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Conserved domains on  [gi|1016201160|ref|WP_062946357|]
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methionine ABC transporter ATP-binding protein MetN [Salmonella enterica]

Protein Classification

methionine ABC transporter ATP-binding protein( domain architecture ID 11485231)

methionine ABC transporter ATP-binding protein MetN is part of the ABC transporter complex MetNIQ that is involved in methionine import; responsible for energy coupling to the transport system

CATH:  3.40.50.300|3.30.70.260
EC:  7.4.2.11
Gene Ontology:  GO:0005524|GO:0033232|GO:0048473|GO:0016887|GO:0042626
PubMed:  22095702|11421270|25750732|24638992
SCOP:  4003976|4001937
TCDB:  3.A.1.24

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 1-343 0e+00

DL-methionine transporter ATP-binding subunit; Provisional


:

Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 678.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK11153    1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11153   81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:PRK11153  161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:PRK11153  241 IQSTLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320

                         330       340
                  ....*....|....*....|...
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLGYV 343
Cdd:PRK11153  321 GDIQAAIAYLQEHGVKVEVLGYV 343
 
Name Accession Description Interval E-value
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 1-343 0e+00

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 678.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK11153    1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11153   81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:PRK11153  161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:PRK11153  241 IQSTLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320

                         330       340
                  ....*....|....*....|...
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLGYV 343
Cdd:PRK11153  321 GDIQAAIAYLQEHGVKVEVLGYV 343
ABC_MetN TIGR02314
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ...
 1-343 0e+00

D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.


Pssm-ID: 131367 [Multi-domain]  Cd Length: 343  Bit Score: 648.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:TIGR02314   1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:TIGR02314  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADSVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320

                         330       340
                  ....*....|....*....|...
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLGYV 343
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVLGYV 343
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-341 0e+00

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 604.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG1135     1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1135    81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:COG1135   161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVpmLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:COG1135   241 LPTVLNDELPEELLARLREAAGGGRL--VRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDD 318

                         330       340
                  ....*....|....*....|.
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLG 341
Cdd:COG1135   319 AAIDAALAYLREQGVVVEVLG 339
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 1-233 1.82e-160

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: 447.80  E-value: 1.82e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:cd03258     1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03258    81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK 233
Cdd:cd03258   161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 21-169 2.64e-51

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: 167.05  E-value: 2.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLsesELTKARRQIGMIFQHFNLLSSRTVF 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD---ERKSLRKEIGYVFQDPQLFPRLTVR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 101 GNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHD----SYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:pfam00005  78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
20-209 7.32e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 102.51  E-value: 7.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVN-LLErPTEGSVQVGGQELttlsESELTKARRQIGMIFQHFNLLSSRT 98
Cdd:NF033858  281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTgLLP-ASEGEAWLFGQPV----DAGDIATRRRVGYMSQAFSLYGELT 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:NF033858  356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1016201160 179 ILELLKDINRRLGLTILLITHEMDVVKRiCD 209
Cdd:NF033858  436 FWRLLIELSREDGVTIFISTHFMNEAER-CD 465
NIL smart00930
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ...
 267-340 6.72e-23

This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.


Pssm-ID: 197998 [Multi-domain]  Cd Length: 76  Bit Score: 90.65  E-value: 6.72e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160  267 PMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQEETQAAIAWLQDHHVKVEVL 340
Cdd:smart00930   3 RLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
GguA NF040905
sugar ABC transporter ATP-binding protein;
6-227 1.06e-21

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 95.63  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   6 NITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLE--RPT---EGSVQVGGQELT--TLSESElt 78
Cdd:NF040905    6 GITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSgvYPHgsyEGEILFDGEVCRfkDIRDSE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNL---LSsrtvfgnVALPLELDNTPK-------EEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQR 148
Cdd:NF040905   77 --ALGIVIIHQELALipyLS-------IAENIFLGNERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIE-----QD 223
Cdd:NF040905  148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtldcrAD 226


                  ....
gi 1016201160 224 TVSE 227
Cdd:NF040905  227 EVTE 230
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-241 6.62e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 75.93  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV-GGQelttLSESeltKARRQIG-----MIfQHF- 91
Cdd:NF033858   15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGD----MADA---RHRRAVCpriayMP-QGLg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  92 -NLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSyPA-NLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:NF033858   87 kNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTT 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 170 ALDPATTRSILELLKDI-NRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHPKTP-LAQKFI 241
Cdd:NF033858  166 GVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADtLEAAFI 238
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
114-242 3.89e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.52  E-value: 3.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 114 KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLT 193
Cdd:NF000106  118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1016201160 194 ILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVfshpKTPLAQKFIQ 242
Cdd:NF000106  197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL----KTKVGGRTLQ 241
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-220 7.82e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 47.48  E-value: 7.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVGGQELTTLSESE--------LTKARRQIGMIF 88
Cdd:NF040905  274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTVSDaidaglayVTEDRKGYGLNL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  89 Q----------HFNLLSSRTVfgnvalpleLDNTpkEEIK-----R-----RVTELLDLVGlgdkhdsypaNLSGGQKQR 148
Cdd:NF040905  354 IddikrnitlaNLGKVSRRGV---------IDEN--EEIKvaeeyRkkmniKTPSVFQKVG----------NLSGGNQQK 412

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:NF040905  413 VVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
 
Name Accession Description Interval E-value
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 1-343 0e+00

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 678.83  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK11153    1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11153   81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:PRK11153  161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:PRK11153  241 IQSTLHLDLPEDYLARLQAEPTTGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320

                         330       340
                  ....*....|....*....|...
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLGYV 343
Cdd:PRK11153  321 GDIQAAIAYLQEHGVKVEVLGYV 343
ABC_MetN TIGR02314
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ...
 1-343 0e+00

D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.


Pssm-ID: 131367 [Multi-domain]  Cd Length: 343  Bit Score: 648.48  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:TIGR02314   1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:TIGR02314  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVPMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQATPFADSVPMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320

                         330       340
                  ....*....|....*....|...
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLGYV 343
Cdd:TIGR02314 321 QDTQAAIAYLQEHNVKVEVLGYV 343
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-341 0e+00

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 604.38  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG1135     1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1135    81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:COG1135   161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKASPETDSVpmLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQ 320
Cdd:COG1135   241 LPTVLNDELPEELLARLREAAGGGRL--VRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDD 318

                         330       340
                  ....*....|....*....|.
gi 1016201160 321 EETQAAIAWLQDHHVKVEVLG 341
Cdd:COG1135   319 AAIDAALAYLREQGVVVEVLG 339
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 1-233 1.82e-160

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: 447.80  E-value: 1.82e-160
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:cd03258     1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03258    81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK 233
Cdd:cd03258   161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-222 7.02e-103

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 301.58  E-value: 7.02e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG1136     4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG1136    84 RRRhIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQ 222
Cdd:COG1136   164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVSD 225
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 1-242 1.26e-100

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 296.52  E-value: 1.26e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtLSESELTKA 80
Cdd:COG1126     1 MIEIENLHKSF--GDL--EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG1126    76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK 239
Cdd:COG1126   156 KVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234


                  ...
gi 1016201160 240 FIQ 242
Cdd:COG1126   235 FLS 237
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-248 5.34e-97

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: 296.81  E-value: 5.34e-97
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQ-GTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTK 79
Cdd:COG1123   260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQIGMIFQH-FNLLSSR-TVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARAL 155
Cdd:COG1123   340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLPPDLaDRYPHELSGGQRQRVAIARAL 419

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTP 235
Cdd:COG1123   420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499

                         250
                  ....*....|...
gi 1016201160 236 LAQKFIQSTLHLD 248
Cdd:COG1123   500 YTRALLAAVPSLD 512
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-241 2.38e-96

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: 285.72  E-value: 2.38e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG1127     5 MIEVRNLTKSF--GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPL-ELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG1127    81 RRRIGMLFQGGALFDSLTVFENVAFPLrEHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKtPLAQK 239
Cdd:COG1127   161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASDD-PWVRQ 239


                  ..
gi 1016201160 240 FI 241
Cdd:COG1127   240 FL 241
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 2-219 2.54e-95

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: 282.07  E-value: 2.54e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKAR 81
Cdd:cd03255     1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 R-QIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03255    81 RrHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGEL 219
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGKI 218
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-221 5.20e-94

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 278.86  E-value: 5.20e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG2884     1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG2884    78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIE 221
Cdd:COG2884   158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVR 217
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 2-240 1.02e-88

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: 265.90  E-value: 1.02e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKAR 81
Cdd:cd03261     1 IELRGLTKSF--GGRTV--LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPL-ELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03261    77 RRMGMLFQSGALFDSLTVFENVAFPLrEHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKtPLAQKF 240
Cdd:cd03261   157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASDD-PLVRQF 235
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 1-248 8.02e-87

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 261.66  E-value: 8.02e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsESELTKA 80
Cdd:COG1124     1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFnlLSS----RTVFGNVALPLELDNTPkeEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARAL 155
Cdd:COG1124    78 RRRVQMVFQDP--YASlhprHTVDRILAEPLRIHGLP--DREERIAELLEQVGLPPSFlDRYPHQLSGGQRQRVAIARAL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTP 235
Cdd:COG1124   154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233

                         250
                  ....*....|...
gi 1016201160 236 LAQKFIQSTLHLD 248
Cdd:COG1124   234 YTRELLAASLAFE 246
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 1-220 1.71e-85

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 258.06  E-value: 1.71e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG3638     2 MLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLeLDNT----------PKEEiKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVA 150
Cdd:COG3638    79 RRRIGMIFQQFNLVPRLSVLTNVLAGR-LGRTstwrsllglfPPED-RERALEALERVGLADKAYQRADQLSGGQQQRVA 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:COG3638   157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV 226
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 1-235 1.65e-82

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: 253.05  E-value: 1.65e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERP--TEGSVQVGGQELTTLSESEL 77
Cdd:COG0444     1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAIlGLLPPPgiTSGEILFDGEDLLKLSEKEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 TKAR-RQIGMIFQhfNLLSS----RTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGDKH---DSYPANLSGGQKQR 148
Cdd:COG0444    81 RKIRgREIQMIFQ--DPMTSlnpvMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPErrlDRYPHELSGGMRQR 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG0444   159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEEL 238


                  ....*..
gi 1016201160 229 FSHPKTP 235
Cdd:COG0444   239 FENPRHP 245
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 2-234 5.07e-82

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: 248.79  E-value: 5.07e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsESELTKAR 81
Cdd:COG1122     1 IELENLSFSYPGGT---PALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1122    75 RKVGLVFQNpDDQLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPE 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKT 234
Cdd:COG1122   155 VLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 1-222 3.25e-80

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: 243.95  E-value: 3.25e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:cd03257     1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQhfNLLSS----RTVFGNVALPLEL--DNTPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIAR 153
Cdd:cd03257    81 RKEIQMVFQ--DPMSSlnprMTIGEQIAEPLRIhgKLSKKEARKEAVLLLLVGVGLPEEVlNRYPHELSGGQRQRVAIAR 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:cd03257   159 ALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEE 227
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-241 8.60e-79

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 244.62  E-value: 8.60e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEseltkA 80
Cdd:COG3842     5 ALELENVSKRY--GDVT--ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-----E 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG3842    76 KRNVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:COG3842   156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADF 235


                  .
gi 1016201160 241 I 241
Cdd:COG3842   236 I 236
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-202 1.23e-78

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 241.15  E-value: 1.23e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlseseltKA 80
Cdd:COG1116     7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT--------GP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG1116    79 GPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG1116   159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVD 200
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 2-219 4.82e-78

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: 237.81  E-value: 4.82e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtLSESELTKAR 81
Cdd:cd03262     1 IEIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03262    76 QKVGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:cd03262   156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 2-220 5.03e-78

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: 239.01  E-value: 5.03e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKAR 81
Cdd:cd03256     1 IEVENLSKTYPNGK---KALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLeLDNTP---------KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIA 152
Cdd:cd03256    78 RQIGMIFQQFNLIERLSVLENVLSGR-LGRRStwrslfglfPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:cd03256   157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIV 224
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 2-218 9.93e-77

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: 233.23  E-value: 9.93e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLsESELTKAR 81
Cdd:cd03229     1 LELKNVSKRYGQ----KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLeldntpkeeikrrvtelldlvglgdkhdsypanlSGGQKQRVAIARALASNPKV 161
Cdd:cd03229    76 RRIGMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPDV 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd03229   122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-228 3.49e-76

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 233.80  E-value: 3.49e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqgtRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEseltKAR 81
Cdd:COG1131     1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPA----EVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:COG1131    73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG1131   153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 2-242 1.22e-75

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: 233.69  E-value: 1.22e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIQAL----------------------NNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTE 59
Cdd:cd03294     1 IKIKGLYKIF--GKNPQKAFkllakgkskeeilkktgqtvgvNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  60 GSVQVGGQELTTLSESELTKARRQ-IGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYP 138
Cdd:cd03294    79 GKVLIDGQDIAAMSRKELRELRRKkISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYP 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 139 ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd03294   159 DELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGR 238

                         250       260
                  ....*....|....*....|....
gi 1016201160 219 LIEQDTVSEVFSHPKTPLAQKFIQ 242
Cdd:cd03294   239 LVQVGTPEEILTNPANDYVREFFR 262
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 1-231 2.57e-75

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of phosphorus-containing organic compound with a stable direct C-P bond rather than a C-O-P linkage. A number of bacterial species have operons, typically about 14 genes in size, with genes for ATP-dependent transport of phosphonates, degradation, and regulation of the expression of the system. Members of this protein family are the ATP-binding cassette component of tripartite ABC transporters of phosphonates. [Transport and binding proteins, Anions]


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 232.19  E-value: 2.57e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:TIGR02315   1 MLEVENLSKVYPNGK---QALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNV---------ALPLELDNTPKEEiKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAI 151
Cdd:TIGR02315  78 RRRIGMIFQHYNLIERLTVLENVlhgrlgykpTWRSLLGRFSEED-KERALSALERVGLADKAYQRADQLSGGQQQRVAI 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSH 231
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 2-241 6.18e-75

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 234.66  E-value: 6.18e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlsesELTKAR 81
Cdd:COG1118     3 IEVRNISKRF--GSF--TLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT----NLPPRE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:COG1118    75 RRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 162 LLCDEATSALDpATTRSILE-LLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:COG1118   155 LLLDEPFGALD-AKVRKELRrWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARF 233


                  .
gi 1016201160 241 I 241
Cdd:COG1118   234 L 234
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 10-235 1.45e-74

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 233.09  E-value: 1.45e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  10 VFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQ 89
Cdd:COG4608    23 LFGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELRPLRRRMQMVFQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  90 H-FNLLSSR-TVFGNVALPLELDN-TPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:COG4608   103 DpYASLNPRmTVGDIIAEPLRIHGlASKAERRERVAELLELVGLRPEHaDRYPHEFSGGQRQRIGIARALALNPKLIVCD 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTP 235
Cdd:COG4608   183 EPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPLHP 252
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 2-259 5.60e-74

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette (ABC) proteins by homology, but belong to energy coupling factor (ECF) transport systems. The architecture in general is two ATPase subunits (or a double-length fusion protein), a T component, and a substrate capture (S) component that is highly variable, and may be interchangeable in genomes with only one T component. This model identifies many but not examples of the downstream member of the pair of ECF ATPases in Firmicutes and Mollicutes. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 229.65  E-value: 5.60e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:TIGR04521   1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQhF--NLLSSRTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARALA 156
Cdd:TIGR04521  81 RKKVGLVFQ-FpeHQLFEETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEEyLERSPFELSGGQMRRVAIAGVLA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPktpl 236
Cdd:TIGR04521 159 MEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDV---- 234

                         250       260
                  ....*....|....*....|....*
gi 1016201160 237 aqKFIQStLHLDIPE--DYQARLKA 259
Cdd:TIGR04521 235 --DELEK-IGLDVPEitELARKLKE 256
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 1-242 1.06e-73

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 232.69  E-value: 1.06e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVF-----------QQG---------TRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEG 60
Cdd:COG4175     3 KIEVRNLYKIFgkrperalkllDQGkskdeilekTGQTVGVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTAG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  61 SVQVGGQELTTLSESELTKARRQ-IGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPA 139
Cdd:COG4175    83 EVLIDGEDITKLSKKELRELRRKkMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYPD 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 140 NLSGGQKQRVAIARALASNPKVLLCDEATSALDPattrsiL-------ELLkDINRRLGLTILLITHEMDVVKRICDCVA 212
Cdd:COG4175   163 ELSGGMQQRVGLARALATDPDILLMDEAFSALDP------LirremqdELL-ELQAKLKKTIVFITHDLDEALRLGDRIA 235

                         250       260       270
                  ....*....|....*....|....*....|
gi 1016201160 213 VISNGELIEQDTVSEVFSHPKTPLAQKFIQ 242
Cdd:COG4175   236 IMKDGRIVQIGTPEEILTNPANDYVADFVE 265
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 2-216 1.21e-73

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: 226.97  E-value: 1.21e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlseseltkAR 81
Cdd:cd03293     1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG--------PG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03293    73 PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISN 216
Cdd:cd03293   153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 2-222 2.78e-73

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: 225.86  E-value: 2.78e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLseselTKAR 81
Cdd:cd03259     1 LELKGLSKTYGS----VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGV-----PPER 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03259    72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGElIEQ 222
Cdd:cd03259   152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGR-IVQ 211
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 3-218 3.66e-73

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: 225.42  E-value: 3.66e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   3 KLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRR 82
Cdd:cd03225     1 ELKNLS--FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKEL---RR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  83 QIGMIFQHFNL-LSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03225    76 KVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd03225   156 LLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-272 7.32e-73

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: 234.41  E-value: 7.32e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPT---EGSVQVGGQELTTLSESEL 77
Cdd:COG1123     4 LLEVRDLSVRYPGGDVP--AVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 tkaRRQIGMIFQHF-NLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1123    82 ---GRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTpl 236
Cdd:COG1123   159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQA-- 236

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1016201160 237 aqkfIQSTLHLDIPEDYQARLKASPEtdsvPMLRME 272
Cdd:COG1123   237 ----LAAVPRLGAARGRAAPAAAAAE----PLLEVR 264
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 2-243 3.44e-71

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: 221.41  E-value: 3.44e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:cd03295     1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKH--DSYPANLSGGQKQRVAIARALASNP 159
Cdd:cd03295    75 RKIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAEfaDRYPHELSGGQQQRVGVARALAADP 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK 239
Cdd:cd03295   155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAE 234


                  ....
gi 1016201160 240 FIQS 243
Cdd:cd03295   235 FVGA 238
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 2-260 6.31e-71

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: 221.54  E-value: 6.31e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGqeLTTLSESELTKAR 81
Cdd:TIGR04520   1 IEVENVSFSYPESEK--PALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLWEIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:TIGR04520  77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD-VVKriCDCVAVISNGELIEQDTVSEVFSHpktplaQK 239
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEeAVL--ADRVIVMNKGKIVAEGTPREIFSQ------VE 228

                         250       260
                  ....*....|....*....|...
gi 1016201160 240 FIQStLHLDIPEDYQ--ARLKAS 260
Cdd:TIGR04520 229 LLKE-IGLDVPFITElaKALKKR 250
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 1-227 8.07e-71

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: 220.00  E-value: 8.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:COG4181     8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELDNTPkeEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:COG4181    88 RARhVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSE 227
Cdd:COG4181   166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 2-219 7.74e-70

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: 216.89  E-value: 7.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKAR 81
Cdd:cd03292     1 IEFINVTKTYPNGTA---ALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03292    78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:cd03292   158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1-246 1.81e-69

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 217.75  E-value: 1.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTT--------- 71
Cdd:COG4598     8 ALEVRDLHKSFGD----LEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLkpdrdgelv 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  72 -LSESELTKARRQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:COG4598    84 pADRRQLQRIRTRLGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVF 229
Cdd:COG4598   164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242

                         250
                  ....*....|....*..
gi 1016201160 230 SHPKTPLAQKFIQSTLH 246
Cdd:COG4598   243 GNPKSERLRQFLSSSLK 259
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-233 8.73e-69

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: 215.67  E-value: 8.73e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkA 80
Cdd:COG0411     4 LLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRI--A 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLE----------LDNTPK-----EEIKRRVTELLDLVGLGDKHDSYPANLSGGQ 145
Cdd:COG0411    78 RLGIARTFQNPRLFPELTVLENVLVAAHarlgrgllaaLLRLPRarreeREARERAEELLERVGLADRADEPAGNLSYGQ 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTV 225
Cdd:COG0411   158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTP 237


                  ....*...
gi 1016201160 226 SEVFSHPK 233
Cdd:COG0411   238 AEVRADPR 245
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-241 1.24e-66

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 213.40  E-value: 1.24e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEseltkA 80
Cdd:COG3839     3 SLELENVSKSYGG----VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPP-----K 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG3839    74 DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDP---ATTRSileLLKDINRRLGLTILLITHE----MdvvkRICDCVAVISNGELIEQDTVSEVFSHPK 233
Cdd:COG3839   154 VFLLDEPLSNLDAklrVEMRA---EIKRLHRRLGTTTIYVTHDqveaM----TLADRIAVMNDGRIQQVGTPEELYDRPA 226


                  ....*...
gi 1016201160 234 TPLAQKFI 241
Cdd:COG3839   227 NLFVAGFI 234
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 2-228 1.44e-66

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: 208.96  E-value: 1.44e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqgtRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVGGQELTTLSESE 76
Cdd:cd03260     1 IELRDLNVYY----GDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  77 LtKARRQIGMIFQHFNLLSSrTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGD--KHDSYPANLSGGQKQRVAIAR 153
Cdd:cd03260    77 L-ELRRRVGMVFQKPNPFPG-SIYDNVAYGLRLhGIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:cd03260   155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 2-241 4.15e-66

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: 208.24  E-value: 4.15e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsesELTKAR 81
Cdd:cd03300     1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-----NLPPHK 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03300    72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:cd03300   152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 2-233 1.07e-65

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: 207.29  E-value: 1.07e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkAR 81
Cdd:cd03219     1 LEVRGLTKRFGG----LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEI--AR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTP----------KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAI 151
Cdd:cd03219    75 LGIGRTFQIPRLFPELTVLENVMVAAQARTGSglllararreEREARERAEELLERVGLADLADRPAGELSYGQQRRLEI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSH 231
Cdd:cd03219   155 ARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNN 233


                  ..
gi 1016201160 232 PK 233
Cdd:cd03219   234 PR 235
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 10-248 1.35e-65

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: 215.70  E-value: 1.35e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  10 VFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLerPTEGSVQVGGQELTTLSESELTKARRQIGMIF 88
Cdd:COG4172   291 LFRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALlRLI--PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVF 368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  89 QH-FNLLSSR-TVFGNVALPLELDNTP--KEEIKRRVTELLDLVGL-GDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:COG4172   369 QDpFGSLSPRmTVGQIIAEGLRVHGPGlsAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLV 448

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQS 243
Cdd:COG4172   449 LDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAA 528


                  ....*
gi 1016201160 244 TLHLD 248
Cdd:COG4172   529 APLLE 533
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 2-241 2.41e-64

