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Conserved domains on  [gi|504427498|ref|WP_014614600|]
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ABC transporter ATP-binding protein [Staphylococcus pseudintermedius]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438980)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ABC transporter complex responsible for coupling the energy of ATP hydrolysis to the transport of one or more from a variety of substrates including hemin, bacitracin, and lipoproteins

CATH:  3.40.50.300
EC:  7.6.2.-
Gene Ontology:  GO:0042626|GO:0140359|GO:0016887|GO:0005524
PubMed:  25750732|24638992|9640644
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-224 3.04e-117

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


:

Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 334.32  E-value: 3.04e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MS-ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQL 79
Cdd:COG1136    1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 SYFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALI 159
Cdd:COG1136   81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
 
Name Accession Description Interval E-value
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-224 3.04e-117

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 334.32  E-value: 3.04e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MS-ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQL 79
Cdd:COG1136    1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 SYFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALI 159
Cdd:COG1136   81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 4-221 1.77e-111

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: 319.44  E-value: 1.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFR 83
Cdd:cd03255    1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 3-222 9.84e-69

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 211.06  E-value: 9.84e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:TIGR02211   1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   83 RKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:TIGR02211  81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIH 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 5-221 2.11e-55

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 180.77  E-value: 2.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRK 84
Cdd:PRK11153   3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAI 164
Cdd:PRK11153  83 Q-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 165 VFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
3-235 1.06e-49

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 166.40  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeaLKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyf 82
Cdd:NF040840   1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:NF040840  71 -KRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIH-----TELFQgdQPVSQF 235
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRLSqvgdvREVFR--RPKNEF 226
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 23-171 2.98e-45

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: 148.95  E-value: 2.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDYNVLHTLTV 102
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498  103 RENIMLPLSITKLSRQEAEMRYQEVTEALGITEIG----SKYPDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
22-216 4.82e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 105.78  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGqditrmsnkqlsyfrKKDVGFIFQDYNVLHTL- 100
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 -TVRENIML----PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALD 175
Cdd:NF040873  72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 176 SKSAQDLLKRLETINQQmKTTIVMVTHDPVAASYANRVIML 216
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
99-221 4.15e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.06  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  99 TLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504427498 179 AQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-198 2.15e-10

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 60.52  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRkk 85
Cdd:NF033858   4 LEGVSHRYGKTV----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  86 dVGFIFQDY--NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGIteigSKYPD----EISGGQKQRTAAARALI 159
Cdd:NF033858  78 -IAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504427498 160 SKPAIVFADEPTGALDSKS-AQ--DLLKRLETINQQMkTTIV 198
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSrRQfwELIDRIRAERPGM-SVLV 193
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-226 4.13e-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: 53.92  E-value: 4.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    32 KGGFVAIMGPSGSGKTTLLN-VISSIDNVTRGTIEINGQDITrmsnkqlsyfrkkdvgfifqdynvlhtltvrenimlpl 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDIL-------------------------------------- 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   111 sitklsrqeaemryqEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLET-- 188
Cdd:smart00382  43 ---------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrl 107

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 504427498   189 ---INQQMKTTIVMVTHDPVAASYANRVIMLkDGQIHTELF 226
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRF-DRRIVLLLI 147
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
22-171 1.03e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.43  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKG---GFVaimGPSGSGKTTLLNVISSIDNVTRGTI-----EINGQDI-TRMsnkqlsyfRkkdVGFIFQ 92
Cdd:NF033858 281 AVDHVSFRIRRGeifGFL---GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIaTRR--------R---VGYMSQ 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498  93 DYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
GguA NF040905
sugar ABC transporter ATP-binding protein;
3-220 6.78e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS------SIDnvtrGTIEINGQ-----DI 71
Cdd:NF040905   1 ILEMRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSYE----GEILFDGEvcrfkDI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  72 tRMSnkqlsyfRKKDVGFIFQDYNVLHTLTVRENIMLPLSITK---LSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQ 148
Cdd:NF040905  73 -RDS-------EALGIVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGK 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 149 KQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIvMVTH--DPVAAsYANRVIMLKDGQ 220
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSI-IISHklNEIRR-VADSITVLRDGR 216
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-175 5.36e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 37.85  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVI---SSIDNVTrGTIEINGQDItRMSN------KQLSYFR--KKDVGFIF 91
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrSYGRNIS-GTVFKDGKEV-DVSTvsdaidAGLAYVTedRKGYGLNL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  92 QDynvlhtlTVRENIMLPlSITKLSR-----QEAEMRY-QEVTEALGIteigsKYPD------EISGGQKQRTAAARALI 159
Cdd:NF040905 354 ID-------DIKRNITLA-NLGKVSRrgvidENEEIKVaEEYRKKMNI-----KTPSvfqkvgNLSGGNQQKVVLSKWLF 420

                        170
                 ....*....|....*.
gi 504427498 160 SKPAIVFADEPTGALD 175
Cdd:NF040905 421 TDPDVLILDEPTRGID 436
 
Name Accession Description Interval E-value
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-224 3.04e-117

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 334.32  E-value: 3.04e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MS-ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQL 79
Cdd:COG1136    1 MSpLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSEREL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 SYFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALI 159
Cdd:COG1136   81 ARLRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:COG1136  161 NRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVSD 225
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 4-221 1.77e-111

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: 319.44  E-value: 1.77e-111
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFR 83
Cdd:cd03255    1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
3-222 1.64e-81

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 243.81  E-value: 1.64e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:COG2884    1 MIRFENVSKRYPGGR---EALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:COG2884   78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINqQMKTTIVMVTHDP-VAASYANRVIMLKDGQIH 222
Cdd:COG2884  157 ELLLADEPTGNLDPETSWEIMELLEEIN-RRGTTVLIATHDLeLVDRMPKRVLELEDGRLV 216
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-225 2.23e-73

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 224.20  E-value: 2.23e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqls 80
Cdd:COG1116    5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPG----- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrkKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:COG1116   80 ----PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 161 KPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKD--GQIHTEL 225
Cdd:COG1116  156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDeAVFLADRVVVLSArpGRIVEEI 223
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 2-224 2.63e-72

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: 220.77  E-value: 2.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:COG4181    7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKKDVGFIFQDYNVLHTLTVRENIMLPLSITklSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:COG4181   87 LRARHVGFVFQSFQLLPTLTALENVMLPLELA--GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 162 PAIVFADEPTGALDSKSAQ---DLLKRLetiNQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:COG4181  165 PAILFADEPTGNLDAATGEqiiDLLFEL---NRERGTTLVLVTHDPALAARCDRVLRLRAGRLVED 227
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
3-221 2.63e-72

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 224.19  E-value: 2.63e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:COG1135    1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:COG1135   81 RRK-IGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG1135  160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEmDVVRRICDRVAVLENGRI 219
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 3-221 2.74e-72

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: 220.53  E-value: 2.74e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:cd03258    1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:cd03258   81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:cd03258  160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEmEVVKRICDRVAVMEKGEV 219
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 4-221 8.39e-72

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: 218.54  E-value: 8.39e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqlsyfR 83
Cdd:cd03259    1 LELKGLSKTYGSVR----ALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPP------E 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03259   71 RRNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:cd03259  151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEeALALADRIAVMNEGRI 209
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 1-235 3.58e-71

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 221.87  E-value: 3.58e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqls 80
Cdd:COG3839    1 MASLELENVSKSYGGV----EALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:COG3839   74 ---DRNIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 161 KPAIVFADEPTGALDSKSAQDL---LKRLetiNQQMKTTIVMVTHDPV-AASYANRVIMLKDGQIH-----TELFqgDQP 231
Cdd:COG3839  151 EPKVFLLDEPLSNLDAKLRVEMraeIKRL---HRRLGTTTIYVTHDQVeAMTLADRIAVMNDGRIQqvgtpEELY--DRP 225


                 ....
gi 504427498 232 VSQF 235
Cdd:COG3839  226 ANLF 229
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 4-225 9.10e-71

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: 216.18  E-value: 9.10e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqlsyfr 83
Cdd:cd03293    1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG-------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03293   73 -PDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDpV--AASYANRVIML--KDGQIHTEL 225
Cdd:cd03293  152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHD-IdeAVFLADRVVVLsaRPGRIVAEV 216
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-235 1.70e-69

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 217.27  E-value: 1.70e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqls 80
Cdd:COG3842    3 MPALELENVSKRYGDVT----ALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfRKKDVGFIFQDYnVL--HtLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARAL 158
Cdd:COG3842   75 --EKRNVGMVFQDY-ALfpH-LTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARAL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 159 ISKPAIVFADEPTGALDSK---SAQDLLKRletINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQIH-----TELFqgD 229
Cdd:COG3842  151 APEPRVLLLDEPLSALDAKlreEMREELRR---LQRELGITFIYVTHDQEeALALADRIAVMNDGRIEqvgtpEEIY--E 225


                 ....*.
gi 504427498 230 QPVSQF 235
Cdd:COG3842  226 RPATRF 231
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 3-222 9.84e-69

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ABC transporter family (pfam00005). LolD is involved in localization of lipoproteins in some bacteria. It works with a transmembrane protein LolC, which in some species is a paralogous pair LolC and LolE. Depending on whether the residue immediately following the new, modified N-terminal Cys residue, the nascent lipoprotein may be carried further by LolA and LolB to the outer membrane, or remain at the inner membrane. The top scoring proteins excluded by this model include homologs from the archaeal genus Methanosarcina. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 211.06  E-value: 9.84e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:TIGR02211   1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   83 RKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:TIGR02211  81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIH 222
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLF 220
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 3-221 2.21e-67

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: 207.74  E-value: 2.21e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:cd03257    1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQD-YNVLH-TLTVRENIMLPLSI-TKLSRQEA-EMRYQEVTEALGITE-IGSKYPDEISGGQKQRTAAARA 157
Cdd:cd03257   81 RKE-IQMVFQDpMSSLNpRMTIGEQIAEPLRIhGKLSKKEArKEAVLLLLVGVGLPEeVLNRYPHELSGGQRQRVAIARA 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 158 LISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:cd03257  160 LALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlGVVAKIADRVAVMYAGKI 224
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 6-216 3.02e-67

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly wide distribution consists of a polypeptide related to the lactococcin 972 (see TIGR01653) and multiple-membrane-spanning putative immunity protein (see TIGR01654). This model represents a small clade within the ABC transporters that regularly are found adjacent to these bacteriocin system gene pairs and are likely serve as export proteins. [Cellular processes, Toxin production and resistance, Transport and binding proteins, Unknown substrate]


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 206.70  E-value: 3.02e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    6 VSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKK 85
Cdd:TIGR03608   1 LKNISKKFGDK----VILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   86 DVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIV 165
Cdd:TIGR03608  77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504427498  166 FADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHDPVAASYANRVIML 216
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDEGK-TIIIVTHDPEVAKQADRVIEL 206
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 2-241 9.15e-67

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 207.22  E-value: 9.15e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:COG3638    1 PMLELRNLSKRYPGGTP---ALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKkDVGFIFQDYNVLHTLTVRENIM--------LPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTA 153
Cdd:COG3638   78 LRR-RIGMIFQQFNLVPRLSVLTNVLagrlgrtsTWRSLLGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 154 AARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQIhteLFQGdqPV 232
Cdd:COG3638  157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVdLARRYADRIIGLRDGRV---VFDG--PP 231


                 ....*....
gi 504427498 233 SQFYQEIIH 241
Cdd:COG3638  232 AELTDAVLR 240
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 3-235 1.26e-65

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: 203.67  E-value: 1.26e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:COG1127    5 MIEVRNLTKSFGDRV----VLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDYNVLHTLTVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:COG1127   81 RRR-IGMLFQGGALFDSLTVFENVAFPLREhTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALD 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIHT-----ELFQGDQP-VSQ 234
Cdd:COG1127  160 PEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDlDSAFAIADRVAVLADGKIIAegtpeELLASDDPwVRQ 239


                 .
gi 504427498 235 F 235
Cdd:COG1127  240 F 240
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 4-221 6.32e-64

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: 199.64  E-value: 6.32e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyFR 83
Cdd:COG1124    2 LEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKA---FR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQD-YNVLH-TLTVRENIMLPLSITKLSRQEAEMRyqEVTEALGIT-EIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:COG1124   79 RR-VQMVFQDpYASLHpRHTVDRILAEPLRIHGLPDREERIA--ELLEQVGLPpSFLDRYPHQLSGGQRQRVAIARALIL 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 161 KPAIVFADEPTGALD-SKSAQ--DLLKRLetiNQQMKTTIVMVTHDPVAASY-ANRVIMLKDGQI 221
Cdd:COG1124  156 EPELLLLDEPTSALDvSVQAEilNLLKDL---REERGLTYLFVSHDLAVVAHlCDRVAVMQNGRI 217
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 3-221 5.29e-63

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: 205.14  E-value: 5.29e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSY-EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:COG1123  260 LLEVRNLSKRYPVRGKGGvRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKkDVGFIFQD-YNVL-HTLTVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGI-TEIGSKYPDEISGGQKQRTAAARA 157
Cdd:COG1123  340 LRR-RVQMVFQDpYSSLnPRMTVGDIIAEPLRLhGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARA 418

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 158 LISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG1123  419 LALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlAVVRYIADRVAVMYDGRI 483
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 3-221 1.18e-62

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


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 195.62  E-value: 1.18e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:TIGR02982   1 VISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   83 RKKdVGFIFQDYNVLHTLTVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:TIGR02982  81 RRR-IGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHH 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:TIGR02982 160 PKLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGKL 219
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 4-229 3.13e-62

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: 194.86  E-value: 3.13e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnKQLSYFR 83
Cdd:COG1122    1 IELENLSFSYPGGTP---ALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITK---KNLRELR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNV-LHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:COG1122   75 RK-VGLVFQNPDDqLFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDP-VAASYANRVIMLKDGQIhteLFQGD 229
Cdd:COG1122  154 EVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLdLVAELADRVIVLDDGRI---VADGT 217
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 4-220 5.01e-61

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: 190.09  E-value: 5.01e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMsNKQLSYFR 83
Cdd:cd03229    1 LELKNVSKRYGQKT----VLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTLTVRENIMLPLSitklsrqeaemryqevtealgiteigskypdeisGGQKQRTAAARALISKPA 163
Cdd:cd03229   76 RR-IGMVFQDFALFPHLTVLENIALGLS----------------------------------GGQQQRVALARALAMDPD 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQ 220
Cdd:cd03229  121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLdEAARLADRVVVLRDGK 178
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 6-246 1.84e-60

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 190.78  E-value: 1.84e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    6 VSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqlsyFRKK 85
Cdd:TIGR00968   3 IANISKRFG----SFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVH------ARDR 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   86 DVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIV 165
Cdd:TIGR00968  73 KIGFVFQHYALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVL 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  166 FADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQIH-----TELFqgDQPVSQFYQEI 239
Cdd:TIGR00968 153 LLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEeAMEVADRIVVMSNGKIEqigspDEVY--DHPANPFVMSF 230


                  ....*..
gi 504427498  240 IHNQSVL 246
Cdd:TIGR00968 231 LGEVNVL 237
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 1-235 2.16e-60

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 193.82  E-value: 2.16e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITrmSNKQLs 80
Cdd:COG1118    1 MSI-EVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLF--TNLPP- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:COG1118   73 --RERRVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAV 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 161 KPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDG---QIHT--ELFqgDQPVSQ 234
Cdd:COG1118  151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEeALELADRVVVMNQGrieQVGTpdEVY--DRPATP 228


                 .
gi 504427498 235 F 235
Cdd:COG1118  229 F 229
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 4-242 2.33e-60

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: 190.47  E-value: 2.33e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFR 83
Cdd:cd03256    1 IEVENLSKTYPNGKK---ALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTLTVRENIM------------LPLSITKLSRQEAemryQEVTEALGITEIGSKYPDEISGGQKQR 151
Cdd:cd03256   78 RQ-IGMIFQQFNLIERLSVLENVLsgrlgrrstwrsLFGLFPKEEKQRA----LAALERVGLLDKAYQRADQLSGGQQQR 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 152 TAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQIhteLFqgDQ 230
Cdd:cd03256  153 VAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVdLAREYADRIVGLKDGRI---VF--DG 227

                        250
                 ....*....|..
gi 504427498 231 PVSQFYQEIIHN 242
Cdd:cd03256  228 PPAELTDEVLDE 239
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-229 8.08e-60

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 188.73  E-value: 8.08e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfr 83
Cdd:COG1131    1 IEVRGLTKRYGDKT----ALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEV----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:COG1131   72 RRRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGD 229
Cdd:COG1131  152 LLILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYlEEAERLCDRVAIIDKGRI---VADGT 214
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 6-235 1.60e-59

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: 188.09  E-value: 1.60e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKK 85
Cdd:cd03261    3 LRGLTKSFGGRT----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  86 dVGFIFQDYNVLHTLTVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAI 164
Cdd:cd03261   79 -MGMLFQSGALFDSLTVFENVAFPLREhTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPEL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 165 VFADEPTGALDSKSA---QDLLKRLetiNQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI-----HTELFQGDQP-VSQ 234
Cdd:cd03261  158 LLYDEPTAGLDPIASgviDDLIRSL---KKELGLTSIMVTHDlDTAFAIADRIAVLYDGKIvaegtPEELRASDDPlVRQ 234


                 .
gi 504427498 235 F 235
Cdd:cd03261  235 F 235
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 3-221 2.96e-59

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 187.51  E-value: 2.96e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITrMSNKQLSYF 82
Cdd:COG1126    1 MIEIENLHKSFGDL----EVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDYNVLHTLTVRENIML-PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:COG1126   76 RRK-VGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG1126  155 PKVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEmGFAREVADRVVFMDGGRI 214
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 5-220 5.11e-59

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: 186.13  E-value: 5.11e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKKQsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfrk 84
Cdd:cd03225    1 ELKNLSFSYPDGAR--PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR---- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KDVGFIFQDYNV-LHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03225   75 RKVGLVFQNPDDqFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDP-VAASYANRVIMLKDGQ 220
Cdd:cd03225  155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLdLLLELADRVIVLEDGK 211
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
 4-240 5.15e-59

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ATP-binding protein is found in a number of genomes in operon-like contexts strongly suggesting a substrate specificity for 2-aminoethylphosphonate (2-AEP). The characterized PhnSTUV system is absent in the genomes in which this system is found. These genomes encode systems for the catabolism of 2-AEP, making the need for a 2-AEP-specific transporter likely. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 190.63  E-value: 5.15e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfr 83
Cdd:TIGR03265   5 LSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQ------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:TIGR03265  75 KRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPG 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAA-SYANRVIMLKDGQIH-----TELFQgdQPVSQFYQ 237
Cdd:TIGR03265 155 LLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEAlSMADRIVVMNHGVIEqvgtpQEIYR--HPATPFVA 232


                  ...
gi 504427498  238 EII 240
Cdd:TIGR03265 233 DFV 235
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 4-240 9.25e-59

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: 185.90  E-value: 9.25e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfr 83
Cdd:cd03300    1 IELENVSKFYGGFV----ALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03300   71 KRPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAA-SYANRVIMLKDG---QIHT--ELFqgDQPVSQFYQ 237
Cdd:cd03300  151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEAlTMSDRIAVMNKGkiqQIGTpeEIY--EEPANRFVA 228


                 ...
gi 504427498 238 EII 240
Cdd:cd03300  229 DFI 231
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 9-221 2.26e-58

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: 184.53  E-value: 2.26e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   9 VSKIYGNkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKdVG 88
Cdd:cd03292    6 VTKTYPN---GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRK-IG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  89 FIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFAD 168
Cdd:cd03292   82 VVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIAD 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504427498 169 EPTGALDSKSAQDLLKRLETINqQMKTTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:cd03292  162 EPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKeLVDTTRHRVIALERGKL 214
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 3-240 5.43e-57

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


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 182.11  E-value: 5.43e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:TIGR02315   1 MLEVENLSKVYPNGKQ---ALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   83 RKKdVGFIFQDYNVLHTLTVRENIM---------LPLSITKLSRQEAEMRYQEVTEaLGITEIGSKYPDEISGGQKQRTA 153
Cdd:TIGR02315  78 RRR-IGMIFQHYNLIERLTVLENVLhgrlgykptWRSLLGRFSEEDKERALSALER-VGLADKAYQRADQLSGGQQQRVA 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  154 AARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGdqPV 232
Cdd:TIGR02315 156 IARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQvDLAKKYADRIVGLKAGEI---VFDG--AP 230


                  ....*...
gi 504427498  233 SQFYQEII 240
Cdd:TIGR02315 231 SELDDEVL 238
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 4-221 6.74e-57

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: 180.53  E-value: 6.74e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfr 83
Cdd:cd03301    1 VELENVTKRFGNVT----ALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPK------ 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03301   71 DRDIAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAA-SYANRVIMLKDGQI 221
Cdd:cd03301  151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAmTMADRIAVMNDGQI 209
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 3-224 7.80e-57

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: 181.78  E-value: 7.80e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyf 82
Cdd:COG1120    1 MLEAENLSVGYGGR----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELA-- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rkKDVGFIFQDYNVLHTLTVRENIML---PLsiTKLSRQEAEMRYQEVTEAL---GITEIGSKYPDEISGGQKQRTAAAR 156
Cdd:COG1120   75 --RRIAYVPQEPPAPFGLTVRELVALgryPH--LGLFGRPSAEDREAVEEALertGLEHLADRPVDELSGGERQRVLIAR 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQIHTE 224
Cdd:COG1120  151 ALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQ 219
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 4-221 8.56e-57

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: 180.42  E-value: 8.56e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmSNKQLSYFR 83
Cdd:cd03262    1 IEIKNLHKSFGDF----HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTLTVRENIML-PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:cd03262   76 QK-VGMVFQQFNLFPHLTVLENITLaPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:cd03262  155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEmGFAREVADRVIFMDDGRI 213
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 1-221 5.20e-56

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: 187.03  E-value: 5.20e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MS-ILKVSHVSKIYGNkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI---DNVTRGTIEINGQDITRMSN 76
Cdd:COG1123    1 MTpLLEVRDLSVRYPG--GDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLlphGGRISGEVLLDGRDLLELSE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 KQlsyfRKKDVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAA 155
Cdd:COG1123   79 AL----RGRRIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:COG1123  155 MALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLgVVAEIADRVVVMDDGRI 221
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 3-215 1.82e-55

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: 180.25  E-value: 1.82e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS---SIDNVTRGTIEINGQDITRMSNKQL 79
Cdd:COG0444    1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILgllPPPGITSGEILFDGEDLLKLSEKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 SYFRKKDVGFIFQD-YNVLH-TLTVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGIT---EIGSKYPDEISGGQKQRTA 153
Cdd:COG0444   81 RKIRGREIQMIFQDpMTSLNpVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVM 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 154 AARALISKPAIVFADEPTGALD-SKSAQ--DLLKRLetiNQQMKTTIVMVTHD-PVAASYANRV-IM 215
Cdd:COG0444  161 IARALALEPKLLIADEPTTALDvTIQAQilNLLKDL---QRELGLAILFITHDlGVVAEIADRVaVM 224
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 5-221 2.11e-55

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 180.77  E-value: 2.11e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRK 84
Cdd:PRK11153   3 ELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARR 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAI 164
Cdd:PRK11153  83 Q-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKV 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 165 VFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK11153 162 LLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEmDVVKRICDRVAVIDAGRL 219
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 1-235 5.27e-55

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: 176.76  E-value: 5.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqls 80
Cdd:cd03296    1 MSI-EVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVP----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQ--EAEMRyQEVTEALGITEI---GSKYPDEISGGQKQRTAAA 155
Cdd:cd03296   71 -VQERNVGFVFQHYALFRHMTVFDNVAFGLRVKPRSERppEAEIR-AKVHELLKLVQLdwlADRYPAQLSGGQRQRVALA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAA-SYANRVIMLKDGQIH-----TELFqgD 229
Cdd:cd03296  149 RALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEAlEVADRVVVMNKGRIEqvgtpDEVY--D 226


                 ....*.
gi 504427498 230 QPVSQF 235
Cdd:cd03296  227 HPASPF 232
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
4-231 1.01e-54

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 175.71  E-value: 1.01e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYealkdiHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqlSYFR 83
Cdd:COG3840    2 LRLDDLTYRYGDFPLRF------DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALP----PAER 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KkdVGFIFQDYNVLHTLTVRENIMLPLSIT-KLSRQEAEmRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:COG3840   72 P--VSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQRA-QVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQIH-----TELFQGDQP 231
Cdd:COG3840  149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEdAARIADRVLLVADGRIAadgptAALLDGEPP 223
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 4-221 4.48e-54

