQQLAELLASLHQSgITLV 189
GguA NF040905
sugar ABC transporter ATP-binding protein;
390-466 1.55e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 1.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 390 DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGLSKH-MTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:NF040905 139 DIGVGKQQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQgITSIIISHKLNEIRRVADSITVLRDGR 216
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 18-211 1.61e-03

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.87  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  18 INNISFEIKKGDFLVITGKSGCGKTTLLRYFKpSLRPKGDidGVIIL-DEEIENDDT----KIGFVFQNPE--------- 83
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLF-GIREKSA--GTITLhGKKINNHNAneaiNHGFALVTEErrstgiyay 340

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  84 -----DQLVMNTVWHEIAFGLknkgISLKQMKRRIGEIVNYFNLQSIINKET-QSLSNGQKQLVALASVMVMNPKVILLD 157
Cdd:PRK10982 341 ldigfNSLISNIRNYKNKVGL----LDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLD 416

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169293994 158 EATAQLDPVNREEFIKILKHINDDfNVTVVFVEHQLEGLLDVANRLIVMDEGKI 211
Cdd:PRK10982 417 EPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 291-476 1.80e-03

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 40.80  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 291 VLKDLEIDILENEILSIVGANGSGKSSFLRCLAGLVDCQG---EISKVGCVD-------RIG-YL-PQDP---TTLFVAD 355
Cdd:PRK15439  26 VLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSgtlEIGGNPCARltpakahQLGiYLvPQEPllfPNLSVKE 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 356 KVIDDLLLVDDVVASVESHLDNFGI-IDLkDAHPFDLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIR 434
Cdd:PRK15439 106 NILFGLPKRQASMQKMKQLLAALGCqLDL-DSSAGSLEVADRQIVEILRGLMRDSRILILDEPTASLTPAETERLFSRIR 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 169293994 435 GL-SKHMTIVVASHDLEFVAKISDRVAMIFNGQMESVDSTREF 476
Cdd:PRK15439 185 ELlAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 279-324 1.93e-03

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 40.05  E-value: 1.93e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 279 KVRDLNFGHDD-IVLKDLEIDILENEILSIVGANGSGKSSFLRCLAG 324
Cdd:COG0396    2 EIKNLHVSVEGkEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMG 48
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 303-325 1.99e-03

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: 40.55  E-value: 1.99e-03
                         10        20
                 ....*....|....*....|...
gi 169293994 303 EILSIVGANGSGKSSFLRCLAGL 325
Cdd:COG4615  359 ELVFIVGGNGSGKSTLAKLLTGL 381
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 27-205 2.18e-03

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: 38.89  E-value: 2.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    27 KGDFLVITGKSGCGKTTLLRYFKPSLRPKGDidGVIILDEEienddtkigfvfqnpedqlvmntvwheiafglknkgisl 106
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGG--GVIYIDGE--------------------------------------- 39

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   107 kqmkrRIGEIVNYFNLQSIINKETQSLSNGQKQLVALASVMVMNPKVILLDEATAQLDPVNR-----EEFIKILKHINDD 181
Cdd:smart00382  40 -----DILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEallllLEELRLLLLLKSE 114

                          170       180
                   ....*....|....*....|....
gi 169293994   182 FNVTVVFVEHQLEGLLDVANRLIV 205
Cdd:smart00382 115 KNLTVILTTNDEKDLGPALLRRRF 138
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 133-177 2.40e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 40.81  E-value: 2.40e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 169293994   133 LSNGQKQLVALA---SVMVMNPKVI-LLDEATAQLDPVNREEFIKILKH 177
Cdd:TIGR02168 1090 LSGGEKALTALAllfAIFKVKPAPFcILDEVDAPLDDANVERFANLLKE 1138
GguA NF040905
sugar ABC transporter ATP-binding protein;
4-212 2.48e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.54  E-value: 2.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   4 IENFSFTYP--KDKKIINNISFEIKKGDFLVITGKSGCGKTTLLRyfkpSL--RPKG-DIDGVIILD-EEIEND------ 71
Cdd:NF040905 260 VKNWTVYHPlhPERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAM----SVfgRSYGrNISGTVFKDgKEVDVStvsdai 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  72 DTKIGFVfqnPEDQ----LV-MNTVWHEIAF----GLKNKGISLKQMKRRIGEivNYFNLQSI----INKETQSLSNGQK 138
Cdd:NF040905 336 DAGLAYV---TEDRkgygLNlIDDIKRNITLanlgKVSRRGVIDENEEIKVAE--EYRKKMNIktpsVFQKVGNLSGGNQ 410