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: 203.72  E-value: 2.41e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltkar 81
Cdd:cd03296     3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLEL----DNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:cd03296    74 RNVGFVFQHYALFRHMTVFDNVAFGLRVkprsERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 158 NPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLA 237
Cdd:cd03296   154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233


                  ....
gi 1016201160 238 QKFI 241
Cdd:cd03296   234 YSFL 237
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 1-228 1.19e-63

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 202.01  E-value: 1.19e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlseSELTKA 80
Cdd:COG4555     1 MIEVENLSKKYGK----VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVR----KEPREA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG4555    73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG4555   153 VLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 11-251 1.25e-63

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: 210.70  E-value: 1.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  11 FQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP---TEGSVQVGGQELTTLSESELTKAR-RQIG 85
Cdd:COG4172    16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPaahPSGSILFDGQDLLGLSERELRRIRgNRIA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  86 MIFQ---------HfnllssrTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGDKH---DSYPANLSGGQKQRVAIA 152
Cdd:COG4172    96 MIFQepmtslnplH-------TIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIA 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHP 232
Cdd:COG4172   169 MALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAP 248

                         250
                  ....*....|....*....
gi 1016201160 233 KTPLAQKFIQSTLHLDIPE 251
Cdd:COG4172   249 QHPYTRKLLAAEPRGDPRP 267
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-235 3.00e-62

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 198.70  E-value: 3.00e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQEL---TTLSESELT 78
Cdd:COG4161     3 IQLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQHFNLLSSRTVFGN-VALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:COG4161    79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 158 NPKVLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTvSEVFSHPKTP 235
Cdd:COG4161   159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD-ASHFTQPQTE 234
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1-242 1.73e-61

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 196.47  E-value: 1.73e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTkA 80
Cdd:PRK09493    1 MIEFKNVSKHFGP----TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERL-I 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK09493   76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK 239
Cdd:PRK09493  156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234


                  ...
gi 1016201160 240 FIQ 242
Cdd:PRK09493  235 FLQ 237
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-241 6.78e-61

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 194.59  E-value: 6.78e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIQAlnnvSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseltKA 80
Cdd:COG3840     1 MLRLDDLT--YRYGDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP-----PA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG3840    70 ERPVSMLFQENNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRP 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKF 240
Cdd:COG3840   150 ILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229


                  .
gi 1016201160 241 I 241
Cdd:COG3840   230 L 230
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 19-241 1.09e-60

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 194.87  E-value: 1.09e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL--ERP---TEGSVQVGGQELTTlSESELTKARRQIGMIFQHFNL 93
Cdd:COG1117    25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIYD-PDVDVVELRRRVGMVFQKPNP 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSrTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:COG1117   104 FPK-SIYDNVAYGLRLhGIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 169 SALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:COG1117   183 SALDPISTAKIEELILELKKD--YTIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-245 1.80e-60

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 194.20  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTT---LSESE- 76
Cdd:PRK11264    3 AIEVKNLVKKFHGQT----VLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTarsLSQQKg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  77 -LTKARRQIGMIFQHFNLLSSRTVFGNVAL-PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARA 154
Cdd:PRK11264   79 lIRQLRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 155 LASNPKVLLCDEATSALDP-------ATTRSILEllkdiNRRlglTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:PRK11264  159 LAMRPEVILFDEPTSALDPelvgevlNTIRQLAQ-----EKR---TMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKA 230

                         250
                  ....*....|....*...
gi 1016201160 228 VFSHPKTPLAQKFIQSTL 245
Cdd:PRK11264  231 LFADPQQPRTRQFLEKFL 248
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-219 1.28e-58

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 188.54  E-value: 1.28e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK10908    1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK10908   78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK10908  158 VLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 1-230 2.47e-58

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: 188.71  E-value: 2.47e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtka 80
Cdd:COG1120     1 MLEAENLS--VGYGGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRREL--- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVAL---P-LELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1120    74 ARRIAYVPQEPPAPFGLTVRELVALgryPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:COG1120   154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-260 6.68e-58

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 188.69  E-value: 6.68e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQeltTLSESELTKAR 81
Cdd:PRK13635    6 IRVEHISFRYPDAAT--YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK13635   81 RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHpktplAQKF 240
Cdd:PRK13635  161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFKS-----GHML 234

                         250       260
                  ....*....|....*....|
gi 1016201160 241 IQSTLHLDIPEDYQARLKAS 260
Cdd:PRK13635  235 QEIGLDVPFSVKLKELLKRN 254
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 2-219 3.41e-57

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: 182.98  E-value: 3.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlsesELTKAR 81
Cdd:cd03230     1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK----EPEEVK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFgnvalpleldntpkeeikrrvtELLDLvglgdkhdsypanlSGGQKQRVAIARALASNPKV 161
Cdd:cd03230    73 RRIGYLPEEPSLYENLTVR----------------------ENLKL--------------SGGMKQRLALAQALLHDPEL 116

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:cd03230   117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-232 3.68e-57

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 185.68  E-value: 3.68e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlseseltKA 80
Cdd:COG1121     6 AIELENLT--VSYGGRPV--LEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPR--------RA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSR--TVFGNVAL----PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARA 154
Cdd:COG1121    74 RRRIGYVPQRAEVDWDFpiTVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVIsNGELIEQDTVSEVFSHP 232
Cdd:COG1121   154 LAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPE 229
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 2-227 4.30e-57

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: 184.50  E-value: 4.30e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlseSELTKAR 81
Cdd:cd03265     1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03265    73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:cd03265   153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 2-235 1.35e-56

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 184.06  E-value: 1.35e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQEL---TTLSESELT 78
Cdd:PRK11124    3 IQLNGINCFY--GAH--QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQHFNLLSSRTVFGN-VALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:PRK11124   79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 158 NPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEvFSHPKTP 235
Cdd:PRK11124  159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQTE 234
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
19-245 2.37e-56

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 184.02  E-value: 2.37e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSES----------ELTKARRQIGMIF 88
Cdd:PRK10619   19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgqlkvadknQLRLLRTRLTMVF 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  89 QHFNLLSSRTVFGNV-ALPLELDNTPKEEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK10619   99 QHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERaQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDE 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 167 ATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTL 245
Cdd:PRK10619  179 PTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGSL 256
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 23-245 5.98e-56

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: 186.07  E-value: 5.98e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQeltTLSESE----LTKARRQIGMIFQHFNLLSSRT 98
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE---VLQDSArgifLPPHRRRIGYVFQEARLFPHLS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNvalpLE--LDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:COG4148    94 VRGN----LLygRKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 177 RSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK-TPLAQKFIQSTL 245
Cdd:COG4148   170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDlLPLAGGEEAGSV 239
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 2-222 9.01e-56

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: 180.91  E-value: 9.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltkar 81
Cdd:cd03301     1 VELENVTKRF--GNVT--ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03301    72 RDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKV 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGElIEQ 222
Cdd:cd03301   152 FLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQ-IQQ 211
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
2-248 1.95e-54

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 181.82  E-value: 1.95e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqgTRTiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseltkAR 81
Cdd:PRK10851    3 IEIANIKKSF---GRT-QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH------AR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 -RQIGMIFQHFNLLSSRTVFGNVALPLEL----DNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK10851   73 dRKVGFVFQHYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGElIEQ-DTVSEVFSHPKTP 235
Cdd:PRK10851  153 VEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQaGTPDQVWREPATR 231

                         250
                  ....*....|...
gi 1016201160 236 LAQKFIQSTLHLD 248
Cdd:PRK10851  232 FVLEFMGEVNRLQ 244
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 14-268 4.35e-54

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 180.16  E-value: 4.35e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  14 GTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQH-FN 92
Cdd:PRK11308   24 PERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQKIQIVFQNpYG 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 LLSSRTVFGNV-ALPLELdNT--PKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:PRK11308  104 SLNPRKKVGQIlEEPLLI-NTslSAAERREKALAMMAKVGLRPEHyDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 169 SALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLD 248
Cdd:PRK11308  183 SALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHPYTQALLSATPRLN 262

                         250       260
                  ....*....|....*....|
gi 1016201160 249 iPEDYQARLKASPETDSvPM 268
Cdd:PRK11308  263 -PDDRRERIKLTGELPS-PL 280
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 2-227 9.89e-54

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: 175.77  E-value: 9.89e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlsesELTKAR 81
Cdd:cd03263     1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03263    75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDInrRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:cd03263   155 LLLDEPTSGLDPASRRAIWDLILEV--RKGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQE 218
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 1-250 1.30e-53

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 177.11  E-value: 1.30e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGqelTTLSESELTKA 80
Cdd:PRK13632    7 MIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDG---ITISKENLKEI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13632   82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD-VVKriCDCVAVISNGELIEQDTVSEVFSHpktplaQ 238
Cdd:PRK13632  162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDeAIL--ADKVIVFSEGKLIAQGKPKEILNN------K 233

                         250
                  ....*....|..
gi 1016201160 239 KFIQStLHLDIP 250
Cdd:PRK13632  234 EILEK-AKIDSP 244
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 2-228 2.05e-53

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: 186.58  E-value: 2.05e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:COG2274   474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASL---R 548

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHfNLLSSRTVFGNVALplELDNTPKEEIKrrvtELLDLVGLGDKHDSYP-----------ANLSGGQKQRVA 150
Cdd:COG2274   549 RQIGVVLQD-VFLFSGTIRENITL--GDPDATDEEII----EAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQRLA 621

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVkRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG2274   622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEEL 696
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 21-241 4.26e-53

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: 174.83  E-value: 4.26e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESeltkaRRQIGMIFQHFNLLSSRTVF 100
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 GNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSIL 180
Cdd:cd03299    90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 181 ELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:cd03299   170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
2-256 2.66e-52

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 173.48  E-value: 2.66e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGT-----RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESE 76
Cdd:COG4167     5 LEVRNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGDYKY 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  77 LTKarrQIGMIFQHFNL-LSSRTVFGNV-ALPLELdNTPKEEIKR--RVTELLDLVGLGDKH-DSYPANLSGGQKQRVAI 151
Cdd:COG4167    85 RCK---HIRMIFQDPNTsLNPRLNIGQIlEEPLRL-NTDLTAEEReeRIFATLRLVGLLPEHaNFYPHMLSSGQKQRVAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSH 231
Cdd:COG4167   161 ARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFAN 240

                         250       260
                  ....*....|....*....|....*
gi 1016201160 232 PKTPLAQKFIQSTLHLDIPEDYQAR 256
Cdd:COG4167   241 PQHEVTKRLIESHFGEALTADAWRR 265
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-219 2.73e-52

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 171.92  E-value: 2.73e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:COG4619     1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSrTVFGNVALPLELDN-TPKEEikrRVTELLDLVGLGDKHDSYPA-NLSGGQKQRVAIARALASNP 159
Cdd:COG4619    74 RQVAYVPQEPALWGG-TVRDNLPFPFQLRErKFDRE---RALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQP 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:COG4619   150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 11-235 5.09e-52

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 174.89  E-value: 5.09e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  11 FQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQH 90
Cdd:PRK15079   27 FWQPPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQD 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 -FNLLSSRTVFGNV-ALPLEL--DNTPKEEIKRRVTELLDLVGL-GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:PRK15079  107 pLASLNPRMTIGEIiAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTP 235
Cdd:PRK15079  187 EPVSALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHP 256
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-202 5.19e-52

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 172.74  E-value: 5.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseltkA 80
Cdd:COG4525     3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG------A 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRqiGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG4525    77 DR--GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG4525   155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVE 196
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 1-234 9.39e-52

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 172.57  E-value: 9.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtLSESELTKA 80
Cdd:PRK13639    1 ILETRDLKYSYPDGT---EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIK-YDKKSLLEV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHF-NLLSSRTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:PRK13639   77 RKTVGIVFQNPdDQLFAPTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMK 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKT 234
Cdd:PRK13639  156 PEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 20-220 1.29e-51

ATP-binding cassette domain of the metal-type transporters; This family includes transporters involved in the uptake of various metallic cations such as iron, manganese, and zinc. The ATPases of this group of transporters are very similar to members of iron-siderophore uptake family suggesting that they share a common ancestor. The best characterized metal-type ABC transporters are the YfeABCD system of Y. pestis, the SitABCD system of Salmonella enterica serovar Typhimurium, and the SitABCD transporter of Shigella flexneri. Moreover other uncharacterized homologs of these metal-type transporters are mainly found in pathogens like Haemophilus or enteroinvasive E. coli isolates.


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 170.02  E-value: 1.29e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlseseltKARRQIGMIFQHFNLLSSR-- 97
Cdd:cd03235    14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLE--------KERKRIGYVPQRRSIDRDFpi 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVALPL----ELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:cd03235    86 SVRDVVLMGLyghkGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDP 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1016201160 174 ATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVIsNGELI 220
Cdd:cd03235   166 KTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLL-NRTVV 210
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 21-169 2.64e-51

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: 167.05  E-value: 2.64e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLsesELTKARRQIGMIFQHFNLLSSRTVF 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDD---ERKSLRKEIGYVFQDPQLFPRLTVR 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 101 GNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHD----SYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:pfam00005  78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
cbiO PRK13637
energy-coupling factor transporter ATPase;
2-229 2.98e-51

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 171.77  E-value: 2.98e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlSESELTKA 80
Cdd:PRK13637    3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITD-KKVKLSDI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNL-LSSRTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLG--DKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13637   82 RKKVGLVFQYPEYqLFEETIEKDIAFgPINL-GLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVF 229
Cdd:PRK13637  161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVF 233
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 2-218 5.62e-51

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: 167.17  E-value: 5.62e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVGGQELTTLSESELt 78
Cdd:cd03228     1 IEFKNVS--FSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLL---KLLLRlydPTSGEILIDGVDLRDLDLESL- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNLLSsRTVFGNValpleldntpkeeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASN 158
Cdd:cd03228    75 --RKNIAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRD 114

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGE 218
Cdd:cd03228   115 PPILILDEATSALDPETEALILEALR--ALAKGKTVIVIAHRLSTIRD-ADRIIVLDDGR 171
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-228 1.28e-50

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 175.59  E-value: 1.28e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqgtRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltkA 80
Cdd:COG1129     4 LLEMRGISKSF----GGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD---A 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELDNTP---KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG1129    77 QAAgIAIIHQELNLVPNLSVAENIFLGREPRRGGlidWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALS 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG1129   157 RDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 3-218 2.24e-50

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: 165.11  E-value: 2.24e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   3 KLSNITKVFQQGTrtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRR 82
Cdd:cd00267     1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL---RR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  83 QIGMIFQhfnllssrtvfgnvalpleldntpkeeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASNPKVL 162
Cdd:cd00267    74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 163 LCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd00267   103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
19-232 2.40e-50

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 168.71  E-value: 2.40e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQH----FNll 94
Cdd:PRK10419   26 TVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVFQDsisaVN-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  95 SSRTVFGNVALPLE-LDNTPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK10419  104 PRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSVlDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNLD 183

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV--FSHP 232
Cdd:PRK10419  184 LVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltFSSP 245
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-241 6.43e-50

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 170.90  E-value: 6.43e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESeltkaR 81
Cdd:PRK09452   15 VELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE-----N 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK09452   86 RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 162 LLCDEATSALDpATTRSILEL-LKDINRRLGLTILLITHEMDVVKRICDCVAVISNGElIEQD-TVSEVFSHPKTPLAQK 239
Cdd:PRK09452  166 LLLDESLSALD-YKLRKQMQNeLKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGR-IEQDgTPREIYEEPKNLFVAR 243


                  ..
gi 1016201160 240 FI 241
Cdd:PRK09452  244 FI 245
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
19-224 1.17e-49

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 174.58  E-value: 1.17e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLS 95
Cdd:COG1132   354 PVLKDISLTIPPGETVALVGPSGSGKSTL---VNLLLRfydPTSGRILIDGVDIRDLTLESL---RRQIGVVPQDTFLFS 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 sRTVFGNVALPLEldNTPKEEIKR--RVTELLDLV-GLGDKHDSY----PANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:COG1132   428 -GTIRENIRYGRP--DATDEEVEEaaKAAQAHEFIeALPDGYDTVvgerGVNLSGGQRQRIAIARALLKDPPILILDEAT 504

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 169 SALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDT 224
Cdd:COG1132   505 SALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQGT 557
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-268 1.67e-49

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 166.83  E-value: 1.67e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsESELTKA 80
Cdd:PRK13650    4 IIEVKNLTFKYKEDQEKYT-LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLT---EENVWDI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13650   80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKrICDCVAVISNGELIEQDTVSEVFSHPKTPLaqk 239
Cdd:PRK13650  160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFSRGNDLL--- 235

                         250       260
                  ....*....|....*....|....*....
gi 1016201160 240 fiqsTLHLDIPedYQARLKASPETDSVPM 268
Cdd:PRK13650  236 ----QLGLDIP--FTTSLVQSLRQNGYDL 258
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-243 4.72e-49

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 168.48  E-value: 4.72e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELttlseSELTKA 80
Cdd:PRK11607   19 LLEIRNLTKSFD----GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDL-----SHVPPY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11607   90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPA-TTRSILELLkDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQK 239
Cdd:PRK11607  170 LLLLDEPMGALDKKlRDRMQLEVV-DILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAE 248


                  ....
gi 1016201160 240 FIQS 243
Cdd:PRK11607  249 FIGS 252
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-262 1.80e-48

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 166.43  E-value: 1.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltkarRQ 83
Cdd:PRK11432    9 LKNITKRF--GSNTV--IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ-----RD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 IGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:PRK11432   80 ICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI-- 241
Cdd:PRK11432  160 FDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMgd 239

                         250       260
                  ....*....|....*....|....*
gi 1016201160 242 ----QSTLHLDIPEDYQARLKASPE 262
Cdd:PRK11432  240 anifPATLSGDYVDIYGYRLPRPAA 264
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1-207 2.90e-48

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 162.29  E-value: 2.90e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK11629    5 LLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAEL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 R-RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK11629   85 RnQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNP 164

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRI 207
Cdd:PRK11629  165 RLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM 212
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 23-223 6.76e-48

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: 160.54  E-value: 6.76e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  23 NVSLHVPaGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGqelTTLSESE----LTKARRQIGMIFQHFNLLSSRT 98
Cdd:cd03297    16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNG---TVLFDSRkkinLPPQQRKIGLVFQQYALFPHLN 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNVALPLELDNtpKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:cd03297    92 VRENLAFGLKRKR--NREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQ 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1016201160 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQD 223
Cdd:cd03297   170 LLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 2-220 1.86e-47

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: 157.59  E-value: 1.86e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltkAR 81
Cdd:cd03216     1 LELRGITKRFGG----VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD---AR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQ-IGMIFQhfnllssrtvfgnvalpleldntpkeeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASNPK 160
Cdd:cd03216    74 RAgIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:cd03216   103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-228 3.56e-47

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 161.43  E-value: 3.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlseseltKA 80
Cdd:COG4152     1 MLELKGLTKRF--GDKT--AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDP-------ED 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIG-----------MifqhfnllssrTVfGNVALPL-ELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQR 148
Cdd:COG4152    70 RRRIGylpeerglypkM-----------KV-GEQLVYLaRLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQK 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG4152   138 VQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 18-228 4.35e-47

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: 158.75  E-value: 4.35e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkARRQIGMIFQHFNLLSSR 97
Cdd:cd03224    13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRIFPEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVALPLELDntPKEEIKRRVTELLDLV-GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:cd03224    91 TVEENLLLGAYAR--RRAKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 177 RSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:cd03224   169 EEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-230 4.38e-47

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 160.64  E-value: 4.38e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVF---QQGTRTIqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGqeLTTLSESEL 77
Cdd:PRK13633    4 MIKCKNVSYKYesnEESTEKL-ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDG--LDTSDEENL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 TKARRQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13633   81 WDIRNKAGMVFQNpDNQIVATIVEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFK 233
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 3-222 6.19e-47

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: 156.83  E-value: 6.19e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   3 KLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRR 82
Cdd:cd03214     1 EVENLS--VGYGGRTV--LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKEL---AR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  83 QIGMIFQhfnllssrtvfgnvalpleldntpkeeikrrvteLLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVL 162
Cdd:cd03214    74 KIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPIL 119

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 163 LCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:cd03214   120 LLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQ 179
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-217 8.89e-47

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: 158.37  E-value: 8.89e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVF---QQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV---GGQ-ELTTLS 73
Cdd:COG4778     4 LLEVENLSKTFtlhLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdGGWvDLAQAS 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  74 ESELTKARRQ-IGMIFQHFNLL---SSRTVfgnVALPLELDNTPKEEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQR 148
Cdd:COG4778    84 PREILALRRRtIGYVSQFLRVIprvSALDV---VAEPLLERGVDREEARARARELLARLNLPERlWDLPPATFSGGEQQR 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:COG4778   161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 2-231 1.32e-46

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: 166.09  E-value: 1.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:COG4988   337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASW---R 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSrTVFGNVAL--PleldNTPKEEIKRrvteLLDLVGLGDKHDSYP-----------ANLSGGQKQR 148
Cdd:COG4988   411 RQIAWVPQNPYLFAG-TIRENLRLgrP----DASDEELEA----ALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQR 481

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEV 228
Cdd:COG4988   482 LALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGTHEEL 558


                  ...
gi 1016201160 229 FSH 231
Cdd:COG4988   559 LAK 561
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 20-251 2.57e-46

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 159.03  E-value: 2.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELT-TLSESELTKARRQIGMIFQhF--NLLSS 96
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNKKLKPLRKKVGIVFQ-FpeHQLFE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  97 RTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:PRK13634  101 ETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPEELlARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 175 TTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPkTPLAQkfiqstLHLDIPE 251
Cdd:PRK13634  180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP-DELEA------IGLDLPE 249
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 1-228 3.12e-46

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 164.04  E-value: 3.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltkA 80
Cdd:COG3845     5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRD---A 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQ-IGMIFQHFNLLSSRTVFGNVAL---PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:COG3845    78 IALgIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALY 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:COG3845   158 RGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAET 228
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 19-245 7.68e-46

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 156.54  E-value: 7.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVGGQELTTlSESELTKARRQIGMIFQHFNL 93
Cdd:PRK14267   18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYS-PDVDPIEVRREVGMVFQYPNP 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSRTVFGNVALPLELDN--TPKEEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:PRK14267   97 FPHLTIYDNVAIGVKLNGlvKSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 168 TSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTL 245
Cdd:PRK14267  177 TANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYVTGAL 252
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 18-246 9.77e-46

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 156.23  E-value: 9.77e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFN 92
Cdd:PRK14247   16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL---RRRVQMVFQIPN 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 LLSSRTVFGNVALPLELDN--TPKEEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK14247   93 PIPNLSIFENVALGLKLNRlvKSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADE 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 167 ATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLH 246
Cdd:PRK14247  173 PTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYVTGRLY 250
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
20-256 1.06e-45

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 160.20  E-value: 1.06e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQ-IGMIFQHFNLLSSRT 98
Cdd:PRK10070   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKkIAMVFQSFALMPHMT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:PRK10070  123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQStlhLDIPEDYQAR 256
Cdd:PRK10070  203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRG---VDISQVFSAK 277
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-220 8.04e-45