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: 175.14  E-value: 4.48e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYE--------------------ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGT 63
Cdd:cd03294    1 IKIKGLYKIFGKNPQKAFkllakgkskeeilkktgqtvGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  64 IEINGQDITRMSNKQLSYFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDE 143
Cdd:cd03294   81 VLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDE 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 144 ISGGQKQRTAAARALISKPAIVFADEPTGALD---SKSAQDLLKRLETinqQMKTTIVMVTHDPVAA-SYANRVIMLKDG 219
Cdd:cd03294  161 LSGGMQQRVGLARALAVDPDILLMDEAFSALDpliRREMQDELLRLQA---ELQKTIVFITHDLDEAlRLGDRIAIMKDG 237


                 ..
gi 504427498 220 QI 221
Cdd:cd03294  238 RL 239
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
2-225 6.47e-54

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 173.85  E-value: 6.47e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:PRK11629   4 ILLQCDNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:PRK11629  84 LRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTEL 225
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
2-221 2.96e-53

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 182.23  E-value: 2.96e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:PRK10535   3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:PRK10535  83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVmVTHDPVAASYANRVIMLKDGQI 221
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVII-VTHDPQVAAQAERVIEIRDGEI 221
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 2-224 4.48e-53

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 171.50  E-value: 4.48e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:PRK10584   5 NIVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:PRK10584  85 LRAKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGR 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK10584 165 PDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQLQEE 227
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 4-228 9.77e-52

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: 169.55  E-value: 9.77e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYgNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY 81
Cdd:TIGR04521   1 IKLKNVSYIY-QPGTPFEkkALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   82 FRKKdVGFIFQdY--NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITE-IGSKYPDEISGGQKQRTAAARAL 158
Cdd:TIGR04521  80 LRKK-VGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498  159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIHtelFQG 228
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGKIV---LDG 225
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 4-221 1.67e-51

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: 167.51  E-value: 1.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeaLKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfr 83
Cdd:cd03299    1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE------ 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03299   70 KRDISYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPK 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:cd03299  150 ILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEeAWALADKVAIMLNGKL 208
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1-221 2.33e-51

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 170.65  E-value: 2.33e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqls 80
Cdd:PRK10851   1 MSI-EIANIKKSFGRTQ----VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA---- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfRKKDVGFIFQDYNVLHTLTVRENIMLPLSItkLSRQE----AEMRyQEVTEALGITEIG---SKYPDEISGGQKQRTA 153
Cdd:PRK10851  72 --RDRKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRErpnaAAIK-AKVTQLLEMVQLAhlaDRYPAQLSGGQKQRVA 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 154 AARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK10851 147 LARALAVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDqEEAMEVADRVVVMSQGNI 215
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 5-222 3.12e-51

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 164.92  E-value: 3.12e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfrk 84
Cdd:cd03214    1 EVENLSVGYGGR----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELA---- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KDVGFIFQdynvlhtltvrenimlplsitklsrqeaemryqeVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAI 164
Cdd:cd03214   73 RKIAYVPQ----------------------------------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPI 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 165 VFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQIH 222
Cdd:cd03214  119 LLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIV 177
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 4-220 2.19e-50

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: 162.55  E-value: 2.19e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqLSYFR 83
Cdd:cd03228    1 IEFKNVSFSYPGRPK--PVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDyNVLHTLTVRENImlplsitklsrqeaemryqevtealgiteigskypdeISGGQKQRTAAARALISKPA 163
Cdd:cd03228   76 KN-IAYVPQD-PFLFSGTIRENI-------------------------------------LSGGQRQRIAIARALLRDPP 116

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQqmKTTIVMVTHDPVAASYANRVIMLKDGQ 220
Cdd:cd03228  117 ILILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 4-221 2.71e-50

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: 162.57  E-value: 2.71e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfr 83
Cdd:cd03230    1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEV----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLplsitklsrqeaemryqevtealgiteigskypdeiSGGQKQRTAAARALISKPA 163
Cdd:cd03230   72 KRRIGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPE 115

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:cd03230  116 LLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHIlEEAERLCDRVAILNNGRI 173
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
3-235 1.06e-49

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 166.40  E-value: 1.06e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeaLKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyf 82
Cdd:NF040840   1 MIRIENLSKDWKEFK-----LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPE----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:NF040840  71 -KRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIH-----TELFQgdQPVSQF 235
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNfEEALSLADRVGIMLNGRLSqvgdvREVFR--RPKNEF 226
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 25-221 2.28e-49

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: 161.31  E-value: 2.28e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  25 DIHFTVEkGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQDYNVLHTLTVRE 104
Cdd:cd03297   16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKINLPPQQRKIGLVFQQYALFPHLNVRE 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 105 NIMLPLSitKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLK 184
Cdd:cd03297   95 NLAFGLK--RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLP 172

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504427498 185 RLETINQQMKTTIVMVTHDPVAASY-ANRVIMLKDGQI 221
Cdd:cd03297  173 ELKQIKKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRL 210
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 4-221 5.59e-49

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: 161.31  E-value: 5.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfR 83
Cdd:cd03295    1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGI--TEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:cd03295   75 RK-IGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAAD 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 162 PAIVFADEPTGALDS---KSAQDLLKRLetiNQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:cd03295  154 PPLLLMDEPFGALDPitrDQLQEEFKRL---QQELGKTIVFVTHDiDEAFRLADRIAIMKNGEI 214
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 4-243 5.64e-48

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: 158.87  E-value: 5.64e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfR 83
Cdd:COG4555    2 IEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPRE-----A 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:COG4555   73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDP-VAASYANRVIMLKDGQIhteLFQGdqPVSQFYQEIIHN 242
Cdd:COG4555  153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMqEVEALCDRVVILHKGKV---VAQG--SLDELREEIGEE 226


                 .
gi 504427498 243 Q 243
Cdd:COG4555  227 N 227
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
4-221 1.62e-47

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 156.51  E-value: 1.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyeaLKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfR 83
Cdd:COG4619    1 LELEGLSFRVGGKPI----LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEW---R 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDyNVLHTLTVRENIMLPLSITKLSRQEAEMRyqEVTEALGITE-IGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:COG4619   74 RQ-VAYVPQE-PALWGGTVRDNLPFPFQLRERKFDRERAL--ELLERLGLPPdILDKPVERLSGGERQRLALIRALLLQP 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:COG4619  150 DVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPeQIERVADRVLTLEAGRL 209
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-222 2.56e-47

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 157.17  E-value: 2.56e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnkqls 80
Cdd:COG1121    4 MPAIELENLTVSYGGR----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRR------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfRKKDVGFIFQDYNVLHT--LTVRENIML----PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAA 154
Cdd:COG1121   73 --ARRRIGYVPQRAEVDWDfpITVRDVVLMgrygRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDP-VAASYANRVIMLKDGQIH 222
Cdd:COG1121  151 ARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLgAVREYFDRVLLLNRGLVA 218
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-203 3.05e-47

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 157.33  E-value: 3.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqls 80
Cdd:COG4525    1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPG----- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrkKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:COG4525   76 ----ADRGVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 504427498 161 KPAIVFADEPTGALDS---KSAQDLLKRLEtinQQMKTTIVMVTHD 203
Cdd:COG4525  152 DPRFLLMDEPFGALDAltrEQMQELLLDVW---QRTGKGVFLITHS 194
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 1-241 1.39e-46

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 155.17  E-value: 1.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQ--DITRMSN-K 77
Cdd:PRK11124   1 MSI-QLNGINCFYG----AHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKkDVGFIFQDYNVLHTLTVREN-IMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAAR 156
Cdd:PRK11124  76 AIRELRR-NVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIAR 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 157 ALISKPAIVFADEPTGALDSK-SAQ--DLLKRLetinQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGD--- 229
Cdd:PRK11124 155 ALMMEPQVLLFDEPTAALDPEiTAQivSIIREL----AETGITQVIVTHEvEVARKTASRVVYMENGHI---VEQGDasc 227

                        250
                 ....*....|....*
gi 504427498 230 --QP-VSQFYQEIIH 241
Cdd:PRK11124 228 ftQPqTEAFKNYLSH 242
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
 8-221 1.76e-46

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 156.79  E-value: 1.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   8 HVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfRKKdV 87
Cdd:COG1125    6 NVTKRYPDGT---VAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVEL---RRR-I 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  88 GFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGI--TEIGSKYPDEISGGQKQRTAAARALISKPAIV 165
Cdd:COG1125   79 GYVIQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPIL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 166 FADEPTGALDS---KSAQDLLKRLEtinQQMKTTIVMVTHDpV--AASYANRVIMLKDGQI 221
Cdd:COG1125  159 LMDEPFGALDPitrEQLQDELLRLQ---RELGKTIVFVTHD-IdeALKLGDRIAVMREGRI 215
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 4-243 1.80e-46

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: 164.24  E-value: 1.80e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqLSYFR 83
Cdd:COG2274  474 IELENVSFRYPG--DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDyNVLHTLTVRENIMlplsitkLSRQEAEMryQEVTEAL---GITEIGSKYPD-----------EISGGQK 149
Cdd:COG2274  549 RQ-IGVVLQD-VFLFSGTIRENIT-------LGDPDATD--EEIIEAArlaGLHDFIEALPMgydtvvgeggsNLSGGQR 617

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 150 QRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMktTIVMVTHDPVAASYANRVIMLKDGQI-----HTE 224
Cdd:COG2274  618 QRLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLKGR--TVIIIAHRLSTIRLADRIIVLDKGRIvedgtHEE 695

                        250
                 ....*....|....*....
gi 504427498 225 LFQgdqpVSQFYQEIIHNQ 243
Cdd:COG2274  696 LLA----RKGLYAELVQQQ 710
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 1-252 2.05e-46

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: 155.20  E-value: 2.05e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLS 80
Cdd:COG0411    2 DPLLEVRGLTKRFG----GLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrKKDVGFIFQDYNVLHTLTVRENIMLP-------------LSITKLSRQEAEMRyQEVTEAL---GITEIGSKYPDEI 144
Cdd:COG0411   78 ---RLGIARTFQNPRLFPELTVLENVLVAaharlgrgllaalLRLPRARREEREAR-ERAEELLervGLADRADEPAGNL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 145 SGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIht 223
Cdd:COG0411  154 SYGQQRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDmDLVMGLADRIVVLDFGRV-- 231

                        250       260       270
                 ....*....|....*....|....*....|...
gi 504427498 224 eLFQGDqpvsqfYQEIIHNQSV----LGGVKHA 252
Cdd:COG0411  232 -IAEGT------PAEVRADPRVieayLGEEAAA 257
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-230 2.12e-46

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 154.79  E-value: 2.12e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDI---TRMSNK 77
Cdd:COG4161    1 MSI-QLKNINCFYG----SHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKKdVGFIFQDYNVLHTLTVREN-IMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAAR 156
Cdd:COG4161   76 AIRLLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIAR 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 157 ALISKPAIVFADEPTGALDSK-SAQ--DLLKRLetinQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGDQ 230
Cdd:COG4161  155 ALMMEPQVLLFDEPTAALDPEiTAQvvEIIREL----SQTGITQVIVTHEvEFARKVASQVVYMEKGRI---IEQGDA 225
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 4-245 5.39e-46

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: 153.36  E-value: 5.39e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfr 83
Cdd:cd03219    1 LEVRGLTKRFGGLV----ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIML--------PLSITKLSRQEAEMRYQ--EVTEALGITEIGSKYPDEISGGQKQRTA 153
Cdd:cd03219   74 RLGIGRTFQIPRLFPELTVLENVMVaaqartgsGLLLARARREEREARERaeELLERVGLADLADRPAGELSYGQQRRLE 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 154 AARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGDqpv 232
Cdd:cd03219  154 IARALATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDmDVVMSLADRVTVLDQGRV---IAEGT--- 226

                        250
                 ....*....|...
gi 504427498 233 sqfYQEIIHNQSV 245
Cdd:cd03219  227 ---PDEVRNNPRV 236
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 4-229 1.44e-45

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: 159.92  E-value: 1.44e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfr 83
Cdd:COG4988  337 IELEDVSFSYPGGR---PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR--- 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kKDVGFIFQDyNVLHTLTVRENIMlplsitkLSRQEAEMryQEVTEAL---GITEIGSKYPD-------E----ISGGQK 149
Cdd:COG4988  411 -RQIAWVPQN-PYLFAGTIRENLR-------LGRPDASD--EELEAALeaaGLDEFVAALPDgldtplgEggrgLSGGQA 479

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 150 QRTAAARALISKPAIVFADEPTGALDSKSAQDLlkrLETINQQMKT-TIVMVTHDPVAASYANRVIMLKDGQI-----HT 223
Cdd:COG4988  480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEI---LQALRRLAKGrTVILITHRLALLAQADRILVLDDGRIveqgtHE 556


                 ....*.
gi 504427498 224 ELFQGD 229
Cdd:COG4988  557 ELLAKN 562
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 23-171 2.98e-45

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: 148.95  E-value: 2.98e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDYNVLHTLTV 102
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSL----RKEIGYVFQDPQLFPRLTV 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498  103 RENIMLPLSITKLSRQEAEMRYQEVTEALGITEIG----SKYPDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:pfam00005  77 RENLRLGLLLKGLSKREKDARAEEALEKLGLGDLAdrpvGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
8-244 4.03e-45

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 159.17  E-value: 4.03e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   8 HVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfRKKdV 87
Cdd:COG1132  344 NVSFSYPGDR---PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESL---RRQ-I 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  88 GFIFQDyNVLHTLTVRENImlplsitKLSRQEAEMryQEVTEAL---GITEIGSKYPD-----------EISGGQKQRTA 153
Cdd:COG1132  417 GVVPQD-TFLFSGTIRENI-------RYGRPDATD--EEVEEAAkaaQAHEFIEALPDgydtvvgergvNLSGGQRQRIA 486

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 154 AARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVmVTHDPVAASYANRVIMLKDGQI-----HTELFQG 228
Cdd:COG1132  487 IARALLKDPPILILDEATSALDTETEALIQEALERLMKG-RTTIV-IAHRLSTIRNADRILVLDDGRIveqgtHEELLAR 564

                        250
                 ....*....|....*.
gi 504427498 229 DqpvsQFYQEIIHNQS 244
Cdd:COG1132  565 G----GLYARLYRLQF 576
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 23-219 5.33e-45

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: 150.69  E-value: 5.33e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrkkdvgFIFQDYNVLHTLTV 102
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---------VVFQNYSLLPWLTV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  103 RENIMLPLS--ITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQ 180
Cdd:TIGR01184  72 RENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRG 151

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 504427498  181 DLLKRLETINQQMKTTIVMVTHDPVAASY-ANRVIMLKDG 219
Cdd:TIGR01184 152 NLQEELMQIWEEHRVTVLMVTHDVDEALLlSDRVVMLTNG 191
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-221 7.74e-45

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 154.33  E-value: 7.74e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQls 80
Cdd:PRK09452  12 SPLVELRGISKSFDGK----EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAEN-- 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrkKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRyqeVTEALGIT---EIGSKYPDEISGGQKQRTAAARA 157
Cdd:PRK09452  86 ----RHVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPR---VMEALRMVqleEFAQRKPHQLSGGQQQRVAIARA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 158 LISKPAIVFADEPTGALD---SKSAQDLLKRLEtinQQMKTTIVMVTHDPVAA-SYANRVIMLKDGQI 221
Cdd:PRK09452 159 VVNKPKVLLLDESLSALDyklRKQMQNELKALQ---RKLGITFVFVTHDQEEAlTMSDRIVVMRDGRI 223
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 5-220 1.03e-44

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: 147.78  E-value: 1.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrK 84
Cdd:cd00267    1 EIENLSFRYGGRT----ALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEEL----R 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KDVGFIFQdynvlhtltvrenimlplsitklsrqeaemryqevtealgiteigskypdeISGGQKQRTAAARALISKPAI 164
Cdd:cd00267   73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 165 VFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDP-VAASYANRVIMLKDGQ 220
Cdd:cd00267  102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPeLAELAADRVIVLKDGK 157
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
3-222 1.66e-44

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 149.25  E-value: 1.66e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYF 82
Cdd:PRK10908   1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:PRK10908  78 RRQ-IGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINqQMKTTIVMVTHDPVAASYAN-RVIMLKDGQIH 222
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFN-RVGVTVLMATHDIGLISRRSyRMLTLSDGHLH 216
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 4-237 4.31e-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: 156.08  E-value: 4.31e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfR 83
Cdd:COG4987  334 LELEDVSFRYPGAGR--PVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDL---R 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTlTVRENImlplsitKLSRQEA---EMRyqEVTEALGITEIGSKYPD-------E----ISGGQK 149
Cdd:COG4987  409 RR-IAVVPQRPHLFDT-TLRENL-------RLARPDAtdeELW--AALERVGLGDWLAALPDgldtwlgEggrrLSGGER 477

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 150 QRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMktTIVMVTHDPVAASYANRVIMLKDGQI-----HTE 224
Cdd:COG4987  478 RRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVLEDGRIveqgtHEE 555

                        250
                 ....*....|...
gi 504427498 225 LFQGDQPVSQFYQ 237
Cdd:COG4987  556 LLAQNGRYRQLYQ 568
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 4-221 1.70e-43

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: 146.94  E-value: 1.70e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS-SIDNV----TRGTIEINGQDITRMSNKQ 78
Cdd:cd03260    1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDLIpgapDEGEVLLDGKDIYDLDVDV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LSYFRKkdVGFIFQDYNVLHtLTVRENIMLPLSITKLSRQEAEMRyqEVTEALGITEIGSK-----YPDEISGGQKQRTA 153
Cdd:cd03260   77 LELRRR--VGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDE--RVEEALRKAALWDEvkdrlHALGLSGGQQQRLC 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 154 AARALISKPAIVFADEPTGALDSKSAQ---DLLKRLetinqQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:cd03260  152 LARALANEPEVLLLDEPTSALDPISTAkieELIAEL-----KKEYTIVIVTHNMQqAARVADRTAFLLNGRL 218
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 5-217 5.64e-43

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: 144.98  E-value: 5.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfrk 84
Cdd:cd03235    1 EVEDLTVSYGGH----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 kdVGFIFQDYNVLHT--LTVRENIMLPL-----SITKLSRQEaemrYQEVTEAL---GITEIGSKYPDEISGGQKQRTAA 154
Cdd:cd03235   70 --IGYVPQRRSIDRDfpISVRDVVLMGLyghkgLFRRLSKAD----KAKVDEALervGLSELADRQIGELSGGQQQRVLL 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHDPVAAS-YANRVIMLK 217
Cdd:cd03235  144 ARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGM-TILVVTHDLGLVLeYFDRVLLLN 206
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 25-221 8.69e-43

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: 148.71  E-value: 8.69e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  25 DIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEING---QDITRmsnkqlSYFR---KKDVGFIFQDYNVLH 98
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGevlQDSAR------GIFLpphRRRIGYVFQEARLFP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  99 TLTVRENIMLPLSITKlsRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:COG4148   91 HLSVRGNLLYGRKRAP--RAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504427498 179 AQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:COG4148  169 KAEILPYLERLRDELDIPILYVSHSLDeVARLADHVVLLEQGRV 212
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 15-221 9.83e-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: 144.56  E-value: 9.83e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  15 NKKQSYEALKDIHF--TVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfrkKDVGFIFQ 92
Cdd:cd03298    4 DKIRFSYGEQPMHFdlTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  93 DYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTG 172
Cdd:cd03298   78 ENNLFAHLTVEQNVGLGLSPGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFA 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504427498 173 ALDSKSAQDLLKRLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:cd03298  158 ALDPALRAEMLDLVLDLHAETKMTVLMVTHQPEdAKRLAQRVVFLDNGRI 207
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 4-224 1.29e-42

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: 145.65  E-value: 1.29e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGNkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDitRMSNKQLSYFR 83
Cdd:TIGR04520   1 IEVENVSFSYPE--SEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 KKdVGFIFQ--DyNVLHTLTVR-------ENIMLPlsitklsRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAA 154
Cdd:TIGR04520  77 KK-VGMVFQnpD-NQFVGATVEddvafglENLGVP-------REEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAI 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:TIGR04520 148 AGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAE 217
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
9-221 3.46e-42

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 143.69  E-value: 3.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   9 VSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItRMSNKQLSYFRKkDVG 88
Cdd:PRK09493   7 VSKHFG----PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKV-NDPKVDERLIRQ-EAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  89 FIFQDYNVLHTLTVRENIML-PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFA 167
Cdd:PRK09493  81 MVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLF 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 168 DEPTGALDSKSAQDLLKRLETINQQ-MktTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK09493 161 DEPTSALDPELRHEVLKVMQDLAEEgM--TMVIVTHEiGFAEKVASRLIFIDKGRI 214
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 3-221 1.70e-41

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 142.53  E-value: 1.70e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIY----GNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkq 78
Cdd:COG1101    1 MLELKNLSKTFnpgtVNEKR---ALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLP--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 lSYFRKKDVGFIFQDyNVLHT---LTVRENIML--------PLSITkLSRQEAEmRYQEVTEALGI-------TEIGSky 140
Cdd:COG1101   75 -EYKRAKYIGRVFQD-PMMGTapsMTIEENLALayrrgkrrGLRRG-LTKKRRE-LFRELLATLGLglenrldTKVGL-- 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 141 pdeISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTH---DpvAASYANRVIMLK 217
Cdd:COG1101  149 ---LSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHnmeQ--ALDYGNRLIMMH 223


                 ....
gi 504427498 218 DGQI 221
Cdd:COG1101  224 EGRI 227
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
27-233 2.71e-41

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 141.26  E-value: 2.71e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  27 HFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfrkKDVGFIFQDYNVLHTLTVRENI 106
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSR------RPVSMLFQENNLFSHLTVAQNI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 107 MLPLSIT-KLSRQEAEMRyQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKR 185
Cdd:PRK10771  93 GLGLNPGlKLNAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 186 LETINQQMKTTIVMVTH---DpvAASYANRVIMLKDGQIH-----TELFQGDQPVS 233
Cdd:PRK10771 172 VSQVCQERQLTLLMVSHsleD--AARIAPRSLVVADGRIAwdgptDELLSGKASAS 225
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 38-249 3.24e-41

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine/putrescine ABC transporter, ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. Polyamines like spermidine and putrescine play vital role in cell proliferation, differentiation, and ion homeostasis. The concentration of polyamines within the cell are regulated by biosynthesis, degradation and transport (uptake and efflux included). [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 143.79  E-value: 3.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   38 IMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfrKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSR 117
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPH------LRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  118 QEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTI 197
Cdd:TIGR01187  75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITF 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498  198 VMVTHDPVAA-SYANRVIMLKDG---QIHT--ELFQgdQPVSQFYQEIIHNQSVLGGV 249
Cdd:TIGR01187 155 VFVTHDQEEAmTMSDRIAIMRKGkiaQIGTpeEIYE--EPANLFVARFIGEINVFEAT 210
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 1-221 8.46e-41

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 140.66  E-value: 8.46e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKiygnKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDI--TRMSNKQ 78
Cdd:PRK11264   1 MSAIEVKNLVK----KFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIdtARSLSQQ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LSYFR--KKDVGFIFQDYNVLHTLTVRENIML-PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAA 155
Cdd:PRK11264  77 KGLIRqlRQHVGFVFQNFNLFPHRTVLENIIEgPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK11264 157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEmSFARDVADRAIFMDQGRI 222
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 8-222 1.83e-40

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 138.16  E-value: 1.83e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   8 HVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmSNKQlsyfRKKDV 87
Cdd:cd03226    1 RIENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKE----RRKSI 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  88 GFIFQD-YNVLHTLTVRENIMLPLSITKLSRQEAEmryqEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVF 166
Cdd:cd03226   74 GYVMQDvDYQLFTDSVREELLLGLKELDAGNEQAE----TVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLI 149

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 167 ADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTHDP-VAASYANRVIMLKDGQIH 222
Cdd:cd03226  150 FDEPTSGLDYKNMERVGELIREL-AAQGKAVIVITHDYeFLAKVCDRVLLLANGAIV 205
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 29-221 2.60e-40

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ATPase subunit ThiQ of the ThiBPQ thiamine (and thiamine pyrophosphate) ABC transporter in several Proteobacteria. This protein is found so far only in Proteobacteria, and is found in complete genomes only if the ThiB and ThiP subunits are also found. [Transport and binding proteins, Other]