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 169293994 139 QLVALASVMVMNPKVILLDEATAQLDPVNREEFIKIlkhIND--DFNVTVVFVEHQLEGLLDVANRLIVMDEGKIV 212
Cdd:NF040905 411 QKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 279-324 2.90e-03

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: 39.05  E-value: 2.90e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 169293994 279 KVRDLNFGHDDI-VLKDLEIDILENEILSIVGANGSGKSSFLRCLAG 324
Cdd:cd03217    2 EIKDLHVSVGGKeILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG 48
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 390-466 4.28e-03

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 39.60  E-value: 4.28e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994 390 DLSSGQKQLVALAKILLTKPQLLLLDEPTKGIDASSKEFLANLIRGL-SKHMTIVVASHDLEFVAKISDRVAMIFNGQ 466
Cdd:PRK10762 141 ELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELkSQGRGIVYISHRLKEIFEICDDVTVFRDGQ 218
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
 123-177 4.44e-03

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 36.44  E-value: 4.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 169293994  123 QSIINKETQSLSNGQKQL---VALASVMVM----------NPKVILLDEATAQLDPVNREEFIKILKH 177
Cdd:pfam13558  23 EVETYRRSGGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 253-449 5.28e-03

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: 39.42  E-value: 5.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 253 EAREALVNFEN-FDI-----KIMDEIDNRILM----KVR--DLNFGHDD--IVLKDLEIDILENEILSIVGANGSGKSSF 318
Cdd:COG5265  321 EIRQALADMERmFDLldqppEVADAPDAPPLVvgggEVRfeNVSFGYDPerPILKGVSFEVPAGKTVAIVGPSGAGKSTL 400

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 319 LRCLAGLVDCQ-GEISkvgcVD--------------RIGYLPQDpTTLF-------VA--------DKVIddlllvddvV 368
Cdd:COG5265  401 ARLLFRFYDVTsGRIL----IDgqdirdvtqaslraAIGIVPQD-TVLFndtiaynIAygrpdaseEEVE---------A 466

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994 369 ASVESHLDNFgIIDLKDAhpFD---------LSSGQKQLVALAKILLTKPQLLLLDEPTKGID-ASSKEFLANLiRGLSK 438
Cdd:COG5265  467 AARAAQIHDF-IESLPDG--YDtrvgerglkLSGGEKQRVAIARTLLKNPPILIFDEATSALDsRTERAIQAAL-REVAR 542

                        250
                 ....*....|..
gi 169293994 439 -HMTIVVAsHDL 449
Cdd:COG5265  543 gRTTLVIA-HRL 553
PTZ00243 PTZ00243
ABC transporter; Provisional
 134-224 6.33e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 39.38  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994  134 SNGQKQLVALASVMVM-NPKVILLDEATAQLDP-VNREefikILKHINDDF-NVTVVFVEHQLEgllDVA--NRLIVMDE 208
Cdd:PTZ00243 1447 SVGQRQLMCMARALLKkGSGFILMDEATANIDPaLDRQ----IQATVMSAFsAYTVITIAHRLH---TVAqyDKIIVMDH 1519

                          90
                  ....*....|....*.
gi 169293994  209 GkividneikmAVDEM 224
Cdd:PTZ00243 1520 G----------AVAEM 1525
COG4637 COG4637
Predicted ATPase [General function prediction only];
292-328 7.48e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 38.76  E-value: 7.48e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 169293994 292 LKDLEIDIleNEILSIVGANGSGKSSFLRCLAGLVDC 328
Cdd:COG4637   13 LRDLELPL--GPLTVLIGANGSGKSNLLDALRFLSDA 47
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 304-352 8.68e-03

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 38.14  E-value: 8.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 169293994  304 ILSIVGANGSGKSSFLRCLAGLVDCQGEISKVGCVDRIGYLPQDPTTLF 352
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDERSRNGGIGGIPSLL 49
AAA_23 pfam13476
AAA domain;
3-143 8.83e-03

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 37.48  E-value: 8.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994    3 KIENFsftypkdkKIINNISFEIKKGDFLvITGKSGCGKTTLLR------YFKPSLRPKGDIDGVIILDEEIENDDTKIG 76
Cdd:pfam13476   2 TIENF--------RSFRDQTIDFSKGLTL-ITGPNGSGKTTILDaiklalYGKTSRLKRKSGGGFVKGDIRIGLEGKGKA 72

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169293994   77 FV---FQNPEDQLVMNTVWHeiafgLKNKGISLKQMKRRIGEIVNYFNLQSIINKETQSLSNGQKQLVAL 143
Cdd:pfam13476  73 YVeitFENNDGRYTYAIERS-----RELSKKKGKTKKKEILEILEIDELQQFISELLKSDKIILPLLVFL 137
 
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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