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 162.20  E-value: 8.04e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK10535    4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQ-IGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK10535   84 RREhFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRiCDCVAVISNGELI 220
Cdd:PRK10535  164 QVILADEPTGALDSHSGEEVMAILHQLRDR-GHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 2-222 1.04e-44

ABC-type multidrug transport system, ATPase component; The biological function of this family is not well characterized, but display ABC domains similar to members of ABCA subfamily. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213231 [Multi-domain]  Cd Length: 211  Bit Score: 152.35  E-value: 1.04e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGtrtiQALNNVSLHVPAGqIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlseSELTKAR 81
Cdd:cd03264     1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03264    72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDI--NRrlglTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:cd03264   152 LIVDEPTAGLDPEERIRFRNLLSELgeDR----IVILSTHIVEDVESLCNQVAVLNKGKLVFE 210
cbiO PRK13640
energy-coupling factor transporter ATPase;
20-267 1.53e-44

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 154.19  E-value: 1.53e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERP---TEGSVQVGGqelTTLSESELTKARRQIGMIFQH-FNLLS 95
Cdd:PRK13640   22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDG---ITLTAKTVWDIREKVGIVFQNpDNQFV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 SRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:PRK13640   99 GATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAG 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 176 TRSILELLKDINRRLGLTILLITHEMDVVKrICDCVAVISNGELIEQDTVSEVFshPKTPLAQKfiqstLHLDIPEDYQA 255
Cdd:PRK13640  179 KEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIF--SKVEMLKE-----IGLDIPFVYKL 250

                         250
                  ....*....|..
gi 1016201160 256 RLKASPETDSVP 267
Cdd:PRK13640  251 KNKLKEKGISVP 262
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-219 2.32e-44

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 152.91  E-value: 2.32e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGgqelttlsESELTKARRQ 83
Cdd:PRK11247   15 LNAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLAG--------TAPLAEARED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 IGMIFQHFNLLSSRTVFGNVALPLeldntpKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:PRK11247   83 TRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK11247  157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 10-241 4.77e-44

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 160.02  E-value: 4.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  10 VFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQ 89
Cdd:PRK10261  329 LLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQ 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  90 --HFNLLSSRTVFGNVALPLELDNT-PKEEIKRRVTELLDLVGLGDKHD-SYPANLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:PRK10261  409 dpYASLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLPEHAwRYPHEFSGGQRQRICIARALALNPKVIIAD 488

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 166 EATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:PRK10261  489 EAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLM 564
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 1-231 5.94e-44

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 152.21  E-value: 5.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsESELTKA 80
Cdd:PRK13648    7 IIVFKNVS--FQYQSDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAIT---DDNFEKL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13648   82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSH 231
Cdd:PRK13648  162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 2-227 9.94e-44

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease components [Energy production and conversion, Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 158.39  E-value: 9.94e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVGGQELTTLSESELt 78
Cdd:COG4987   334 LELEDVS--FRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTL---LALLLRfldPQSGSITLGGVDLRDLDEDDL- 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNLLSSrTVFGN--VALPlelDNTPKEeikrrVTELLDLVGLGDKHDSYP-----------ANLSGGQ 145
Cdd:COG4987   408 --RRRIAVVPQRPHLFDT-TLRENlrLARP---DATDEE-----LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGE 476

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTV 225
Cdd:COG4987   477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLER-MDRILVLEDGRIVEQGTH 553


                  ..
gi 1016201160 226 SE 227
Cdd:COG4987   554 EE 555
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 1-230 1.00e-43

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 151.92  E-value: 1.00e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtLSESELTKA 80
Cdd:PRK13636    5 ILKVEELNYNYSDGT---HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQH-FNLLSSRTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:PRK13636   81 RESVGMVFQDpDNQLFSASVYQDVSFgAVNL-KLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK13636  160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFA 231
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 2-222 1.23e-43

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: 149.29  E-value: 1.23e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEseltkAR 81
Cdd:cd03268     1 LKTNDLTKTYG----KKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIE-----AL 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03268    72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:cd03268   148 LILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEE 207
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 2-227 1.83e-43

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: 150.00  E-value: 1.83e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTlirCVNLLER---PTEGSVQVGGQELTTLSESEL 77
Cdd:cd03249     1 IEFKNVS--FRYPSRpDVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLERfydPTSGEILLDGVDIRDLNLRWL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 tkaRRQIGMIFQHFNLLSsRTVFGNVALplELDNTPKEEIKR--RVTELLDLV-GLGDKHDS----YPANLSGGQKQRVA 150
Cdd:cd03249    76 ---RSQIGLVSQEPVLFD-GTIAENIRY--GKPDATDEEVEEaaKKANIHDFImSLPDGYDTlvgeRGSQLSGGQKQRIA 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 151 IARALASNPKVLLCDEATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSE 227
Cdd:cd03249   150 IARALLRNPKILLLDEATSALDAESEKLVQEALD--RAMKGRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDE 223
cbiO PRK13646
energy-coupling factor transporter ATPase;
2-251 2.16e-43

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 151.09  E-value: 2.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGT-RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLS-ESELTK 79
Cdd:PRK13646    3 IRFDNVSYTYQKGTpYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTkDKYIRP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQIGMIFQhfnLLSSRTVFGNVALPLELD----NTPKEEIKRRVTELLDLVGLG-DKHDSYPANLSGGQKQRVAIARA 154
Cdd:PRK13646   83 VRKRIGMVFQ---FPESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHpKT 234
Cdd:PRK13646  160 LAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKD-KK 238

                         250
                  ....*....|....*..
gi 1016201160 235 PLAQkfiqstLHLDIPE 251
Cdd:PRK13646  239 KLAD------WHIGLPE 249
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 21-241 2.84e-43

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 150.20  E-value: 2.84e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQEL---TTLSESELTKARRQIGMIFQHFNLLSSR 97
Cdd:PRK14246   26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLyfgKDIFQIDAIKLRKEVGMVFQQPNPFPHL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVALPLELDNTP-KEEIKRRVTELLDLVGLG----DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK14246  106 SIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLWkevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 173 PATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:PRK14246  186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEKYV 252
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 25-222 3.55e-43

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: 148.41  E-value: 3.55e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  25 SLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseltKARRQIGMIFQHFNLLSSRTVFGNVA 104
Cdd:cd03298    18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAP-----PADRPVSMLFQENNLFAHLTVEQNVG 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 105 LPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLK 184
Cdd:cd03298    93 LGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVL 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1016201160 185 DINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:cd03298   173 DLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQ 210
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 1-220 4.78e-43

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: 148.28  E-value: 4.78e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlsesELTKA 80
Cdd:cd03266     1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK----EPAEA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:cd03266    77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:cd03266   157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVV 215
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 24-245 2.10e-42

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]


Pssm-ID: 131197 [Multi-domain]  Cd Length: 354  Bit Score: 150.65  E-value: 2.10e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  24 VSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGqelTTLSESE----LTKARRQIGMIFQHFNLLSSRTV 99
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNG---RTLFDSRkgifLPPEKRRIGYVFQEARLFPHLSV 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLElDNTPKEEIKR--RVTELLdlvGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR 177
Cdd:TIGR02142  93 RGNLRYGMK-RARPSERRISfeRVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKY 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 178 SILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTL 245
Cdd:TIGR02142 169 EILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSL 236
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 15-250 3.84e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 147.64  E-value: 3.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  15 TRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsESELTKARRQIGMIFQHFN-L 93
Cdd:PRK13652   14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPIT---KENIREVRKFVGLVFQNPDdQ 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSRTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK13652   91 IFSPTVEQDIAFgPINL-GLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLD 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 173 PATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKtplaqkfIQSTLHLDIP 250
Cdd:PRK13652  170 PQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD-------LLARVHLDLP 240
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 2-220 4.05e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 148.31  E-value: 4.05e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRT-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV-----GGQELTTLSES 75
Cdd:PRK13651    3 IKVKNIVKIFNKKLPTeLKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeKNKKKTKEKEK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  76 ELTKA----------------RRQIGMIFQ--HFNLLSSRT----VFGNVALpleldNTPKEEIKRRVTELLDLVGLGDK 133
Cdd:PRK13651   83 VLEKLviqktrfkkikkikeiRRRVGVVFQfaEYQLFEQTIekdiIFGPVSM-----GVSKEEAKKRAAKYIELVGLDES 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 134 H-DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVA 212
Cdd:PRK13651  158 YlQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTI 236


                  ....*...
gi 1016201160 213 VISNGELI 220
Cdd:PRK13651  237 FFKDGKII 244
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 21-217 1.06e-41

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 144.92  E-value: 1.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkarrqigMIFQHFNLLSSRTVF 100
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 GNVALPLE--LDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:TIGR01184  73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1016201160 179 ILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 18-233 1.66e-41

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


Pssm-ID: 440179 [Multi-domain]  Cd Length: 236  Bit Score: 144.74  E-value: 1.66e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkARRQIGMIFQHFNLLSSR 97
Cdd:COG0410    16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRI--ARLGIGYVPEGRRIFPSL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVALPLELdNTPKEEIKRRVTELLDL--VgLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:COG0410    94 TVEENLLLGAYA-RRDRAEVRADLERVYELfpR-LKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLI 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 176 TRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK 233
Cdd:COG0410   172 VEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAELLADPE 228
cbiO PRK13649
energy-coupling factor transporter ATPase;
2-248 4.47e-41

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 144.89  E-value: 4.47e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSES-ELTK 79
Cdd:PRK13649    3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNkDIKQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQIGMIFQhF--NLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13649   83 IRKKVGLVFQ-FpeSQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESlFEKNPFELSGGQMRRVAIAGILA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSH----- 231
Cdd:PRK13649  162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfle 240

                         250       260
                  ....*....|....*....|....
gi 1016201160 232 ------PK-TPLAQKFIQSTLHLD 248
Cdd:PRK13649  241 ekqlgvPKiTKFAQRLADRGISFS 264
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 2-270 7.06e-41

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 144.11  E-value: 7.06e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:PRK13647    5 IEVEDLHFRYKDGTK---ALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---R 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQH-FNLLSSRTVFGNVAL-PLELDNTPkEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13647   79 SKVGLVFQDpDDQVFSSTVWDDVAFgPVNMGLDK-DEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGE---------LIEQDTVSEvfS 230
Cdd:PRK13647  158 DVIVLDEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRvlaegdkslLTDEDIVEQ--A 234

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1016201160 231 HPKTPLAQKfiqstLHLDIPEDYQARLKASPEtDSVPMLR 270
Cdd:PRK13647  235 GLRLPLVAQ-----IFEDLPELGQSKLPLTVK-EAVQIIR 268
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 1-222 8.27e-41

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 142.61  E-value: 8.27e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK10584    6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 R-RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK10584   86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQ 222
Cdd:PRK10584  166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-243 8.41e-41

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 146.14  E-value: 8.41e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltka 80
Cdd:PRK11650    3 GLKLQAVRKSYDGKT---QVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 rRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11650   76 -RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDpATTRSILEL-LKDINRRLGLTILLITHE----MDVVKRIcdcvaVISNGELIEQ-DTVSEVFSHPKT 234
Cdd:PRK11650  155 VFLFDEPLSNLD-AKLRVQMRLeIQRLHRRLKTTSLYVTHDqveaMTLADRV-----VVMNGGVAEQiGTPVEVYEKPAS 228


                  ....*....
gi 1016201160 235 PLAQKFIQS 243
Cdd:PRK11650  229 TFVASFIGS 237
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 2-222 1.41e-40

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 141.65  E-value: 1.41e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqgtRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLseseltkAR 81
Cdd:cd03269     1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA-------AR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03269    70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:cd03269   150 LILDEPFSGLDPVNVELLKDVIREL-ARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLY 209
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 1-244 1.62e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 144.61  E-value: 1.62e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGT-RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVG----GQELTTLSES 75
Cdd:PRK13631   21 ILRVKNLYCVFDEKQeNELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  76 ELT---------KARRQIGMIFQ--HFNLLSSrTV-----FGNVALpleldNTPKEEIKRRVTELLDLVGLGDKH-DSYP 138
Cdd:PRK13631  101 TNPyskkiknfkELRRRVSMVFQfpEYQLFKD-TIekdimFGPVAL-----GVKKSEAKKLAKFYLNKMGLDDSYlERSP 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 139 ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDiNRRLGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:PRK13631  175 FGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILD-AKANNKTVFVITHTMEHVLEVADEVIVMDKGK 253

                         250       260
                  ....*....|....*....|....*.
gi 1016201160 219 LIEQDTVSEVFSHpktplaQKFIQST 244
Cdd:PRK13631  254 ILKTGTPYEIFTD------QHIINST 273
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 1-200 8.54e-40

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: 139.15  E-value: 8.54e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESeltkA 80
Cdd:COG4133     2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARED----Y 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEikRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:COG4133    74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDiNRRLGLTILLITHE 200
Cdd:COG4133   152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-201 9.05e-40

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 140.99  E-value: 9.05e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRT-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESeltK 79
Cdd:COG1101     1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEY---K 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQIGMIFQhfNLL----SSRTVFGNVALPLE----------LDNTPKEEIKRRVtELLDLvGLGDKHDSYPANLSGGQ 145
Cdd:COG1101    78 RAKYIGRVFQ--DPMmgtaPSMTIEENLALAYRrgkrrglrrgLTKKRRELFRELL-ATLGL-GLENRLDTKVGLLSGGQ 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEM 201
Cdd:COG1101   154 RQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 1-230 1.54e-39

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: 146.10  E-value: 1.54e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVG-GQE---LTTLSES 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRgVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEwvdMTKPGPD 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  76 ELTKARRQIGMIFQHFNLLSSRTVFGNV--ALPLELdntPKEEIKRRVTELLDLVGLGDKH-----DSYPANLSGGQKQR 148
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLteAIGLEL---PDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHR 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515


                  ..
gi 1016201160 229 FS 230
Cdd:TIGR03269 516 VE 517
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 1-230 4.22e-39

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 139.14  E-value: 4.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLE---RPTEGSVQVGGQELTTLSESEL 77
Cdd:PRK13548    2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLR---ALSgelSPDSGEVRLNGRPLADWSPAEL 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 TKARrqiGMIFQHFNLLSSRTVFGNVAL---PLELDNTPKEEIKRRVTELLDLVGLGDKhdSYPAnLSGGQKQRVAIARA 154
Cdd:PRK13548   75 ARRR---AVLPQHSSLSFPFTVEEVVAMgraPHGLSRAEDDALVAAALAQVDLAHLAGR--DYPQ-LSGGEQQRVQLARV 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 155 LA------SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:PRK13548  149 LAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEV 228


                  ..
gi 1016201160 229 FS 230
Cdd:PRK13548  229 LT 230
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
11-257 5.36e-39

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 139.13  E-value: 5.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  11 FQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQH 90
Cdd:PRK11831   15 FTRGNRCI--FDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 FNLLSSRTVFGNVALPL-ELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK11831   93 GALFTDMNVFDNVAYPLrEHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKtPLAQKFIQSTLHLDI 249
Cdd:PRK11831  173 GQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQFLDGIADGPV 251

                         250
                  ....*....|...
gi 1016201160 250 P-----EDYQARL 257
Cdd:PRK11831  252 PfrypaGDYHADL 264
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-233 6.36e-39

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 137.85  E-value: 6.36e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltKA 80
Cdd:COG1137     3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK--RA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGM------IFQhfNLlssrTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARA 154
Cdd:COG1137    77 RLGIGYlpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 155 LASNPKVLLCDEATSALDPATTRSIlellKDINRRL---GLTIlLIT-HEmdvVK---RICDCVAVISNGELIEQDTVSE 227
Cdd:COG1137   151 LATNPKFILLDEPFAGVDPIAVADI----QKIIRHLkerGIGV-LITdHN---VRetlGICDRAYIISEGKVLAEGTPEE 222


                  ....*.
gi 1016201160 228 VFSHPK 233
Cdd:COG1137   223 ILNNPL 228
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 19-227 9.77e-39

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: 137.36  E-value: 9.77e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLER---PTEGSVQVGGQELTTLSESELtkaRRQIGMIFQH---FN 92
Cdd:cd03253    15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILR---LLFRfydVSSGSILIDGQDIREVTLDSL---RRAIGVVPQDtvlFN 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 llssRTVFGNVALPlELDNTPKEEIK-RRVTELLDLV-GLGDKHDSYPAN----LSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:cd03253    89 ----DTIGYNIRYG-RPDATDEEVIEaAKAAQIHDKImRFPDGYDTIVGErglkLSGGEKQRVAIARAILKNPPILLLDE 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 167 ATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSE 227
Cdd:cd03253   164 ATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEE 221
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 1-202 9.92e-39

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 136.84  E-value: 9.92e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkVFQQGTRTIQALNnvsLHVPAGQIYGVIGASGAGKSTLIRCVN-LLERP--TEGSVQVGGQELTTLSesel 77
Cdd:COG4136     1 MLSLENLT-ITLGGRPLLAPLS---LTVAPGEILTLMGPSGSGKSTLLAAIAgTLSPAfsASGEVLLNGRRLTALP---- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 tKARRQIGMIFQ------HFNllssrtVFGNV--ALPlelDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:COG4136    73 -AEQRRIGILFQddllfpHLS------VGENLafALP---PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARV 142

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMD 202
Cdd:COG4136   143 ALLRALLAEPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEE 195
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 2-233 1.14e-38

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 137.29  E-value: 1.14e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltKAR 81
Cdd:cd03218     1 LRAENLSKRY--GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK--RAR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03218    75 LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKF 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK 233
Cdd:cd03218   155 LLLDEPFAGVDPIAVQDIQKIIKILKDR-GIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 16-220 2.54e-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: 135.46  E-value: 2.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELttlSESELtkaRRQIGMIFQHFNlls 95
Cdd:cd03226    11 KGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKER---RKSIGYVMQDVD--- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 sRTVFGN-VALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:cd03226    82 -YQLFTDsVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYK 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1016201160 175 TTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:cd03226   161 NMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 2-223 3.11e-38

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: 136.31  E-value: 3.11e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQ-----------------QGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV 64
Cdd:cd03267     1 IEVSNLSKSYRvyskepgligslkslfkRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  65 GGQelttLSESELTKARRQIGMIF-QHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSG 143
Cdd:cd03267    81 AGL----VPWKRRKKFLRRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQD 223
Cdd:cd03267   157 GQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 1-272 4.58e-38

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 142.15  E-value: 4.58e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP----TEGSVQVGGQELTTLSES 75
Cdd:PRK15134    5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  76 ELTKAR-RQIGMIFQH--FNLLSSRTVFGNVALPLELDNTPKEEIKR-RVTELLDLVGL---GDKHDSYPANLSGGQKQR 148
Cdd:PRK15134   85 TLRGVRgNKIAMIFQEpmVSLNPLHTLEKQLYEVLSLHRGMRREAARgEILNCLDRVGIrqaAKRLTDYPHQLSGGERQR 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:PRK15134  165 VMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATL 244

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1016201160 229 FSHPKTPLAQKFIQSTlhldiPEDYQARLKAspetDSVPMLRME 272
Cdd:PRK15134  245 FSAPTHPYTQKLLNSE-----PSGDPVPLPE----PASPLLDVE 279
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 20-241 4.85e-38

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 136.45  E-value: 4.85e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLER--PT---EGSVQVGGQELTTlSESELTKARRQIGMIFQHFNLL 94
Cdd:PRK14243   25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGfrvEGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  95 SsRTVFGNVA-------LPLELDNTPKEEIKRRVteLLDLVGlgDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:PRK14243  104 P-KSIYDNIAygaringYKGDMDELVERSLRQAA--LWDEVK--DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEP 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 168 TSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVIS---------NGELIEQDTVSEVFSHPKTPLAQ 238
Cdd:PRK14243  179 CSALDPISTLRIEELMHELKEQ--YTIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQATR 256


                  ...
gi 1016201160 239 KFI 241
Cdd:PRK14243  257 DYV 259
cbiO PRK13642
energy-coupling factor transporter ATPase;
18-253 5.51e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 136.76  E-value: 5.51e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlseSELTKARRQIGMIFQH-FNLLSS 96
Cdd:PRK13642   20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTA---ENVWNLRRKIGMVFQNpDNQFVG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  97 RTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:PRK13642   97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 177 RSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHPK--------TPLAQKFIQS--TLH 246
Cdd:PRK13642  177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFATSEdmveigldVPFSSNLMKDlrKNG 255


                  ....*..
gi 1016201160 247 LDIPEDY 253
Cdd:PRK13642  256 FDLPEKY 262
cbiO PRK13641
energy-coupling factor transporter ATPase;
2-233 6.90e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 136.88  E-value: 6.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESE-LTK 79
Cdd:PRK13641    3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnLKK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQIGMIFQhF--NLLSSRTVFGNVAL-PLELDNTpKEEIKRRVTELLDLVGLGDK-HDSYPANLSGGQKQRVAIARAL 155
Cdd:PRK13641   83 LRKKVSLVFQ-FpeAQLFENTVLKDVEFgPKNFGFS-EDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVM 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK 233
Cdd:PRK13641  161 AYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 2-219 7.31e-38

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: 133.11  E-value: 7.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:cd03246     1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNEL---G 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSsrtvfGNVAlplelDNTpkeeikrrvtelldlvglgdkhdsypanLSGGQKQRVAIARALASNPKV 161
Cdd:cd03246    76 DHVGYLPQDDELFS-----GSIA-----ENI----------------------------LSGGQRQRLGLARALYGNPRI 117

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRiCDCVAVISNGEL 219
Cdd:cd03246   118 LVLDEPNSHLDVEGERALNQAIAALKAA-GATRIVIAHRPETLAS-ADRILVLEDGRV 173
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 19-241 8.35e-38

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 135.67  E-value: 8.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVGGQELTTlSESELTKARRQIGMIFQHFNL 93
Cdd:PRK14239   19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYS-PRTDTVDLRKEIGMVFQQPNP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSrTVFGNVALPLELDNTP-KEEIKRRVTELLDLVGLGDK-----HDSyPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:PRK14239   98 FPM-SIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIWDEvkdrlHDS-ALGLSGGQQQRVCIARVLATSPKIILLDEP 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 168 TSALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:PRK14239  176 TSALDPISAGKIEETL--LGLKDDYTMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 20-230 1.60e-37

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: 134.54  E-value: 1.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHfNLLSSRTV 99
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWL---RRQVGVVLQE-NVLFNRSI 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPlelDNTPKeeiKRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:cd03252    93 RDNIALA---DPGMS---MERVIEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEAT 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 169 SALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFS 230
Cdd:cd03252   167 SALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 1-234 1.66e-37

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 136.76  E-value: 1.66e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVF-----QQG------------TRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQ 63
Cdd:COG4586     1 IIEVENLSKTYrvyekEPGlkgalkglfrreYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  64 VGGqelttLSESELTKA-RRQIGMIFQH-------------FNLLssRTVFGnvalpleldnTPKEEIKRRVTELLDLVG 129
Cdd:COG4586    81 VLG-----YVPFKRRKEfARRIGVVFGQrsqlwwdlpaidsFRLL--KAIYR----------IPDAEYKKRLDELVELLD 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 130 LGDKHDSyPA-NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRIC 208
Cdd:COG4586   144 LGELLDT-PVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALC 222