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 138.07  E-value: 2.60e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   29 TVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfrkKDVGFIFQDYNVLHTLTVRENIML 108
Cdd:TIGR01277  20 NVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQ------RPVSMLFQENNLFAHLTVRQNIGL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  109 PLSIT-KLSRQEAEmRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLE 187
Cdd:TIGR01277  94 GLHPGlKLNAEQQE-KVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVK 172

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 504427498  188 TINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:TIGR01277 173 QLCSERQRTLLMVTHHLSdARAIASQIAVVSQGKI 207
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 1-221 5.06e-40

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: 144.44  E-value: 5.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKT----TLLNVISSIDNVTRGTIEINGQDITRMSN 76
Cdd:COG4172    4 MPLLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 KQLSYFRKKDVGFIFQD----YNVLHTltVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGITEIGSK---YPDEISGGQ 148
Cdd:COG4172   84 RELRRIRGNRIAMIFQEpmtsLNPLHT--IGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPERRldaYPHQLSGGQ 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 149 KQRTAAARALISKPAIVFADEPTGALD-SKSAQ--DLLKRLetiNQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG4172  162 RQRVMIAMALANEPDLLIADEPTTALDvTVQAQilDLLKDL---QRELGMALLLITHDlGVVRRFADRVAVMRQGEI 235
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-235 9.92e-40

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 140.36  E-value: 9.92e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQls 80
Cdd:PRK11650   1 MAGLKLQAVRKSYDGKTQ---VIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrkKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRyqeVTEALGITEIGS---KYPDEISGGQKQRTAAARA 157
Cdd:PRK11650  76 ----RDIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEER---VAEAARILELEPlldRKPRELSGGQRQRVAMGRA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 158 LISKPAIVFADEPTGALDSKsaqdlLK---RLE--TINQQMKTTIVMVTHDPVAA-SYANRVIMLKDG---QIHT--ELF 226
Cdd:PRK11650 149 IVREPAVFLFDEPLSNLDAK-----LRvqmRLEiqRLHRRLKTTSLYVTHDQVEAmTLADRVVVMNGGvaeQIGTpvEVY 223


                 ....*....
gi 504427498 227 qgDQPVSQF 235
Cdd:PRK11650 224 --EKPASTF 230
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-221 3.86e-39

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 136.74  E-value: 3.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGN-----KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS 75
Cdd:PRK10419   1 MTLLNVSGLSHHYAHgglsgKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 NKQLSYFRkKDVGFIFQD----YNVLHtlTVRENIMLPLS-ITKLSRQEAEMRYQEVTEALGIT-EIGSKYPDEISGGQK 149
Cdd:PRK10419  81 RAQRKAFR-RDIQMVFQDsisaVNPRK--TVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQL 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 150 QRTAAARALISKPAIVFADEPTGALD---SKSAQDLLKRLEtinQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK10419 158 QRVCLARALAVEPKLLILDEAVSNLDlvlQAGVIRLLKKLQ---QQFGTACLFITHDlRLVERFCQRVMVMDNGQI 230
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 3-203 8.14e-39

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 137.56  E-value: 8.14e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIY-------GNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS 75
Cdd:COG4608    7 LLEVRDLKKHFpvrgglfGRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 NKQLSYFRKKdVGFIFQD-YNVLHT-LTVRENIMLPLSI-TKLSRQEAEMRYQEVTEALGI-TEIGSKYPDEISGGQKQR 151
Cdd:COG4608   87 GRELRPLRRR-MQMVFQDpYASLNPrMTVGDIIAEPLRIhGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQR 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 152 TAAARALISKPAIVFADEPTGALD-SKSAQ--DLLKRLEtinQQMKTTIVMVTHD 203
Cdd:COG4608  166 IGIARALALNPKLIVCDEPVSALDvSIQAQvlNLLEDLQ---DELGLTYLFISHD 217
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 22-221 2.01e-38

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: 140.20  E-value: 2.01e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTL----LNVISSidnvtRGTIEINGQDITRMSNKQLSYFRKkDVGFIFQD-YNV 96
Cdd:COG4172  301 AVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIPS-----EGEIRFDGQDLDGLSRRALRPLRR-RMQVVFQDpFGS 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  97 LHT-LTVRENIMLPLSI--TKLSRQEaemRYQEVTEALgiTEIG------SKYPDEISGGQKQRTAAARALISKPAIVFA 167
Cdd:COG4172  375 LSPrMTVGQIIAEGLRVhgPGLSAAE---RRARVAEAL--EEVGldpaarHRYPHEFSGGQRQRIAIARALILEPKLLVL 449

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 168 DEPTGALD-SKSAQ--DLLKRLetiNQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG4172  450 DEPTSALDvSVQAQilDLLRDL---QREHGLAYLFISHDlAVVRALAHRVMVMKDGKV 504
cbiO PRK13637
energy-coupling factor transporter ATPase;
1-221 2.49e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 135.18  E-value: 2.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYgNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKq 78
Cdd:PRK13637   1 MSI-KIENLTHIY-MEGTPFEkkALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LSYFRKKdVGFIFQ--DYNvLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGIT--EIGSKYPDEISGGQKQRTAA 154
Cdd:PRK13637  78 LSDIRKK-VGLVFQypEYQ-LFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTH--DPVaASYANRVIMLKDGQI 221
Cdd:PRK13637 156 AGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHsmEDV-AKLADRIIVMNKGKC 223
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
4-235 2.90e-38

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 136.77  E-value: 2.90e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfr 83
Cdd:PRK11432   7 VVLKNITKRFGSNT----VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQ----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEaemRYQEVTEALGITEI---GSKYPDEISGGQKQRTAAARALIS 160
Cdd:PRK11432  78 -RDICMVFQSYALFPHMSLGENVGYGLKMLGVPKEE---RKQRVKEALELVDLagfEDRYVDQISGGQQQRVALARALIL 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 161 KPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAA-SYANRVIMLKDGQIH-----TELFQgdQPVSQ 234
Cdd:PRK11432 154 KPKVLLFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAfAVSDTVIVMNKGKIMqigspQELYR--QPASR 231


                 .
gi 504427498 235 F 235
Cdd:PRK11432 232 F 232
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 4-221 2.91e-38

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


Pssm-ID: 213191 [Multi-domain]  Cd Length: 222  Bit Score: 132.94  E-value: 2.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfr 83
Cdd:cd03224    1 LEVENLNAGYG----KSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERA--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSItkLSRQEAEMRYQEVTE---ALGitEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:cd03224   74 RAGIGYVPEGRRIFPELTVEENLLLGAYA--RRRAKRKARLERVYElfpRLK--ERRKQLAGTLSGGEQQMLAIARALMS 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 161 KPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:cd03224  150 RPKLLLLDEPSEGLAPKIVEEIFEAIRELRDE-GVTILLVEQNaRFALEIADRAYVLERGRV 210
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
4-221 3.21e-38

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 134.16  E-value: 3.21e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItRM--------- 74
Cdd:COG4598    9 LEVRDLHKSFG----DLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEI-RLkpdrdgelv 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  75 --SNKQLSYFRKKdVGFIFQDYNVLHTLTVRENIML-PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQR 151
Cdd:COG4598   84 paDRRQLQRIRTR-LGMVFQSFNLWSHMTVLENVIEaPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQR 162

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 152 TAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVmVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG4598  163 AAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLV-VTHEmGFARDVSSHVVFLHQGRI 232
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
4-224 4.12e-38

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 133.94  E-value: 4.12e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDIT--RMSNKQLSY 81
Cdd:PRK10619   6 LNVIDLHKRYG----EHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvRDKDGQLKV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKKDV-------GFIFQDYNVLHTLTVRENIM-LPLSITKLSRQEAEMRYQEVTEALGITEIG-SKYPDEISGGQKQRT 152
Cdd:PRK10619  82 ADKNQLrllrtrlTMVFQHFNLWSHMTVLENVMeAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 153 AAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVmVTHD-PVAASYANRVIMLKDGQIHTE 224
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEmGFARHVSSHVIFLHQGKIEEE 233
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 7-225 4.15e-38

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: 133.12  E-value: 4.15e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   7 SHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmSNKQLSYFRKKd 86
Cdd:cd03253    4 ENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI---REVTLDSLRRA- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  87 VGFIFQDyNVLHTLTVRENImlplSITKLSRQEAEMRyqEVTEALGITEIGSKYPD-----------EISGGQKQRTAAA 155
Cdd:cd03253   77 IGVVPQD-TVLFNDTIGYNI----RYGRPDATDEEVI--EAAKAAQIHDKIMRFPDgydtivgerglKLSGGEKQRVAIA 149

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVmVTHDPVAASYANRVIMLKDGQI-----HTEL 225
Cdd:cd03253  150 RAILKNPPILLLDEATSALDTHTEREIQAALRDVSKG-RTTIV-IAHRLSTIVNADKIIVLKDGRIvergtHEEL 222
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 25-221 7.20e-38

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: 135.62  E-value: 7.20e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   25 DIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQDYNVLHTLTVRE 104
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPEKRRIGYVFQEARLFPHLSVRG 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  105 NimLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLK 184
Cdd:TIGR02142  95 N--LRYGMKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILP 172

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 504427498  185 RLETINQQMKTTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:TIGR02142 173 YLERLHAEFGIPILYVSHSLQeVLRLADRVVVLEDGRV 210
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 1-221 9.37e-38

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 134.06  E-value: 9.37e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYgNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNK- 77
Cdd:PRK13651   1 MQI-KVKNIVKIF-NKKLPTElkALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTk 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 -----------QLSYFRK--------KDVGFIFQ--DYNvLHTLTVRENIML-PLSItKLSRQEAEMRYQEVTEALGITE 135
Cdd:PRK13651  79 ekekvleklviQKTRFKKikkikeirRRVGVVFQfaEYQ-LFEQTIEKDIIFgPVSM-GVSKEEAKKRAAKYIELVGLDE 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 136 -IGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHD-PVAASYANRV 213
Cdd:PRK13651 157 sYLQRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDlDNVLEWTKRT 235


                 ....*...
gi 504427498 214 IMLKDGQI 221
Cdd:PRK13651 236 IFFKDGKI 243
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 4-221 2.08e-37

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: 130.70  E-value: 2.08e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYfr 83
Cdd:cd03263    1 LQIRNLTKTYKKGTKP--AVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQS-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kkdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03263   77 ---LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 164 IVFADEPTGALDSKSaqdllKRL--ETINQQMK-TTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:cd03263  154 VLLLDEPTSGLDPAS-----RRAiwDLILEVRKgRSIILTTHSMdEAEALCDRIAIMSDGKL 210
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 5-227 2.28e-37

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: 131.19  E-value: 2.28e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfRK 84
Cdd:cd03254    4 EFENVNFSYDEKKP---VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSL---RS 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KdVGFIFQDyNVLHTLTVRENImlplsitKLSRQEAEM-RYQEVTEALGITEIGSKYPD-----------EISGGQKQRT 152
Cdd:cd03254   78 M-IGVVLQD-TFLFSGTIMENI-------RLGRPNATDeEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLL 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 153 AAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIvMVTHDPVAASYANRVIMLKDGQI-----HTELFQ 227
Cdd:cd03254  149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKG-RTSI-IIAHRLSTIKNADKILVLDDGKIieegtHDELLA 226
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 6-224 5.49e-37

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: 129.80  E-value: 5.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfrKK 85
Cdd:cd03265    3 VENLVKKYG----DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREV-----RR 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  86 DVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIV 165
Cdd:cd03265   74 RIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 166 FADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIHTE 224
Cdd:cd03265  154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYmEEAEQLCDRVAIIDHGRIIAE 213
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 4-216 7.75e-37

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 129.14  E-value: 7.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS---SIDNVTRGTIEINGQDITRMSNKQls 80
Cdd:COG4136    2 LSLENLTITLGGR----PLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAgtlSPAFSASGEVLLNGRRLTALPAEQ-- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfRKkdVGFIFQDynVL---HtLTVRENIM--LPLSITKLSRQEaemRYQEVTEALGITEIGSKYPDEISGGQKQRTAAA 155
Cdd:COG4136   76 --RR--IGILFQD--DLlfpH-LSVGENLAfaLPPTIGRAQRRA---RVEQALEEAGLAGFADRDPATLSGGQRARVALL 145

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 156 RALISKPAIVFADEPTGALDsksaQDLlkRLEtINQQMKTTI-------VMVTHDPVAASYANRVIML 216
Cdd:COG4136  146 RALLAEPRALLLDEPFSKLD----AAL--RAQ-FREFVFEQIrqrgipaLLVTHDEEDAPAAGRVLDL 206
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
15-249 9.90e-37

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 133.04  E-value: 9.90e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  15 NKKQSYE---ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfrkKDVGFIF 91
Cdd:PRK11607  24 NLTKSFDgqhAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  92 QDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:PRK11607  98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 172 GALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDG---QIHT--ELFQgdQPVSQFYQEIIHNQSV 245
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDqEEAMTMAGRIAIMNRGkfvQIGEpeEIYE--HPTTRYSAEFIGSVNV 255


                 ....
gi 504427498 246 LGGV 249
Cdd:PRK11607 256 FEGV 259
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 9-221 1.25e-36

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 128.86  E-value: 1.25e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   9 VSKIYGNKKQsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVG 88
Cdd:cd03245    8 VSFSYPNQEI--PALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADL----RRNIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  89 FIFQDyNVLHTLTVRENIMLplsitklSRQEAE-MRYQEVTEALGITEIGSKYPD-----------EISGGQKQRTAAAR 156
Cdd:cd03245   82 YVPQD-VTLFYGTLRDNITL-------GAPLADdERILRAAELAGVTDFVNKHPNgldlqigergrGLSGGQRQAVALAR 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLKRLetinQQMK--TTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03245  154 ALLNDPPILLLDEPTSAMDMNSEERLKERL----RQLLgdKTLIIITHRPSLLDLVDRIIVMDSGRI 216
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 2-228 2.10e-36

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: 127.28  E-value: 2.10e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISS--IDNVTRGTIEINGQDITRMSnkql 79
Cdd:cd03213    7 RNLTVTVKSSPSKSGKQ---LLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGrrTGLGVSGEVLINGRPLDKRS---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 syFRKKdVGFIFQDYNVLHTLTVRENIMLplsitklsrqEAEMRyqevtealgiteigskypdEISGGQKQRTAAARALI 159
Cdd:cd03213   80 --FRKI-IGYVPQDDILHPTLTVRETLMF----------AAKLR-------------------GLSGGERKRVSIALELV 127

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHDPVAASYA--NRVIMLKDGQIhteLFQG 228
Cdd:cd03213  128 SNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGR-TIICSIHQPSSEIFElfDKLLLLSQGRV---IYFG 194
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-224 2.50e-36

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 129.75  E-value: 2.50e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYgnKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsy 81
Cdd:PRK13635   4 EIIRVEHISFRY--PDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDV-- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 fRKKdVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:PRK13635  80 -RRQ-VGMVFQNPdNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLAL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 161 KPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK13635 158 QPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGEILEE 221
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 4-245 3.62e-36

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: 128.04  E-value: 3.62e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfr 83
Cdd:cd03218    1 LRAENLSKRYGKRK----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRA--- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03218   74 RLGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 164 IVFADEPTGALDSKSAQDLLKrleTINQQMKTTI-VMVTHDPV--AASYANRVIMLKDGQIhteLFQGDQpvsqfyQEII 240
Cdd:cd03218  154 FLLLDEPFAGVDPIAVQDIQK---IIKILKDRGIgVLITDHNVreTLSITDRAYIIYEGKV---LAEGTP------EEIA 221


                 ....*
gi 504427498 241 HNQSV 245
Cdd:cd03218  222 ANELV 226
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 5-221 4.37e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 128.96  E-value: 4.37e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   5 KVSHVSKIYGNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnKQLSYFRK 84
Cdd:PRK13632   9 KVENVSFSYPNSENN--ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISK---ENLKEIRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  85 KdVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:PRK13632  84 K-IGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPE 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:PRK13632 163 IIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKL 220
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 4-218 5.31e-36

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: 126.82  E-value: 5.31e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnKQLSYFR 83
Cdd:COG4133    3 LEAENLSCRRGERL----LFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD---AREDYRR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kkDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRqeAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:COG4133   76 --RLAYLGHADGLKPELTVRENLRFWAALYGLRA--DREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDPVAASyANRVIMLKD 218
Cdd:COG4133  152 LWLLDEPFTALDAAGVALLAELIAAHLAR-GGAVLLTTHQPLELA-AARVLDLGD 204
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 1-221 5.38e-36

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: 127.79  E-value: 5.38e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLS 80
Cdd:COG0410    1 MPMLEVENLHAGYGG----IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrKKDVGFIFQDYNVLHTLTVRENIMLPLSITKlSRQEAEMRYQEVTE----------ALGITeigskypdeISGGQKQ 150
Cdd:COG0410   77 ---RLGIGYVPEGRRIFPSLTVEENLLLGAYARR-DRAEVRADLERVYElfprlkerrrQRAGT---------LSGGEQQ 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 151 RTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG0410  144 MLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNaRFALEIADRAYVLERGRI 214
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-221 6.81e-36

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 127.87  E-value: 6.81e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIeingqditRMSNKQLSYFR 83
Cdd:PRK11247  13 LLLNAVSKRYGER----TVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL--------LAGTAPLAEAR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KkDVGFIFQDYNVLHTLTVRENIMLPLSITklSRQEAEmryqEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:PRK11247  81 E-DTRLMFQDARLLPWKKVIDNVGLGLKGQ--WRDAAL----QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPG 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 164 IVFADEPTGALDSKS---AQDLLKRLEtinQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK11247 154 LLLLDEPLGALDALTrieMQDLIESLW---QQHGFTVLLVTHDvSEAVAMADRVLLIEEGKI 212
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 4-228 8.07e-36

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: 126.54  E-value: 8.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFvAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyFR 83
Cdd:cd03264    1 LQLENLTKRYGKKR----ALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTLTVRE--NIMLPLSitKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:cd03264   72 RR-IGYLPQEFGVYPNFTVREflDYIAWLK--GIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGD 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 162 PAIVFADEPTGALDSKSA---QDLLKRLEtinqqmKTTIVMV-TH--DPVAASyANRVIMLKDGQIHtelFQG 228
Cdd:cd03264  149 PSILIVDEPTAGLDPEERirfRNLLSELG------EDRIVILsTHivEDVESL-CNQVAVLNKGKLV---FEG 211
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 20-221 9.94e-36

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 128.27  E-value: 9.94e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  20 YEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItRMSNKQLSYFRKKdVGFIFQDY-NVLH 98
Cdd:PRK13639  15 TEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEVRKT-VGIVFQNPdDQLF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  99 TLTVRENIML-PLSItKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSK 177
Cdd:PRK13639  93 APTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504427498 178 SAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHDvDLVPVYADKVYVMSDGKI 215
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 1-221 1.55e-35

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: 126.74  E-value: 1.55e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSiDN--VTRGTIEINGQDITRMSNKQ 78
Cdd:COG1119    1 DPLLELRNVTVRRGGKT----ILDDISWTVKPGEHWAILGPNGAGKSTLLSLITG-DLppTYGNDVRLFGERRGGEDVWE 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LsyfrKKDVGF----IFQDYNVlhTLTVRE--------NIMLPLSITKLSRQEAEmryqEVTEALGITEIGSKYPDEISG 146
Cdd:COG1119   76 L----RKRIGLvspaLQLRFPR--DETVLDvvlsgffdSIGLYREPTDEQRERAR----ELLELLGLAHLADRPFGTLSQ 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 147 GQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTH--DPVAASYaNRVIMLKDGQI 221
Cdd:COG1119  146 GEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHhvEEIPPGI-THVLLLKDGRV 221
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 4-221 1.61e-35

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: 124.64  E-value: 1.61e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqLSYFR 83
Cdd:cd03246    1 LEVENVSFRYPGAEP--PVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNvLHTLTVRENIMlplsitklsrqeaemryqevtealgiteigskypdeiSGGQKQRTAAARALISKPA 163
Cdd:cd03246   76 DH-VGYLPQDDE-LFSGSIAENIL-------------------------------------SGGQRQRLGLARALYGNPR 116

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLetinQQMK---TTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03246  117 ILVLDEPNSHLDVEGERALNQAI----AALKaagATRIVIAHRPETLASADRILVLEDGRV 173
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-221 2.23e-35

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 129.38  E-value: 2.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSyealKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditRMSNKQLS 80
Cdd:PRK11000   1 MASVTLRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---RMNDVPPA 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALIS 160
Cdd:PRK11000  74 ---ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 161 KPAIVFADEPTGALDskSAQDLLKRLET--INQQMKTTIVMVTHDPVAA-SYANRVIMLKDGQI 221
Cdd:PRK11000 151 EPSVFLLDEPLSNLD--AALRVQMRIEIsrLHKRLGRTMIYVTHDQVEAmTLADKIVVLDAGRV 212
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 1-221 1.15e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 125.52  E-value: 1.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIYgNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDIT-RMSNK 77
Cdd:PRK13634   1 MDI-TFQKVEHRY-QYKTPFErrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITaGKKNK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKKdVGFIFQ-DYNVLHTLTVRENIML-PLSItKLSRQEAEMRYQEVTEALGITE-IGSKYPDEISGGQKQRTAA 154
Cdd:PRK13634  79 KLKPLRKK-VGIVFQfPEHQLFEETVEKDICFgPMNF-GVSEEDAKQKAREMIELVGLPEeLLARSPFELSGGQMRRVAI 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTH---DpvAASYANRVIMLKDGQI 221
Cdd:PRK13634 157 AGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHsmeD--AARYADQIVVMHKGTV 224
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
2-221 1.31e-34

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 124.74  E-value: 1.31e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYgnkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI---DNVTRGTIEINGQDITRmSNKQ 78
Cdd:PRK09984   3 TIIRVEKLAKTF----NQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQR-EGRL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LSYFRKK--DVGFIFQDYNVLHTLTVRENIML------PLSITKL---SRQEAEMRYQEVTEaLGITEIGSKYPDEISGG 147
Cdd:PRK09984  78 ARDIRKSraNTGYIFQQFNLVNRLSVLENVLIgalgstPFWRTCFswfTREQKQRALQALTR-VGMVHFAHQRVSTLSGG 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 148 QKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK09984 157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQvDYALRYCERIVALRQGHV 231
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 1-186 1.13e-33

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 121.67  E-value: 1.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRM-----S 75
Cdd:COG1137    1 MMTLEAENLVKSYGKRT----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLpmhkrA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 NKQLSY-------FRKkdvgfifqdynvlhtLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQ 148
Cdd:COG1137   77 RLGIGYlpqeasiFRK---------------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGE 141

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 149 KQRTAAARALISKPAIVFADEPTGALDSKSA---QDLLKRL 186
Cdd:COG1137  142 RRRVEIARALATNPKFILLDEPFAGVDPIAVadiQKIIRHL 182
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1-221 1.99e-33

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 121.87  E-value: 1.99e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGN-----KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS 75
Cdd:COG4167    2 SALLEVRNLSKTFKYrtglfRRQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEYGD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 NKQlsyfRKKDVGFIFQDYNvlHTLTVRENI--ML--PLSI-TKLSRQEaemRYQEVTEALG----ITEIGSKYPDEISG 146
Cdd:COG4167   82 YKY----RCKHIRMIFQDPN--TSLNPRLNIgqILeePLRLnTDLTAEE---REERIFATLRlvglLPEHANFYPHMLSS 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 147 GQKQRTAAARALISKPAIVFADEPTGALD-SKSAQdLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:COG4167  153 GQKQRVALARALILQPKIIIADEALAALDmSVRSQ-IINLMLELQEKLGISYIYVSQHLgIVKHISDKVLVMHQGEV 228
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 3-224 2.47e-33

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: 120.17  E-value: 2.47e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsNKQLSyf 82
Cdd:cd03266    1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK--EPAEA-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:cd03266   77 -RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 163 AIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHD-PVAASYANRVIMLKDGQIHTE 224
Cdd:cd03266  156 PVLLLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHImQEVERLCDRVVVLHRGRVVYE 217
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
3-203 2.94e-33

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 120.96  E-value: 2.94e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyf 82
Cdd:PRK11248   1 MLQISHLYADYGGKP----ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rkkdvGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:PRK11248  73 -----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANP 147

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 504427498 163 AIVFADEPTGALDS---KSAQDLLKRL--ETINQqmkttIVMVTHD 203
Cdd:PRK11248 148 QLLLLDEPFGALDAftrEQMQTLLLKLwqETGKQ-----VLLITHD 188
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 15-204 4.81e-33