                         250       260
                  ....*....|....*....|....*....
gi 1016201160 209 DCVAVISNGELIEQDTVSEV---FSHPKT 234
Cdd:COG4586   223 DRVIVIDHGRIIYDGSLEELkerFGPYKT 251
cbiO PRK13645
energy-coupling factor transporter ATPase;
2-258 3.26e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 135.14  E-value: 3.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSES--ELT 78
Cdd:PRK13645    7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPANLKKikEVK 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQ--HFNLLSSrTVFGNVAL-PLELdNTPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARA 154
Cdd:PRK13645   87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNL-GENKQEAYKKVPELLKLVQLPEDYvKRSPFELSGGQKRRVALAGI 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 155 LASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKt 234
Cdd:PRK13645  165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSNQE- 243

                         250       260
                  ....*....|....*....|....
gi 1016201160 235 plaqkfIQSTLHLDIPEDYQARLK 258
Cdd:PRK13645  244 ------LLTKIEIDPPKLYQLMYK 261
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-217 3.79e-37

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 133.17  E-value: 3.79e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIqalnnvSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseltKA 80
Cdd:PRK10771    1 MLKLTDITWLYHHLPMRF------DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTP-----PS 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK10771   70 RRPVSMLFQENNLFSHLTVAQNIGLGLNPGLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQP 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK10771  150 ILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADG 206
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1-230 5.55e-37

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 133.32  E-value: 5.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkA 80
Cdd:COG4559     1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWEL--A 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQiGMIFQHFNLLSSRTVFGNVAL---PLELDNTPKEEIKRRVTELLDLVGLGDKHdsYPAnLSGGQKQRVAIARALA- 156
Cdd:COG4559    75 RRR-AVLPQHSSLAFPFTVEEVVALgraPHGSSAAQDRQIVREALALVGLAHLAGRS--YQT-LSGGEQQRVQLARVLAq 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 157 ------SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:COG4559   151 lwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLT 229
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
20-202 5.58e-37

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 133.29  E-value: 5.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseltkARRqiGMIFQHFNLLSSRTV 99
Cdd:PRK11248   16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPG------AER--GVVFQNEGLLPWRNV 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:PRK11248   88 QDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQM 167

                         170       180
                  ....*....|....*....|...
gi 1016201160 180 LELLKDINRRLGLTILLITHEMD 202
Cdd:PRK11248  168 QTLLLKLWQETGKQVLLITHDIE 190
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-219 5.95e-37

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 133.60  E-value: 5.95e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGtrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL---ERPTEGSVQVGGQELTTLSE--S 75
Cdd:PRK09984    4 IIRVEKLAKTFNQH----QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGRlaR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  76 ELTKARRQIGMIFQHFNLLSSRTVFGNVaLPLELDNTP---------KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQK 146
Cdd:PRK09984   80 DIRKSRANTGYIFQQFNLVNRLSVLENV-LIGALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK09984  159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHV 231
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 2-245 7.99e-37

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 133.24  E-value: 7.99e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLL-----ERPTEGSVQVGGQELTTlSESE 76
Cdd:PRK14258    8 IKVNNLS--FYYDTQKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYE-RRVN 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  77 LTKARRQIGMIFQHFNLLSsRTVFGNVALPLELDN-TPKEEIKRRVTELLDLVGLGD--KHDSYPA--NLSGGQKQRVAI 151
Cdd:PRK14258   83 LNRLRRQVSMVHPKPNLFP-MSVYDNVAYGVKIVGwRPKLEIDDIVESALKDADLWDeiKHKIHKSalDLSGGQQQRLCI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISN-----GELIEQDTVS 226
Cdd:PRK14258  162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241

                         250
                  ....*....|....*....
gi 1016201160 227 EVFSHPKTPLAQKFIQSTL 245
Cdd:PRK14258  242 KIFNSPHDSRTREYVLSRL 260
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
17-270 9.02e-37

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 135.03  E-value: 9.02e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  17 TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLE---RPTEGSVQVGGQELTTLSESELTK-ARRQIGMIFQHF 91
Cdd:COG4170    19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAiCGITKdnwHVTADRFRWNGIDLLKLSPRERRKiIGREIAMIFQEP 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  92 N--LLSSRTVFGNValpleLDNTPKEEI-----------KRRVTELLDLVGLGDKHD---SYPANLSGGQKQRVAIARAL 155
Cdd:COG4170    99 SscLDPSAKIGDQL-----IEAIPSWTFkgkwwqrfkwrKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAI 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTP 235
Cdd:COG4170   174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHP 253

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1016201160 236 LAQKFIQSTLHLDIPEDYQARLKASPetDSVPMLR 270
Cdd:COG4170   254 YTKALLRSMPDFRQPLPHKSRLNTLP--GSIPPLQ 286
cbiO PRK13643
energy-coupling factor transporter ATPase;
1-229 1.80e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 133.32  E-value: 1.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTR-TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLS-ESELT 78
Cdd:PRK13643    1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKH-DSYPANLSGGQKQRVAIARALA 156
Cdd:PRK13643   81 PVRKKVGVVFQFpESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGILA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVF 229
Cdd:PRK13643  161 MEPEVLVLDEPTAGLDPKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 2-227 2.68e-36

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 138.55  E-value: 2.68e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaR 81
Cdd:TIGR03797 452 IEVDRVT--FRYRPDGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGLDVQAV---R 526

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSrTVFGNVA--LPLELDntpkeeikrRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQR 148
Cdd:TIGR03797 527 RQLGVVLQNGRLMSG-SIFENIAggAPLTLD---------EAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQR 596

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKdinrRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSE 227
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLE----RLKVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDE 670
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 2-227 2.84e-36

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: 130.81  E-value: 2.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVGGQELTTLSESELt 78
Cdd:cd03251     1 VEFKNVT--FRYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTL---VNLIPRfydVDSGRILIDGHDVRDYTLASL- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNLLSSrTVFGNVALPLEldNTPKEEIKR--RVTELLDLV-GLGDKHDSY----PANLSGGQKQRVAI 151
Cdd:cd03251    75 --RRQIGLVSQDVFLFND-TVAENIAYGRP--GATREEVEEaaRAANAHEFImELPEGYDTVigerGVKLSGGQRQRIAI 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTR----SILELLKdiNRrlglTILLITHEMDVVKRIcDCVAVISNGELIEQDTVSE 227
Cdd:cd03251   150 ARALLKDPPILILDEATSALDTESERlvqaALERLMK--NR----TTFVIAHRLSTIENA-DRIVVLEDGKIVERGTHEE 222
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-231 5.28e-36

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 130.59  E-value: 5.28e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQ------------------QGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSV 62
Cdd:COG1134     4 MIEVENVSKSYRlyhepsrslkelllrrrrTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  63 QVGGQ-----ELTTLSESELTkARRQIGMIFQHFNLlssrtvfgnvalpleldntPKEEIKRRVTELLDLVGLGDKHD-- 135
Cdd:COG1134    84 EVNGRvsallELGAGFHPELT-GRENIYLNGRLLGL-------------------SRKEIDEKFDEIVEFAELGDFIDqp 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 136 --SYpanlSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAV 213
Cdd:COG1134   144 vkTY----SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIW 218

                         250
                  ....*....|....*...
gi 1016201160 214 ISNGELIEQDTVSEVFSH 231
Cdd:COG1134   219 LEKGRLVMDGDPEEVIAA 236
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 16-224 5.43e-36

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: 137.26  E-value: 5.43e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLER---PTEGSVQVGGQELTTLSESELtkaRRQIGMIFQH-- 90
Cdd:COG5265   371 RPI--LKGVSFEVPAGKTVAIVGPSGAGKSTLAR---LLFRfydVTSGRILIDGQDIRDVTQASL---RAAIGIVPQDtv 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 -FNllssRTVFGNVALPlELDNTPkEEIKR--RVTELLDLV-GLGDKHDSYPA----NLSGGQKQRVAIARALASNPKVL 162
Cdd:COG5265   443 lFN----DTIAYNIAYG-RPDASE-EEVEAaaRAAQIHDFIeSLPDGYDTRVGerglKLSGGEKQRVAIARTLLKNPPIL 516

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 163 LCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDT 224
Cdd:COG5265   517 IFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGT 575
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-232 6.42e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 131.26  E-value: 6.42e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGqeLTTLSESELTKA 80
Cdd:PRK13644    1 MIRLENVSYSYPDGT---PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSG--IDTGDFSKLQGI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNL-LSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK13644   76 RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVkRICDCVAVISNGELIEQDTVSEVFSHP 232
Cdd:PRK13644  156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 20-261 1.46e-35

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 131.77  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP--TEGSVQVGGQELTTLSESELTKAR-RQIGMIFQhfNLLS 95
Cdd:PRK09473   31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRaEQISMIFQ--DPMT 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 SRTVFGNVA------LPLELDNTPKEEIKRRVtELLDLVGLGDKHDS---YPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK09473  109 SLNPYMRVGeqlmevLMLHKGMSKAEAFEESV-RMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIADE 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 167 ATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLH 246
Cdd:PRK09473  188 PTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAVPR 267

                         250
                  ....*....|....*
gi 1016201160 247 LDIPEDYQARLKASP 261
Cdd:PRK09473  268 LDAEGESLLTIPGNP 282
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 19-228 2.76e-35

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 128.41  E-value: 2.76e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltKARRQIG------MIFQHFn 92
Cdd:TIGR03410  14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE--RARAGIAyvpqgrEIFPRL- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 llssrTVFGNvaLPLELDNTPKEEiKRRVTELLDLvglgdkhdsYPA----------NLSGGQKQRVAIARALASNPKVL 162
Cdd:TIGR03410  91 -----TVEEN--LLTGLAALPRRS-RKIPDEIYEL---------FPVlkemlgrrggDLSGGQQQQLAIARALVTRPKLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 163 LCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:TIGR03410 154 LLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 19-242 6.73e-35

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 133.68  E-value: 6.73e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKST----LIRCVNllerpTEGSVQVGGQELTTLSESELTKARRQIGMIFQHFN-L 93
Cdd:PRK15134  300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsS 374

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSR-TVFGNVALPLELDNTP--KEEIKRRVTELLDLVGLG-DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK15134  375 LNPRlNVLQIIEEGLRVHQPTlsAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQ 242
Cdd:PRK15134  455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLA 527
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
1-245 1.53e-34

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 129.61  E-value: 1.53e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLsNITKvfQQGTRTIQalnnVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQeltTLSESE---- 76
Cdd:PRK11144    1 MLEL-NFKQ--QLGDLCLT----VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAEkgic 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  77 LTKARRQIGMIFQHFNLLSSRTVFGNvaLPLELDNTPKEEIKRrVTELLdlvGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK11144   71 LPPEKRRIGYVFQDARLFPHYKVRGN--LRYGMAKSMVAQFDK-IVALL---GIEPLLDRYPGSLSGGEKQRVAIGRALL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPK-TP 235
Cdd:PRK11144  145 TAPELLLMDEPLASLDLPRKRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASSAmRP 224

                         250
                  ....*....|
gi 1016201160 236 LAQKFIQSTL 245
Cdd:PRK11144  225 WLPKEEQSSI 234
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 20-214 2.22e-34

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: 132.03  E-value: 2.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLSSrTV 99
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---RDQIAWVPQHPFLFAG-TI 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPlELDNTPkEEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:TIGR02857 413 AENIRLA-RPDASD-AEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALARAFLRDAPLLLLDEPTAHLD 490

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016201160 173 PATTRSILELLKDINRrlGLTILLITHEmDVVKRICDCVAVI 214
Cdd:TIGR02857 491 AETEAEVLEALRALAQ--GRTVLLVTHR-LALAALADRIVVL 529
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 18-229 2.62e-34

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 125.80  E-value: 2.62e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHfNLL 94
Cdd:cd03254    16 KPVLKDINFSIKPGETVAIVGPTGAGKTTLI---NLLMRfydPQKGQILIDGIDIRDISRKSL---RSMIGVVLQD-TFL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  95 SSRTVFGNVALPlelDNTPKEEikrRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLL 163
Cdd:cd03254    89 FSGTIMENIRLG---RPNATDE---EVIEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILI 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 164 CDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVF 229
Cdd:cd03254   163 LDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELL 225
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 2-231 4.90e-34

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 131.38  E-value: 4.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVGGQELTTLSESELt 78
Cdd:TIGR02203 331 VEFRNVT--FRYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYTLASL- 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNLLSSrTVFGNVALPlELDNTPKEEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAI 151
Cdd:TIGR02203 405 --RRQVALVSQDVVLFND-TIANNIAYG-RTEQADRAEIERalAAAYAQDFVdklplGLDTPIGENGVLLSGGQRQRLAI 480

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSH 231
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLAR 557
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
2-243 4.93e-34

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 128.61  E-value: 4.93e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIQalNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELttlseSELTKAR 81
Cdd:PRK11000    4 VTLRNVTKAY--GDVVIS--KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRM-----NDVPPAE 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK11000   75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:PRK11000  155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFI 234


                  ..
gi 1016201160 242 QS 243
Cdd:PRK11000  235 GS 236
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 19-261 1.02e-33

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 126.78  E-value: 1.02e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERP---TEGSVQVGGQELTTLSEseltKARRQI-----GMIFQ 89
Cdd:PRK11022   21 RAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE----KERRNLvgaevAMIFQ 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  90 H--FNLLSSRTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGD---KHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:PRK11022   97 DpmTSLNPCYTVGFQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDpasRLDVYPHQLSGGMSQRVMIAMAIACRPKLLI 176

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 164 CDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQS 243
Cdd:PRK11022  177 ADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRA 256

                         250       260
                  ....*....|....*....|
gi 1016201160 244 tlhldIPE--DYQARLKASP 261
Cdd:PRK11022  257 -----LPEfaQDKARLASLP 271
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 20-224 3.44e-33

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: 122.60  E-value: 3.44e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseLTKARRQIGMIFQHFNLLSSrTV 99
Cdd:cd03244    19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIG---LHDLRSRISIIPQDPVLFSG-TI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVAlPL------ELDNTPKE-EIKRRVTELLDlvGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:cd03244    95 RSNLD-PFgeysdeELWQALERvGLKEFVESLPG--GLDTVVEEGGENLSVGQRQLLCLARALLRKSKILVLDEATASVD 171

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 173 PATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDT 224
Cdd:cd03244   172 PETDALIQKTIR--EAFKDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFDS 220
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 1-228 3.94e-33

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 123.27  E-value: 3.94e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkA 80
Cdd:COG4604     1 MIEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSREL--A 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRqIGMIFQHfNLLSSR-TV-----FG-------NvalpleldntPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQ 147
Cdd:COG4604    75 KR-LAILRQE-NHINSRlTVrelvaFGrfpyskgR----------LTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 148 RVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:COG4604   143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222


                  .
gi 1016201160 228 V 228
Cdd:COG4604   223 I 223
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-261 6.74e-33

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 124.15  E-value: 6.74e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEseltKAR 81
Cdd:PRK13537    8 IDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR----HAR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK13537   80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNG---------ELIEQDT---VSEVF 229
Cdd:PRK13537  160 LVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGrkiaegaphALIESEIgcdVIEIY 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1016201160 230 SHPK-------TPLAQKFIQS--TL--HLDIPEDYQARLKASP 261
Cdd:PRK13537  239 GPDPvalrdelAPLAERTEISgeTLfcYVRDPEPLHARLKGRA 281
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 21-241 7.06e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 123.28  E-value: 7.06e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEG-----SVQVGGQELttLSESELTKARRQIGMIFQHFNLLS 95
Cdd:PRK14271   37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSI--FNYRDVLEFRRRVGMLFQRPNPFP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 sRTVFGNVALPLELDN-TPKEEIKRRVTELLDLVGL----GDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:PRK14271  115 -MSIMDNVLAGVRAHKlVPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSA 193

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 171 LDPATTRSILELLKDINRRlgLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFI 241
Cdd:PRK14271  194 LDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYV 262
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
1-243 9.21e-33

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 122.59  E-value: 9.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGT-----RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlseS 75
Cdd:PRK15112    4 LLEVRNLSKTFRYRTgwfrrQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHF---G 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  76 ELTKARRQIGMIFQH-FNLLSSRTVFGNVA-LPLELdNT--PKEEIKRRVTELLDLVGLGDKHDSY-PANLSGGQKQRVA 150
Cdd:PRK15112   81 DYSYRSQRIRMIFQDpSTSLNPRQRISQILdFPLRL-NTdlEPEQREKQIIETLRQVGLLPDHASYyPHMLAPGQKQRLG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 151 IARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK15112  160 LARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLA 239

                         250
                  ....*....|...
gi 1016201160 231 HPKTPLAQKFIQS 243
Cdd:PRK15112  240 SPLHELTKRLIAG 252
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 20-232 1.40e-32

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 121.64  E-value: 1.40e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkARRQIGMIFQHFNLLSSRTV 99
Cdd:PRK11300   20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI--ARMGVVRTFQHVRLFREMTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGN--VALPLELD--------NTP-----KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLC 164
Cdd:PRK11300   98 IENllVAQHQQLKtglfsgllKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILML 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 165 DEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHP 232
Cdd:PRK11300  178 DEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRNNP 245
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 23-247 1.41e-32

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 121.73  E-value: 1.41e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  23 NVSLHVPAGQIYGVIGASGAGKStlIRCVNLLERPTEGSVQVGGQELTTLSESELTKAR-RQIGMIFQH----FNLLssR 97
Cdd:PRK10418   21 GVSLTLQRGRVLALVGGSGSGKS--LTCAAALGILPAGVRQTAGRVLLDGKPVAPCALRgRKIATIMQNprsaFNPL--H 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVALPLELDNTPKEEikRRVTELLDLVGLGDKH---DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:PRK10418   97 TMHTHARETCLALGKPADD--ATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVV 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 175 TTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHL 247
Cdd:PRK10418  175 AQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSAHLAL 247
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 1-199 2.12e-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: 120.96  E-value: 2.12e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITkvFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEG-SVQVGGQELTTLSESELtk 79
Cdd:COG1119     3 LLELRNVT--VRRGGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWEL-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 aRRQIGMI--FQHFNLLSSRTV--------FGNVALPLELDntpkEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:COG1119    77 -RKRIGLVspALQLRFPRDETVldvvlsgfFDSIGLYREPT----DEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1016201160 150 AIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITH 199
Cdd:COG1119   152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTH 201
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 1-241 5.07e-32

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 126.12  E-value: 5.07e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKS-TLIRCVNLLERpTEGSVQVGGQ----------EL 69
Cdd:PRK10261   12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviEL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  70 TTLSESELTKAR-RQIGMIFQH--FNLLSSRTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGDKH---DSYPANLS 142
Cdd:PRK10261   91 SEQSAAQMRHVRgADMAMIFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLS 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 143 GGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQ 222
Cdd:PRK10261  171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVET 250

                         250
                  ....*....|....*....
gi 1016201160 223 DTVSEVFSHPKTPLAQKFI 241
Cdd:PRK10261  251 GSVEQIFHAPQHPYTRALL 269
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 2-229 6.28e-32

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: 125.30  E-value: 6.28e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLE--RPTEGSV----------------- 62
Cdd:TIGR03269   1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGRIiyhvalcekcgyverps 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  63 ------QVGGQELTT-------LSESELTKARRQIGMIFQH-FNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLV 128
Cdd:TIGR03269  77 kvgepcPVCGGTLEPeevdfwnLSDKLRRRIRKRIAIMLQRtFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 129 GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236

                         250       260
                  ....*....|....*....|....
gi 1016201160 209 DCVAVISNGELIEQ---DTVSEVF 229
Cdd:TIGR03269 237 DKAIWLENGEIKEEgtpDEVVAVF 260
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
 2-227 8.73e-32

gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 118.66  E-value: 8.73e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlseseltKAR 81
Cdd:TIGR03740   1 LETKNLSKRFGKQT----AVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR-------KDL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:TIGR03740  70 HKIGSLIESPPLYENLTARENLKVHTTLLGLPDSRID----EVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKL 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:TIGR03740 146 LILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKINK 210
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 20-219 3.47e-31

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: 115.99  E-value: 3.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA--------RRQIGmifqhf 91
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG------ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  92 nLLSSRTVFGNVALPLELdntpkeeikrrvtelldlvglgdkhdsypanlSGGQKQRVAIARALASNPKVLLCDEATSAL 171
Cdd:cd03215    89 -LVLDLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGV 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1016201160 172 DPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:cd03215   136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 18-220 8.41e-31

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic bacteriocins of lactic acid bacteria are produced as precursors which have N-terminal leader peptides that share similarities in amino acid sequence and contain a conserved processing site of two glycine residues in positions -1 and -2. A dedicated ATP-binding cassette (ABC) transporter is responsible for the proteolytic cleavage of the leader peptides and subsequent translocation of the bacteriocins across the cytoplasmic membrane.


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 116.15  E-value: 8.41e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  18 IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLSSr 97
Cdd:cd03245    17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL---RRNIGYVPQDVTLFYG- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVAL--PLELDntpkeeikRRVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLLC 164
Cdd:cd03245    93 TLRDNITLgaPLADD--------ERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLL 164

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 165 DEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKrICDCVAVISNGELI 220
Cdd:cd03245   165 DEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIV 217
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-220 1.84e-30

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 118.39  E-value: 1.84e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESeltkAR 81
Cdd:PRK13536   42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARL----AR 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK13536  114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:PRK13536  194 LILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVLEAGRKI 251
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
2-246 2.70e-30

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 120.89  E-value: 2.70e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLER---PTEGSVQVGGQELttlSESELT 78
Cdd:PRK11176  342 IEFRNVT--FTYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTI---ANLLTRfydIDEGEILLDGHDL---RDYTLA 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQHFNLLSSrTVFGNVALPLElDNTPKEEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAI 151
Cdd:PRK11176  414 SLRNQVALVSQNVHLFND-TIANNIAYART-EQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAI 491

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDI--NRrlglTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVf 229
Cdd:PRK11176  492 ARALLRDSPILILDEATSALDTESERAIQAALDELqkNR----TSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAEL- 565

                         250
                  ....*....|....*..
gi 1016201160 230 shpktpLAQKFIQSTLH 246
Cdd:PRK11176  566 ------LAQNGVYAQLH 576
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
19-227 7.10e-30

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 119.68  E-value: 7.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHfNLLS 95
Cdd:PRK13657  349 QGVEDVSFEAKPGQTVAIVGPTGAGKSTLI---NLLQRvfdPQSGRILIDGTDIRTVTRASL---RRNIAVVFQD-AGLF 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 SRTVFGNVALPLElDNTPkEEIKR--RVTELLDLVGlgDKHDSYPAN-------LSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK13657  422 NRSIEDNIRVGRP-DATD-EEMRAaaERAQAHDFIE--RKPDGYDTVvgergrqLSGGERQRLAIARALLKDPPILILDE 497

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 167 ATSALDPATTRSILELLKDInrRLGLTILLITHEMDVVkRICDCVAVISNGELIEQDTVSE 227
Cdd:PRK13657  498 ATSALDVETEAKVKAALDEL--MKGRTTFIIAHRLSTV-RNADRILVFDNGRVVESGSFDE 555
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
4-228 1.07e-29

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 118.48  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKArrQ 83
Cdd:PRK11288    7 FDGIGKTFP----GVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALAA--G 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 IGMIFQHFNLLSSRTVFGNV---ALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK11288   81 VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 161 VLLCDEATSALdpaTTRSIlELLKDINRRL---GLTILLITHEMDVVKRICDCVAVISNGELIEQ-DTVSEV 228
Cdd:PRK11288  161 VIAFDEPTSSL---SAREI-EQLFRVIRELraeGRVILYVSHRMEEIFALCDAITVFKDGRYVATfDDMAQV 228
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 2-221 3.20e-29

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: 111.86  E-value: 3.20e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVF------------------QQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQ 63
Cdd:cd03220     1 IELENVSKSYptykggssslkklgilgrKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  64 VGGQ-----ELTTLSESELTkARRqigmifqhfnllssrtvfgNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYP 138
Cdd:cd03220    81 VRGRvssllGLGGGFNPELT-GRE-------------------NIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPV 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 139 ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd03220   141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGK 219


                  ...
gi 1016201160 219 LIE 221
Cdd:cd03220   220 IRF 222
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 6-220 3.36e-29

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: 111.98  E-value: 3.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   6 NITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLERPTEGSVQVGGQELTTLSESELTKARRQIG 85
Cdd:cd03234     8 DVGLKAKNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLL---DAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVA 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  86 MIFQHFNLLSSRTVFGNV--ALPLELDNTPKEEIKRRVTELLDLVGLGDKH--DSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03234    85 YVRQDDILLPGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRDLALTRigGNLVKGISGGERRRVSIAVQLLWDPKV 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRRlGLTILLITHE--MDVVkRICDCVAVISNGELI 220
Cdd:cd03234   165 LILDEPTSGLDSFTALNLVSTLSQLARR-NRIVILTIHQprSDLF-RLFDRILLLSSGEIV 223
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 6-220 7.09e-29

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 116.18  E-value: 7.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   6 NITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLeRPT---EGSVQVGGQELT--TLSESEltka 80
Cdd:PRK13549   10 NITKTFG----GVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHgtyEGEIIFEGEELQasNIRDTE---- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELdnTPK-----EEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARAL 155
Cdd:PRK13549   81 RAGIAIIHQELALVKELSVLENIFLGNEI--TPGgimdyDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKAL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:PRK13549  159 NKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHI 222
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 11-211 7.29e-29

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 110.96  E-value: 7.29e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  11 FQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQH 90
Cdd:PRK10247   15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIY---RQQVSYCAQT 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 FNLLSSrTVFGNVALPLELDNTPKEEikRRVTELLDLVGLGDKHDSYPAN-LSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK10247   90 PTLFGD-TVYDNLIFPWQIRNQQPDP--AIFLDDLERFALPDTILTKNIAeLSGGEKQRISLIRNLQFMPKVLLLDEITS 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1016201160 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCV 211
Cdd:PRK10247  167 ALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKV 207
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-228 9.41e-29

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 116.04  E-value: 9.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESelTKA 80
Cdd:PRK09700    5 YISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK--LAA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNV---ALPLE----LDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIAR 153
Cdd:PRK09700   79 QLGIGIIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 154 ALASNPKVLLCDEATSALdpatTRSILELLKDINRRL---GLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:PRK09700  159 TLMLDAKVIIMDEPTSSL----TNKEVDYLFLIMNQLrkeGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 13-220 9.81e-29

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: 109.95  E-value: 9.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  13 QGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVN--LLERPTEGSVQVGGqelTTLSESELtkaRRQIGMIFQH 90
Cdd:cd03213    19 KSGKQL--LKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLING---RPLDKRSF---RKIIGYVPQD 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 FNLLSSRTVFGNVALPLELdntpkeeikrrvtelldlvglgdkhdsypANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:cd03213    91 DILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 171 LDPATTRSILELLKDInRRLGLTILLITHE-MDVVKRICDCVAVISNGELI 220
Cdd:cd03213   142 LDSSSALQVMSLLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRVI 191
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 4-219 1.19e-28

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: 117.04  E-value: 1.19e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160    4 LSNITKVFQQGTRTiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELttlsESELTKARRQ 83
Cdd:TIGR01257  931 VKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS 1004

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   84 IGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLL 163
Cdd:TIGR01257 1005 LGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVV 1084

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160  164 CDEATSALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:TIGR01257 1085 LDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRL 1138
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 19-232 1.68e-28

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 116.36  E-value: 1.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTlirCVNLLER---PTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHfNLLS 95
Cdd:TIGR00958 495 PVLKGLTFTLHPGEVVALVGPSGSGKST---VAALLQNlyqPTGGQVLLDGVPLVQYDHHYL---HRQVALVGQE-PVLF 567

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 SRTVFGNVALPLelDNTPKEEIKRRVTELLDLVGLGDKHDSYPAN-------LSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:TIGR00958 568 SGSVRENIAYGL--TDTPDEEIMAAAKAANAHDFIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEAT 645

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 169 SALDPATTRsileLLKDINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHP 232
Cdd:TIGR00958 646 SALDAECEQ----LLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
19-230 2.73e-28

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 110.87  E-value: 2.73e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtLSESELTKARRQIGMIFQHfnllSSRT 98
Cdd:PRK13638   15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQVATVFQD----PEQQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VF-----GNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:PRK13638   90 IFytdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 174 ATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK13638  170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 6-230 4.04e-28

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 109.60  E-value: 4.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   6 NITKVFQqGTRTIQalnNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESEltKARRQIG 85
Cdd:PRK10895    8 NLAKAYK-GRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  86 MIFQHFNLLSSRTVFGNVALPLEL-DNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLC 164
Cdd:PRK10895   82 YLPQEASIFRRLSVYDNLMAVLQIrDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 165 DEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK10895  162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQ 226
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 2-231 5.82e-28

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 114.07  E-value: 5.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLeRPTEGSVQVGGQELTTLSESELtka 80
Cdd:COG4618   331 LSVENLTVVPPGSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLlVGVW-PPTAGSVRLDGADLSQWDREEL--- 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQhfnllssrtvfgNVALpleLDNTPKEEIKR-------RVTELLDLVGLgdkHD---SYP-----------A 139
Cdd:COG4618   405 GRHIGYLPQ------------DVEL---FDGTIAENIARfgdadpeKVVAAAKLAGV---HEmilRLPdgydtrigeggA 466

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 140 NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVkRICDCVAVISNGEL 219
Cdd:COG4618   467 RLSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLL-AAVDKLLVLRDGRV 544

                         250
                  ....*....|..
gi 1016201160 220 IEQDTVSEVFSH 231
Cdd:COG4618   545 QAFGPRDEVLAR 556
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-268 7.99e-28

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 111.05  E-value: 7.99e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV------NLleRPTEGSVQVGGQELTTLSE 74
Cdd:PRK15093    3 LLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAIcgvtkdNW--RVTADRMRFDDIDLLRLSP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  75 SELTK-ARRQIGMIFQHfnllssrtvfgnvalPLE-LDntPKEEI------------------------KRRVTELLDLV 128
Cdd:PRK15093   81 RERRKlVGHNVSMIFQE---------------PQScLD--PSERVgrqlmqnipgwtykgrwwqrfgwrKRRAIELLHRV 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 129 GLGDKHD---SYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVK 205
Cdd:PRK15093  144 GIKDHKDamrSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLS 223

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 206 RICDCVAVISNGELIEQDTVSEVFSHPKTPLAQKFIQSTLHLDIPEDYQARLK----ASPETDSVPM 268
Cdd:PRK15093  224 QWADKINVLYCGQTVETAPSKELVTTPHHPYTQALIRAIPDFGSAMPHKSRLNtlpgAIPLLEHLPI 290
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-222 8.75e-28

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 113.77  E-value: 8.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLER---PTEGSVQVGGQELTTLSESELt 78
Cdd:PRK11160  339 LTLNNVS--FTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL---QLLTRawdPQQGEILLNGQPIADYSEAAL- 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNLLSSrTVFGNVALPLEldnTPKEEikrRVTELLDLVGLGDKHDSYPA----------NLSGGQKQR 148
Cdd:PRK11160  413 --RQAISVVSQRVHLFSA-TLRDNLLLAAP---NASDE---ALIEVLQQVGLEKLLEDDKGlnawlgeggrQLSGGEQRR 483

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITH------EMDvvkRICdcvaVISNGELIEQ 222
Cdd:PRK11160  484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHrltgleQFD---RIC----VMDNGQIIEQ 554
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-230 9.04e-28

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 108.95  E-value: 9.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTka 80
Cdd:PRK11231    2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 rRQIGMIFQHFNLLSSRTVFGNVAL---P-LELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:PRK11231   76 -RRLALLPQHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK11231  155 QDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMT 227
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 20-199 1.03e-27

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: 113.22  E-value: 1.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLSSrTV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEV---RRRVSVCAQDAHLFDT-TV 425

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLElDNTPKEeikrrVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:TIGR02868 426 RENLRLARP-DATDEE-----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEPT 499

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1016201160 169 SALDPATTRSILELLKDINRrlGLTILLITH 199
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALS--GRTVVLITH 528
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 2-219 1.41e-27

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: 107.56  E-value: 1.41e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRT-IQALNNVSLHVPAGQIYGVIGASGAGKSTlirCVNLLER---PTEGSVQVGGQELTTLSESEL 77
Cdd:cd03248    12 VKFQNVT--FAYPTRPdTLVLQDVSFTLHPGEVTALVGPSGSGKST---VVALLENfyqPQGGQVLLDGKPISQYEHKYL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 tkaRRQIGMIFQHfNLLSSRTVFGNVALPLEldNTPKEEIKRR---------VTELLDlvGLGDKHDSYPANLSGGQKQR 148
Cdd:cd03248    87 ---HSKVSLVGQE-PVLFARSLQDNIAYGLQ--SCSFECVKEAaqkahahsfISELAS--GYDTEVGEKGSQLSGGQKQR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRiCDCVAVISNGEL 219
Cdd:cd03248   159 VAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAHRLSTVER-ADQILVLDGGRI 226
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
16-228 7.52e-27

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 106.80  E-value: 7.52e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeselTKA-RRQIGMIFQHFNLL 94
Cdd:PRK10575   24 RTL--LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWS----SKAfARKVAYLPQQLPAA 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  95 SSRTVFGNVAL---PLE--LDNTPKEEiKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK10575   98 EGMTVRELVAIgryPWHgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTS 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:PRK10575  177 ALDIAHQVDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 19-224 9.28e-27

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: 104.80  E-value: 9.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLsesELTKARRQIGMIFQHFNLLSsrt 98
Cdd:cd03369    22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLRSSLTIIPQDPTLFS--- 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 vfGNVALPLELDNtpkEEIKRRVTELLDLVGLGDkhdsypaNLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT--- 175
Cdd:cd03369    96 --GTIRSNLDPFD---EYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATdal 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1016201160 176 -TRSILELLKDInrrlglTILLITHEMDVVKRiCDCVAVISNGELIEQDT 224
Cdd:cd03369   164 iQKTIREEFTNS------TILTIAHRLRTIID-YDKILVMDAGEVKEYDH 206
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-220 1.16e-26

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 110.15  E-value: 1.16e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQElttlseseltkarrQ 83
Cdd:COG0488     1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKGL--------------R 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 IGMIFQHFNLLSSRTVFGNV--------ALPLELD------NTPKEEIKR--RVTELLD--------------LVGLG-- 131
Cdd:COG0488    63 IGYLPQEPPLDDDLTVLDTVldgdaelrALEAELEeleaklAEPDEDLERlaELQEEFEalggweaearaeeiLSGLGfp 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 132 -DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINRrlglTILLITHE---MD-VVK 205
Cdd:COG0488   143 eEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD-LESIEWLEeFLKNYPG----TVLVVSHDryfLDrVAT 217

                         250
                  ....*....|....*
gi 1016201160 206 RICDcvavISNGELI 220
Cdd:COG0488   218 RILE----LDRGKLT 228
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 1-221 3.46e-26

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 108.61  E-value: 3.46e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGgqelTTLseseltka 80
Cdd:COG0488   315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKLG----ETV-------- 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 rrQIGMIFQHFNLlssrtvfgnvalpLELDNTPKEEIKR-----RVTELLDLVGL----GDKHDSYPANLSGGQKQRVAI 151
Cdd:COG0488   379 --KIGYFDQHQEE-------------LDPDKTVLDELRDgapggTEQEVRGYLGRflfsGDDAFKPVGVLSGGEKARLAL 443

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINrrlGlTILLITHEMDVVKRICDCVAVISNGELIE 221
Cdd:COG0488   444 AKLLLSPPNVLLLDEPTNHLDIETLEALEEALDDFP---G-TVLLVSHDRYFLDRVATRILEFEDGGVRE 509
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 1-220 3.98e-26

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 108.37  E-value: 3.98e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIR--CVNLLERPTEGSVQVGGQEL--TTLSESE 76
Cdd:TIGR02633   1 LLEMKGIVKTFG----GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKilSGVYPHGTWDGEIYWSGSPLkaSNIRDTE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  77 ltkaRRQIGMIFQHFNLLSSRTVFGNVALPLEL----DNTPKEEIKRRVTELLDLVGLGDKHDSYP-ANLSGGQKQRVAI 151
Cdd:TIGR02633  77 ----RAGIVIIHQELTLVPELSVAENIFLGNEItlpgGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEI 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:TIGR02633 153 AKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV 220
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 19-227 5.55e-26

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 108.39  E-value: 5.55e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLE--RPTEGSVQVGGQELTTLsesELTKARRQIGMIFQHFNLLSS 96
Cdd:PRK11174  364 TLAGPLNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG 437

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  97 rTVFGNVALPLEldNTPKEEIKR-----RVTELLDLVGLGDKHD--SYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK11174  438 -TLRDNVLLGNP--DASDEQLQQalenaWVSEFLPLLPQGLDTPigDQAAGLSVGQAQRLALARALLQPCQLLLLDEPTA 514

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 170 ALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSE 227
Cdd:PRK11174  515 SLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQGDYAE 569
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-217 1.04e-25

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 106.08  E-value: 1.04e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTka 80
Cdd:PRK09536    3 MIDVSDLSVEF--GDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 rRQIGMIFQHFNL---LSSRTVfgnvalpLELDNTPK--------EEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRV 149
Cdd:PRK09536   77 -RRVASVPQDTSLsfeFDVRQV-------VEMGRTPHrsrfdtwtETDRAAVERAMERTGVAQFADRPVTSLSGGERQRV 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 150 AIARALASNPKVLLCDEATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK09536  149 LLARALAQATPVLLLDEPTASLDINHQVRTLELV----RRLvddGKTAVAAIHDLDLAARYCDELVLLADG 215
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 6-245 1.49e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 103.08  E-value: 1.49e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   6 NITKVFqqGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQ-----ELTTLSESEL-TK 79
Cdd:PRK11701   11 GLTKLY--GPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEAERrRL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQIGMIFQHF--NLLSSRTVFGNVALPL-ELDNTPKEEIKRRVTELLDLVGLG-DKHDSYPANLSGGQKQRVAIARAL 155
Cdd:PRK11701   87 LRTEWGFVHQHPrdGLRMQVSAGGNIGERLmAVGARHYGDIRATAGDWLERVEIDaARIDDLPTTFSGGMQQRLQIARNL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKTP 235
Cdd:PRK11701  167 VTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVLDDPQHP 246

                         250
                  ....*....|
gi 1016201160 236 LAQKFIQSTL 245
Cdd:PRK11701  247 YTQLLVSSVL 256
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-224 4.62e-25

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 101.11  E-value: 4.62e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQgtrtIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTka 80
Cdd:PRK11614    5 MLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTAKIM-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNtpKEEIKRRVTELLDLVG-LGDKHDSYPANLSGGQKQRVAIARALASNP 159
Cdd:PRK11614   79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAE--RDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 160 KVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDT 224
Cdd:PRK11614  157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLEDT 220
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 20-224 2.92e-24

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: 103.67  E-value: 2.92e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLSSrTV 99
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTL---RQFINYLPQEPYIFSG-SI 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLElDNTPKEEIKR--RVTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:TIGR01193 565 LENLLLGAK-ENVSQDEIWAacEIAEIKDDIenmplGYQTELSEEGSSISGGQKQRIALARALLTDSKVLILDESTSNLD 643

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 173 PATTRSILELLKDINRRlglTILLITHEMDVVKRIcDCVAVISNGELIEQDT 224
Cdd:TIGR01193 644 TITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQGS 691
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 21-205 3.09e-24

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 98.49  E-value: 3.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVGGQELTTlseseltkarrqigmifqhfnllssrt 98
Cdd:COG2401    46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGR--------------------------- 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 vfgNVALpleLDNTPKEEIKRRVTELLDLVGLGDKHdSY---PANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:COG2401    99 ---EASL---IDAIGRKGDFKDAVELLNAVGLSDAV-LWlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQT 171

                         170       180       190
                  ....*....|....*....|....*....|
gi 1016201160 176 TRSILELLKDINRRLGLTILLITHEMDVVK 205
Cdd:COG2401   172 AKRVARNLQKLARRAGITLVVATHHYDVID 201
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
20-209 7.32e-24

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 102.51  E-value: 7.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVN-LLErPTEGSVQVGGQELttlsESELTKARRQIGMIFQHFNLLSSRT 98
Cdd:NF033858  281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTgLLP-ASEGEAWLFGQPV----DAGDIATRRRVGYMSQAFSLYGELT 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:NF033858  356 VRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDM 435

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1016201160 179 ILELLKDINRRLGLTILLITHEMDVVKRiCD 209
Cdd:NF033858  436 FWRLLIELSREDGVTIFISTHFMNEAER-CD 465
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 2-222 1.28e-23

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: 95.84  E-value: 1.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITkvFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnLLER---PTEGSVQVGGQELTTLSESelt 78
Cdd:cd03247     1 LSINNVS--FSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQ---LLTGdlkPQQGEITLDGVPVSDLEKA--- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kARRQIGMIFQHFNLLSsrtvfgnvalpleldntpkeeikrrvTELLDLVGlgdkhdsypANLSGGQKQRVAIARALASN 158
Cdd:cd03247    73 -LSSLISVLNQRPYLFD--------------------------TTLRNNLG---------RRFSGGERQRLALARILLQD 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRIcDCVAVISNGELIEQ 222
Cdd:cd03247   117 APIVLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQ 177
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 20-218 2.19e-23

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: 95.61  E-value: 2.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnLLE-RPTEGSVQVGGQelttlseseltkarrqIGMIFQhFNLLSSRT 98
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSAL-LGElEKLSGSVSVPGS----------------IAYVSQ-EPWIQNGT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNVALPLELDntpkEEIKRRV---------TELL---DLVGLGDKHdsypANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:cd03250    82 IRENILFGKPFD----EERYEKVikacalepdLEILpdgDLTEIGEKG----INLSGGQKQRISLARAVYSDADIYLLDD 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 167 ATSALDPATTRSILE--LLKDInrRLGLTILLITHEMDVVKRiCDCVAVISNGE 218
Cdd:cd03250   154 PLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPH-ADQIVVLDNGR 204
NIL smart00930
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ...
 267-340 6.72e-23

This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.


Pssm-ID: 197998 [Multi-domain]  Cd Length: 76  Bit Score: 90.65  E-value: 6.72e-23
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160  267 PMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQEETQAAIAWLQDHHVKVEVL 340
Cdd:smart00930   3 RLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLREQGVEVEVL 76
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
14-230 1.02e-22

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 95.44  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  14 GTRTIQalNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTkarRQIGMIFQHFNL 93
Cdd:PRK10253   18 GKYTVA--ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA---RRIGLLAQNATT 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSRTVFGNVA---LPLE-LDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK10253   93 PGDITVQELVArgrYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 170 ALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:PRK10253  173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVT 233
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 21-199 1.31e-22

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 98.73  E-value: 1.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQElttlseseltkarrqiGMIF--QH--FNLLSS 96
Cdd:COG4178   379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------------RVLFlpQRpyLPLGTL 442

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  97 RTVfgnVALPLELDNTPKEEIKrrvtELLDLVGLG------DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:COG4178   443 REA---LLYPATAEAFSDAELR----EALEAVGLGhlaerlDEEADWDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSA 515

                         170       180
                  ....*....|....*....|....*....
gi 1016201160 171 LDPATTRSILELLKDinRRLGLTILLITH 199
Cdd:COG4178   516 LDEENEAALYQLLRE--ELPGTTVISVGH 542
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 16-220 1.33e-22

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 98.18  E-value: 1.33e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeselTKARRQIGMIF-----QH 90
Cdd:COG3845   269 RGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLS----PRERRRLGVAYipedrLG 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 FNLLSSRTVFGNVALpLELDNTP--------KEEIKRRVTELLDlvglgdKHD------SYPA-NLSGGQKQRVAIARAL 155
Cdd:COG3845   345 RGLVPDMSVAENLIL-GRYRRPPfsrggfldRKAIRAFAEELIE------EFDvrtpgpDTPArSLSGGNQQKVILAREL 417

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:COG3845   418 SRDPKLLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIV 481
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
21-224 2.35e-22

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 97.87  E-value: 2.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLircVNLLE---RPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLSSr 97
Cdd:PRK10790  357 LQNINLSVPSRGFVALVGHTGSGKSTL---ASLLMgyyPLTEGEIRLDGRPLSSLSHSVL---RQGVAMVQQDPVVLAD- 429

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVALPLELDntpkEEikrRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK10790  430 TFLANVTLGRDIS----EE---QVWQALETVQLAELARSLPDglytplgeqgnNLSVGQKQLLALARVLVQTPQILILDE 502

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 167 ATSALDPATTRSILELLKDINRRlgLTILLITHEMDVVKRiCDCVAVISNGELIEQDT 224
Cdd:PRK10790  503 ATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 21-200 9.20e-22

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 96.27  E-value: 9.20e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVF 100
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLM---NALAFRSPKGVKGSGSVLLNGMPIDAKEMRAISAYVQQDDLFIPTLTVR 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 GNVALPLEL---DNTPKEEIKRRVTELLDLVGLGDKHDS------YPANLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
Cdd:TIGR00955 118 EHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGL 197

                         170       180
                  ....*....|....*....|....*....
gi 1016201160 172 DPATTRSILELLKDINRRlGLTILLITHE 200
Cdd:TIGR00955 198 DSFMAYSVVQVLKGLAQK-GKTIICTIHQ 225
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
20-227 1.03e-21

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 95.47  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESE--------LTKARRQIGmifqhf 91
Cdd:COG1129   267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDairagiayVPEDRKGEG------ 340

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  92 nLLSSRTVFGNVALPLeLDNT-------PKEEiKRRVTELLDLVGLGDKHDSYPA-NLSGGQKQRVAIARALASNPKVLL 163
Cdd:COG1129   341 -LVLDLSIRENITLAS-LDRLsrgglldRRRE-RALAEEYIKRLRIKTPSPEQPVgNLSGGNQQKVVLAKWLATDPKVLI 417

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 164 CDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL---IEQDTVSE 227
Cdd:COG1129   418 LDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIvgeLDREEATE 483
GguA NF040905
sugar ABC transporter ATP-binding protein;
6-227 1.06e-21

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 95.63  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   6 NITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLE--RPT---EGSVQVGGQELT--TLSESElt 78
Cdd:NF040905    6 GITKTFP----GVKALDDVNLSVREGEIHALCGENGAGKSTLM---KVLSgvYPHgsyEGEILFDGEVCRfkDIRDSE-- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 kaRRQIGMIFQHFNL---LSsrtvfgnVALPLELDNTPK-------EEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQR 148
Cdd:NF040905   77 --ALGIVIIHQELALipyLS-------IAENIFLGNERAkrgvidwNETNRRARELLAKVGLDESPDTLVTDIGVGKQQL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIE-----QD 223
Cdd:NF040905  148 VEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIEtldcrAD 226


                  ....
gi 1016201160 224 TVSE 227
Cdd:NF040905  227 EVTE 230
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 1-227 1.47e-21

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 95.07  E-value: 1.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA 80
Cdd:PRK10762    4 LLQLKGIDKAFP----GVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQEA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 rrQIGMIFQHFNLLSSRTVFGNVALPLELDNT----PKEEIKRRVTELLDLVGLgdKHDSYP--ANLSGGQKQRVAIARA 154
Cdd:PRK10762   80 --GIGIIHQELNLIPQLTIAENIFLGREFVNRfgriDWKKMYAEADKLLARLNL--RFSSDKlvGELSIGEQQMVEIAKV 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 155 LASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:PRK10762  156 LSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAEREVAD 227
NIL pfam09383
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ...
 267-339 4.91e-21

NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.