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: 119.68  E-value: 4.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  15 NKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS---SIDNVTRGTIEINGQDITRmsnkqlsYFRKKDVGFIF 91
Cdd:cd03234   15 NWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKP-------DQFQKCVAYVR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  92 QDYNVLHTLTVRENI----MLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFA 167
Cdd:cd03234   88 QDDILLPGLTVRETLtytaILRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLIL 167

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504427498 168 DEPTGALDSKSAQDLLKRLETINQQMKTTIVMVtHDP 204
Cdd:cd03234  168 DEPTSGLDSFTALNLVSTLSQLARRNRIVILTI-HQP 203
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 23-222 5.18e-33

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 125.54  E-value: 5.18e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfrkKDVGFIFQDYNvLHTLTV 102
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFG----KHIGYLPQDVE-LFPGTV 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  103 RENImlplsitklSRQEAEMRYQEVTEAL---GITEIGSKYPD-----------EISGGQKQRTAAARALISKPAIVFAD 168
Cdd:TIGR01842 409 AENI---------ARFGENADPEKIIEAAklaGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLD 479

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504427498  169 EPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDPVAASYANRVIMLKDGQIH 222
Cdd:TIGR01842 480 EPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLGCVDKILVLQDGRIA 532
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 21-229 9.73e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 120.23  E-value: 9.73e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfRKKdVGFIFQDYN-VLHT 99
Cdd:PRK13647  19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSK-VGLVFQDPDdQVFS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 100 LTVRENIML-PLSItKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:PRK13647  95 STVWDDVAFgPVNM-GLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504427498 179 AQDLLKRLETINQQMKTtIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGD 229
Cdd:PRK13647 174 QETLMEILDRLHNQGKT-VIVATHDvDLAAEWADQVIVLKEGRV---LAEGD 221
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 15-243 1.03e-32

The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 125.16  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   15 NKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSID--NVTR-GTIEINGQDITRMSNKQLSyfrkkdvGFIF 91
Cdd:TIGR00955  33 RERPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSpkGVKGsGSVLLNGMPIDAKEMRAIS-------AYVQ 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   92 QDYNVLHTLTVRENIM------LPLSITKLSRQEaemRYQEVTEALGI-----TEIGSkyPDE---ISGGQKQRTAAARA 157
Cdd:TIGR00955 106 QDDLFIPTLTVREHLMfqahlrMPRRVTKKEKRE---RVDEVLQALGLrkcanTRIGV--PGRvkgLSGGERKRLAFASE 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  158 LISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHDPVAASYA--NRVIMLKDGQIhteLFQG--DQPVs 233
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGK-TIICTIHQPSSELFElfDKIILMAEGRV---AYLGspDQAV- 255

                         250
                  ....*....|
gi 504427498  234 QFYQEIIHNQ 243
Cdd:TIGR00955 256 PFFSDLGHPC 265
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 22-221 1.89e-32

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. This model is related to models TIGR01842 and TIGR01846, and to bacteriocin ABC transporters that cleave their substrates during export. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 124.98  E-value: 1.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITrmsnkQLS-YFRKKDVGFIFQDyNVLHTL 100
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIR-----QIDpADLRRNIGYVPQD-PRLFYG 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  101 TVRENIMLplsiTKLSRQEAEMryQEVTEALGITEIGSKYPD-----------EISGGQKQRTAAARALISKPAIVFADE 169
Cdd:TIGR03375 554 TLRDNIAL----GAPYADDEEI--LRAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILLLDE 627

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 504427498  170 PTGALDSKSAQDLLKRLETINQQMktTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:TIGR03375 628 PTSAMDNRSEERFKDRLKRWLAGK--TLVLVTHRTSLLDLVDRIIVMDNGRI 677
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 21-243 2.10e-32

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: 118.41  E-value: 2.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmSNKQLSYFRKKdVGFIFQDyNVLHTL 100
Cdd:cd03249   17 PILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDI---RDLNLRWLRSQ-IGLVSQE-PVLFDG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENImlplsitKLSRQEAEMryQEVTEAL---GITEIGSKYPD-----------EISGGQKQRTAAARALISKPAIVF 166
Cdd:cd03249   92 TIAENI-------RYGKPDATD--EEVEEAAkkaNIHDFIMSLPDgydtlvgergsQLSGGQKQRIAIARALLRNPKILL 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 167 ADEPTGALDSKSAQDLlkrLETINQQMK-TTIVMVTHDPVAASYANRVIMLKDGQI-----HTELFQGDQPvsqfYQEII 240
Cdd:cd03249  163 LDEATSALDAESEKLV---QEALDRAMKgRTTIVIAHRLSTIRNADLIAVLQNGQVveqgtHDELMAQKGV----YAKLV 235


                 ...
gi 504427498 241 HNQ 243
Cdd:cd03249  236 KAQ 238
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 4-222 2.64e-32

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 118.72  E-value: 2.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFR 83
Cdd:PRK13548   3 LEARNLSVRLGGR----TLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 -----KKDVGFIFqdynvlhtlTVRENIMLPLSITKLSRQEAEmryQEVTEALGITEI----GSKYPdEISGGQKQRTAA 154
Cdd:PRK13548  79 avlpqHSSLSFPF---------TVEEVVAMGRAPHGLSRAEDD---ALVAAALAQVDLahlaGRDYP-QLSGGEQQRVQL 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 155 ARALI------SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIH 222
Cdd:PRK13548 146 ARVLAqlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDlNLAARYADRIVLLHQGRLV 220
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 4-216 3.59e-32

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: 123.17  E-value: 3.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfr 83
Cdd:TIGR02857 322 LEFSGVSVAYPGRR---PALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSW---- 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 KKDVGFIFQDYNVLHTlTVRENIMLPLS-ITKLSRQEAEMR--YQEVTEALGI---TEIGSKyPDEISGGQKQRTAAARA 157
Cdd:TIGR02857 395 RDQIAWVPQHPFLFAG-TIAENIRLARPdASDAEIREALERagLDEFVAALPQgldTPIGEG-GAGLSGGQAQRLALARA 472

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498  158 LISKPAIVFADEPTGALDSKSAQDLLKRLETINQqmKTTIVMVTHDPVAASYANRVIML 216
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 9-203 6.61e-32

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 119.30  E-value: 6.61e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   9 VSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKdVG 88
Cdd:PRK11308  17 VKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKLLRQK-IQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  89 FIFQdyNVLHTLTVRENI--ML--PLSI-TKLSRQEAEMRYQEVTEALGI-TEIGSKYPDEISGGQKQRTAAARALISKP 162
Cdd:PRK11308  96 IVFQ--NPYGSLNPRKKVgqILeePLLInTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDP 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504427498 163 AIVFADEPTGALD-SKSAQdLLKRLETINQQMKTTIVMVTHD 203
Cdd:PRK11308 174 DVVVADEPVSALDvSVQAQ-VLNLMMDLQQELGLSYVFISHD 214
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 8-225 1.11e-31

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: 116.56  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   8 HVSKIYGNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDV 87
Cdd:cd03251    5 NVTFRYPGDGPP--VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASL----RRQI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  88 GFIFQDyNVLHTLTVRENIMlplsitkLSRQEAEMryQEVTEALG-------ITEIGSKYPDEI-------SGGQKQRTA 153
Cdd:cd03251   79 GLVSQD-VFLFNDTVAENIA-------YGRPGATR--EEVEEAARaanahefIMELPEGYDTVIgergvklSGGQRQRIA 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 154 AARALISKPAIVFADEPTGALDSKS---AQDLLKRLetinQQMKTTIVmVTHDPVAASYANRVIMLKDGQI-----HTEL 225
Cdd:cd03251  149 IARALLKDPPILILDEATSALDTESerlVQAALERL----MKNRTTFV-IAHRLSTIENADRIVVLEDGKIvergtHEEL 223
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 4-220 1.56e-31

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: 115.26  E-value: 1.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSYE-ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditrmsnkqlsyf 82
Cdd:cd03250    1 ISVEDASFTWDSGEQETSfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS------------- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rkkdVGFIFQdYNVLHTLTVRENIMLplsitklSRQEAEMRYQEVTEA-----------LGI-TEIGSKypdEI--SGGQ 148
Cdd:cd03250   68 ----IAYVSQ-EPWIQNGTIRENILF-------GKPFDEERYEKVIKAcalepdleilpDGDlTEIGEK---GInlSGGQ 132

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 149 KQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLetINQQMK--TTIVMVTHDPVAASYANRVIMLKDGQ 220
Cdd:cd03250  133 KQRISLARAVYSDADIYLLDDPLSAVDAHVGRHIFENC--ILGLLLnnKTRILVTHQLQLLPHADQIVVLDNGR 204
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-226 1.67e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 117.14  E-value: 1.67e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYgNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnKQLS 80
Cdd:PRK13650   2 SNIIEVKNLTFKY-KEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTE---ENVW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 YFRKKdVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALI 159
Cdd:PRK13650  78 DIRHK-IGMVFQNPdNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHT-----ELF 226
Cdd:PRK13650 157 MRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVEStstprELF 228
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 3-220 2.84e-31

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: 115.22  E-value: 2.84e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIY-----GNKKqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQ----DITR 73
Cdd:COG4778    4 LLEVENLSKTFtlhlqGGKR--LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  74 MSNKQLSYFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITE-IGSKYPDEISGGQKQRT 152
Cdd:COG4778   82 ASPREILALRRRTIGYVSQFLRVIPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErLWDLPPATFSGGEQQRV 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 153 AAARALISKPAIVFADEPTGALDSKSAQ---DLLKRLetinQQMKTTIVMVTHDP-VAASYANRVIMLKDGQ 220
Cdd:COG4778  162 NIARGFIADPPLLLLDEPTASLDAANRAvvvELIEEA----KARGTAIIGIFHDEeVREAVADRVVDVTPFS 229
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 6-228 3.24e-31

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: 115.12  E-value: 3.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIY-----------------GNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEING 68
Cdd:cd03267    3 VSNLSKSYrvyskepgligslkslfKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  69 QDITRMSNKQLsyfrkKDVGFIF-QDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGG 147
Cdd:cd03267   83 LVPWKRRKKFL-----RRIGVVFgQKTQLWWDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 148 QKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD--PVAAsYANRVIMLKDGQIhteL 225
Cdd:cd03267  158 QRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYmkDIEA-LARRVLVIDKGRL---L 233


                 ...
gi 504427498 226 FQG 228
Cdd:cd03267  234 YDG 236
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 19-221 5.06e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 115.01  E-value: 5.06e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  19 SYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNV-----TRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQD 93
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELypearVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  94 YNVLHTLTVRENIMLPLSITKLSRQEAEMrYQEVTEALGITEIGSKYPD-------EISGGQKQRTAAARALISKPAIVF 166
Cdd:PRK14247  91 PNPIPNLSIFENVALGLKLNRLVKSKKEL-QERVRWALEKAQLWDEVKDrldapagKLSGGQQQRLCIARALAFQPEVLL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 167 ADEPTGALDSKSAQDLLKRLETINQQMktTIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQqAARISDYVAFLYKGQI 223
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
2-221 6.77e-31

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 114.73  E-value: 6.77e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSy 81
Cdd:PRK11231   1 MTLRTENLTVGYGTKR----ILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 frkKDVGFIFQDYNVLHTLTVRENI------MLPLsITKLSrQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAA 155
Cdd:PRK11231  76 ---RRLALLPQHHLTPEGITVRELVaygrspWLSL-WGRLS-AEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVmVTHDPVAAS-YANRVIMLKDGQI 221
Cdd:PRK11231 151 MVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGKTVVT-VLHDLNQASrYCDHLVVLANGHV 216
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 25-241 7.10e-31

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


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 114.39  E-value: 7.10e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   25 DIHFTVEKGGFVAIMGPSGSGKTT----LLNVISSIDNVTRGTIEINGQDITRMSnkqlsyFRKKDVGFIFQD----YNV 96
Cdd:TIGR02770   4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLS------IRGRHIATIMQNprtaFNP 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   97 LHTLT--VRENIMLPLSITKLSRQEAEMRYQEVTEALGiTEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGAL 174
Cdd:TIGR02770  78 LFTMGnhAIETLRSLGKLSKQARALILEALEAVGLPDP-EEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498  175 DSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI-----HTELFQgdQPVSQFYQEIIH 241
Cdd:TIGR02770 157 DVVNQARVLKLLRELRQLFGTGILLITHDlGVVARIADEVAVMDDGRIvergtVKEIFY--NPKHETTRKLLS 227
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 1-244 1.06e-30

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 114.02  E-value: 1.06e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MS-ILKVSHVSKIY------------------GNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTR 61
Cdd:COG1134    1 MSsMIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  62 GTIEINGqditRMSnkqlSYFrkkDVGFIFQdynvlHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEalgITEIGsKYP 141
Cdd:COG1134   81 GRVEVNG----RVS----ALL---ELGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVE---FAELG-DFI 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 142 DE----ISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDP-VAASYANRVIML 216
Cdd:COG1134  141 DQpvktYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMgAVRRLCDRAIWL 219

                        250       260
                 ....*....|....*....|....*....
gi 504427498 217 KDGQIHtelFQGD-QPVSQFYQEIIHNQS 244
Cdd:COG1134  220 EKGRLV---MDGDpEEVIAAYEALLAGRE 245
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-221 1.39e-30

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 118.20  E-value: 1.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyF 82
Cdd:COG1129    4 LLEMRGISKSFGGVK----ALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRD---A 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKDVGFIFQDYNVLHTLTVRENIMLPLSITK---LSRQEAEMRYQEVTEALGI-----TEIGskypdEISGGQKQRTAA 154
Cdd:COG1129   77 QAAGIAIIHQELNLVPNLSVAENIFLGREPRRgglIDWRAMRRRARELLARLGLdidpdTPVG-----DLSVAQQQLVEI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTH--DPVAAsYANRVIMLKDGQI 221
Cdd:COG1129  152 ARALSRDARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHrlDEVFE-IADRVTVLRDGRL 218
cbiO PRK13641
energy-coupling factor transporter ATPase;
1-246 5.24e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 113.39  E-value: 5.24e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIY--GNKKQSyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDIT-RMSNK 77
Cdd:PRK13641   1 MSI-KFENVDYIYspGTPMEK-KGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITpETGNK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKKdVGFIFQ-DYNVLHTLTVRENIML-PLSItKLSRQEAEMRYQEVTEALGITE-IGSKYPDEISGGQKQRTAA 154
Cdd:PRK13641  79 NLKKLRKK-VSLVFQfPEAQLFENTVLKDVEFgPKNF-GFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTH--DPVaASYANRVIMLKdgqiHTELFQGDQPv 232
Cdd:PRK13641 157 AGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDY-QKAGHTVILVTHnmDDV-AEYADDVLVLE----HGKLIKHASP- 229

                        250
                 ....*....|....
gi 504427498 233 sqfyQEIIHNQSVL 246
Cdd:PRK13641 230 ----KEIFSDKEWL 239
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 23-221 5.54e-30

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: 117.16  E-value: 5.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfrkKDVGFIFQDynVlhTL-- 100
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELG----RHIGYLPQD--V--ELfd 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 -TVRENImlplsitklSR-QEAEMryQEVTEAL---GITEIGSKYPD----EI-------SGGQKQRTAAARALISKPAI 164
Cdd:COG4618  420 gTIAENI---------ARfGDADP--EKVVAAAklaGVHEMILRLPDgydtRIgeggarlSGGQRQRIGLARALYGDPRL 488

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 165 VFADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:COG4618  489 VVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLLAAVDKLLVLRDGRV 544
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 16-203 6.74e-30

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 114.03  E-value: 6.74e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  16 KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKkDVGFIFQDyn 95
Cdd:PRK15079  30 PPKTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRS-DIQMIFQD-- 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  96 VLHTL----TVRENIMLPLSI--TKLSRQEAEMRYQEVTEALGITE-IGSKYPDEISGGQKQRTAAARALISKPAIVFAD 168
Cdd:PRK15079 107 PLASLnprmTIGEIIAEPLRTyhPKLSRQEVKDRVKAMMLKVGLLPnLINRYPHEFSGGQCQRIGIARALILEPKLIICD 186

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504427498 169 EPTGALD-SKSAQ--DLLKRLEtinQQMKTTIVMVTHD 203
Cdd:PRK15079 187 EPVSALDvSIQAQvvNLLQQLQ---REMGLSLIFIAHD 221
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 2-222 1.06e-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: 111.09  E-value: 1.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMsnkqlsy 81
Cdd:cd03220   17 SSSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLL------- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 frkkDVGFIFQDynvlhTLTVRENIMLPLSITKLSRQEAEMRYQEVTEalgITEIGSKYPDEI---SGGQKQRTAAARAL 158
Cdd:cd03220   90 ----GLGGGFNP-----ELTGRENIYLNGRLLGLSRKEIDEKIDEIIE---FSELGDFIDLPVktySSGMKARLAFAIAT 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTHDPVA-ASYANRVIMLKDGQIH 222
Cdd:cd03220  158 ALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSiKRLCDRALVLEKGKIR 221
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
22-221 1.37e-29

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 114.36  E-value: 1.37e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQDYNVLHTLT 101
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPHMT 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 VRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQD 181
Cdd:PRK10070 123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 182 LLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK10070 203 MQDELVKLQAKHQRTIVFISHDlDEAMRIGDRIAIMQNGEV 243
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 1-221 1.44e-29

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 112.91  E-value: 1.44e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKT-TLLNVISSID---NVTRGTIEINGQDITRMSN 76
Cdd:PRK11022   1 MALLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDypgRVMAEKLEFNGQDLQRISE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 KQLSYFRKKDVGFIFQD--YNVLHTLTVRENIMLPLSITKL-SRQEAEMRYQEVTEALGITEIGSK---YPDEISGGQKQ 150
Cdd:PRK11022  81 KERRNLVGAEVAMIFQDpmTSLNPCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQ 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 151 RTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK11022 161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDlALVAEAAHKIIVMYAGQV 232
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 4-221 2.66e-29

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: 109.92  E-value: 2.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGnkkQSyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqlSYFR 83
Cdd:TIGR03410   1 LEVSNLNVYYG---QS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLP----PHER 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 -KKDVGFIFQDYNVLHTLTVRENIMLPLsitklsrqeaemryqevtEALGitEIGSKYPDEI------------------ 144
Cdd:TIGR03410  73 aRAGIAYVPQGREIFPRLTVEENLLTGL------------------AALP--RRSRKIPDEIyelfpvlkemlgrrggdl 132

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498  145 SGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMV-THDPVAASYANRVIMLKDGQI 221
Cdd:TIGR03410 133 SGGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVeQYLDFARELADRYYVMERGRV 210
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 2-202 2.96e-29

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 110.51  E-value: 2.96e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVI----SSIDNV-TRGTIEINGQDItrmsn 76
Cdd:COG1117   10 PKIEVRNLNVYYGDKQ----ALKDINLDIPENKVTALIGPSGCGKSTLLRCLnrmnDLIPGArVEGEILLDGEDI----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 kqlsYFRKKD-------VGFIFQDYNVLhTLTVRENIMLPLSIT-KLSRQEAEMRyqeVTEAL---GIteigskyPDEI- 144
Cdd:COG1117   81 ----YDPDVDvvelrrrVGMVFQKPNPF-PKSIYDNVAYGLRLHgIKSKSELDEI---VEESLrkaAL-------WDEVk 145

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 145 ----------SGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQ---DLLKRLETinqqmKTTIVMVTH 202
Cdd:COG1117  146 drlkksalglSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAkieELILELKK-----DYTIVIVTH 211
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 4-221 4.02e-29

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: 108.91  E-value: 4.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGqditrmsnKQLSYFR 83
Cdd:cd03269    1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDG--------KPLDIAA 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03269   69 RNRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPE 148

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 164 IVFADEPTGALDSKSaQDLLKRLetINQQMK--TTIVMVTH--DPVAAsYANRVIMLKDGQI 221
Cdd:cd03269  149 LLILDEPFSGLDPVN-VELLKDV--IRELARagKTVILSTHqmELVEE-LCDRVLLLNKGRA 206
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-221 1.31e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 109.50  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTT---LLNVISSIDNVTRGTIEINGqdiTRMSNKQ 78
Cdd:PRK13640   4 NIVEFKHVSFTYPDSKKP--ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDG---ITLTAKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LSYFRKKdVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARA 157
Cdd:PRK13640  79 VWDIREK-VGIVFQNPdNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGI 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 158 LISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:PRK13640 158 LAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKL 221
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 3-228 1.35e-28

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 109.55  E-value: 1.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITrMSNKQLSYF 82
Cdd:PRK13636   5 ILKVEELNYNYSD---GTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPID-YSRKGLMKL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKkDVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:PRK13636  81 RE-SVGMVFQDPdNQLFSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQG 228
Cdd:PRK13636 160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDiDIVPLYCDNVFVMKEGRV---ILQG 224
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 22-229 1.35e-28

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 113.26  E-value: 1.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTT----LLNVISSidnvtRGTIEINGQDITRMSNKQLSYFRKKdVGFIFQDYNvl 97
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPN-- 372

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  98 HTLTVRENIM------LPLSITKLSRQEAEMRYQEVTEALGI-TEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:PRK15134 373 SSLNPRLNVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEP 452

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 171 TGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGD 229
Cdd:PRK15134 453 TSSLDKTVQAQILALLKSLQQKHQLAYLFISHDlHVVRALCHQVIVLRQGEV---VEQGD 509
cbiO PRK13643
energy-coupling factor transporter ATPase;
3-221 2.04e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 109.44  E-value: 2.04e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYG-NKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS-NKQLS 80
Cdd:PRK13643   1 MIKFEKVNYTYQpNSPFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSkQKEIK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 YFRKKdVGFIFQ-DYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGIT-EIGSKYPDEISGGQKQRTAAARAL 158
Cdd:PRK13643  81 PVRKK-VGVVFQfPESQLFEETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGIL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTH--DPVaASYANRVIMLKDGQI 221
Cdd:PRK13643 160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ-TVVLVTHlmDDV-ADYADYVYLLEKGHI 222
cbiO PRK13649
energy-coupling factor transporter ATPase;
22-249 2.10e-28

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 109.06  E-value: 2.10e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS-NKQLSYFRKKdVGFIFQ-DYNVLHT 99
Cdd:PRK13649  22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSkNKDIKQIRKK-VGLVFQfPESQLFE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 100 LTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITE-IGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:PRK13649 101 ETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKG 180

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 179 AQDLLKRLETINQQmKTTIVMVTH--DPVaASYANRVIMLKDGQihteLFQGDQPvSQFYQEIIHNQSVLGGV 249
Cdd:PRK13649 181 RKELMTLFKKLHQS-GMTIVLVTHlmDDV-ANYADFVYVLEKGK----LVLSGKP-KDIFQDVDFLEEKQLGV 246
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
13-224 2.80e-28

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 108.54  E-value: 2.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  13 YGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfrkKDVGFIFQ 92
Cdd:PRK10253  17 YGK----YTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQ 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  93 DYNVLHTLTVRENIM------LPLsITKLsRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVF 166
Cdd:PRK10253  89 NATTPGDITVQELVArgryphQPL-FTRW-RKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIML 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 167 ADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQIHTE 224
Cdd:PRK10253 167 LDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDlNQACRYASHLIALREGKIVAQ 225
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 3-221 4.75e-28

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 107.32  E-value: 4.75e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQ-----DITRMSNK 77
Cdd:PRK11701   6 LLSVRGLTKLYGPRK----GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKKDVGFIFQD------YNVLHTLTVRENIMlplsiTKLSRQEAEMRyQEVTEALGITEIGSKYPDEI----SGG 147
Cdd:PRK11701  82 ERRRLLRTEWGFVHQHprdglrMQVSAGGNIGERLM-----AVGARHYGDIR-ATAGDWLERVEIDAARIDDLpttfSGG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 148 QKQRTAAARALISKPAIVFADEPTGALDSkSAQ----DLLKRLETinqQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK11701 156 MQQRLQIARNLVTHPRLVFMDEPTGGLDV-SVQarllDLLRGLVR---ELGLAVVIVTHDlAVARLLAHRLLVMKQGRV 230
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
22-216 4.82e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 105.78  E-value: 4.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGqditrmsnkqlsyfrKKDVGFIFQDYNVLHTL- 100
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAG---------------GARVAYVPQRSEVPDSLp 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 -TVRENIML----PLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALD 175
Cdd:NF040873  72 lTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 176 SKSAQDLLKRLETINQQmKTTIVMVTHDPVAASYANRVIML 216
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRRADPCVLL 191
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 4-204 6.42e-28