Pssm-ID: 462781 [Multi-domain]  Cd Length: 73  Bit Score: 85.58  E-value: 4.91e-21
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 267 PMLRMEFTGQSVDAPLLSETARRFNVNNNIISAQLDYAGGVKFGIMLTEMHGTQEETQAAIAWLQDHHVKVEV 339
Cdd:pfam09383   1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLREQGVEVEV 73
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 4-227 5.66e-21

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 93.64  E-value: 5.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFQqgtrTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKArrQ 83
Cdd:PRK10982    1 MSNISKSFP----GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALEN--G 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 IGMIFQHFNLLSSRTVFGNVAL---PLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPK 160
Cdd:PRK10982   75 ISMVHQELNLVLQRSVMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAK 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160 161 VLLCDEATSALdpaTTRSILELLKDIN--RRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSE 227
Cdd:PRK10982  155 IVIMDEPTSSL---TEKEVNHLFTIIRklKERGCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAG 220
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 1-217 6.22e-21

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 93.58  E-value: 6.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQqGTRTIQALNnVSLHvpAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEselTKA 80
Cdd:PRK15439   11 LLCARSISKQYS-GVEVLKGID-FTLH--AGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTP---AKA 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 rRQIG--MIFQHFNLLSSRTVFGNVALPLeldntPK-EEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:PRK15439   84 -HQLGiyLVPQEPLLFPNLSVKENILFGL-----PKrQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 158 NPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK15439  158 DSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKLPEIRQLADRISVMRDG 216
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 21-230 1.30e-20

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 89.13  E-value: 1.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLerPTEGSVQVGGQELTTLSESELtkARRQiGMIFQHFNLLSSRTV 99
Cdd:COG4138    12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAEL--ARHR-AYLSQQQSPPFAMPV 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLElDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARAL-----ASNP--KVLLCDEATSALD 172
Cdd:COG4138    87 FQYLALHQP-AGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPegQLLLLDEPMNSLD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1016201160 173 PATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFS 230
Cdd:COG4138   166 VAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMT 222
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 2-218 1.45e-20

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: 86.35  E-value: 1.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGgqelttlseseltkar 81
Cdd:cd03221     1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWG---------------- 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 rqigmifqhfnllssrtvfgnvalpleldntPKEEIkrrvtelldlvglgdkhdSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:cd03221    61 -------------------------------STVKI------------------GYFEQLSGGEKMRLALAKLLLENPNL 91

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDINRrlglTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd03221    92 LLLDEPTNHLDLESIEALEEALKEYPG----TVILVSHDRYFLDQVATKIIELEDGK 144
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 24-240 3.06e-20

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 88.45  E-value: 3.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  24 VSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLerPTEGSVQVGGQELTTLSESELTKARrqiGMIFQHFNLLSSRTVFGN 102
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHR---AYLSQQQTPPFAMPVFQY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 103 VALPLElDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARAL-----ASNP--KVLLCDEATSALDPAT 175
Cdd:PRK03695   90 LTLHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPagQLLLLDEPMNSLDVAQ 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 176 TRSILELLKDINrRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSHPKtpLAQKF 240
Cdd:PRK03695  169 QAALDRLLSELC-QQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN--LAQVF 230
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
2-214 9.83e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 87.25  E-value: 9.83e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTrtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKAR 81
Cdd:PRK15056    7 IVVNDVTVTWRNGH---TALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNLVAYV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 RQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKV 161
Cdd:PRK15056   84 PQSEEVDWSFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQV 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 162 LLCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVI 214
Cdd:PRK15056  164 ILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCDYTVMV 215
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 23-199 1.52e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 82.61  E-value: 1.52e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQElttlseSELTKARRQIGMIfQHFNLL-SSRTVFG 101
Cdd:PRK13539   20 GLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGD------IDDPDVAEACHYL-GHRNAMkPALTVAE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 102 NVALPLELDNTPKeeikRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE 181
Cdd:PRK13539   93 NLEFWAAFLGGEE----LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVALFAE 168

                         170       180
                  ....*....|....*....|
gi 1016201160 182 LlkdINRRL--GLTILLITH 199
Cdd:PRK13539  169 L---IRAHLaqGGIVIAATH 185
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 21-221 2.37e-18

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: 81.80  E-value: 2.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVGGQELTTLSESEltKARRQIGMIFQHfnllssrt 98
Cdd:cd03217    16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQY-------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 vfgnvalPLELDNTpkeeikrRVTELLDLVGLGdkhdsypanLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:cd03217    86 -------PPEIPGV-------KNADFLRYVNEG---------FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1016201160 179 ILELLKDInRRLGLTILLITHEMDVVKRI-CDCVAVISNGELIE 221
Cdd:cd03217   143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVK 185
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 3-232 4.63e-18

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 85.47  E-value: 4.63e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160    3 KLSNITKV------FQQGTRT-IQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQEltTLSES 75
Cdd:PTZ00265   376 KLKDIKKIqfknvrFHYDTRKdVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDI 453

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   76 ELTKARRQIGMIFQHfNLLSSRTVFGNVALPL--------------ELDNTPKEEIKRRV-------------------T 122
Cdd:PTZ00265   454 NLKWWRSKIGVVSQD-PLLFSNSIKNNIKYSLyslkdlealsnyynEDGNDSQENKNKRNscrakcagdlndmsnttdsN 532

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  123 ELL------------------------DLV-GLGDKHD----SYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDp 173
Cdd:PTZ00265   533 ELIemrknyqtikdsevvdvskkvlihDFVsALPDKYEtlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLD- 611

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160  174 atTRSILELLKDINRRLG----LTIlLITHEMDVVkRICDCVAVISNGELIEQDTVSEVFSHP 232
Cdd:PTZ00265   612 --NKSEYLVQKTINNLKGnenrITI-IIAHRLSTI-RYANTIFVLSNRERGSTVDVDIIGEDP 670
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 21-200 5.68e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 80.76  E-value: 5.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELttlsESELTKARRQIGMIFQHFNLLSSRTVF 100
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQLCFVGHRSGINPYLTLR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 GNVALPLELDNTPKEeikrrVTELLDLVGLGDKHDsYPAN-LSGGQKQRVAIARALASNPKVLLCDEATSALDpatTRSI 179
Cdd:PRK13540   93 ENCLYDIHFSPGAVG-----ITELCRLFSLEHLID-YPCGlLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD---ELSL 163

                         170       180
                  ....*....|....*....|...
gi 1016201160 180 LELLKDI--NRRLGLTILLITHE 200
Cdd:PRK13540  164 LTIITKIqeHRAKGGAVLLTSHQ 186
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
20-232 1.20e-17

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 83.61  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIrcvNLLERP---TEGSVQVGGQELTTLsesELTKARRQIGMIFQHfNLLSS 96
Cdd:PRK10789  330 ALENVNFTLKPGQMLGICGPTGSGKSTLL---SLIQRHfdvSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQT-PFLFS 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  97 RTVFGNVAL--PlelDNTPK--EEIKRRVTELLDLVGLGDKHDSYPAN----LSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:PRK10789  403 DTVANNIALgrP---DATQQeiEHVARLASVHDDILRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDAL 479

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 169 SALDPATTRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHP 232
Cdd:PRK10789  480 SAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-204 1.24e-17

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 80.93  E-value: 1.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRtiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQvggqelttlseselTKA 80
Cdd:PRK09544    4 LVSLENVSVSF--GQR--RVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK--------------RNG 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLlssrtvfgNVALPLELD-------NTPKEEIkrrvTELLDLVGLGDKHDSYPANLSGGQKQRVAIAR 153
Cdd:PRK09544   66 KLRIGYVPQKLYL--------DTTLPLTVNrflrlrpGTKKEDI----LPALKRVQAGHLIDAPMQKLSGGETQRVLLAR 133

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 154 ALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVV 204
Cdd:PRK09544  134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 1-252 3.08e-17

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


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 83.14  E-value: 3.08e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160    1 MIKLSNITKVFQqGTRTiQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTlsesELTKA 80
Cdd:TIGR01257 1937 ILRLNELTKVYS-GTSS-PAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT----NISDV 2010

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   81 RRQIGMIFQHF---NLLSSRTvfgNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALAS 157
Cdd:TIGR01257 2011 HQNMGYCPQFDaidDLLTGRE---HLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  158 NPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVsevfSHPKTPLA 237
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTI----QHLKSKFG 2162

                          250
                   ....*....|....*
gi 1016201160  238 QKFIqSTLHLDIPED 252
Cdd:TIGR01257 2163 DGYI-VTMKIKSPKD 2176
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 20-231 6.57e-17

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 81.48  E-value: 6.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQElttlseseltkarrqiGMIFQHFNLLSSRTV 99
Cdd:PRK13545   39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA----------------ALIAISSGLNGQLTG 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:PRK13545  103 IENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKC 182

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 180 LELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSH 231
Cdd:PRK13545  183 LDKMNEFKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 82-216 1.92e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 80.84  E-value: 1.92e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   82 RQIGMIFQHFNLLSSRTVFGNVALPLEldNTPKEEIKR-----RVTELLDlvGLGDKHDS----YPANLSGGQKQRVAIA 152
Cdd:PTZ00265  1295 RNLFSIVSQEPMLFNMSIYENIKFGKE--DATREDVKRackfaAIDEFIE--SLPNKYDTnvgpYGKSLSGGQKQRIAIA 1370

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160  153 RALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRiCDCVAVISN 216
Cdd:PTZ00265  1371 RALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR-SDKIVVFNN 1433
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 23-219 2.01e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 80.09  E-value: 2.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeselTKARRQIGMIF-----QHFNLLSSR 97
Cdd:PRK15439  281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALS----TAQRLARGLVYlpedrQSSGLYLDA 356

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  98 TVFGNVA------LPLELDntPKEEiKRRVTELLDLVGLGDKHDSYPA-NLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:PRK15439  357 PLAWNVCalthnrRGFWIK--PARE-NAVLERYRRALNIKFNHAEQAArTLSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1016201160 171 LDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK15439  434 VDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 12-199 2.21e-16

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: 76.24  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  12 QQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSEsELTKARRQIGmifqHF 91
Cdd:TIGR01189   9 SRGERML--FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRD-EPHENILYLG----HL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  92 NLLSSR-TVFGNVALPLELDNTPKeeikRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:TIGR01189  82 PGLKPElSALENLHFWAAIHGGAQ----RTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTA 157

                         170       180
                  ....*....|....*....|....*....
gi 1016201160 171 LDPATTRSILELLKDINRRLGLtILLITH 199
Cdd:TIGR01189 158 LDKAGVALLAGLLRAHLARGGI-VLLTTH 185
PLN03130 PLN03130
ABC transporter C family member; Provisional
 21-242 3.54e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 79.78  E-value: 3.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIrcvnllerptegSVQVGgqELTTLSESELTKARR-----QIGMIFqhfnlls 95
Cdd:PLN03130   633 LSNINLDVPVGSLVAIVGSTGEGKTSLI------------SAMLG--ELPPRSDASVVIRGTvayvpQVSWIF------- 691

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   96 SRTVFGNVALPLELDnTPKEEIKRRVTEL---LDLVGLGDKHD--SYPANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:PLN03130   692 NATVRDNILFGSPFD-PERYERAIDVTALqhdLDLLPGGDLTEigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160  171 LDPATTRSILEllKDINRRL-GLTILLITHEMDVVKRIcDCVAVISNGELIEQDTVSEVFSHpkTPLAQKFIQ 242
Cdd:PLN03130   771 LDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGMIKEEGTYEELSNN--GPLFQKLME 838
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 21-199 5.13e-16

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: 74.50  E-value: 5.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQElttlseseltkarrqiGMIFqhfnlLSSRTVF 100
Cdd:cd03223    17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEGE----------------DLLF-----LPQRPYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 GNVALpleldntpKEEIkrrvtelldlvglgdkhdSYP--ANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:cd03223    76 PLGTL--------REQL------------------IYPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129

                         170       180
                  ....*....|....*....|.
gi 1016201160 179 ILELLKDinrrLGLTILLITH 199
Cdd:cd03223   130 LYQLLKE----LGITVISVGH 146
PLN03232 PLN03232
ABC transporter C family member; Provisional
 21-244 5.48e-15

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 76.17  E-value: 5.48e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseLTKARRQIGMIFQHFNLLSSRTVF 100
Cdd:PLN03232  1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRRVLSIIPQSPVLFSGTVRF 1328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  101 GNVALPLELDNTPKEEIKRrvTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:PLN03232  1329 NIDPFSEHNDADLWEALER--AHIKDVIdrnpfGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDVRT 1406

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160  176 TRSILELLKDINRrlGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHPKTPLAqKFIQST 244
Cdd:PLN03232  1407 DSLIQRTIREEFK--SCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRDTSAFF-RMVHST 1471
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
22-227 5.54e-15

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 75.59  E-value: 5.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  22 NNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESE--------LTKARRQIGMiFQHFNL 93
Cdd:PRK09700  280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDavkkgmayITESRRDNGF-FPNFSI 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSsrtvfgNVALPLELDN----------TPKEEIK--RRVTELLDLvglgdKHDSYPAN---LSGGQKQRVAIARALASN 158
Cdd:PRK09700  359 AQ------NMAISRSLKDggykgamglfHEVDEQRtaENQRELLAL-----KCHSVNQNiteLSGGNQQKVLISKWLCCC 427

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIE----QDTVSE 227
Cdd:PRK09700  428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVFCEGRLTQiltnRDDMSE 499
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-217 6.57e-15

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 75.97  E-value: 6.57e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnllerptegsvqvggqelTTLSESELTKAR----RQIGMIFQHFNLLSS 96
Cdd:PTZ00243   676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISEGRvwaeRSIAYVPQQAWIMNA 735

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   97 rTVFGNVaLPLELDNTPKEEIKRRVTEL-LDLVGLGDKHDS----YPANLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
Cdd:PTZ00243   736 -TVRGNI-LFFDEEDAARLADAVRVSQLeADLAQLGGGLETeigeKGVNLSGGQKARVSLARAVYANRDVYLLDDPLSAL 813

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1016201160  172 DPATTRSILELLKdINRRLGLTILLITHEMDVVKRiCDCVAVISNG 217
Cdd:PTZ00243   814 DAHVGERVVEECF-LGALAGKTRVLATHQVHVVPR-ADYVVALGDG 857
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-241 6.62e-15

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 75.93  E-value: 6.62e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQV-GGQelttLSESeltKARRQIG-----MIfQHF- 91
Cdd:NF033858   15 VALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVlGGD----MADA---RHRRAVCpriayMP-QGLg 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  92 -NLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSyPA-NLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:NF033858   87 kNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADR-PAgKLSGGMKQKLGLCCALIHDPDLLILDEPTT 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 170 ALDPATTRSILELLKDI-NRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVFSHPKTP-LAQKFI 241
Cdd:NF033858  166 GVDPLSRRQFWELIDRIrAERPGMSVLVATAYMEEAER-FDWLVAMDAGRVLATGTPAELLARTGADtLEAAFI 238
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 2-220 1.70e-14

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 71.14  E-value: 1.70e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPT---EGSVQVGGQElttlSESELT 78
Cdd:cd03233     4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIP----YKEFAE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQHFNLLSSRTVFgnvalpleldntpkeeikrrvtELLDLVgLGDKHDSYPANLSGGQKQRVAIARALASN 158
Cdd:cd03233    80 KYPGEIIYVSEEDVHFPTLTVR----------------------ETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVSR 136

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHE-----MDVVKRICdcvaVISNGELI 220
Cdd:cd03233   137 ASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQasdeiYDLFDKVL----VLYEGRQI 199
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 21-199 1.87e-14

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: 70.98  E-value: 1.87e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESeLTKARRQIGmifqHFNLLSSR-TV 99
Cdd:cd03231    16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLG----HAPGIKTTlSV 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLELDNTPKeeikrrVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:cd03231    91 LENLRFWHADHSDEQ------VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARF 164

                         170       180
                  ....*....|....*....|
gi 1016201160 180 LELLKDINRRLGLtILLITH 199
Cdd:cd03231   165 AEAMAGHCARGGM-VVLTTH 183
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 2-208 2.44e-14

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 73.82  E-value: 2.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGgqelTTLseseltkar 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIG----ETV--------- 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 rQIGMIFQ-HFNLLSSRTVFGNVALPLELDNTPKEEIKRRVtelldLVGL----GDKHDSYPANLSGGQKQRVAIARALA 156
Cdd:TIGR03719 386 -KLAYVDQsRDALDPNKTVWEEISGGLDIIKLGKREIPSRA-----YVGRfnfkGSDQQKKVGQLSGGERNRVHLAKTLK 459

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 157 SNPKVLLCDEATSALDPATTRSILELLKDinrrLGLTILLITHEMDVVKRIC 208
Cdd:TIGR03719 460 SGGNVLLLDEPTNDLDVETLRALEEALLN----FAGCAVVISHDRWFLDRIA 507
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 4-184 3.63e-14

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 73.79  E-value: 3.63e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160    4 LSNITKVFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnLLERPTEGSVQVGGQELTTLSeseLTKARRQ 83
Cdd:TIGR01271 1220 VQGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLSAL-LRLLSTEGEIQIDGVSWNSVT---LQTWRKA 1293

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   84 IGMIFQHFNLLSSrtVFGNVALPLEldNTPKEEIKRRVTElldlVGLGDKHDSYPANL-----------SGGQKQRVAIA 152
Cdd:TIGR01271 1294 FGVIPQKVFIFSG--TFRKNLDPYE--QWSDEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLA 1365

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1016201160  153 RALASNPKVLLCDEATSALDPATTRSILELLK 184
Cdd:TIGR01271 1366 RSILSKAKILLLDEPSAHLDPVTLQIIRKTLK 1397
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 7-201 4.98e-14

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: 70.44  E-value: 4.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   7 ITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQ-ELTTLSESELTKARRQIG 85
Cdd:cd03290     3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKnESEPSFEATRSRNRYSVA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  86 MIFQHFNLLSSrTVFGNVALPLELDntpKEEIKRrVTEL------LDLVGLGDKHD--SYPANLSGGQKQRVAIARALAS 157
Cdd:cd03290    83 YAAQKPWLLNA-TVEENITFGSPFN---KQRYKA-VTDAcslqpdIDLLPFGDQTEigERGINLSGGQRQRICVARALYQ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1016201160 158 NPKVLLCDEATSALDPATT-----RSILELLKDINRrlglTILLITHEM 201
Cdd:cd03290   158 NTNIVFLDDPFSALDIHLSdhlmqEGILKFLQDDKR----TLVLVTHKL 202
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 21-230 5.39e-14

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 73.06  E-value: 5.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLLSsrtvf 100
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDL---RFKITIIPQDPVLFS----- 1373

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  101 GNVALPLELDNTPKEEikrRVTELLDLVGLGDKHDSYPA-----------NLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:TIGR00957 1374 GSLRMNLDPFSQYSDE---EVWWALELAHLKTFVSALPDkldhecaeggeNLSVGQRQLVCLARALLRKTKILVLDEATA 1450

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160  170 ALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRICDcVAVISNGELIEQDTVSEVFS 230
Cdd:TIGR00957 1451 AVDLETDNLIQSTIR--TQFEDCTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNLLQ 1508
cyc_pep_trnsptr TIGR01194
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...
 20-222 7.32e-14

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]


Pssm-ID: 130262 [Multi-domain]  Cd Length: 555  Bit Score: 72.30  E-value: 7.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHFNLlssrtv 99
Cdd:TIGR01194 357 ALGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDY---RDLFSAIFADFHL------ 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNVALPLELDNTPKEEIKRRVT--ELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR 177
Cdd:TIGR01194 428 FDDLIGPDEGEHASLDNAQQYLQrlEIADKVKIEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKR 507

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1016201160 178 SIL-ELLKDINRRlGLTILLITHEmDVVKRICDCVAVISNGELIEQ 222
Cdd:TIGR01194 508 FFYeELLPDLKRQ-GKTIIIISHD-DQYFELADQIIKLAAGCIVKD 551
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 21-232 8.80e-14

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 72.67  E-value: 8.80e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQH-FNLLSSRTV 99
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQNDSLRENILFGKaLNEKYYQQV 733

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  100 FGNVALPLELDNTPKEeikrrvtellDLVGLGDKHdsypANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSI 179
Cdd:TIGR00957  734 LEACALLPDLEILPSG----------DRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHI 799

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  180 LE-------LLKDINRrlgltiLLITHEMDVVKRIcDCVAVISNGElieqdtVSEVFSHP 232
Cdd:TIGR00957  800 FEhvigpegVLKNKTR------ILVTHGISYLPQV-DVIIVMSGGK------ISEMGSYQ 846
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 2-230 1.40e-13

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: 69.88  E-value: 1.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTL----IRCVNllerpTEGSVQVGGQELTTLSeseL 77
Cdd:cd03289     3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---L 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 TKARRQIGMIFQHFNLLSsrtvfGNVALPLELDNTPKEEIKRRVTELldlVGLGDKHDSYPANL-----------SGGQK 146
Cdd:cd03289    73 QKWRKAFGVIPQKVFIFS-----GTFRKNLDPYGKWSDEEIWKVAEE---VGLKSVIEQFPGQLdfvlvdggcvlSHGHK 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 147 QRVAIARALASNPKVLLCDEATSALDPATTRSILELLKdiNRRLGLTILLITHEMDVVKRiCDCVAVISNGELIEQDTVS 226
Cdd:cd03289   145 QLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLK--QAFADCTVILSEHRIEAMLE-CQRFLVIEENKVRQYDSIQ 221