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: 111.30  E-value: 6.42e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGnkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfr 83
Cdd:TIGR02868 335 LELRDLSAGYP---GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVR--- 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 kKDVGFIFQDYNVLHTlTVRENIMlplsitkLSRQEA---EMRyqEVTEALGITEIGSKYPD-----------EISGGQK 149
Cdd:TIGR02868 409 -RRVSVCAQDAHLFDT-TVRENLR-------LARPDAtdeELW--AALERVGLADWLRALPDgldtvlgeggaRLSGGER 477

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498  150 QRTAAARALISKPAIVFADEPTGALDSKSAQDLlkrLETINQQMK-TTIVMVTHDP 204
Cdd:TIGR02868 478 QRLALARALLADAPILLLDEPTEHLDAETADEL---LEDLLAALSgRTVVLITHHL 530
cbiO PRK13646
energy-coupling factor transporter ATPase;
1-221 1.14e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 107.17  E-value: 1.14e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIlKVSHVSKIY--GNKKQsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDIT-RMSNK 77
Cdd:PRK13646   1 MTI-RFDNVSYTYqkGTPYE-HQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITIThKTKDK 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKKdVGFIFQ-DYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGIT-EIGSKYPDEISGGQKQRTAAA 155
Cdd:PRK13646  79 YIRPVRKR-IGMVFQfPESQLFEDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIV 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSI 224
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 19-225 1.94e-27

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: 110.29  E-value: 1.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  19 SYEA----LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDy 94
Cdd:COG5265  366 GYDPerpiLKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASL----RAAIGIVPQD- 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  95 NVLHTLTVRENImlplsitKLSRQEAEMryQEVTEALGITEIG---SKYPD-----------EISGGQKQRTAAARALIS 160
Cdd:COG5265  441 TVLFNDTIAYNI-------AYGRPDASE--EEVEAAARAAQIHdfiESLPDgydtrvgerglKLSGGEKQRVAIARTLLK 511

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 161 KPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVM------VTHdpvaasyANRVIMLKDGQI-----HTEL 225
Cdd:COG5265  512 NPPILIFDEATSALDSRTERAIQAALREVARG-RTTLVIahrlstIVD-------ADEILVLEAGRIvergtHAEL 579
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
34-221 2.19e-27

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 107.65  E-value: 2.19e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  34 GFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQDYNVLHTLTVRENimLPLSIT 113
Cdd:PRK11144  25 GITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGICLPPEKRRIGYVFQDARLFPHYKVRGN--LRYGMA 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 114 KLSRQEaemrYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQM 193
Cdd:PRK11144 103 KSMVAQ----FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREI 178

                        170       180       190
                 ....*....|....*....|....*....|
gi 504427498 194 KTTIVMVTH--DPVaASYANRVIMLKDGQI 221
Cdd:PRK11144 179 NIPILYVSHslDEI-LRLADRVVVLEQGKV 207
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
25-239 4.51e-27

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 105.23  E-value: 4.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  25 DIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKdVGFIFQDYNVLHTLTVRE 104
Cdd:PRK11831  25 NISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKR-MSMLFQSGALFTDMNVFD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 105 NIMLPLSitKLSRQEAEMRYQEVT---EALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQD 181
Cdd:PRK11831 104 NVAYPLR--EHTQLPAPLLHSTVMmklEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 182 LLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI-----HTELFQGDQP-VSQFYQEI 239
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDvPEVLSIADHAYIVADKKIvahgsAQALQANPDPrVRQFLDGI 246
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 21-237 7.21e-27

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: 103.72  E-value: 7.21e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDitrMSNKQLSYFRKKdVGFIFQDyNVLHTL 100
Cdd:cd03252   16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHD---LALADPAWLRRQ-VGVVLQE-NVLFNR 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENIMLPLSITKLSRQEAEMRYQEVTE-----ALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALD 175
Cdd:cd03252   91 SIRDNIALADPGMSMERVIEAAKLAGAHDfiselPEGYDTIVGEQGAGLSGGQRQRIAIARALIHNPRILIFDEATSALD 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 176 SKSAQDLLKRLETINQqmKTTIVMVTHDPVAASYANRVIMLKDGQI-----HTELFQGDQPVSQFYQ 237
Cdd:cd03252  171 YESEHAIMRNMHDICA--GRTVIIIAHRLSTVKNADRIIVMEKGRIveqgsHDELLAENGLYAYLYQ 235
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 23-220 9.06e-27

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 107.97  E-value: 9.06e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEI-NGQDITRMSnkQLSYFrkkdvgfifqdynVLHTLt 101
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP--QRPYL-------------PLGTL- 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 vRENIMLPLSITKLSRQEaemrYQEVTEALGITEIGSKYPDE------ISGGQKQRTAAARALISKPAIVFADEPTGALD 175
Cdd:COG4178  443 -REALLYPATAEAFSDAE----LREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSALD 517

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504427498 176 SKSAQDLLKRLETinQQMKTTIVMVTHDPVAASYANRVIMLKDGQ 220
Cdd:COG4178  518 EENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDG 560
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 4-221 1.46e-26

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: 101.62  E-value: 1.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyfR 83
Cdd:cd03247    1 LSINNVSFSYPE--QEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA-----L 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTlTVRENIMLPLSitklsrqeaemryqevtealgiteigskypdeisGGQKQRTAAARALISKPA 163
Cdd:cd03247   74 SSLISVLNQRPYLFDT-TLRNNLGRRFS----------------------------------GGERQRLALARILLQDAP 118

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLlkrLETINQQMK-TTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03247  119 IVLLDEPTVGLDPITERQL---LSLIFEVLKdKTLIWITHHLTGIEHMDKILFLENGKI 174
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 3-221 1.64e-26

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


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 103.37  E-value: 1.64e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQD-----ITRMSNK 77
Cdd:TIGR02323   3 LLQVSGLSKSYGGGK----GCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSgaeleLYQLSEA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   78 QLSYFRKKDVGFIFQdyNVLHTLTVR----ENIMLPLSITKLS-----RQEAEMRYQEVTEALGITEigsKYPDEISGGQ 148
Cdd:TIGR02323  79 ERRRLMRTEWGFVHQ--NPRDGLRMRvsagANIGERLMAIGARhygniRATAQDWLEEVEIDPTRID---DLPRAFSGGM 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498  149 KQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:TIGR02323 154 QQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDlGVARLLAQRLLVMQQGRV 227
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 4-224 3.34e-26

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: 101.14  E-value: 3.34e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyfr 83
Cdd:cd03268    1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEAL----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEmryqEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:cd03268   72 -RRIGALIEAPGFYPNLTARENLRLLARLLGIRKKRID----EVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPD 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVmvthdpvaASY--------ANRVIMLKDGQIHTE 224
Cdd:cd03268  147 LLILDEPTNGLDPDGIKELRELILSLRDQGITVLI--------SSHllseiqkvADRIGIINKGKLIEE 207
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 2-224 3.49e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 102.91  E-value: 3.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYgnkkQSYEA--LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQL 79
Cdd:PRK13648   6 SIIVFKNVSFQY----QSDASftLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 syfrKKDVGFIFQD-YNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARAL 158
Cdd:PRK13648  82 ----RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKE 223
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
8-221 4.21e-26

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 106.20  E-value: 4.21e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   8 HVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDV 87
Cdd:PRK13657 339 DVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASL----RRNI 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  88 GFIFQDyNVLHTLTVRENImlplSITKLSRQEAEMRYQ-EVTEALG------------ITEIGSKypdeISGGQKQRTAA 154
Cdd:PRK13657 412 AVVFQD-AGLFNRSIEDNI----RVGRPDATDEEMRAAaERAQAHDfierkpdgydtvVGERGRQ----LSGGERQRLAI 482

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVmVTHDPVAASYANRVIMLKDGQI 221
Cdd:PRK13657 483 ARALLKDPPILILDEATSALDVETEAKVKAALDELMKG-RTTFI-IAHRLSTVRNADRILVFDNGRV 547
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 22-220 6.22e-26

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 103.27  E-value: 6.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKT----TLLNVISSiDNVTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQD---- 93
Cdd:PRK09473  31 AVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAA-NGRIGGSATFNGREILNLPEKELNKLRAEQISMIFQDpmts 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  94 ---YnvlhtLTVRENIMLPLSITK-LSRQEAEMRYQEVTEALGITEIGSK---YPDEISGGQKQRTAAARALISKPAIVF 166
Cdd:PRK09473 110 lnpY-----MRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLI 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 167 ADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQ 220
Cdd:PRK09473 185 ADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDlGVVAGICDKVLVMYAGR 239
cbiO PRK13642
energy-coupling factor transporter ATPase;
3-224 6.80e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 102.48  E-value: 6.80e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYgNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditRMSNKQLSYF 82
Cdd:PRK13642   4 ILEVENLVFKY-EKESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGE---LLTAENVWNL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDY-NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:PRK13642  80 RRK-IGMVFQNPdNQFVGATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK13642 159 PEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKE 221
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
3-224 7.12e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 102.09  E-value: 7.12e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqLS 80
Cdd:PRK13633   4 MIKCKNVSYKYESNEESTEklALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 YFRKKdVGFIFQ--DYNVLHTLtVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARAL 158
Cdd:PRK13633  82 DIRNK-AGMVFQnpDNQIVATI-VEEDVAFGPENLGIPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGIL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK13633 160 AMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVME 225
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 3-221 1.16e-25

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 104.88  E-value: 1.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGN-KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEIN-GQDITRMSNK--Q 78
Cdd:TIGR03269 279 IIKVRNVSKRYISvDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPgpD 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   79 LSYFRKKDVGFIFQDYNVLHTLTVRENIMLPLSItKLSRQEAEMRYQEVTEALGITE-----IGSKYPDEISGGQKQRTA 153
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEekaeeILDKYPDELSEGERHRVA 437

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498  154 AARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDmDFVLDVCDRAALMRDGKI 506
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 7-225 1.22e-25

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 105.19  E-value: 1.22e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    7 SHVSKIYGNKKqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsYFRKKd 86
Cdd:TIGR00958 482 QDVSFSYPNRP-DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHH---YLHRQ- 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   87 VGFIFQDyNVLHTLTVRENIMLPLSITklsrQEAEMR--YQEVTEALGITEIGSKYPDEI-------SGGQKQRTAAARA 157
Cdd:TIGR00958 557 VALVGQE-PVLFSGSVRENIAYGLTDT----PDEEIMaaAKAANAHDFIMEFPNGYDTEVgekgsqlSGGQKQRIAIARA 631

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498  158 LISKPAIVFADEPTGALDSKSAQdllkRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI-----HTEL 225
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVvemgtHKQL 700
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 3-220 1.87e-25

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 104.55  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKT-TLLNVISSIDNvTRGTIEINGQ----------DI 71
Cdd:PRK10261  12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviEL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  72 TRMSNKQLSYFRKKDVGFIFQD--YNVLHTLTVRENIMLPLSITK-LSRQEAEMRYQEVTEALGITE---IGSKYPDEIS 145
Cdd:PRK10261  91 SEQSAAQMRHVRGADMAMIFQEpmTSLNPVFTVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEaqtILSRYPHQLS 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 146 GGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQ 220
Cdd:PRK10261 171 GGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDmGVVAEIADRVLVMYQGE 246
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 23-216 2.01e-25

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 99.79  E-value: 2.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyFRKKdVGFIFQDyNVLHTLTV 102
Cdd:PRK10247  23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEI---YRQQ-VSYCAQT-PTLFGDTV 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENIMLPLSITKLSRQEAEMRYQEVTEALGITeIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDL 182
Cdd:PRK10247  98 YDNLIFPWQIRNQQPDPAIFLDDLERFALPDT-ILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNV 176

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504427498 183 LKRLETINQQMKTTIVMVTHDPVAASYANRVIML 216
Cdd:PRK10247 177 NEIIHRYVREQNIAVLWVTHDKDEINHADKVITL 210
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 13-221 2.27e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 100.30  E-value: 2.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  13 YGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI-----DNVTRGTIEINGQDItrMSNKQLSYFRKKDV 87
Cdd:PRK14267  14 YGSN----HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNI--YSPDVDPIEVRREV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  88 GFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMR------------YQEVTEALgiteigSKYPDEISGGQKQRTAAA 155
Cdd:PRK14267  88 GMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELDervewalkkaalWDEVKDRL------NDYPSNLSGGQRQRLVIA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 156 RALISKPAIVFADEPTGALDSKSAqdllKRLETINQQMKT--TIVMVTHDPV-AASYANRVIMLKDGQI 221
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGT----AKIEELLFELKKeyTIVLVTHSPAqAARVSDYVAFLYLGKL 226
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 26-238 2.45e-25

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 104.16  E-value: 2.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  26 IHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVtRGTIEINGQDITRMSnkqLSYFRKKdVGFIFQDYNVLHTlTVREN 105
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRELD---PESWRKH-LSWVGQNPQLPHG-TLRDN 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 106 IMLplsitklSRQEA-EMRYQEVTEALGITEIGSKYPD-----------EISGGQKQRTAAARALISKPAIVFADEPTGA 173
Cdd:PRK11174 443 VLL-------GNPDAsDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTAS 515

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 174 LDSKSAQDLLKRLETINQQmKTTIvMVTH--DPVAAsyANRVIMLKDGQI-----HTELFQGDQPVSQFYQE 238
Cdd:PRK11174 516 LDAHSEQLVMQALNAASRR-QTTL-MVTHqlEDLAQ--WDQIWVMQDGQIvqqgdYAELSQAGGLFATLLAH 583
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
 4-202 3.91e-25

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: 99.01  E-value: 3.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnKQLsyfr 83
Cdd:TIGR03740   1 LETKNLSKRFGKQ----TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWTR---KDL---- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 kKDVGFIFQDYNVLHTLTVRENimlpLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:TIGR03740  70 -HKIGSLIESPPLYENLTAREN----LKVHTTLLGLPDSRIDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPK 144

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 504427498  164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTH 202
Cdd:TIGR03740 145 LLILDEPTNGLDPIGIQELRELIRSFPEQ-GITVILSSH 182
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 23-221 4.15e-25

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 99.74  E-value: 4.15e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQ------DITRMSNKQLsyfrKKDVGFIFQDYNV 96
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKL----RKEVGMVFQQPNP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  97 LHTLTVRENIMLPLSITKLS-RQEAEMRYQEVTEALGI-TEIGSKY---PDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:PRK14246 102 FPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPT 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504427498 172 GALDSKSAQDLLKRLETINQQMktTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:PRK14246 182 SMIDIVNSQAIEKLITELKNEI--AIVIVSHNPqQVARVADYVAFLYNGEL 230
PLN03211 PLN03211
ABC transporter G-25; Provisional
 33-240 1.08e-24

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 102.27  E-value: 1.08e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  33 GGFVAIMGPSGSGKTTLLNVISS--IDNVTRGTIEINGQDITRMSNKQlsyfrkkdVGFIFQDYNVLHTLTVRENIM--- 107
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILKR--------TGFVTQDDILYPHLTVRETLVfcs 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 108 ---LPLSitkLSRQEAEMRYQEVTEALGITE-----IGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSA 179
Cdd:PLN03211 166 llrLPKS---LTKQEKILVAESVISELGLTKcentiIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAA 242

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 180 QDLLKRLETINQQMKtTIVMVTHDPVAASYA--NRVIMLKDGQIhteLFQGDQPVSQFYQEII 240
Cdd:PLN03211 243 YRLVLTLGSLAQKGK-TIVTSMHQPSSRVYQmfDSVLVLSEGRC---LFFGKGSDAMAYFESV 301
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 3-208 1.26e-24

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 98.31  E-value: 1.26e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISS----IDNVT-RGTIEINGQDI--TRMS 75
Cdd:PRK14239   5 ILQVSDLSVYYNKKK----ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndlNPEVTiTGSIVYNGHNIysPRTD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 NKQLsyfrKKDVGFIFQDYNVLhTLTVRENIMLPLSITKLSRQ-------EAEMR----YQEVTEALGITEIGskypdeI 144
Cdd:PRK14239  81 TVDL----RKEIGMVFQQPNPF-PMSIYENVVYGLRLKGIKDKqvldeavEKSLKgasiWDEVKDRLHDSALG------L 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 145 SGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMktTIVMVTHDPVAAS 208
Cdd:PRK14239 150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQAS 211
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 4-221 2.12e-24

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: 95.19  E-value: 2.12e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfR 83
Cdd:cd03216    1 LELRGITKRFGGVK----ALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDA---R 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQdynvlhtltvrenimlplsitklsrqeaemryqevtealgiteigskypdeISGGQKQRTAAARALISKPA 163
Cdd:cd03216   74 RAGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNAR 102

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTH--DPVAAsYANRVIMLKDGQI 221
Cdd:cd03216  103 LLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHrlDEVFE-IADRVTVLRDGRV 160
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 3-221 3.25e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 98.77  E-value: 3.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYgNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEI----NGQDITRMSN 76
Cdd:PRK13631  21 ILRVKNLYCVF-DEKQENElvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyIGDKKNNHEL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 ------KQLSYFRK--KDVGFIFQ--DYNVLHTlTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITE-IGSKYPDEIS 145
Cdd:PRK13631 100 itnpysKKIKNFKElrRRVSMVFQfpEYQLFKD-TIEKDIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLS 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 146 GGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIvMVTH--DPVaASYANRVIMLKDGQI 221
Cdd:PRK13631 179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVF-VITHtmEHV-LEVADEVIVMDKGKI 254
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 1-222 5.37e-24

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 99.15  E-value: 5.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLS 80
Cdd:PRK09536   1 MPMIDVSDLSVEFG----DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrkKDVGFIFQDYNVLHTLTVRENIMLPLS--ITKLSRQ-EAEMR-YQEVTEALGITEIGSKYPDEISGGQKQRTAAAR 156
Cdd:PRK09536  77 ----RRVASVPQDTSLSFEFDVRQVVEMGRTphRSRFDTWtETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVtHD-PVAASYANRVIMLKDGQIH 222
Cdd:PRK09536 153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDlDLAARYCDELVLLADGRVR 218
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 22-221 6.62e-24

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 95.64  E-value: 6.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfRKKdVGFIFQDyNVLHTLT 101
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDL---RSR-ISIIPQD-PVLFSGT 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 VRENIMlPLSItklsRQEAEMryQEVTEALGITEIGSKYPDEI-----------SGGQKQRTAAARALISKPAIVFADEP 170
Cdd:cd03244   94 IRSNLD-PFGE----YSDEEL--WQALERVGLKEFVESLPGGLdtvveeggenlSVGQRQLLCLARALLRKSKILVLDEA 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504427498 171 TGALDSKSAQDLLKrleTINQQMK-TTIVMVTH--DPVAASyaNRVIMLKDGQI 221
Cdd:cd03244  167 TASVDPETDALIQK---TIREAFKdCTVLTIAHrlDTIIDS--DRILVLDKGRV 215
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-220 6.90e-24

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 99.72  E-value: 6.90e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyf 82
Cdd:COG3845    5 ALELRGITKRFGGVV----ANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDA--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKDVGFIFQDYNVLHTLTVRENIML---PLSITKLSRQEAEMRyqevtealgITEIGSKY-----PD----EISGGQKQ 150
Cdd:COG3845   78 IALGIGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARAR---------IRELSERYgldvdPDakveDLSVGEQQ 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 151 RTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLetinQQMK---TTIVMVTH--DPVAAsYANRVIMLKDGQ 220
Cdd:COG3845  149 RVEILKALYRGARILILDEPTAVLTPQEADELFEIL----RRLAaegKSIIFITHklREVMA-IADRVTVLRRGK 218
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 1-221 1.35e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 96.03  E-value: 1.35e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYgnkKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLs 80
Cdd:PRK13652   1 MHLIETRDLCYSY---SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfrKKDVGFIFQ--DYNVLHTlTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARAL 158
Cdd:PRK13652  77 ---RKFVGLVFQnpDDQIFSP-TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVI 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK13652 153 AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQlDLVPEMADYIYVMDKGRI 216
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 21-221 1.45e-23

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 96.69  E-value: 1.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsyFRKKdVGFIF-Q------D 93
Cdd:COG4586   36 EAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPFKRRKE----FARR-IGVVFgQrsqlwwD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  94 ynvlhtLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGA 173
Cdd:COG4586  111 ------LPAIDSFRLLKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIG 184

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504427498 174 LD--SKSA-QDLLKRletINQQMKTTIVMVTHDP--VAAsYANRVIMLKDGQI 221
Cdd:COG4586  185 LDvvSKEAiREFLKE---YNRERGTTILLTSHDMddIEA-LCDRVIVIDHGRI 233
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 6-223 3.00e-23

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 97.83  E-value: 3.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISsidnvtrGTIEINGQDITRMSNKQLSYFRkk 85
Cdd:COG0488    1 LENLSKSFGGRP----LLDDVSLSINPGDRIGLVGRNGAGKSTLLKILA-------GELEPDSGEVSIPKGLRIGYLP-- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  86 dvgfifQDYNVLHTLTVRENIMLPLS-----ITKLSRQEAEM--------RYQEVTE-------------------ALGI 133
Cdd:COG0488   68 ------QEPPLDDDLTVLDTVLDGDAelralEAELEELEAKLaepdedleRLAELQEefealggweaearaeeilsGLGF 141

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 134 TEI-GSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDsksaqdllkrLETIN------QQMKTTIVMVTHD--- 203
Cdd:COG0488  142 PEEdLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----------LESIEwleeflKNYPGTVLVVSHDryf 211

                        250       260
                 ....*....|....*....|..
gi 504427498 204 --PVaasyANRVIMLKDGQIHT 223
Cdd:COG0488  212 ldRV----ATRILELDRGKLTL 229
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 10-221 3.77e-23

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 98.00  E-value: 3.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  10 SKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKkDVGF 89
Cdd:PRK10261 327 SGLLNRVTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRR-DIQF 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  90 IFQD-YNVLHT-LTVRENIMLPLSITKLSR-QEAEMRYQEVTEALGIT-EIGSKYPDEISGGQKQRTAAARALISKPAIV 165
Cdd:PRK10261 406 IFQDpYASLDPrQTVGDSIMEPLRVHGLLPgKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVI 485

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 166 FADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK10261 486 IADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDmAVVERISHRVAVMYLGQI 542
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 23-218 4.99e-23

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: 91.83  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINgqditrmsnkqlsyfRKKDVGFIFQD-YNVLHTLt 101
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMP---------------EGEDLLFLPQRpYLPLGTL- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 vRENIMLPLSitklsrqeaemryqevtealgiteigskypDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQD 181
Cdd:cd03223   81 -REQLIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDR 129

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504427498 182 LLKRLetinQQMKTTIVMVTHDPVAASYANRVIMLKD 218
Cdd:cd03223  130 LYQLL----KELGITVISVGHRPSLWKFHDRVLDLDG 162
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 4-239 1.14e-22

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 96.43  E-value: 1.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfr 83
Cdd:PRK11160 339 LTLNNVSFTYPDQPQP--VLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAAL---- 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTlTVRENimlpLSITKLSRQEAEMRyqEVTEALGITEI--GSKYPD--------EISGGQKQRTA 153
Cdd:PRK11160 413 RQAISVVSQRVHLFSA-TLRDN----LLLAAPNASDEALI--EVLQQVGLEKLleDDKGLNawlgeggrQLSGGEQRRLG 485

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 154 AARALISKPAIVFADEPTGALDSKSAQDLlkrLETINQQMK-TTIVMVTHDPVAASYANRVIMLKDGQI-----HTELFQ 227
Cdd:PRK11160 486 IARALLHDAPLLLLDEPTEGLDAETERQI---LELLAEHAQnKTVLMITHRLTGLEQFDRICVMDNGQIieqgtHQELLA 562

                        250
                 ....*....|..
gi 504427498 228 GDQPVSQFYQEI 239
Cdd:PRK11160 563 QQGRYYQLKQRL 574
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 22-221 1.37e-22

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: 90.95  E-value: 1.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyFRKKDVGFIFQD---YNVLH 98
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRD---AIRAGIAYVPEDrkrEGLVL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  99 TLTVRENIMLPLSItklsrqeaemryqevtealgiteigskypdeiSGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:cd03215   92 DLSVAENIALSSLL--------------------------------SGGNQQKVVLARWLARDPRVLILDEPTRGVDVGA 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504427498 179 AQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03215  140 KAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 1-187 1.86e-22

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 92.26  E-value: 1.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqLS 80
Cdd:PRK10895   1 MATLTAKNLAKAYKGRR----VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLP---LH 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 YFRKKDVGFIFQDYNVLHTLTVRENIMLPLSITK-LSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALI 159
Cdd:PRK10895  74 ARARRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153

                        170       180
                 ....*....|....*....|....*...
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLE 187
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIE 181
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
6-237 1.92e-22

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 95.94  E-value: 1.92e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKK 85
Cdd:PRK10790 343 IDNVSFAYRDDNL---VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVL----RQ 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  86 DVGFIFQDYNVLHTlTVRENImlplsitKLSRQEAEMRYQEVTEALGITEIGSKYPDEI-----------SGGQKQRTAA 154
Cdd:PRK10790 416 GVAMVQQDPVVLAD-TFLANV-------TLGRDISEEQVWQALETVQLAELARSLPDGLytplgeqgnnlSVGQKQLLAL 487

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmkTTIVMVTHDPVAASYANRVIMLKDGQI-----HTELFQGD 229
Cdd:PRK10790 488 ARVLVQTPQILILDEATANIDSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAveqgtHQQLLAAQ 565


                 ....*...
gi 504427498 230 QPVSQFYQ 237
Cdd:PRK10790 566 GRYWQMYQ 573
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 1-221 3.30e-22

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: 90.78  E-value: 3.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISsidNVTRGTIEINGqDIT--RMSNKQ 78
Cdd:cd03233    1 ASTLSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALA---NRTEGNVSVEG-DIHynGIPYKE 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 LSYFRKKDVGFIFQDYNVLHTLTVRENImlplsitklsrqEAEMRYQevtealgiteiGSKYPDEISGGQKQRTAAARAL 158
Cdd:cd03233   77 FAEKYPGEIIYVSEEDVHFPTLTVRETL------------DFALRCK-----------GNEFVRGISGGERKRVSIAEAL 133

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYA--NRVIMLKDGQI 221
Cdd:cd03233  134 VSRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQASDEIYDlfDKVLVLYEGRQ 198
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 3-221 5.54e-22

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 92.09  E-value: 5.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSY- 81
Cdd:COG4152    1 MLELKGLTKRFGDKT----AVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRRIGYl 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 ------FRKkdvgfifqdynvlhtLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAA 155
Cdd:COG4152   77 peerglYPK---------------MKVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLI 141

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 156 RALISKPAIVFADEPTGALDSkSAQDLLKrlETINQQMK--TTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:COG4152  142 AALLHDPELLILDEPFSGLDP-VNVELLK--DVIRELAAkgTTVIFSSHQmELVEELCDRIVIINKGRK 207
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 4-224 6.79e-22

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 94.10  E-value: 6.79e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDN------------------------- 58
Cdd:TIGR03269   1 IEVKNLTKKFDGK----EVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyeptsgriiyhvalcekcgyverps 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   59 -------VTRGTIEINGQDITRMSNKQLSYFRKKdVGFIFQDYNVLH-TLTVRENIMLPLSITKLSRQEAEMRYQEVTEA 130
Cdd:TIGR03269  77 kvgepcpVCGGTLEPEEVDFWNLSDKLRRRIRKR-IAIMLQRTFALYgDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEM 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  131 LGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASY 209
Cdd:TIGR03269 156 VQLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPeVIEDL 235

                         250
                  ....*....|....*
gi 504427498  210 ANRVIMLKDGQIHTE 224
Cdd:TIGR03269 236 SDKAIWLENGEIKEE 250
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 3-221 1.42e-21

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: 89.45  E-value: 1.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQSyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlsYF 82
Cdd:cd03248   11 IVKFQNVTFAYPTRPDT-LVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKdVGFIFQDyNVLHTLTVRENIMLPLSITKLSR-QEAEMRYQE---VTE-ALGI-TEIGSKyPDEISGGQKQRTAAAR 156
Cdd:cd03248   87 HSK-VSLVGQE-PVLFARSLQDNIAYGLQSCSFECvKEAAQKAHAhsfISElASGYdTEVGEK-GSQLSGGQKQRVAIAR 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLKRLETINQqmKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03248  164 ALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVERADQILVLDGGRI 226
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 16-219 1.81e-21

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: 88.45  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  16 KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISS--IDNVTRGTIEINGQDITRMSNKQLSYFRKKDVgfifqd 93
Cdd:cd03232   16 KGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNFQRSTGYVEQQDV------ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  94 ynvlH--TLTVRENIMLplsitklsrqEAEMRyqevtealgiteigskypdEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:cd03232   90 ----HspNLTVREALRF----------SALLR-------------------GLSVEQRKRLTIGVELAAKPSILFLDEPT 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504427498 172 GALDSKSAQ---DLLKRLETINQqmktTIVMVTHDPVAA--SYANRVIMLKDG 219
Cdd:cd03232  137 SGLDSQAAYnivRFLKKLADSGQ----AILCTIHQPSASifEKFDRLLLLKRG 185
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 3-203 3.15e-21

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: 92.31  E-value: 3.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNvtrgtiEINGQDITRMSNKqlsyf 82
Cdd:TIGR03719   4 IYTMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------DFNGEARPQPGIK----- 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   83 rkkdVGFIFQDYNVLHTLTVRENIMLPLSITK------------LSRQEAEM--------RYQEVTEALGITEIGSKY-- 140
Cdd:TIGR03719  70 ----VGYLPQEPQLDPTKTVRENVEEGVAEIKdaldrfneisakYAEPDADFdklaaeqaELQEIIDAADAWDLDSQLei 145

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498  141 -------PD------EISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLetinQQMKTTIVMVTHD 203
Cdd:TIGR03719 146 amdalrcPPwdadvtKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHL----QEYPGTVVAVTHD 217
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
2-221 3.50e-21

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 89.46  E-value: 3.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNK-----KQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditrmsn 76
Cdd:PRK15112   3 TLLEVRNLSKTFRYRtgwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 kQLSY----FRKKDVGFIFQDYNVlhTLTVRENIM----LPLSI-TKLSRQEAEMRYQEVTEALGI-TEIGSKYPDEISG 146
Cdd:PRK15112  76 -PLHFgdysYRSQRIRMIFQDPST--SLNPRQRISqildFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAP 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 147 GQKQRTAAARALISKPAIVFADEPTGALD-SKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:PRK15112 153 GQKQRLGLARALILRPKVIIADEALASLDmSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEV 228
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 1-220 4.01e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 91.69  E-value: 4.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKT-TLLNVI----SSIDNVTRGTIEINGQDITRMS 75
Cdd:PRK15134   3 QPLLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpSPPVVYPSGDIRFHGESLLHAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 NKQLSYFRKKDVGFIFQD----YNVLHTLtvRENIMLPLSITKLSRQEAEmRYQEVT--EALGITEIGSK---YPDEISG 146
Cdd:PRK15134  83 EQTLRGVRGNKIAMIFQEpmvsLNPLHTL--EKQLYEVLSLHRGMRREAA-RGEILNclDRVGIRQAAKRltdYPHQLSG 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 147 GQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQ 220
Cdd:PRK15134 160 GERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNlSIVRKLADRVAVMQNGR 234
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 23-221 4.28e-21

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 88.59  E-value: 4.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDN--VTRGTIEINGQDITRMSNKQlsyfR-KKDVGFIFQD------ 93
Cdd:COG0396   16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPDE----RaRAGIFLAFQYpveipg 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  94 ---YNVLHTLT--VRENimlplsitKLSRQEAEMRYQEVTEALGI-TEIGSKYPDE-ISGGQKQRTAAARALISKPAIVF 166
Cdd:COG0396   92 vsvSNFLRTALnaRRGE--------ELSAREFLKLLKEKMKELGLdEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 167 ADEPTGALDSksaqDLLKRL-ETINQQMK--TTIVMVTHDPVAASY--ANRVIMLKDGQI 221
Cdd:COG0396  164 LDETDSGLDI----DALRIVaEGVNKLRSpdRGILIITHYQRILDYikPDFVHVLVDGRI 219
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 3-229 9.38e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 90.51  E-value: 9.38e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKQsyeaLKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEInGQDItrmsnkQLSYF 82
Cdd:COG0488  315 VLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV------KIGYF 383

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RkkdvgfifQDYNVLH-TLTVRENImlplsitklsRQEAE-MRYQEVTEALGI---------TEIGSkypdeISGGQKQR 151
Cdd:COG0488  384 D--------QHQEELDpDKTVLDEL----------RDGAPgGTEQEVRGYLGRflfsgddafKPVGV-----LSGGEKAR 440

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 152 TAAARALISKPAIVFADEPTGALDsksaqdllkrLETIN------QQMKTTIVMVTHDPvaasY-----ANRVIMLKDGQ 220
Cdd:COG0488  441 LALAKLLLSPPNVLLLDEPTNHLD----------IETLEaleealDDFPGTVLLVSHDR----YfldrvATRILEFEDGG 506


                 ....*....
gi 504427498 221 IhtELFQGD 229
Cdd:COG0488  507 V--REYPGG 513
cbiO PRK13645
energy-coupling factor transporter ATPase;
6-221 1.08e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 88.53  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGNKKQ-SYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLN-----VISSIDNVTRGTIEINGqDITRMsnKQL 79
Cdd:PRK13645   9 LDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQltnglIISETGQTIVGDYAIPA-NLKKI--KEV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 SYFRKkDVGFIFQ--DYNVLHTlTVRENIML-PLSITKlSRQEAemrYQEVTEALGITEIGSKY----PDEISGGQKQRT 152
Cdd:PRK13645  86 KRLRK-EIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGE-NKQEA---YKKVPELLKLVQLPEDYvkrsPFELSGGQKRRV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 153 AAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTH--DPVaASYANRVIMLKDGQI 221
Cdd:PRK13645 160 ALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHnmDQV-LRIADEVIVMHEGKV 229
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 4-242 1.47e-20

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: 90.57  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    4 LKVSHVSKIYGNKKqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFr 83
Cdd:TIGR01193 474 IVINDVSYSYGYGS---NILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQF- 549

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   84 kkdVGFIFQDyNVLHTLTVRENIMLPlsitklSRQEAEMryQEVTEALGITEIG--------------SKYPDEISGGQK 149
Cdd:TIGR01193 550 ---INYLPQE-PYIFSGSILENLLLG------AKENVSQ--DEIWAACEIAEIKddienmplgyqtelSEEGSSISGGQK 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  150 QRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmktTIVMVTHDPVAASYANRVIMLKDGQI-----HTE 224
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQSDKIIVLDHGKIieqgsHDE 694

                         250
                  ....*....|....*...
gi 504427498  225 LFQGDqpvsQFYQEIIHN 242
Cdd:TIGR01193 695 LLDRN----GFYASLIHN 708
cbiO PRK13644
energy-coupling factor transporter ATPase;
22-224 4.36e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 86.58  E-value: 4.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkQLSYFRKKdVGFIFQDYNVLHT-L 100
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGIRKL-VGIVFQNPETQFVgR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENimLPLSITKLSRQEAEMRyQEVTEALGITEIGsKY----PDEISGGQKQRTAAARALISKPAIVFADEPTGALDS 176
Cdd:PRK13644  94 TVEED--LAFGPENLCLPPIEIR-KRVDRALAEIGLE-KYrhrsPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504427498 177 KSAQDLLKRLETINQQMKtTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK13644 170 DSGIAVLERIKKLHEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLE 216
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
4-237 5.58e-20

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 88.54  E-value: 5.58e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmSNKQLSYFR 83
Cdd:PRK11176 342 IEFRNVTFTYPGKEVP--ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLR 416

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQdyNV-LHTLTVRENIMLPlSITKLSRQE----AEMRY-QEVTEAL--GI-TEIGskypdE----ISGGQKQ 150
Cdd:PRK11176 417 NQ-VALVSQ--NVhLFNDTIANNIAYA-RTEQYSREQieeaARMAYaMDFINKMdnGLdTVIG-----EngvlLSGGQRQ 487

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 151 RTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETInQQMKTTIVmVTHDPVAASYANRVIMLKDGQI-----HTEL 225
Cdd:PRK11176 488 RIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLV-IAHRLSTIEKADEILVVEDGEIvergtHAEL 565

                        250
                 ....*....|..
gi 504427498 226 FQGDQPVSQFYQ 237
Cdd:PRK11176 566 LAQNGVYAQLHK 577
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 24-221 7.26e-20

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 85.52  E-value: 7.26e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  24 KDIHFTVEKGGFVAIMGPSGSGKT----TLLNVISSIDNVTRGTIEINGQDITrmsnkqLSYFRKKDVGFIFQD----YN 95
Cdd:PRK10418  20 HGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA------PCALRGRKIATIMQNprsaFN 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  96 VLHTLT--VREnimlplSITKLSRQEAEMRYQEVTEALGITE---IGSKYPDEISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:PRK10418  94 PLHTMHthARE------TCLALGKPADDATLTAALEAVGLENaarVLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEP 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504427498 171 TGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK10418 168 TTDLDVVAQARILDLLESIVQKRALGMLLVTHDmGVVARLADDVAVMSHGRI 219
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-202 1.47e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 85.63  E-value: 1.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   2 SILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqlsy 81
Cdd:PRK13537   6 APIDFRNVEKRYGDKL----VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRAR----- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 FRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:PRK13537  77 HARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTH 202
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLARGK-TILLTTH 196
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 21-221 7.84e-19

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 81.69  E-value: 7.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmSNKQLSYFRKKdVGFIFQDyNVLHTL 100
Cdd:cd03369   22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDI---STIPLEDLRSS-LTIIPQD-PTLFSG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENImlplsitklsrqEAEMRY--QEVTEALGITEIGSKypdeISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:cd03369   97 TIRSNL------------DPFDEYsdEEIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504427498 179 AQDLLKrleTINQQMK-TTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:cd03369  161 DALIQK---TIREEFTnSTILTIAHRLRTIIDYDKILVMDAGEV 201
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 9-203 1.16e-18

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 84.79  E-value: 1.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   9 VSKIYGNKKQsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNvtrgtiEINGQ-----DITrmsnkqlsyfr 83
Cdd:PRK11819  12 VSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDK------EFEGEarpapGIK----------- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kkdVGFIFQDYNVLHTLTVRENIMLPLSITK--LSRQE-----------------AEM-RYQEVTEALGITEIGSKY--- 140
Cdd:PRK11819  72 ---VGYLPQEPQLDPEKTVRENVEEGVAEVKaaLDRFNeiyaayaepdadfdalaAEQgELQEIIDAADAWDLDSQLeia 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 141 --------PDE----ISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLetinQQMKTTIVMVTHD 203
Cdd:PRK11819 149 mdalrcppWDAkvtkLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESVAWLEQFL----HDYPGTVVAVTHD 219
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
22-220 1.68e-18

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 83.03  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI--DN--VTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQDynvl 97
Cdd:COG4170   22 AVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGItkDNwhVTADRFRWNGIDLLKLSPRERRKIIGREIAMIFQE---- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  98 htltvrenimlPLS----ITKLSRQEAEM----------------RYQEVTEAL---GITE---IGSKYPDEISGGQKQR 151
Cdd:COG4170   98 -----------PSScldpSAKIGDQLIEAipswtfkgkwwqrfkwRKKRAIELLhrvGIKDhkdIMNSYPHELTEGECQK 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 152 TAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVA-ASYANRVIMLKDGQ 220
Cdd:COG4170  167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESiSQWADTITVLYCGQ 236
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 3-203 2.26e-18

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 81.57  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyf 82
Cdd:PRK11300   5 LLSVSGLMMRFG----GLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 rKKDVGFIFQDYNVLHTLTVRENIMLP------------LSITKLSRQ---EAEMRYQEVTEALGITEIGSKYPDEISGG 147
Cdd:PRK11300  79 -RMGVVRTFQHVRLFREMTVIENLLVAqhqqlktglfsgLLKTPAFRRaesEALDRAATWLERVGLLEHANRQAGNLAYG 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 148 QKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD 203
Cdd:PRK11300 158 QQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
4-219 3.49e-18

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 83.30  E-value: 3.49e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqLSYfr 83
Cdd:PRK09700   6 ISMAGIGKSFG----PVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK-LAA-- 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDYNVLHTLTVRENIMLPLSITK-------LSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAAR 156
Cdd:PRK09700  79 QLGIGIIYQELSVIDELTVLENLYIGRHLTKkvcgvniIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAK 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLkrleTINQQMK---TTIVMVTHD-PVAASYANRVIMLKDG 219
Cdd:PRK09700 159 TLMLDAKVIIMDEPTSSLTNKEVDYLF----LIMNQLRkegTAIVYISHKlAEIRRICDRYTVMKDG 221
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
17-243 4.67e-18

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 82.84  E-value: 4.67e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  17 KQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMsnkQLSYFRKK-----DVGFIF 91
Cdd:PRK10789 325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRlavvsQTPFLF 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  92 QDynvlhtlTVRENIMLPLSITKLSRQEAEMRYQEVTEalGITEIGSKYPDEI-------SGGQKQRTAAARALISKPAI 164
Cdd:PRK10789 402 SD-------TVANNIALGRPDATQQEIEHVARLASVHD--DILRLPQGYDTEVgergvmlSGGQKQRISIARALLLNAEI 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 165 VFADEPTGALDSKSAQDLLKRLETINQQmkTTIVMVTHDPVAASYANRVIMLKDGQI-----HTELFQgdqpVSQFYQEI 239
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGEG--RTVIISAHRLSALTEASEILVMQHGHIaqrgnHDQLAQ----QSGWYRDM 546


                 ....
gi 504427498 240 IHNQ 243
Cdd:PRK10789 547 YRYQ 550
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-224 7.87e-18

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 79.92  E-value: 7.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITrmsNKQLS 80
Cdd:PRK11614   3 KVMLSFDKVSAHYGK----IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDIT---DWQTA 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 YFRKKDVGFIFQDYNVLHTLTVRENimLPLSITKLSRQEAEMRYQEVTEALG-ITEIGSKYPDEISGGQKQRTAAARALI 159
Cdd:PRK11614  76 KIMREAVAIVPEGRRVFSRMTVEEN--LAMGGFFAERDQFQERIKWVYELFPrLHERRIQRAGTMSGGEQQMLAIGRALM 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 21-216 8.23e-18

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: 78.94  E-value: 8.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSN---KQLSYFRKKDvgfifqdyNVL 97
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDephENILYLGHLP--------GLK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   98 HTLTVRENimlpLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDsK 177
Cdd:TIGR01189  86 PELSALEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-K 160

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 504427498  178 SAQDLLKRLETINQQMKTTIVMVTHDPVAASYAnRVIML 216
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA-RELRL 198
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
4-202 9.98e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 81.03  E-value: 9.98e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnkQLSYFR 83
Cdd:PRK13536  42 IDLAGVSKSYGDKA----VVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLAR 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKdVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPA 163
Cdd:PRK13536 114 AR-IGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTH 202
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLARGK-TILLTTH 230
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 16-219 1.01e-17

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 82.46  E-value: 1.01e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    16 KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISsiDNVTRGTIEingqDITRMSNkqlsyFRKKD------VGF 89
Cdd:TIGR00956  772 KKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLA--ERVTTGVIT----GGDRLVN-----GRPLDssfqrsIGY 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    90 IFQDYNVLHTLTVRENIM------LPLSITKlsrqEAEMRY-QEVTEALGITEigskYPDEISG--------GQKQRTAA 154
Cdd:TIGR00956  841 VQQQDLHLPTSTVRESLRfsaylrQPKSVSK----SEKMEYvEEVIKLLEMES----YADAVVGvpgeglnvEQRKRLTI 912

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498   155 ARALISKPA-IVFADEPTGALDSKSAQ---DLLKRLETINQQMKTTIvmvtHDPVAASYA--NRVIMLKDG 219
Cdd:TIGR00956  913 GVELVAKPKlLLFLDEPTSGLDSQTAWsicKLMRKLADHGQAILCTI----HQPSAILFEefDRLLLLQKG 979
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 37-244 1.55e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 79.75  E-value: 1.55e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  37 AIMGPSGSGKTTLLNVISSI-DNVT----RGTIEINGQDItrMSNKQLSYFRKKdVGFIFQDYNVLhTLTVRENIMLPLS 111
Cdd:PRK14271  51 SLMGPTGSGKTTFLRTLNRMnDKVSgyrySGDVLLGGRSI--FNYRDVLEFRRR-VGMLFQRPNPF-PMSIMDNVLAGVR 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 112 ITKL-SRQE----AEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRL 186
Cdd:PRK14271 127 AHKLvPRKEfrgvAQARLTEVGLWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFI 206

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498 187 ETINQQMktTIVMVTHD-PVAASYANRVIMLKDGQIHTElfqgdQPVSQFYQEIIHNQS 244
Cdd:PRK14271 207 RSLADRL--TVIIVTHNlAQAARISDRAALFFDGRLVEE-----GPTEQLFSSPKHAET 258
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
23-229 1.83e-17

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 79.06  E-value: 1.83e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKqlSYFRKkdVGFIFQDYNVLHTLTV 102
Cdd:PRK10575  27 LHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSK--AFARK--VAYLPQQLPAAEGMTV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENImlplSITK------LSRQEAEMRyQEVTEAL---GITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGA 173
Cdd:PRK10575 103 RELV----AIGRypwhgaLGRFGAADR-EKVEEAIslvGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 174 LDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI-----HTELFQGD 229
Cdd:PRK10575 178 LDIAHQVDVLALVHRLSQERGLTVIAVLHDiNMAARYCDYLVALRGGEMiaqgtPAELMRGE 239
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 23-204 1.93e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 77.99  E-value: 1.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS-NKQLSYFRKKdvgfifqdyNVLH-TL 100
Cdd:PRK13539  18 FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDvAEACHYLGHR---------NAMKpAL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENIMLPLSItklsRQEAEMRYQEVTEALG---ITEIGSKYpdeISGGQKQRTAAARALISKPAIVFADEPTGALDSk 177
Cdd:PRK13539  89 TVAENLEFWAAF----LGGEELDIAAALEAVGlapLAHLPFGY---LSAGQKRRVALARLLVSNRPIWILDEPTAALDA- 160

                        170       180
                 ....*....|....*....|....*..
gi 504427498 178 SAQDLLKRLETINQQMKTTIVMVTHDP 204
Cdd:PRK13539 161 AAVALFAELIRAHLAQGGIVIAATHIP 187
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-225 2.46e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 80.83  E-value: 2.46e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSkiygnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQ---- 78
Cdd:COG1129  256 VLEVEGLS--------VGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaira 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 -LSYF---RKKDvGfIFQDynvlhtLTVRENIMLPL--SITK---LSRQEAEMRYQEVTEALGIteigsKYPD------E 143
Cdd:COG1129  328 gIAYVpedRKGE-G-LVLD------LSIRENITLASldRLSRgglLDRRRERALAEEYIKRLRI-----KTPSpeqpvgN 394

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 144 ISGGQKQRTAAARALISKPAIVFADEPT-----GAldsKSA-QDLLKRLetiNQQmKTTIVMVTHD-PVAASYANRVIML 216
Cdd:COG1129  395 LSGGNQQKVVLAKWLATDPKVLILDEPTrgidvGA---KAEiYRLIREL---AAE-GKAVIVISSElPELLGLSDRILVM 467


                 ....*....
gi 504427498 217 KDGQIHTEL 225
Cdd:COG1129  468 REGRIVGEL 476
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 23-219 4.93e-17

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: 77.37  E-value: 4.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRKKDVGFIFQDYNVLHTlTV 102
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-TV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENIMLPLSITKlsrqeaeMRYQEVTEALGI------------TEIGSKYPDeISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:cd03290   96 EENITFGSPFNK-------QRYKAVTDACSLqpdidllpfgdqTEIGERGIN-LSGGQRQRICVARALYQNTNIVFLDDP 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504427498 171 TGALDSKSAQDLLKR--LETInQQMKTTIVMVTHDPVAASYANRVIMLKDG 219
Cdd:cd03290  168 FSALDIHLSDHLMQEgiLKFL-QDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 4-221 5.26e-17

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: 76.80  E-value: 5.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDN--VTRGTIEINGQDITRMSNKQLSy 81
Cdd:cd03217    1 LEIKDLHVSVGGK----EILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPEERA- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  82 frKKDVGFIFQDynvlhtltvrenimlPLSITKLSRQEAeMRYqeVTEALgiteigskypdeiSGGQKQRTAAARALISK 161
Cdd:cd03217   76 --RLGIFLAFQY---------------PPEIPGVKNADF-LRY--VNEGF-------------SGGEKKRNEILQLLLLE 122