                  ....
gi 1016201160 227 EVFS 230
Cdd:cd03289   222 KLLN 225
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 19-200 5.38e-13

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 70.14  E-value: 5.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCvnLLERPTEGSVQvGGQELTTLSESELTKARRqIGMIFQHFNLLSSRT 98
Cdd:TIGR00956  777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNV--LAERVTTGVIT-GGDRLVNGRPLDSSFQRS-IGYVQQQDLHLPTST 852

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   99 V-----F-GNVALPLELdntPKEEIKRRVTELLDLVGLGDKHDSYPA----NLSGGQKQRVAIARALASNPKVLL-CDEA 167
Cdd:TIGR00956  853 VreslrFsAYLRQPKSV---SKSEKMEYVEEVIKLLEMESYADAVVGvpgeGLNVEQRKRLTIGVELVAKPKLLLfLDEP 929

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1016201160  168 TSALDPATTRSILELLkdinRRL---GLTILLITHE 200
Cdd:TIGR00956  930 TSGLDSQTAWSICKLM----RKLadhGQAILCTIHQ 961
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 5-200 6.12e-13

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 66.50  E-value: 6.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   5 SNITKVFQQGTRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCvnLLERPTEGSvqVGGQelTTLSESELTKA-RRQ 83
Cdd:cd03232     7 KNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDV--LAGRKTAGV--ITGE--ILINGRPLDKNfQRS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 IGMIFQHFNLLSSRTVfgnvalpleldntpKEEIKrrvtelldlvglgdkhdsYPANLSG---GQKQRVAIARALASNPK 160
Cdd:cd03232    81 TGYVEQQDVHSPNLTV--------------REALR------------------FSALLRGlsvEQRKRLTIGVELAAKPS 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1016201160 161 VLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHE 200
Cdd:cd03232   129 ILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQ 167
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-228 1.13e-12

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 67.16  E-value: 1.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIR------CVNLLER--PTEGSVQVGGQELTTLSESELTKARRQIGMIFQHFN 92
Cdd:PRK13547   17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKalagdlTGGGAPRgaRVTGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 LLSSRTV-----FGNVALPLELDNTPKEeIKRRVTELLDLVGLgDKHDSypANLSGGQKQRVAIARALA---------SN 158
Cdd:PRK13547   97 AFSAREIvllgrYPHARRAGALTHRDGE-IAWQALALAGATAL-VGRDV--TTLSGGELARVQFARVLAqlwpphdaaQP 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEV 228
Cdd:PRK13547  173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADV 242
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 4-200 3.10e-12

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: 67.27  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFQqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGsvqvggqelttlseseltKARRQ 83
Cdd:TIGR03719   7 MNRVSKVVP-PKKEI--LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG------------------EARPQ 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  84 ----IGMIFQHFNLLSSRTVFGNVALPL--------ELD------NTPKEEIK---RRVTELLDLVGLGDKH-------- 134
Cdd:TIGR03719  66 pgikVGYLPQEPQLDPTKTVRENVEEGVaeikdaldRFNeisakyAEPDADFDklaAEQAELQEIIDAADAWdldsqlei 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 135 ----------DSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINrrlGlTILLITHE 200
Cdd:TIGR03719 146 amdalrcppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD-AESVAWLErHLQEYP---G-TVVAVTHD 217
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 2-181 3.27e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.07  E-value: 3.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGgqelTTLseseltkar 81
Cdd:PRK11819  325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIG----ETV--------- 387

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  82 rQIGMIFQ-HFNLLSSRTVFgnvalpleldntpkEEIkrrvTELLDLVGLGDKHDSYPA-----------------NLSG 143
Cdd:PRK11819  388 -KLAYVDQsRDALDPNKTVW--------------EEI----SGGLDIIKVGNREIPSRAyvgrfnfkggdqqkkvgVLSG 448

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1016201160 144 GQKQRVAIARALASNPKVLLCDEATSALDPATTRSiLE 181
Cdd:PRK11819  449 GERNRLHLAKTLKQGGNVLLLDEPTNDLDVETLRA-LE 485
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 21-219 3.53e-12

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 66.95  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERpTEGSVQVGGQELTTLSESE--------LTKARRQ----IGMI 87
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGALPR-TSGYVTLDGHEVVTRSPQDglangivyISEDRKRdglvLGMS 346

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  88 FQHFNLLSSRTVFGNVALPLEldntpKEEIKRRVTELLDLVGLGD-KHDSYPANLSGGQKQRVAIARALASNPKVLLCDE 166
Cdd:PRK10762  347 VKENMSLTALRYFSRAGGSLK-----HADEQQAVSDFIRLFNIKTpSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 167 ATSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK10762  422 PTRGVDVGAKKEIYQL---INQfkAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
PLN03211 PLN03211
ABC transporter G-25; Provisional
 3-217 4.47e-12

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 66.83  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   3 KLSNITKVFQQgtRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnllerptEGSVQVGGQELTTLSES-ELTK-A 80
Cdd:PLN03211   70 KISDETRQIQE--RTI--LNGVTGMASPGEILAVLGPSGSGKSTLLNAL-------AGRIQGNNFTGTILANNrKPTKqI 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQH---FNLLSSRTVFGNVALpLELDNTPKEEIKRRVTE-LLDLVGLGDKHDSYPAN-----LSGGQKQRVAI 151
Cdd:PLN03211  139 LKRTGFVTQDdilYPHLTVRETLVFCSL-LRLPKSLTKQEKILVAEsVISELGLTKCENTIIGNsfirgISGGERKRVSI 217

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 152 ARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHE-MDVVKRICDCVAVISNG 217
Cdd:PLN03211  218 AHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQK-GKTIVTSMHQpSSRVYQMFDSVLVLSEG 283
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
16-231 4.70e-12

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 65.22  E-value: 4.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQelttlseseltkarrqIGMIFQHFNLLS 95
Cdd:PRK13546   35 KTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLSG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  96 SRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPAT 175
Cdd:PRK13546   99 QLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTF 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 176 TRSILELLKDInRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVFSH 231
Cdd:PRK13546  179 AQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
23-199 4.89e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 64.05  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  23 NVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSES---ELTkarrQIGmifqHFNLLSSR-T 98
Cdd:PRK13538   19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRDEyhqDLL----YLG----HQPGIKTElT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  99 VFGNVALPLELDNTPKEEikrRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRS 178
Cdd:PRK13538   91 ALENLRFYQRLHGPGDDE---ALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQGVAR 167

                         170       180
                  ....*....|....*....|.
gi 1016201160 179 ILELLKDINRRLGLTIlLITH 199
Cdd:PRK13538  168 LEALLAQHAEQGGMVI-LTTH 187
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 16-219 6.02e-12

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 66.39  E-value: 6.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERPTEGSVQVGGQELTTLSESELTKA--------RRQIGM 86
Cdd:TIGR02633 271 PHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVDIRNPAQAIRAgiamvpedRKRHGI 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  87 IFQ-------HFNLLSSRTVFGNVALPLELDNTpKEEIKRrvtelldlVGLGDKHDSYP-ANLSGGQKQRVAIARALASN 158
Cdd:TIGR02633 351 VPIlgvgkniTLSVLKSFCFKMRIDAAAELQII-GSAIQR--------LKVKTASPFLPiGRLSGGNQQKAVLAKMLLTN 421

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 159 PKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:TIGR02633 422 PRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PLN03232 PLN03232
ABC transporter C family member; Provisional
 21-248 7.34e-12

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 66.54  E-value: 7.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQHfNLLSSR-- 97
Cdd:PLN03232   633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAmLGELSHAETSSVVIRGSVAYVPQVSWIFNATVRENILFGS-DFESERyw 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   98 TVFGNVALPLELDNTPKEeikrrvtellDLVGLGDKHdsypANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTR 177
Cdd:PLN03232   712 RAIDVTALQHDLDLLPGR----------DLTEIGERG----VNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAH 777

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160  178 SILE-LLKDINRrlGLTILLITHEMDVVKRIcDCVAVISNGELIEQDTVSEVFShpKTPLAQKFIQSTLHLD 248
Cdd:PLN03232   778 QVFDsCMKDELK--GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELSK--SGSLFKKLMENAGKMD 844
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
24-219 8.19e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 66.09  E-value: 8.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  24 VSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKA--------RRQIGMIFQHF---N 92
Cdd:PRK11288  272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDAIRAgimlcpedRKAEGIIPVHSvadN 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 L-LSSR---TVFGNValpleLDNTPKEEIKRRVTELLDLVGLGDKHDSypANLSGGQKQRVAIARALASNPKVLLCDEAT 168
Cdd:PRK11288  352 InISARrhhLRAGCL-----INNRWEAENADRFIRSLNIKTPSREQLI--MNLSGGNQQKAILGRWLSEDMKVILLDEPT 424

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 169 SALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK11288  425 RGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474
PLN03130 PLN03130
ABC transporter C family member; Provisional
 21-244 8.85e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 66.30  E-value: 8.85e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSeseLTKARRQIGMIFQHFNLLSsrtvf 100
Cdd:PLN03130  1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLFS----- 1326

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  101 GNVALPLELDNTPK-----EEIKRrvTELLDLV-----GLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSA 170
Cdd:PLN03130  1327 GTVRFNLDPFNEHNdadlwESLER--AHLKDVIrrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAA 1404

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1016201160  171 LDPAT----TRSILELLKdinrrlGLTILLITHEMDVVkrI-CDCVAVISNGELIEQDTVSEVFSHPKTPLAqKFIQST 244
Cdd:PLN03130  1405 VDVRTdaliQKTIREEFK------SCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSNEGSAFS-KMVQST 1474
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 15-298 1.31e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 65.42  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  15 TRTIQaLNNVSLHvpAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKArrqIGMIFQHFN-- 92
Cdd:PRK10938   16 TKTLQ-LPSLTLN--AGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQLQKL---VSDEWQRNNtd 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 LLS-SRTVFGNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYpanLSGGQKQRVAIARALASNPKVLLCDEATSAL 171
Cdd:PRK10938   90 MLSpGEDDTGRTTAEIIQDEVKDPARCEQLAQQFGITALLDRRFKY---LSTGETRKTLLCQALMSEPDLLILDEPFDGL 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 172 DPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVfshpktpLAQKFIQSTLHLDipe 251
Cdd:PRK10938  167 DVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEI-------LQQALVAQLAHSE--- 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1016201160 252 dyQARLKASPETDSVPMLrmeftgqsvdaPLLSETARRFNVNNNIIS 298
Cdd:PRK10938  236 --QLEGVQLPEPDEPSAR-----------HALPANEPRIVLNNGVVS 269
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 17-226 1.65e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 63.51  E-value: 1.65e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  17 TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCvnLLERP----TEGSVQVGGQELTTLSESEltKARRQIGMIFQH-- 90
Cdd:CHL00131   19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPaykiLEGDILFKGESILDLEPEE--RAHLGIFLAFQYpi 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 ---------FNLLS--SRTVFGNvaLPlELDntPKE--EIkrrVTELLDLVGLGDKHDSYPAN--LSGGQKQRVAIARAL 155
Cdd:CHL00131   95 eipgvsnadFLRLAynSKRKFQG--LP-ELD--PLEflEI---INEKLKLVGMDPSFLSRNVNegFSGGEKKRNEILQMA 166

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 156 ASNPKVLLCDEATSALDPATTRSILELLKDInRRLGLTILLITHE---MDVVKRicDCVAVISNGELIEQDTVS 226
Cdd:CHL00131  167 LLDSELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITHYqrlLDYIKP--DYVHVMQNGKIIKTGDAE 237
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 16-219 1.94e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 64.95  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  16 RTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLERPTEGSVQVGGQELTTLSESELTKA--------RRQIGM 86
Cdd:PRK13549  273 PHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQAIAQgiamvpedRKRDGI 352

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  87 IF-----QHFNL--LSSRTVFGNVALPLELDnTPKEEIKR-RV-TELLDLVglgdkhdsyPANLSGGQKQRVAIARALAS 157
Cdd:PRK13549  353 VPvmgvgKNITLaaLDRFTGGSRIDDAAELK-TILESIQRlKVkTASPELA---------IARLSGGNQQKAVLAKCLLL 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1016201160 158 NPKVLLCDEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PRK13549  423 NPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 2-237 1.94e-11

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: 63.39  E-value: 1.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   2 IKLSNITKVFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTL----IRCVNLLErpteGSVQVGGQELTTLSeseL 77
Cdd:cd03288    20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 TKARRQIGMIFQHFNLLSsrtvfGNVALPLELDNTPKEEikrRVTELLDLVGLGDKHDSYPA-----------NLSGGQK 146
Cdd:cd03288    91 HTLRSRLSIILQDPILFS-----GSIRFNLDPECKCTDD---RLWEALEIAQLKNMVKSLPGgldavvteggeNFSVGQR 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 147 QRVAIARALASNPKVLLCDEATSALDPAtTRSILE--LLKDINRRlglTILLITHEMDVVKRiCDCVAVISNGELIEQDT 224
Cdd:cd03288   163 QLFCLARAFVRKSSILIMDEATASIDMA-TENILQkvVMTAFADR---TVVTIAHRVSTILD-ADLVLVLSRGILVECDT 237

                         250
                  ....*....|...
gi 1016201160 225 VSEVFSHPKTPLA 237
Cdd:cd03288   238 PENLLAQEDGVFA 250
PTZ00243 PTZ00243
ABC transporter; Provisional
 21-221 3.00e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 64.80  E-value: 3.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELtkaRRQIGMIFQHfNLLSSRTVF 100
Cdd:PTZ00243  1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL---RRQFSMIPQD-PVLFDGTVR 1401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  101 GNVAlPLeLDNTPKEeikrrVTELLDLVGLGDKHDSYP-----------ANLSGGQKQRVAIARA-LASNPKVLLCDEAT 168
Cdd:PTZ00243  1402 QNVD-PF-LEASSAE-----VWAALELVGLRERVASESegidsrvleggSNYSVGQRQLMCMARAlLKKGSGFILMDEAT 1474

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1016201160  169 SALDPATTRSILELLkdINRRLGLTILLITHEMDVVKRiCDCVAVISNGELIE 221
Cdd:PTZ00243  1475 ANIDPALDRQIQATV--MSAFSAYTVITIAHRLHTVAQ-YDKIIVMDHGAVAE 1524
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 20-221 1.40e-10

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 62.30  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTtlsESELTKARRQIGMIFQHFNLlssrtv 99
Cdd:PRK10522  338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYRKLFSAVFTDFHL------ 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FGNValpLELDNTPKEEikRRVTELLDLVGLGDK---HDSYPAN--LSGGQKQRVAIARALASNPKVLLCDEATSALDPA 174
Cdd:PRK10522  409 FDQL---LGPEGKPANP--ALVEKWLERLKMAHKlelEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAADQDPH 483

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1016201160 175 TTRSILELLKDINRRLGLTILLITHE---MDVVKRICDcvavISNGELIE 221
Cdd:PRK10522  484 FRREFYQVLLPLLQEMGKTIFAISHDdhyFIHADRLLE----MRNGQLSE 529
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 20-206 2.15e-10

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: 58.87  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRcvnllerptegsvQVGGQELTTLSESELTKARRQigmifqhfnllssRTV 99
Cdd:cd03238    10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRN-------------KLI 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 100 FgnvalpleLDNTpkeeikRRVTEL-LDLVGLGDKHDSypanLSGGQKQRVAIARALASNPK--VLLCDEATSALDPATT 176
Cdd:cd03238    64 F--------IDQL------QFLIDVgLGYLTLGQKLST----LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDI 125

                         170       180       190
                  ....*....|....*....|....*....|
gi 1016201160 177 RSILELLKDInRRLGLTILLITHEMDVVKR 206
Cdd:cd03238   126 NQLLEVIKGL-IDLGNTVILIEHNLDVLSS 154
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
114-242 3.89e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.52  E-value: 3.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 114 KEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRlGLT 193
Cdd:NF000106  118 RKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GAT 196

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1016201160 194 ILLITHEMDVVKRICDCVAVISNGELIEQDTVSEVfshpKTPLAQKFIQ 242
Cdd:NF000106  197 VLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL----KTKVGGRTLQ 241
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 1-219 4.67e-10

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 60.68  E-value: 4.67e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFqqGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCV-NLLErPTEGSVQVG-GQELTTLseselt 78
Cdd:PRK15064    1 MLSTANITMQF--GAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKILgGDLE-PSAGNVSLDpNERLGKL------ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 karRQIGMIFQHFNLLSsrTVF-GNV-------------ALP-----------------LELDNTPKEEikrRVTELLDL 127
Cdd:PRK15064   70 ---RQDQFAFEEFTVLD--TVImGHTelwevkqerdriyALPemseedgmkvadlevkfAEMDGYTAEA---RAGELLLG 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 128 VGLG-DKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRrlglTILLITHEMDVVKR 206
Cdd:PRK15064  142 VGIPeEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINTIRWLEDVLNERNS----TMIIISHDRHFLNS 217

                         250
                  ....*....|...
gi 1016201160 207 ICDCVAVISNGEL 219
Cdd:PRK15064  218 VCTHMADLDYGEL 230
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 1-199 5.79e-10

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: 60.53  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNITKVFQQGTRTIQALNnvsLHVPAGQIYGVIGASGAGKSTLIRCVNLLeRPTEGSVqvggqelttlseseLTKA 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDVLIESLS---FEVPSGNNLLICGPNGCGKSSLFRILGEL-WPVYGGR--------------LTKP 512

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  81 RRQIGMIFQHFNLLSSRTVFGNVALPLEldntpKEEIKRR------VTELLDLVGLGD---KHDSYPA------NLSGGQ 145
Cdd:TIGR00954 513 AKGKLFYVPQRPYMTLGTLRDQIIYPDS-----SEDMKRRglsdkdLEQILDNVQLTHileREGGWSAvqdwmdVLSGGE 587

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 146 KQRVAIARALASNPKVLLCDEATSALDPATTRSILELLkdinRRLGLTILLITH 199
Cdd:TIGR00954 588 KQRIAMARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 21-209 7.33e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 59.96  E-value: 7.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRC-------------------VNLLE----RPTEGSV--------------- 62
Cdd:PRK11147   19 LDNAELHIEDNERVCLVGRNGAGKSTLMKIlngevllddgriiyeqdliVARLQqdppRNVEGTVydfvaegieeqaeyl 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  63 ----QVGGQELTTLSESELTK-ARRQIgmIFQHFNLLssrtvfgnvalplELDNtpkeeikrRVTELLDLVGLgdKHDSY 137
Cdd:PRK11147   99 kryhDISHLVETDPSEKNLNElAKLQE--QLDHHNLW-------------QLEN--------RINEVLAQLGL--DPDAA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 138 PANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINrrlGlTILLITHEMDVVK----RICD 209
Cdd:PRK11147  154 LSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFISHDRSFIRnmatRIVD 225
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 22-214 1.09e-09

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: 58.15  E-value: 1.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  22 NNVSLH---VPA-GQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQ-----------VGGQEL----TTLSESELTKARR 82
Cdd:cd03236    13 NSFKLHrlpVPReGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELqnyfTKLLEGDVKVIVK 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  83 QigmifQHFNLLSsRTVFGNVALPLEldNTPKEEIKRRVTELLDLVGLGDKHDSypaNLSGGQKQRVAIARALASNPKVL 162
Cdd:cd03236    93 P-----QYVDLIP-KAVKGKVGELLK--KKDERGKLDELVDQLELRHVLDRNID---QLSGGELQRVAIAAALARDADFY 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160 163 LCDEATSALDP----ATTRSILELLKDINrrlglTILLITHEMDVVKRICDCVAVI 214
Cdd:cd03236   162 FFDEPSSYLDIkqrlNAARLIRELAEDDN-----YVLVVEHDLAVLDYLSDYIHCL 212
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 20-217 1.22e-09

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 59.36  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  20 ALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESE--------LTKARRQIGmIFQH- 90
Cdd:PRK10982  263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfalVTEERRSTG-IYAYl 341

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  91 ---FNLLSS--RTVFGNVALpleLDNTpkeEIKRRVTELLDLVGLGD-KHDSYPANLSGGQKQRVAIARALASNPKVLLC 164
Cdd:PRK10982  342 digFNSLISniRNYKNKVGL---LDNS---RMKSDTQWVIDSMRVKTpGHRTQIGSLSGGNQQKVIIGRWLLTQPEILML 415

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1016201160 165 DEATSALDPATTRSILELLKDINRRlGLTILLITHEMDVVKRICDCVAVISNG 217
Cdd:PRK10982  416 DEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNG 467
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 1-199 1.88e-09

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 58.59  E-value: 1.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSnitKVFQqGTRTIqaLNNVSLH-VPAGQIyGVIGASGAGKSTLIRCVNLLERPTEGsvqvggqelttlseseltK 79
Cdd:PRK11819    9 MNRVS---KVVP-PKKQI--LKDISLSfFPGAKI-GVLGLNGAGKSTLLRIMAGVDKEFEG------------------E 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  80 ARRQ----IGMIFQHFNLLSSRTVFGNV---------------------ALPL-ELDNTPKEEIKrrVTELLDLVGLGD- 132
Cdd:PRK11819   64 ARPApgikVGYLPQEPQLDPEKTVRENVeegvaevkaaldrfneiyaayAEPDaDFDALAAEQGE--LQEIIDAADAWDl 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 133 --------------KHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILE-LLKDINrrlGlTILLI 197
Cdd:PRK11819  142 dsqleiamdalrcpPWDAKVTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLEqFLHDYP---G-TVVAV 216


                  ..
gi 1016201160 198 TH 199
Cdd:PRK11819  217 TH 218
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 31-206 2.34e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 55.46  E-value: 2.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   31 GQIYGVIGASGAGKSTLIRCV-NLLERPTEGSVQVGGQELTtlseseltkarrqigmifqhfnllssrtvfgnvalplel 109
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALaRELGPPGGGVIYIDGEDIL--------------------------------------- 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  110 dntpkeeikrrvtELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEL-----LK 184
Cdd:smart00382  43 -------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrlLL 109

                          170       180
                   ....*....|....*....|..
gi 1016201160  185 DINRRLGLTILLITHEMDVVKR 206
Cdd:smart00382 110 LLKSEKNLTVILTTNDEKDLGP 131
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 19-172 5.71e-09

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: 55.88  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAG-----QIYGVIGASGAGKSTLIRCVNLLERPTEGSVqvgGQELTTLSESELTKARRQIGMIFQhfnL 93
Cdd:cd03237     8 KTLGEFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDI---EIELDTVSYKPQYIKADYEGTVRD---L 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 LSSRT-VFGN-------VALPLELDNTpkeeIKRRVTElldlvglgdkhdsypanLSGGQKQRVAIARALASNPKVLLCD 165
Cdd:cd03237    82 LSSITkDFYThpyfkteIAKPLQIEQI----LDREVPE-----------------LSGGELQRVAIAACLSKDADIYLLD 140


                  ....*..
gi 1016201160 166 EATSALD 172
Cdd:cd03237   141 EPSAYLD 147
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
21-172 5.78e-09