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498 162 PAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDPVAASY--ANRVIMLKDGQI 221
Cdd:cd03217  123 PDLAILDEPDSGLDIDALRLVAEVINKLREE-GKSVLIITHYQRLLDYikPDRVHVLYDGRI 183
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 22-226 4.62e-16

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: 77.36  E-value: 4.62e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmsNKQLSYFRKKdVGFIFQDYNVLHTLT 101
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDI----ETNLDAVRQS-LGMCPQHNILFHHLT 1019

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   102 VRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALD---SKS 178
Cdd:TIGR01257 1020 VAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDpysRRS 1099

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 504427498   179 AQDLLKRLETinqqmKTTIVMVTHDPVAAS-YANRVIMLKDGQIH---TELF 226
Cdd:TIGR01257 1100 IWDLLLKYRS-----GRTIIMSTHHMDEADlLGDRIAIISQGRLYcsgTPLF 1146
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 4-203 5.86e-16

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 72.48  E-value: 5.86e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTieingqdITRMSNKQLSYFr 83
Cdd:cd03221    1 IELENLSKTYGGKL----LLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI-------VTWGSTVKIGYF- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kkdvgfifqdynvlhtltvrenimlplsitklsrqeaemryqevtealgiteigskypDEISGGQKQRTAAARALISKPA 163
Cdd:cd03221   69 ----------------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504427498 164 IVFADEPTGALDSKSaqdllkrLETINQQMKT---TIVMVTHD 203
Cdd:cd03221   91 LLLLDEPTNHLDLES-------IEALEEALKEypgTVILVSHD 126
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 15-218 8.27e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 76.61  E-value: 8.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   15 NKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINgqDITRMSNKQLSYFRKKdVGFIFQDy 94
Cdd:PTZ00265  393 DTRKDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIIN--DSHNLKDINLKWWRSK-IGVVSQD- 468

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   95 NVLHTLTVRENIMLPLSITK----LSRQ---------------------------------------EAEMRYQ------ 125
Cdd:PTZ00265  469 PLLFSNSIKNNIKYSLYSLKdleaLSNYynedgndsqenknkrnscrakcagdlndmsnttdsneliEMRKNYQtikdse 548

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  126 --EVTEALGITEIGSKYPDE-----------ISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQ 192
Cdd:PTZ00265  549 vvDVSKKVLIHDFVSALPDKyetlvgsnaskLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGN 628

                         250       260
                  ....*....|....*....|....*.
gi 504427498  193 MKTTIVMVTHDPVAASYANRVIMLKD 218
Cdd:PTZ00265  629 ENRITIIIAHRLSTIRYANTIFVLSN 654
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 23-235 9.22e-16

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 76.52  E-value: 9.22e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLN-VISSIDNVtRGTIEINGQditrmsnkqlsyfrkkdVGFIFQDyNVLHTLT 101
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDKV-EGHVHMKGS-----------------VAYVPQQ-AWIQNDS 714

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   102 VRENIMLplsitklSRQEAEMRYQEVTEALGI------------TEIGSKYPDeISGGQKQRTAAARALISKPAIVFADE 169
Cdd:TIGR00957  715 LRENILF-------GKALNEKYYQQVLEACALlpdleilpsgdrTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDD 786

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504427498   170 PTGALDSKSAQDLLKRLETINQQMKT-TIVMVTHDPVAASYANRVIMLKDGQI-----HTELFQGDQPVSQF 235
Cdd:TIGR00957  787 PLSAVDAHVGKHIFEHVIGPEGVLKNkTRILVTHGISYLPQVDVIIVMSGGKIsemgsYQELLQRDGAFAEF 858
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 23-204 9.55e-16

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 73.84  E-value: 9.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIssidnvtrgtieingqdITRMSNKQLSYFRKKDVGFIFQDYNVLhtltv 102
Cdd:COG2401   46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLL-----------------AGALKGTPVAGCVDVPDNQFGREASLI----- 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 rENIMLPLSITklsrqeaemryqEVTEALGITEIGSKY-----PDEISGGQKQRTAAARALISKPAIVFADEPTGALDSK 177
Cdd:COG2401  104 -DAIGRKGDFK------------DAVELLNAVGLSDAVlwlrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170

                        170       180
                 ....*....|....*....|....*..
gi 504427498 178 SAQDLLKRLETINQQMKTTIVMVTHDP 204
Cdd:COG2401  171 TAKRVARNLQKLARRAGITLVVATHHY 197
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 3-208 1.12e-15

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 74.43  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNkkqsYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNV-----TRGTIEINGQDITRMSNK 77
Cdd:PRK14243  10 VLRTENLNVYYGS----FLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDLipgfrVEGKVTFHGKNLYAPDVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 QLSYFRKkdVGFIFQDYNVLHTlTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDE---ISGGQKQRTAA 154
Cdd:PRK14243  86 PVEVRRR--IGMVFQKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCI 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAqdllKRLETINQQMKT--TIVMVTHDPVAAS 208
Cdd:PRK14243 163 ARAIAVQPEVILMDEPCSALDPIST----LRIEELMHELKEqyTIIIVTHNMQQAA 214
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 3-221 1.18e-15

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 75.86  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGnkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS-NK--QL 79
Cdd:PRK15439  11 LLCARSISKQYS----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpAKahQL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 SYFrkkdvgFIFQDYNVLHTLTVRENIMLPLSitklSRQEAEMRYQEVtealgITEIGSKYPDEISGG-----QKQRTAA 154
Cdd:PRK15439  87 GIY------LVPQEPLLFPNLSVKENILFGLP----KRQASMQKMKQL-----LAALGCQLDLDSSAGslevaDRQIVEI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK15439 152 LRGLMRDSRILILDEPTASLTPAETERLFSRIREL-LAQGVGIVFISHKlPEIRQLADRISVMRDGTI 218
hmuV PRK13547
heme ABC transporter ATP-binding protein;
23-221 1.71e-15

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 74.09  E-value: 1.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS-------SIDNVT-RGTIEINGQDITRMSNKQLSYFR-----KKDVGF 89
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAgdltgggAPRGARvTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPAF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  90 IFqdynvlhtlTVRENIML-----PLSITKLSRQEAEMRYQEVTEAlGITEIGSKYPDEISGGQKQRTAAARAL------ 158
Cdd:PRK13547  97 AF---------SAREIVLLgryphARRAGALTHRDGEIAWQALALA-GATALVGRDVTTLSGGELARVQFARVLaqlwpp 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498 159 ---ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDP-VAASYANRVIMLKDGQI 221
Cdd:PRK13547 167 hdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPnLAARHADRIAMLADGAI 233
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
22-220 1.76e-15

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 75.33  E-value: 1.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditrmsnkQLSYFRKKD-----VGFIFQDYNV 96
Cdd:PRK11288  19 ALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQ--------EMRFASTTAalaagVAIIYQELHL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  97 LHTLTVRENIML---PLSITKLSRQEAEMRYQEVTEALGItEIGSKYP-DEISGGQKQRTAAARALISKPAIVFADEPTG 172
Cdd:PRK11288  91 VPEMTVAENLYLgqlPHKGGIVNRRLLNYEAREQLEHLGV-DIDPDTPlKYLSIGQRQMVEIAKALARNARVIAFDEPTS 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504427498 173 ALDSKSAQDLLKRLETINQQMKtTIVMVTH--DPVAAsYANRVIMLKDGQ 220
Cdd:PRK11288 170 SLSAREIEQLFRVIRELRAEGR-VILYVSHrmEEIFA-LCDAITVFKDGR 217
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-186 1.99e-15

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 75.06  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSkIYGNKKQsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyF 82
Cdd:COG3845  257 VLEVENLS-VRDDRGV--PALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRE---R 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKDVGFIFQD---YNVLHTLTVRENIMLPLSITK-------LSRQEAEMRYQEVTEALGI------TEIGSkypdeISG 146
Cdd:COG3845  331 RRLGVAYIPEDrlgRGLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEFDVrtpgpdTPARS-----LSG 405

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504427498 147 GQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRL 186
Cdd:COG3845  406 GNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRL 445
PLN03130 PLN03130
ABC transporter C family member; Provisional
 23-224 2.00e-15

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 75.54  E-value: 2.00e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLN-VISSIDNVTRGTIEINGQditrmsnkqLSYFRKkdVGFIFQdynvlhtLT 101
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISaMLGELPPRSDASVVIRGT---------VAYVPQ--VSWIFN-------AT 694

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  102 VRENIMLPLSItklsrqEAEmRYQEVTEALGI------------TEIGSKYPDeISGGQKQRTAAARALISKPAIVFADE 169
Cdd:PLN03130  695 VRDNILFGSPF------DPE-RYERAIDVTALqhdldllpggdlTEIGERGVN-ISGGQKQRVSMARAVYSNSDVYIFDD 766

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498  170 PTGALDSKSAQDLLKRleTINQQMK-TTIVMVTHDPVAASYANRVIMLKDGQIHTE 224
Cdd:PLN03130  767 PLSALDAHVGRQVFDK--CIKDELRgKTRVLVTNQLHFLSQVDRIILVHEGMIKEE 820
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 11-237 1.19e-14

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 73.22  E-value: 1.19e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    11 KIYGNKKQSYE--ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISS-IDNVTR---GTIEINGQDITRMSNkqlsyFRK 84
Cdd:TIGR00956   63 RKLKKFRDTKTfdILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASnTDGFHIgveGVITYDGITPEEIKK-----HYR 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    85 KDVGFIFQDYNVLHTLTVRENIML----------PLSITKLSRQEAEMRYQEVTEALGI---TEIGSKYPDEISGGQKQR 151
Cdd:TIGR00956  138 GDVVYNAETDVHFPHLTVGETLDFaarcktpqnrPDGVSREEYAKHIADVYMATYGLSHtrnTKVGNDFVRGVSGGERKR 217

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   152 TAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYA--NRVIMLKDGQIhteLFQGD 229
Cdd:TIGR00956  218 VSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQ---IYFGP 294


                   ....*....
gi 504427498   230 -QPVSQFYQ 237
Cdd:TIGR00956  295 aDKAKQYFE 303
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 1-203 1.20e-14

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 71.30  E-value: 1.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSIL-KVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditrmsnkql 79
Cdd:PRK09544   1 MTSLvSLENVSVSFGQRR----VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK---------- 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  80 syFRkkdVGFIFQDYNVLHTLtvrenimlPLSITKLSRQEAEMRYQEVTEALGITEIGS--KYP-DEISGGQKQRTAAAR 156
Cdd:PRK09544  67 --LR---IGYVPQKLYLDTTL--------PLTVNRFLRLRPGTKKEDILPALKRVQAGHliDAPmQKLSGGETQRVLLAR 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD 203
Cdd:PRK09544 134 ALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHD 180
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 4-203 1.92e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 70.84  E-value: 1.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTL---LNVISSIDNVTR--GTIEINGQDI-TRMSNk 77
Cdd:PRK14258   8 IKVNNLSFYYDTQK----ILEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVRveGRVEFFNQNIyERRVN- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  78 qLSYFRKKdVGFIFQDYNvLHTLTVRENIMLPLS------------ITKLSRQEAEMrYQEVTEALgiteigSKYPDEIS 145
Cdd:PRK14258  83 -LNRLRRQ-VSMVHPKPN-LFPMSVYDNVAYGVKivgwrpkleiddIVESALKDADL-WDEIKHKI------HKSALDLS 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 146 GGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD 203
Cdd:PRK14258 153 GGQQQRLCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHN 210
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 23-187 5.05e-14

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 68.44  E-value: 5.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmsNKQLSYFRKKdVGFIFQDYNVLHTLTV 102
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQKQ-LCFVGHRSGINPYLTL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENIMLPLSITKLSrqeaemryQEVTEALGITEIGS--KYP-DEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSA 179
Cdd:PRK13540  92 RENCLYDIHFSPGA--------VGITELCRLFSLEHliDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSL 163


                 ....*...
gi 504427498 180 QDLLKRLE 187
Cdd:PRK13540 164 LTIITKIQ 171
PLN03232 PLN03232
ABC transporter C family member; Provisional
 17-242 7.11e-14

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 71.16  E-value: 7.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   17 KQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLN-VISSIDNVTRGTIEINGQditrmsnkqLSYFRKkdVGFIFQdyn 95
Cdd:PLN03232  627 KTSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISaMLGELSHAETSSVVIRGS---------VAYVPQ--VSWIFN--- 692

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   96 vlhtLTVRENIMLPlsitklSRQEAEmRYQEVTEALGI------------TEIGSKYPDeISGGQKQRTAAARALISKPA 163
Cdd:PLN03232  693 ----ATVRENILFG------SDFESE-RYWRAIDVTALqhdldllpgrdlTEIGERGVN-ISGGQKQRVSMARAVYSNSD 760

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  164 IVFADEPTGALDSKSAQDLLKRLETINQQMKTTiVMVTHDPVAASYANRVIMLKDGQIHTE-LFQGDQPVSQFYQEIIHN 242
Cdd:PLN03232  761 IYIFDDPLSALDAHVAHQVFDSCMKDELKGKTR-VLVTNQLHFLPLMDRIILVSEGMIKEEgTFAELSKSGSLFKKLMEN 839
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-220 1.26e-13

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 69.06  E-value: 1.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   1 MSILKVSHVSKIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI--DN--VTRGTIEINGQDITRMSN 76
Cdd:PRK15093   1 MPLLDIRNLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkDNwrVTADRMRFDDIDLLRLSP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  77 KQlsyfRKKDVG----FIFQDYNvlHTLTVRENIMLPL--SITKLS-----RQEAEMRYQEVTEAL---GITE---IGSK 139
Cdd:PRK15093  81 RE----RRKLVGhnvsMIFQEPQ--SCLDPSERVGRQLmqNIPGWTykgrwWQRFGWRKRRAIELLhrvGIKDhkdAMRS 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 140 YPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHD-PVAASYANRVIMLKD 218
Cdd:PRK15093 155 FPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDlQMLSQWADKINVLYC 234


                 ..
gi 504427498 219 GQ 220
Cdd:PRK15093 235 GQ 236
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 23-231 1.99e-13

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 69.55  E-value: 1.99e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGqditRMS-NKQLSYFRKKdvgfifqdynvlhtlT 101
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG----RISfSPQTSWIMPG---------------T 502

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   102 VRENIMLPLSITklsrqeaEMRYQEVTEALGITEIGSKYPDE-----------ISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:TIGR01271  503 IKDNIIFGLSYD-------EYRYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 575

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498   171 TGALDSKSAQDLLKRLETINQQMKTTIVmVTHDPVAASYANRVIMLKDGQIH-----TELfQGDQP 231
Cdd:TIGR01271  576 FTHLDVVTEKEIFESCLCKLMSNKTRIL-VTSKLEHLKKADKILLLHEGVCYfygtfSEL-QAKRP 639
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 23-187 4.86e-13

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 68.40  E-value: 4.86e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNvTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDYNVLhTLTV 102
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTW----RKAFGVIPQKVFIF-SGTF 1308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   103 RENImlplsitKLSRQEAEMRYQEVTEALGITEIGSKYPDE-----------ISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:TIGR01271 1309 RKNL-------DPYEQWSDEEIWKVAEEVGLKSVIEQFPDKldfvlvdggyvLSNGHKQLMCLARSILSKAKILLLDEPS 1381

                          170
                   ....*....|....*.
gi 504427498   172 GALDSKSAQDLLKRLE 187
Cdd:TIGR01271 1382 AHLDPVTLQIIRKTLK 1397
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
25-207 5.32e-13

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 65.60  E-value: 5.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  25 DIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqlSYFRK----------KDVgfifqdy 94
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQRD---EYHQDllylghqpgiKTE------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  95 nvlhtLTVRENIMLPLSITKLSRQEAemryqeVTEALGitEIG-SKYPD----EISGGQKQRTAAARALISKPAIVFADE 169
Cdd:PRK13538  89 -----LTALENLRFYQRLHGPGDDEA------LWEALA--QVGlAGFEDvpvrQLSAGQQRRVALARLWLTRAPLWILDE 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504427498 170 PTGALDSKSAQDLLKRLETINQQ--MkttIVMVTHDPVAA 207
Cdd:PRK13538 156 PFTAIDKQGVARLEALLAQHAEQggM---VILTTHQDLPV 192
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 4-240 5.40e-13

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 68.11  E-value: 5.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKiygnkkqsyEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQ----- 78
Cdd:PRK10762 258 LKVDNLSG---------PGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglang 328

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 ---LSYFRKKDvGFIFQdynvlhtLTVRENIMLPlSITKLSRQEAEMRYQEVTEALG--ITEIGSKYPD------EISGG 147
Cdd:PRK10762 329 ivyISEDRKRD-GLVLG-------MSVKENMSLT-ALRYFSRAGGSLKHADEQQAVSdfIRLFNIKTPSmeqaigLLSGG 399

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 148 QKQRTAAARALISKPAIVFADEPTGALDSKSAQDLlkrLETINQ--QMKTTIVMVTHD-PVAASYANRVIMLKDGQIhte 224
Cdd:PRK10762 400 NQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEI---YQLINQfkAEGLSIILVSSEmPEVLGMSDRILVMHEGRI--- 473

                        250
                 ....*....|....*.
gi 504427498 225 lfQGDQPVSQFYQEII 240
Cdd:PRK10762 474 --SGEFTREQATQEKL 487
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 24-218 5.59e-13

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 68.13  E-value: 5.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   24 KDIHFTVEKGGFVAIMGPSGSGKTTLLNVI----------------SSIDNVTR------------GTIEINGQDITRMS 75
Cdd:PTZ00265 1185 KDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkndhhivfknEHTNDMTNeqdyqgdeeqnvGMKNVNEFSLTKEG 1264

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   76 NKQLSYFRKKDVGFIFQD------YNV-----LHTLTVRENIMLPLSI---TKLSRQEAEMR-YQEVTEALGITEIGSKY 140
Cdd:PTZ00265 1265 GSGEDSTVFKNSGKILLDgvdicdYNLkdlrnLFSIVSQEPMLFNMSIyenIKFGKEDATREdVKRACKFAAIDEFIESL 1344

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  141 PDE-----------ISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASY 209
Cdd:PTZ00265 1345 PNKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKR 1424


                  ....*....
gi 504427498  210 ANRVIMLKD 218
Cdd:PTZ00265 1425 SDKIVVFNN 1433
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 3-237 5.97e-13

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 68.12  E-value: 5.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498     3 ILKVSHVSKIYGNkkQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDI-TRMSNKQlsy 81
Cdd:TIGR01257 1937 ILRLNELTKVYSG--TSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVH--- 2011

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    82 frkKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISK 161
Cdd:TIGR01257 2012 ---QNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGC 2088

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   162 PAIVFADEPTGALDSKSAQDLLKRLETINQQMKtTIVMVTH--DPVAASYANRVIMLK-----------------DGQIH 222
Cdd:TIGR01257 2089 PPLVLLDEPTTGMDPQARRMLWNTIVSIIREGR-AVVLTSHsmEECEALCTRLAIMVKgafqclgtiqhlkskfgDGYIV 2167

                          250       260
                   ....*....|....*....|...
gi 504427498   223 T--------ELFQGDQPVSQFYQ 237
Cdd:TIGR01257 2168 TmkikspkdDLLPDLNPVEQFFQ 2190
PLN03140 PLN03140
ABC transporter G family member; Provisional
 23-239 6.29e-13

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 68.33  E-value: 6.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSidNVTRGTIEingQDItrmsnkQLSYFRKKDVGFI----FQDYNVLH 98
Cdd:PLN03140  896 LREVTGAFRPGVLTALMGVSGAGKTTLMDVLAG--RKTGGYIE---GDI------RISGFPKKQETFArisgYCEQNDIH 964

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   99 T--LTVRENIM------LPLSITKlsrqEAEMRYqeVTEALGITEIGSkYPDEISG---------GQKQRTAAARALISK 161
Cdd:PLN03140  965 SpqVTVRESLIysaflrLPKEVSK----EEKMMF--VDEVMELVELDN-LKDAIVGlpgvtglstEQRKRLTIAVELVAN 1037

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  162 PAIVFADEPTGALDSKSAQDLLKrleTINQQMKT--TIVMVTHDP---VAASYANRVIMLKDGQI--HTELFQGDQPVSQ 234
Cdd:PLN03140 1038 PSIIFMDEPTSGLDARAAAIVMR---TVRNTVDTgrTVVCTIHQPsidIFEAFDELLLMKRGGQViySGPLGRNSHKIIE 1114


                  ....*
gi 504427498  235 FYQEI 239
Cdd:PLN03140 1115 YFEAI 1119
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 28-204 9.58e-13

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: 65.21  E-value: 9.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  28 FTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNkqlSYFRkkDVGFIFQDYNVLHTLTVRENim 107
Cdd:cd03231   21 FTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD---SIAR--GLLYLGHAPGIKTTLSVLEN-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 108 lplsITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLE 187
Cdd:cd03231   94 ----LRFWHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVARFAEAMA 169

                        170
                 ....*....|....*..
gi 504427498 188 TINQQmKTTIVMVTHDP 204
Cdd:cd03231  170 GHCAR-GGMVVLTTHQD 185
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 3-220 1.05e-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: 67.16  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI--DNVTRGTIEINGQDITRMSnkqLS 80
Cdd:TIGR02633   1 LLEMKGIVKTFGGVK----ALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASN---IR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   81 YFRKKDVGFIFQDYNVLHTLTVRENIMLPLSIT----KLSRQEAEMRYQEVTEALGITEIGSKYP-DEISGGQKQRTAAA 155
Cdd:TIGR02633  74 DTERAGIVIIHQELTLVPELSVAENIFLGNEITlpggRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498  156 RALISKPAIVFADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTH--DPVAAsYANRVIMLKDGQ 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDL-KAHGVACVYISHklNEVKA-VCDTICVIRDGQ 218
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
4-217 2.08e-12

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 65.29  E-value: 2.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNkkqSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfr 83
Cdd:PRK15056   7 IVVNDVTVTWRN---GHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 kkdVGFIFQDYNVLHT--LTVRENIMLPL--SITKLSRQEAEMRyQEVTEAL---GITEIGSKYPDEISGGQKQRTAAAR 156
Cdd:PRK15056  80 ---VAYVPQSEEVDWSfpVLVEDVVMMGRygHMGWLRRAKKRDR-QIVTAALarvDMVEFRHRQIGELSGGQKKRVFLAR 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 157 ALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLK 217
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLGSVTEFCDYTVMVK 216
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 23-223 2.10e-12

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: 65.26  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNvTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDYNVLhTLTV 102
Cdd:cd03289   20 LENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKW----RKAFGVIPQKVFIF-SGTF 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENIMlplSITKLSRQEaemrYQEVTEALGITEIGSKYPDE-----------ISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:cd03289   94 RKNLD---PYGKWSDEE----IWKVAEEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSKAKILLLDEPS 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504427498 172 GALDSKSAQDLLKrleTINQQMKT-TIVMVTHDPVAASYANRVIMLKDGQIHT 223
Cdd:cd03289  167 AHLDPITYQVIRK---TLKQAFADcTVILSEHRIEAMLECQRFLVIEENKVRQ 216
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 23-220 3.25e-12

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 64.88  E-value: 3.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGqditRMS-NKQLSYFRKKdvgfifqdynvlhtlT 101
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG----RISfSSQFSWIMPG---------------T 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 VRENIMLPLSITklsrqeaEMRYQEVTEALGITEIGSKYPDE-----------ISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:cd03291  114 IKENIIFGVSYD-------EYRYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSP 186

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504427498 171 TGALDSKSAQDLLKRLETINQQMKTTIvMVTHDPVAASYANRVIMLKDGQ 220
Cdd:cd03291  187 FGYLDVFTEKEIFESCVCKLMANKTRI-LVTSKMEHLKKADKILILHEGS 235
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
24-225 3.68e-12

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 65.58  E-value: 3.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  24 KDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSyfrKKDVGFIFQ---DYNVLHTL 100
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPLDAV---KKGMAYITEsrrDNGFFPNF 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENIMLPLSITK--------LSRQEAEMRYQEVTEALGITEIGS--KYPDEISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:PRK09700 357 SIAQNMAISRSLKDggykgamgLFHEVDEQRTAENQRELLALKCHSvnQNITELSGGNQQKVLISKWLCCCPEVIIFDEP 436

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 171 TGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTEL 225
Cdd:PRK09700 437 TRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQIL 491
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 23-220 8.17e-12