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.13  E-value: 5.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIY-----GVIGASGAGKSTLIRCVNLLERPTEGSVQVG------GQELTTLSESELTKARRQIGMIFq 89
Cdd:PRK13409  350 LGDFSLEVEGGEIYegeviGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykPQYIKPDYDGTVEDLLRSITDDL- 428

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  90 hfnllSSRTVFGNVALPLELDntpkeeikrrvtELLDlvglgdkhdSYPANLSGGQKQRVAIARALASNPKVLLCDEATS 169
Cdd:PRK13409  429 -----GSSYYKSEIIKPLQLE------------RLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPSA 482


                  ...
gi 1016201160 170 ALD 172
Cdd:PRK13409  483 HLD 485
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
27-173 1.29e-08

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 54.47  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  27 HVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIFQHFNLLSSRTVfgnvalp 106
Cdd:PRK13543   33 HVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLKADLSTLENLHF------- 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 107 leLDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:PRK13543  106 --LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDL 170
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 21-172 1.76e-08

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: 55.95  E-value: 1.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIY-----GVIGASGAGKSTLIRCVNLLERPTEGSVqvggqelttlsESELT---KArrqigmifQHFN 92
Cdd:COG1245   351 YGGFSLEVEGGEIRegevlGIVGPNGIGKTTFAKILAGVLKPDEGEV-----------DEDLKisyKP--------QYIS 411

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  93 LLSSRTVFGNvalpLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:COG1245   412 PDYDGTVEEF----LRSANTDDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD 487
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
31-233 1.86e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.59  E-value: 1.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  31 GQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVG-----------GQELTT----LSESELTKARR--QIGMIfqhfnl 93
Cdd:PRK13409   99 GKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEpswdevlkrfrGTELQNyfkkLYNGEIKVVHKpqYVDLI------ 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  94 lsSRTVFGNVAlplE-LDNTPKEEIKRRVTELLDLVGLGDKHDSypaNLSGGQKQRVAIARALASNPKVLLCDEATSALD 172
Cdd:PRK13409  173 --PKVFKGKVR---ElLKKVDERGKLDEVVERLGLENILDRDIS---ELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1016201160 173 P----ATTRSILELLKDInrrlglTILLITHEMDVVKRICDCVaVISNGElieqDTVSEVFSHPK 233
Cdd:PRK13409  245 IrqrlNVARLIRELAEGK------YVLVVEHDLAVLDYLADNV-HIAYGE----PGAYGVVSKPK 298
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 15-196 5.00e-08

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 54.73  E-value: 5.00e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   15 TRTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnllERPTEGS-VQVGGQ-ELTTLSESELTKARRQ----IGMIF 88
Cdd:TIGR00956   71 TKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTI---ASNTDGFhIGVEGViTYDGITPEEIKKHYRGdvvyNAETD 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   89 QHFNLLSSRTVFGNVAL----PLELDNTPKEEIKRRVTEL-LDLVGLGDKHDSYPAN-----LSGGQKQRVAIARALASN 158
Cdd:TIGR00956  148 VHFPHLTVGETLDFAARcktpQNRPDGVSREEYAKHIADVyMATYGLSHTRNTKVGNdfvrgVSGGERKRVSIAEASLGG 227

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1016201160  159 PKVLLCDEATSALDPATTRSILELLKDINRRLGLTILL 196
Cdd:TIGR00956  228 AKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLV 265
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 36-218 6.36e-08

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 52.22  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  36 VIGASGAGKSTLIRCVNLL---ERPTEGSVQVGGQELTTLSESeltkaRRQIGMIFQHFN---LLSSRT--VFGNVALpl 107
Cdd:cd03240    27 IVGQNGAGKTTIIEALKYAltgELPPNSKGGAHDPKLIREGEV-----RAQVKLAFENANgkkYTITRSlaILENVIF-- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 108 eldnTPKEEIKrrvTELLDLVGlgdkhdsypaNLSGGQKQ------RVAIARALASNPKVLLCDEATSALDPATTR-SIL 180
Cdd:cd03240   100 ----CHQGESN---WPLLDMRG----------RCSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEENIEeSLA 162

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1016201160 181 ELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNGE 218
Cdd:cd03240   163 EIIEERKSQKNFQLIVITHDEELVDAADHIYRVEKDGR 200
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 56-263 7.80e-08

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: 53.86  E-value: 7.80e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  56 RPTEGSVQVGGQELTTLSESELTKArrqigMIFqhFNLLSSRTVFGNVALPLeldntpKEEIKRRVTELLDlVGLGDKHD 135
Cdd:TIGR00630 417 KPEALAVTVGGKSIADVSELSIREA-----HEF--FNQLTLTPEEKKIAEEV------LKEIRERLGFLID-VGLDYLSL 482

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 136 SYPAN-LSGGQKQRVAIARALASN-PKVL-LCDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVkRICDCV- 211
Cdd:TIGR00630 483 SRAAGtLSGGEAQRIRLATQIGSGlTGVLyVLDEPSIGLHQRDNRRLINTLKRL-RDLGNTLIVVEHDEDTI-RAADYVi 560

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 212 -----AVISNGELIEQDTVSEVFSHPKTpLAQKFIQSTLHLDIPEDyqaRLKASPET 263
Cdd:TIGR00630 561 digpgAGEHGGEVVASGTPEEILANPDS-LTGQYLSGRKKIEVPAE---RRPGNGKF 613
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 25-214 8.83e-08

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: 53.63  E-value: 8.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  25 SLHVP-AGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGG---QELTTLSESELtkarrqigmiFQHFNLLSSRTVf 100
Cdd:COG1245    92 GLPVPkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdEVLKRFRGTEL----------QDYFKKLANGEI- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 gNVA--------LPLELDNTPKEEIKR-----RVTELLDLVGLGDKHDSYPANLSGGQKQRVAIARALASNPKVLLCDEA 167
Cdd:COG1245   161 -KVAhkpqyvdlIPKVFKGTVRELLEKvdergKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1016201160 168 TSALDP----ATTRSILELLKDinrrlGLTILLITHEMDVVKRICDCVAVI 214
Cdd:COG1245   240 SSYLDIyqrlNVARLIRELAEE-----GKYVLVVEHDLAILDYLADYVHIL 285
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 21-205 1.07e-07

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 51.87  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLirCVNLLErpTEGSVQVggqeLTTLSeselTKARRQIGM-------------- 86
Cdd:cd03270    11 LKNVDVDIPRNKLVVITGVSGSGKSSL--AFDTIY--AEGQRRY----VESLS----AYARQFLGQmdkpdvdsieglsp 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  87 ---IFQHFNLLSSRTVFGNVAlplELDNT-----PKEEIKRRVTELLDlVGLGDKHDSYPAN-LSGGQKQRVAIARALAS 157
Cdd:cd03270    79 aiaIDQKTTSRNPRSTVGTVT---EIYDYlrllfARVGIRERLGFLVD-VGLGYLTLSRSAPtLSGGEAQRIRLATQIGS 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1016201160 158 NPKVLL--CDEATSALDPATTRSILELLKDInRRLGLTILLITHEMDVVK 205
Cdd:cd03270   155 GLTGVLyvLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIR 203
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 21-295 1.19e-07

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: 53.38  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGMIF-------QHFNL 93
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGRISFSPQTSWIMPGTIKDNIIFglsydeyRYTSV 521

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   94 LSSRTVFGNVALPLELDNTPkeeikrrvtelldlvgLGDKHdsypANLSGGQKQRVAIARALASNPKVLLCDEATSALDP 173
Cdd:TIGR01271  522 IKACQLEEDIALFPEKDKTV----------------LGEGG----ITLSGGQRARISLARAVYKDADLYLLDSPFTHLDV 581

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  174 ATTRSILE--LLKDINRRlglTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEVfsHPKTPlaqkfiqstlhldipe 251
Cdd:TIGR01271  582 VTEKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL--QAKRP---------------- 639

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1016201160  252 DYQARLKASPETDSVPMLRMEftgqsvdaPLLSETARRFNVNNN 295
Cdd:TIGR01271  640 DFSSLLLGLEAFDNFSAERRN--------SILTETLRRVSIDGD 675
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 21-209 1.73e-07

ATP-binding cassette domain II 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: 213238 [Multi-domain]  Cd Length: 261  Bit Score: 51.85  E-value: 1.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLI----------RCVNLLERPTEGSVQVGGQELTTL---SESEL---------- 77
Cdd:cd03271    11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlypalarRLHLKKEQPGNHDRIEGLEHIDKViviDQSPIgrtprsnpat 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  78 -TKARRQIGMIF------QHFN--LLSSRTVFGNVALPLEL---------DNTPKeeIKRRVTELLDlVGLGDKHDSYPA 139
Cdd:cd03271    91 yTGVFDEIRELFcevckgKRYNreTLEVRYKGKSIADVLDMtveealeffENIPK--IARKLQTLCD-VGLGYIKLGQPA 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 140 -NLSGGQKQRVAIARALA--SNPKVL-LCDEATSALDPATTRSILELLkdinRRL---GLTILLITHEMDVVKrICD 209
Cdd:cd03271   168 tTLSGGEAQRIKLAKELSkrSTGKTLyILDEPTTGLHFHDVKKLLEVL----QRLvdkGNTVVVIEHNLDVIK-CAD 239
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 21-228 2.67e-07

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: 51.40  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTEGSVQVGGQelttLSESEltkarrqigmifqHFNLLSSRTVF 100
Cdd:cd03291    53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR----ISFSS-------------QFSWIMPGTIK 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 101 GNVALPLELDNTPKEEIKRRVTELLDLVGLGDKHDSYPA----NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATT 176
Cdd:cd03291   116 ENIIFGVSYDEYRYKSVVKACQLEEDITKFPEKDNTVLGeggiTLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 177 RSILE--LLKDINRRlglTILLITHEMDVVKRiCDCVAVISNGELIEQDTVSEV 228
Cdd:cd03291   196 KEIFEscVCKLMANK---TRILVTSKMEHLKK-ADKILILHEGSSYFYGTFSEL 245
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 38-205 2.34e-06

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 47.56  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  38 GASGAGKSTLIRCVNLLERPTEGSVQVGGQELTTLSESELTKARRQIGmifqhfnLLSSRTVFGNVALPLELDNTpKEEI 117
Cdd:PRK13541   33 GANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIGHNLG-------LKLEMTVFENLKFWSEIYNS-AETL 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 118 KRRVT--ELLDLVglgdkhDSYPANLSGGQKQRVAIARALASNPKVLLCDEATSALDpATTRSILELLKDINRRLGLTIL 195
Cdd:PRK13541  105 YAAIHyfKLHDLL------DEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS-KENRDLLNNLIVMKANSGGIVL 177

                         170
                  ....*....|
gi 1016201160 196 LITHEMDVVK 205
Cdd:PRK13541  178 LSSHLESSIK 187
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 1-221 2.40e-06

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 48.25  E-value: 2.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   1 MIKLSNItKVFQQGTRTIQALNnvsLHVPAGQIYGVIGASGAGKSTLIRCVNLLE--RPTEGSVQVGGQELTTLSESElt 78
Cdd:PRK09580    1 MLSIKDL-HVSVEDKAILRGLN---LEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED-- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  79 KARRQIGMIFQ----------HFNLLSSRTVFGNVALPLELDNTPKEEIKRRVTELLDLvglgdkhdsyPANL------- 141
Cdd:PRK09580   75 RAGEGIFMAFQypveipgvsnQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKM----------PEDLltrsvnv 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 142 --SGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILE---LLKDINRrlglTILLITHEMDVVKRI-CDCVAVIS 215
Cdd:PRK09580  145 gfSGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADgvnSLRDGKR----SFIIVTHYQRILDYIkPDYVHVLY 220


                  ....*.
gi 1016201160 216 NGELIE 221
Cdd:PRK09580  221 QGRIVK 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 110-205 4.88e-06

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: 48.47  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 110 DNTPKeeIKRRVTELLDlVGLGDKHDSYPA-NLSGGQKQRVAIARAL---ASNPKVLLCDEATSALDPATTRSILELLKD 185
Cdd:TIGR00630 801 EAVPS--ISRKLQTLCD-VGLGYIRLGQPAtTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQR 877

                          90       100
                  ....*....|....*....|
gi 1016201160 186 InRRLGLTILLITHEMDVVK 205
Cdd:TIGR00630 878 L-VDKGNTVVVIEHNLDVIK 896
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 10-218 7.23e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 47.70  E-value: 7.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  10 VFQQGTRTIqaLNNVSLHVPAGQIYGVIGASGAGKSTLIRCVnllerpTEGSVQVGGQELTtlseseLTKARRQIGM--- 86
Cdd:PRK10938  267 VVSYNDRPI--LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLI------TGDHPQGYSNDLT------LFGRRRGSGEtiw 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  87 -IFQHFNLLSSR--------TVFGNVALPLELDN-----TPKEEIKRRVTELLDLVGLGDKHDSYP-ANLSGGQKQRVAI 151
Cdd:PRK10938  333 dIKKHIGYVSSSlhldyrvsTSVRNVILSGFFDSigiyqAVSDRQQKLAQQWLDILGIDKRTADAPfHSLSWGQQRLALI 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1016201160 152 ARALASNPKVLLCDEATSALDPattrsilellkdINRRLgltillithemdvVKRICDcvAVISNGE 218
Cdd:PRK10938  413 VRALVKHPTLLILDEPLQGLDP------------LNRQL-------------VRRFVD--VLISEGE 452
GguA NF040905
sugar ABC transporter ATP-binding protein;
19-220 7.82e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 47.48  E-value: 7.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  19 QALNNVSLHVPAGQIYGVIGASGAGKSTLIRCV--NLLERPTEGSVQVGGQELTTLSESE--------LTKARRQIGMIF 88
Cdd:NF040905  274 KVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTVSDaidaglayVTEDRKGYGLNL 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  89 Q----------HFNLLSSRTVfgnvalpleLDNTpkEEIK-----R-----RVTELLDLVGlgdkhdsypaNLSGGQKQR 148
Cdd:NF040905  354 IddikrnitlaNLGKVSRRGV---------IDEN--EEIKvaeeyRkkmniKTPSVFQKVG----------NLSGGNQQK 412

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1016201160 149 VAIARALASNPKVLLCDEATSALDPATTRSILELlkdINR--RLGLTILLITHEMDVVKRICDCVAVISNGELI 220
Cdd:NF040905  413 VVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTI---INElaAEGKGVIVISSELPELLGMCDRIYVMNEGRIT 483
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 115-257 8.09e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.90  E-value: 8.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  115 EEIKRRVTELLDLvGLGD-KHDSYPANLSGGQKQRVAIARALASNPK--VLLCDEATSALDPATTRSILELLKDInRRLG 191
Cdd:PRK00635   451 QGLKSRLSILIDL-GLPYlTPERALATLSGGEQERTALAKHLGAELIgiTYILDEPSIGLHPQDTHKLINVIKKL-RDQG 528

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1016201160  192 LTILLITHEMDVVK---RICDC--VAVISNGELIEQDTVSEvFSHPKTPLAQKFIQSTLHLDIPEDYQARL 257
Cdd:PRK00635   529 NTVLLVEHDEQMISladRIIDIgpGAGIFGGEVLFNGSPRE-FLAKSDSLTAKYLRQELTIPIPEKRTNSL 598
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-172 9.09e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 47.19  E-value: 9.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   4 LSNITKVFQQGTrtiqALNNVSLHVPAGQIYGVIGASGAGKSTLIRC-VNLLErPTEGSV------QVG--GQELTTLSE 74
Cdd:PRK15064  322 VENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTlVGELE-PDSGTVkwsenaNIGyyAQDHAYDFE 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  75 SELT-----KARRQIGMIFQHFNLLSSRTVFGNvalpleldntpkEEIKRRVTelldlvglgdkhdsypaNLSGGQKQRV 149
Cdd:PRK15064  397 NDLTlfdwmSQWRQEGDDEQAVRGTLGRLLFSQ------------DDIKKSVK-----------------VLSGGEKGRM 447

                         170       180
                  ....*....|....*....|...
gi 1016201160 150 AIARALASNPKVLLCDEATSALD 172
Cdd:PRK15064  448 LFGKLMMQKPNVLVMDEPTNHMD 470
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
110-205 1.17e-05

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 46.94  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 110 DNTPKeeIKRRVTELLDlVGLGdkhdsY-----PAN-LSGGQKQRVAIARALA--SNPKVL-LCDEATSALDPATTRSIL 180
Cdd:COG0178   798 ENIPK--IARKLQTLQD-VGLG-----YiklgqPATtLSGGEAQRVKLASELSkrSTGKTLyILDEPTTGLHFHDIRKLL 869

                          90       100
                  ....*....|....*....|....*...
gi 1016201160 181 ELLkdinRRL---GLTILLITHEMDVVK 205
Cdd:COG0178   870 EVL----HRLvdkGNTVVVIEHNLDVIK 893
PLN03073 PLN03073
ABC transporter F family; Provisional
 21-172 3.13e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 45.62  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  21 LNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLE---RPTEGSV-----QVGGQELTTL-----SESELTKARRQIGMI 87
Cdd:PLN03073  193 IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAidgIPKNCQIlhveqEVVGDDTTALqcvlnTDIERTQLLEEEAQL 272

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  88 FQHFNLLSSRTVFGNVALP----LELDNTPK--EEIKRRVtELLD-----------LVGLG---DKHDSYPANLSGGQKQ 147
Cdd:PLN03073  273 VAQQRELEFETETGKGKGAnkdgVDKDAVSQrlEEIYKRL-ELIDaytaearaasiLAGLSftpEMQVKATKTFSGGWRM 351

                         170       180
                  ....*....|....*....|....*
gi 1016201160 148 RVAIARALASNPKVLLCDEATSALD 172
Cdd:PLN03073  352 RIALARALFIEPDLLLLDEPTNHLD 376
uvrA PRK00349
excinuclease ABC subunit UvrA;
110-205 6.01e-05

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 45.06  E-value: 6.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 110 DNTPKeeIKRRVTELLDlVGLGdkhdsY-----PAN-LSGGQKQRVAIARALA--SNPKVL-LCDEATSALDPATTRSIL 180
Cdd:PRK00349  802 EAIPK--IARKLQTLVD-VGLG-----YiklgqPATtLSGGEAQRVKLAKELSkrSTGKTLyILDEPTTGLHFEDIRKLL 873

                          90       100
                  ....*....|....*....|....*...
gi 1016201160 181 ELLKdinrRL---GLTILLITHEMDVVK 205
Cdd:PRK00349  874 EVLH----RLvdkGNTVVVIEHNLDVIK 897
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 17-247 1.24e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 44.05  E-value: 1.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   17 TIQALNNVSLHVPAGQIYGVIGASGAGKSTLIR--CVNLLERPTEG------SVQVGGQE------------------LT 70
Cdd:PRK00635   607 TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQgfcsnlSIQWGAISrlvhitrdlpgrsqrsipLT 686

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160   71 TLSE--------SELTKARRQiGMIFQHFNL------------LSSRTVFGN---------------------------V 103
Cdd:PRK00635   687 YIKAfddlrelfAEQPRSKRL-GLTKSHFSFntplgacaecqgLGSITTTDNrtsipcpsclgkrflpqvlevrykgknI 765

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  104 ALPLELD---------NTPK--EEIKRRVTELLDLVGLGDKHDSypanLSGGQKQRVAIARALAS---NPKVLLCDEATS 169
Cdd:PRK00635   766 ADILEMTayeaekfflDEPSihEKIHALCSLGLDYLPLGRPLSS----LSGGEIQRLKLAYELLApskKPTLYVLDEPTT 841

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  170 ALDPATTRSILELLKDINRrLGLTILLITHEMDVVKrICDCV---------------AVISNGELIEQDTvsevfshPKT 234
Cdd:PRK00635   842 GLHTHDIKALIYVLQSLTH-QGHTVVIIEHNMHVVK-VADYVlelgpeggnlggyllASCSPEELIHLHT-------PTA 912

                          330
                   ....*....|...
gi 1016201160  235 PLAQKFIQSTLHL 247
Cdd:PRK00635   913 KALRPYLSSPQEL 925
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
 139-185 3.30e-04

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: 39.14  E-value: 3.30e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 139 ANLSGGQKQR---VAIARALAS----------NPKVLLCDEATSALDPATTRSILELLKD 185
Cdd:pfam13558  31 GGLSGGEKQLlayLPLAAALAAqygsaegrppAPRLVFLDEAFAKLDEENIRTALELLRA 90
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 140-233 4.69e-04

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: 40.63  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 140 NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILLITHEMDVVKRICDCVAVISNgel 219
Cdd:cd03222    71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEG--- 147

                          90
                  ....*....|....
gi 1016201160 220 ieQDTVSEVFSHPK 233
Cdd:cd03222   148 --EPGVYGIASQPK 159
PLN03140 PLN03140
ABC transporter G family member; Provisional
 141-196 8.92e-04

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 41.37  E-value: 8.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1016201160  141 LSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILELLKDINRRLGLTILL 196
Cdd:PLN03140   337 ISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLM 392
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 141-206 1.34e-03

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: 38.88  E-value: 1.34e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 141 LSGGQKQRVAIARALAS---NPKVLLC-DEATSALDPATTRSILELLKDiNRRLGLTILLITHEMDVVKR 206
Cdd:cd03227    78 LSGGEKELSALALILALaslKPRPLYIlDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITHLPELAEL 146
PLN03073 PLN03073
ABC transporter F family; Provisional
 36-219 2.24e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 39.84  E-value: 2.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  36 VIGASGAGKSTLIRCVNLLERPTEGSVqvggqelttlseseLTKARRQIGMIFQH----FNLLSSRTVFGNVALPleldN 111
Cdd:PLN03073  540 MVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQHhvdgLDLSSNPLLYMMRCFP----G 601

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160 112 TPKEEIKRRVTELldlvGLGDKHDSYPA-NLSGGQKQRVAIARALASNPKVLLCDEATSALDPATTRSILEllkdinrrl 190
Cdd:PLN03073  602 VPEQKLRAHLGSF----GVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQ--------- 668

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1016201160 191 GLT-----ILLITHEMDVVKRICDCVAVISNGEL 219
Cdd:PLN03073  669 GLVlfqggVLMVSHDEHLISGSVDELWVVSEGKV 702
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
33-199 6.20e-03

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 37.30  E-value: 6.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  33 IYGVIGASGAGKSTLIRCVNL-LERPTEGSVQVGGQELTTLSES---ELT--------KARRQIGMIFQHFNLLSS---- 96
Cdd:COG0419    25 LNLIVGPNGAGKSTILEAIRYaLYGKARSRSKLRSDLINVGSEEasvELEfehggkryRIERRQGEFAEFLEAKPSerke 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1016201160  97 --RTVFG------------NVALPLELDNTPKEEIKRRVTELL-DLVGLGDkhdsyPANLSGGQKQRVAIARALAsnpkv 161
Cdd:COG0419   105 alKRLLGleiyeelkerlkELEEALESALEELAELQKLKQEILaQLSGLDP-----IETLSGGERLRLALADLLS----- 174

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1016201160 162 LLCDeaTSALDPATTRSILELLKDINrrlgltilLITH 199
Cdd:COG0419   175 LILD--FGSLDEERLERLLDALEELA--------IITH 202
 
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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