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 63.20  E-value: 8.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGF-----VAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDItrmsnkqlSYFRKKdvgfIFQDYnvl 97
Cdd:cd03237   10 LGEFTLEVEGGSIsesevIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV--------SYKPQY----IKADY--- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  98 hTLTVRENIMlplSITKLSRQEAEMRyQEVTEALGITEIGSKYPDEISGGQKQRTAAArALISKPA-IVFADEPTGALDS 176
Cdd:cd03237   75 -EGTVRDLLS---SITKDFYTHPYFK-TEIAKPLQIEQILDREVPELSGGELQRVAIA-ACLSKDAdIYLLDEPSAYLDV 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504427498 177 KS---AQDLLKRLetINQQMKTTIVmVTHDPVAASY-ANRVIMLkDGQ 220
Cdd:cd03237  149 EQrlmASKVIRRF--AENNEKTAFV-VEHDIIMIDYlADRLIVF-EGE 192
PLN03232 PLN03232
ABC transporter C family member; Provisional
 23-221 1.66e-11

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 63.84  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqLSYFRKkdVGFIFQDYNVLHTLTV 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFG---LTDLRR--VLSIIPQSPVLFSGTV 1326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  103 RENIMlPLSitklSRQEAEMryQEVTEALGITEIGSKYP-----------DEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:PLN03232 1327 RFNID-PFS----EHNDADL--WEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEAT 1399

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504427498  172 GALDSKSaQDLLKRleTINQQMKT-TIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:PLN03232 1400 ASVDVRT-DSLIQR--TIREEFKScTMLVIAHRLNTIIDCDKILVLSSGQV 1447
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 3-220 2.52e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 63.02  E-value: 2.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSI--DNVTRGTIEINGQDITRMSNKQLs 80
Cdd:PRK13549   5 LLEMKNITKTFGGVK----ALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVypHGTYEGEIIFEGEELQASNIRDT- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  81 yfRKKDVGFIFQDYNVLHTLTVRENIMLPLSITKLSRQE-AEM--RYQEVTEALGI-----TEIGskypdEISGGQKQRT 152
Cdd:PRK13549  80 --ERAGIAIIHQELALVKELSVLENIFLGNEITPGGIMDyDAMylRAQKLLAQLKLdinpaTPVG-----NLGLGQQQLV 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 153 AAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTH--DPVAAsYANRVIMLKDGQ 220
Cdd:PRK13549 153 EIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHklNEVKA-ISDTICVIRDGR 220
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 27-200 2.71e-11

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 62.72  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  27 HFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDYNvlhtltvreNI 106
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL----QKLVSDEWQRNN---------TD 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 107 MLPLSITKLSRQEAEM---------RYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSK 177
Cdd:PRK10938  90 MLSPGEDDTGRTTAEIiqdevkdpaRCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVA 169

                        170       180
                 ....*....|....*....|...
gi 504427498 178 SAQDLLKRLETINQQmKTTIVMV 200
Cdd:PRK10938 170 SRQQLAELLASLHQS-GITLVLV 191
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 3-234 2.82e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 62.71  E-value: 2.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQlsyF 82
Cdd:PRK10762   4 LLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS---S 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKDVGFIFQDYNVLHTLTVRENIMLPLSIT-KLSRQEAEMRYQEVTE---ALGITEIGSKYPDEISGGQKQRTAAARAL 158
Cdd:PRK10762  77 QEAGIGIIHQELNLIPQLTIAENIFLGREFVnRFGRIDWKKMYAEADKllaRLNLRFSSDKLVGELSIGEQQMVEIAKVL 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 159 ISKPAIVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTH---------DpvaasyanRVIMLKDGQihtelFQGD 229
Cdd:PRK10762 157 SFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHrlkeifeicD--------DVTVFRDGQ-----FIAE 222


                 ....*
gi 504427498 230 QPVSQ 234
Cdd:PRK10762 223 REVAD 227
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
99-221 4.15e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 62.06  E-value: 4.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  99 TLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:NF000106 100 SFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRT 179

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 504427498 179 AQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:NF000106 180 RNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRV 222
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 3-229 6.24e-11

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 61.87  E-value: 6.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEInGQDItrmsnkQLSY- 81
Cdd:TIGR03719 322 VIEAENLTKAFGDKL----LIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV------KLAYv 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   82 --FRKkdvgfifqdynvlhTLTVRENImlplsitklsrqeaemrYQEVTEALGITEIGS--------------------K 139
Cdd:TIGR03719 391 dqSRD--------------ALDPNKTV-----------------WEEISGGLDIIKLGKreipsrayvgrfnfkgsdqqK 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  140 YPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSksaqDLLKRLETINQQMKTTIVMVTHDpvaASYANRV---IML 216
Cdd:TIGR03719 440 KVGQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD---RWFLDRIathILA 512

                         250
                  ....*....|...
gi 504427498  217 KDGQIHTELFQGD 229
Cdd:TIGR03719 513 FEGDSHVEWFEGN 525
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 23-221 7.83e-11

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 61.89  E-value: 7.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYfrkkDVGFIFQDyNVLHTLTV 102
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRF----KITIIPQD-PVLFSGSL 1376

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   103 RENIMlPLSitklsrQEAEmryQEVTEALGITEIG---SKYPDE-----------ISGGQKQRTAAARALISKPAIVFAD 168
Cdd:TIGR00957 1377 RMNLD-PFS------QYSD---EEVWWALELAHLKtfvSALPDKldhecaeggenLSVGQRQLVCLARALLRKTKILVLD 1446

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 504427498   169 EPTGALDSKSaQDLLKrlETINQQMKT-TIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:TIGR00957 1447 EATAAVDLET-DNLIQ--STIRTQFEDcTVLTIAHRLNTIMDYTRVIVLDKGEV 1497
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
6-198 2.15e-10

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 60.52  E-value: 2.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   6 VSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLSYFRkk 85
Cdd:NF033858   4 LEGVSHRYGKTV----ALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRAVCPR-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  86 dVGFIFQDY--NVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGIteigSKYPD----EISGGQKQRTAAARALI 159
Cdd:NF033858  78 -IAYMPQGLgkNLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGL----APFADrpagKLSGGMKQKLGLCCALI 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504427498 160 SKPAIVFADEPTGALDSKS-AQ--DLLKRLETINQQMkTTIV 198
Cdd:NF033858 153 HDPDLLILDEPTTGVDPLSrRQfwELIDRIRAERPGM-SVLV 193
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 21-221 5.60e-10

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 58.11  E-value: 5.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSID--NVTRGTIEINGQDITRMSNKQLSyfrKKDVGFIFQdYNV-L 97
Cdd:CHL00131  21 EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERA---HLGIFLAFQ-YPIeI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  98 HTLTVRENIMLPLSITKLSRQEAEMR----YQEVTEALGITEIGSKY-----PDEISGGQKQRTAAARALISKPAIVFAD 168
Cdd:CHL00131  97 PGVSNADFLRLAYNSKRKFQGLPELDplefLEIINEKLKLVGMDPSFlsrnvNEGFSGGEKKRNEILQMALLDSELAILD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 169 EPTGALDSksaqDLLKRL-ETINQQMKTT--IVMVTHDPVAASY--ANRVIMLKDGQI 221
Cdd:CHL00131 177 ETDSGLDI----DALKIIaEGINKLMTSEnsIILITHYQRLLDYikPDYVHVMQNGKI 230
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 4-245 1.18e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 57.98  E-value: 1.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   4 LKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEingqditrmsnkqlsYFR 83
Cdd:PRK15064 320 LEVENLTKGFDNGP----LFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVK---------------WSE 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  84 KKDVGFIFQDynvlHTLTVRENIMLPLSITKLsRQEAEMRyQEVTEALGITEIGS----KYPDEISGGQKQRTAAARALI 159
Cdd:PRK15064 381 NANIGYYAQD----HAYDFENDLTLFDWMSQW-RQEGDDE-QAVRGTLGRLLFSQddikKSVKVLSGGEKGRMLFGKLMM 454

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 160 SKPAIVFADEPTGALDSKSAQDLLKRLEtinqQMKTTIVMVTHD-PVAASYANRVIMLKDGQIHTelFQGDqpvsqfYQE 238
Cdd:PRK15064 455 QKPNVLVMDEPTNHMDMESIESLNMALE----KYEGTLIFVSHDrEFVSSLATRIIEITPDGVVD--FSGT------YEE 522


                 ....*..
gi 504427498 239 IIHNQSV 245
Cdd:PRK15064 523 YLRSQGI 529
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
26-207 2.04e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.01  E-value: 2.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  26 IHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSnkqlsyfRKKDVGFIFQDYNVLHTLTVREN 105
Cdd:PRK13543  30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGD-------RSRFMAYLGHLPGLKADLSTLEN 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 106 IMLplsITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAqDLLKR 185
Cdd:PRK13543 103 LHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGI-TLVNR 178

                        170       180
                 ....*....|....*....|..
gi 504427498 186 LETINQQMKTTIVMVTHDPVAA 207
Cdd:PRK13543 179 MISAHLRGGGAALVTTHGAYAA 200
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 23-238 2.98e-09

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 56.07  E-value: 2.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDyNVLHTLTV 102
Cdd:cd03288   37 LKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTL----RSRLSIILQD-PILFSGSI 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENIMLPLSITKLSRQEA-EM-RYQEVTEAL--GITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKS 178
Cdd:cd03288  112 RFNLDPECKCTDDRLWEAlEIaQLKNMVKSLpgGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMAT 191

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 179 AQDLLKRLETINQQmkTTIVMVTHDPVAASYANRVIMLKDGQihteLFQGDQPVSQFYQE 238
Cdd:cd03288  192 ENILQKVVMTAFAD--RTVVTIAHRVSTILDADLVLVLSRGI----LVECDTPENLLAQE 245
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 3-225 2.99e-09

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 56.76  E-value: 2.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    3 ILKVSHVSkIYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVI-SSIDNVTRGTIEINGQDI-TRMSNKQLs 80
Cdd:TIGR02633 257 ILEARNLT-CWDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQALfGAYPGKFEGNVFINGKPVdIRNPAQAI- 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   81 yfrKKDVGFIFQD---YNVLHTLTVRENIMLPL--SITKLSRQEAEMRYQEVTEALGITEIGSKYPD----EISGGQKQR 151
Cdd:TIGR02633 335 ---RAGIAMVPEDrkrHGIVPILGVGKNITLSVlkSFCFKMRIDAAAELQIIGSAIQRLKVKTASPFlpigRLSGGNQQK 411

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498  152 TAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQIHTEL 225
Cdd:TIGR02633 412 AVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKLKGDF 485
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-226 4.13e-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: 53.92  E-value: 4.13e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498    32 KGGFVAIMGPSGSGKTTLLN-VISSIDNVTRGTIEINGQDITrmsnkqlsyfrkkdvgfifqdynvlhtltvrenimlpl 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDIL-------------------------------------- 42

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   111 sitklsrqeaemryqEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLET-- 188
Cdd:smart00382  43 ---------------EEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELrl 107

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 504427498   189 ---INQQMKTTIVMVTHDPVAASYANRVIMLkDGQIHTELF 226
Cdd:smart00382 108 lllLKSEKNLTVILTTNDEKDLGPALLRRRF-DRRIVLLLI 147
PTZ00243 PTZ00243
ABC transporter; Provisional
 23-229 6.61e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 55.94  E-value: 6.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIeingqditrmsnkqlsyFRKKDVGFIFQDYNVLHTlTV 102
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV-----------------WAERSIAYVPQQAWIMNA-TV 737

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  103 RENIMLplsitklSRQEAEMRYQEVT-----EA----LGI---TEIGSKYPDeISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:PTZ00243  738 RGNILF-------FDEEDAARLADAVrvsqlEAdlaqLGGgleTEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDP 809

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498  171 TGALDSKSAQDLLKRLETINQQMKTTiVMVTHDPVAASYANRVIMLKDGQIHtelFQGD 229
Cdd:PTZ00243  810 LSALDAHVGERVVEECFLGALAGKTR-VLATHQVHVVPRADYVVALGDGRVE---FSGS 864
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 23-203 7.96e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.73  E-value: 7.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINgQD--ITRM-----SNKQLSYFRK-----KDVGFI 90
Cdd:PRK11147  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARLqqdppRNVEGTVYDFvaegiEEQAEY 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  91 FQDYNvlHTLTVRENIMLPLSITKLSR-QEA---------EMRYQEVTEALGITeigskyPD----EISGGQKQRTAAAR 156
Cdd:PRK11147  98 LKRYH--DISHLVETDPSEKNLNELAKlQEQldhhnlwqlENRINEVLAQLGLD------PDaalsSLSGGWLRKAALGR 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504427498 157 ALISKPAIVFADEPTGALDSksaqDLLKRLETINQQMKTTIVMVTHD 203
Cdd:PRK11147 170 ALVSNPDVLLLDEPTNHLDI----ETIEWLEGFLKTFQGSIIFISHD 212
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
18-229 1.29e-08

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 54.24  E-value: 1.29e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  18 QSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITrMSNKQLSYFRKKdVGFIFQD--YN 95
Cdd:PRK13638  12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLD-YSKRGLLALRQQ-VATVFQDpeQQ 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  96 VLHTlTVRENImlPLSITKLSRQEAEMRyQEVTEALGITEIGS--KYPDE-ISGGQKQRTAAARALISKPAIVFADEPTG 172
Cdd:PRK13638  90 IFYT-DIDSDI--AFSLRNLGVPEAEIT-RRVDEALTLVDAQHfrHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 173 ALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQIhteLFQGD 229
Cdd:PRK13638 166 GLDPAGRTQMIAIIRRIVAQ-GNHVIISSHDiDLIYEISDAVYVLRQGQI---LTHGA 219
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 28-222 1.49e-08

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 53.78  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  28 FTVEKGGFVAIMGPSGSGKTTLLNVISSIdNVTRGTIEINGQDITRMSNKQLSYFRkkdvGFIFQDYNVLHTLTVRENIM 107
Cdd:PRK03695  17 AEVRAGEILHLVGPNGAGKSTLLARMAGL-LPGSGSIQFAGQPLEAWSAAELARHR----AYLSQQQTPPFAMPVFQYLT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 108 LPLSiTKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTA-AARALISKPAI------VFADEPTGALD--SKS 178
Cdd:PRK03695  92 LHQP-DKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRlAAVVLQVWPDInpagqlLLLDEPMNSLDvaQQA 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504427498 179 AQDLLkrLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQIH 222
Cdd:PRK03695 171 ALDRL--LSELCQQ-GIAVVMSSHDlNHTLRHADRVWLLKQGKLL 212
PLN03130 PLN03130
ABC transporter C family member; Provisional
 23-221 1.57e-08

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 55.13  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDyNVLHTLTV 102
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDL----RKVLGIIPQA-PVLFSGTV 1329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  103 RENIMlPLSITK-----LSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSK 177
Cdd:PLN03130 1330 RFNLD-PFNEHNdadlwESLERAHLKDVIRRNSLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 504427498  178 SaqDLLKRlETINQQMKT-TIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:PLN03130 1409 T--DALIQ-KTIREEFKScTMLIIAHRLNTIIDCDRILVLDAGRV 1450
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 29-203 1.79e-08

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: 53.52  E-value: 1.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  29 TVEKGGFVAIMGPSGSGKTTLLNVISS--IDNVTRGTIEINGQDItrmsnkqLSYFRkkdvGFIFQDY-NVLHTLTVREN 105
Cdd:cd03236   22 VPREGQVLGLVGPNGIGKSTALKILAGklKPNLGKFDDPPDWDEI-------LDEFR----GSELQNYfTKLLEGDVKVI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 106 I------MLPLSITK-----LSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGAL 174
Cdd:cd03236   91 VkpqyvdLIPKAVKGkvgelLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL 170

                        170       180
                 ....*....|....*....|....*....
gi 504427498 175 DSKSAQDLLKRLETINQQMKTTIVmVTHD 203
Cdd:cd03236  171 DIKQRLNAARLIRELAEDDNYVLV-VEHD 198
PTZ00243 PTZ00243
ABC transporter; Provisional
 23-206 2.12e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 54.40  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfrKKDVGFIFQDyNVLHTLTV 102
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLREL----RRQFSMIPQD-PVLFDGTV 1400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  103 RENIMlPLsitkLSRQEAE---------MRYQEVTEALGIT----EIGSKYpdeiSGGQKQRTAAARALISK-PAIVFAD 168
Cdd:PTZ00243 1401 RQNVD-PF----LEASSAEvwaalelvgLRERVASESEGIDsrvlEGGSNY----SVGQRQLMCMARALLKKgSGFILMD 1471

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504427498  169 EPTG----ALDSK---------SAQDLLK---RLETINQQMKtTIVMvTHDPVA 206
Cdd:PTZ00243 1472 EATAnidpALDRQiqatvmsafSAYTVITiahRLHTVAQYDK-IIVM-DHGAVA 1523
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
12-203 2.28e-08

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 53.28  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  12 IYGNKKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGqditrmsnkqlsyfrkkDVGFIF 91
Cdd:PRK13546  29 IPKHKNKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------------EVSVIA 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  92 QDYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:PRK13546  92 ISAGLSGQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEAL 171

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504427498 172 GALDSKSAQDLLKRLETINQQMKtTIVMVTHD 203
Cdd:PRK13546 172 SVGDQTFAQKCLDKIYEFKEQNK-TIFFVSHN 202
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 3-229 2.72e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 54.02  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISsidnvtrGTIEINGQDITRMSNKQLSYF 82
Cdd:PRK10636 312 LLKMEKVSAGYGDRI----ILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLA-------GELAPVSGEIGLAKGIKLGYF 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  83 RKKDVGFIFQDYNVLHTLTvrenimlplsitKLSRQEAEmryQEVTEALG--------ITEIGSKYpdeiSGGQKQRTAA 154
Cdd:PRK10636 381 AQHQLEFLRADESPLQHLA------------RLAPQELE---QKLRDYLGgfgfqgdkVTEETRRF----SGGEKARLVL 441

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 155 ARALISKPAIVFADEPTGALDSKSAQDLLKRLetinQQMKTTIVMVTHDP-VAASYANRVIMLKDGQIhtELFQGD 229
Cdd:PRK10636 442 ALIVWQRPNLLLLDEPTNHLDLDMRQALTEAL----IDFEGALVVVSHDRhLLRSTTDDLYLVHDGKV--EPFDGD 511
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 21-225 8.66e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 52.36  E-value: 8.66e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQ-----LSYF-RKKDVGFIFQD- 93
Cdd:PRK15439 277 EGFRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlargLVYLpEDRQSSGLYLDa 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  94 ---YNVLhTLTVREnimLPLSItKLSRQEAEM-RYQEvteALGIteigsKYPDE------ISGGQKQRTAAARALISKPA 163
Cdd:PRK15439 357 plaWNVC-ALTHNR---RGFWI-KPARENAVLeRYRR---ALNI-----KFNHAeqaartLSGGNQQKVLIAKCLEASPQ 423

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504427498 164 IVFADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQIHTEL 225
Cdd:PRK15439 424 LLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDlEEIEQMADRVLVMHQGEISGAL 485
PLN03140 PLN03140
ABC transporter G family member; Provisional
 16-228 9.69e-08

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 52.54  E-value: 9.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   16 KKQSYEALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS-----SIDnvTRGTIEINGQDITR-MSNKQLSYFRKKDVGF 89
Cdd:PLN03140  174 KKTKLTILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAgkldpSLK--VSGEITYNGYRLNEfVPRKTSAYISQNDVHV 251

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   90 -----------------IFQDYNVLHTLTVRE---------NIMLPLSITKLSRQEAEMRYQEVTEALGI-----TEIGS 138
Cdd:PLN03140  252 gvmtvketldfsarcqgVGTRYDLLSELARREkdagifpeaEVDLFMKATAMEGVKSSLITDYTLKILGLdickdTIVGD 331

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  139 KYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYA--NRVIML 216
Cdd:PLN03140  332 EMIRGISGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDlfDDIILL 411

                         250
                  ....*....|..
gi 504427498  217 KDGQIhteLFQG 228
Cdd:PLN03140  412 SEGQI---VYQG 420
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
29-203 1.01e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 52.12  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  29 TVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEIngqDITrmsnkqLSYfrKKDvgFIFQDYNVlhtlTVRENIMl 108
Cdd:PRK13409 361 EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDP---ELK------ISY--KPQ--YIKPDYDG----TVEDLLR- 422

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 109 plSITklSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSK---SAQDLLKR 185
Cdd:PRK13409 423 --SIT--DDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEqrlAVAKAIRR 498

                        170
                 ....*....|....*...
gi 504427498 186 LetINQQMKTTIVmVTHD 203
Cdd:PRK13409 499 I--AEEREATALV-VDHD 513
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
22-171 1.03e-07

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.43  E-value: 1.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKG---GFVaimGPSGSGKTTLLNVISSIDNVTRGTI-----EINGQDI-TRMsnkqlsyfRkkdVGFIFQ 92
Cdd:NF033858 281 AVDHVSFRIRRGeifGFL---GSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIaTRR--------R---VGYMSQ 346

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504427498  93 DYNVLHTLTVRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPT 171
Cdd:NF033858 347 AFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 25-204 1.10e-07

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 52.06  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   25 DIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTieingqditrmsnkqLSYFRKKDVGFIFQD-YNVLHTLtvR 103
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGR---------------LTKPAKGKLFYVPQRpYMTLGTL--R 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  104 ENIMLPLSITK-----LSRQEAEMRYQEV------TEALGITEIgSKYPDEISGGQKQRTAAARALISKPAIVFADEPTG 172
Cdd:TIGR00954 533 DQIIYPDSSEDmkrrgLSDKDLEQILDNVqlthilEREGGWSAV-QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTS 611

                         170       180       190
                  ....*....|....*....|....*....|..
gi 504427498  173 ALdsksAQDLLKRLETINQQMKTTIVMVTHDP 204
Cdd:TIGR00954 612 AV----SVDVEGYMYRLCREFGITLFSVSHRK 639
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 29-203 1.41e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 51.71  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  29 TVEKGGFVAIMGPSGSGKTTLLNVISsidnvtrGTIEINGQDITRMSNKQ--LSYFRkkdvGFIFQDY---------NVL 97
Cdd:COG1245   95 VPKKGKVTGILGPNGIGKSTALKILS-------GELKPNLGDYDEEPSWDevLKRFR----GTELQDYfkklangeiKVA 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  98 H------------TLTVREnimlpLsitkLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIV 165
Cdd:COG1245  164 HkpqyvdlipkvfKGTVRE-----L----LEKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFY 234

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504427498 166 FADEPTGALD-------SKSAQDLLKrletinqqMKTTIVMVTHD 203
Cdd:COG1245  235 FFDEPSSYLDiyqrlnvARLIRELAE--------EGKYVLVVEHD 271
PLN03073 PLN03073
ABC transporter F family; Provisional
 24-203 1.58e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.78  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  24 KDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIeingqditrmsnkqlsyFRKKDVGF-IFQDYNVlHTLTV 102
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMaVFSQHHV-DGLDL 587

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 103 RENIMLPLSITKLSRQEAEMRYQevTEALGIT---EIGSKYpdEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSA 179
Cdd:PLN03073 588 SSNPLLYMMRCFPGVPEQKLRAH--LGSFGVTgnlALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAV 663

                        170       180
                 ....*....|....*....|....
gi 504427498 180 QDLLKRLETinqqMKTTIVMVTHD 203
Cdd:PLN03073 664 EALIQGLVL----FQGGVLMVSHD 683
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 29-203 1.84e-07

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 51.32  E-value: 1.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  29 TVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEingqditrmSNKQLSYfrKKDvgFIFQDYNvlhtLTVRENIML 108
Cdd:COG1245  362 EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---------EDLKISY--KPQ--YISPDYD----GTVEEFLRS 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 109 PLSitklSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALiSKPAIVFA-DEPTGALDSK---SAQDLLK 184
Cdd:COG1245  425 ANT----DDFGSSYYKTEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACL-SRDADLYLlDEPSAHLDVEqrlAVAKAIR 499

                        170
                 ....*....|....*....
gi 504427498 185 RLetINQQMKTTIVmVTHD 203
Cdd:COG1245  500 RF--AENRGKTAMV-VDHD 515
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 22-220 2.50e-07

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: 49.24  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNvissidnvtrgtiEINGQDITRMSNKQLSYFRKKDVGFIFQdynvLHTLt 101
Cdd:cd03238   10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFSRNKLIFIDQ----LQFL- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 vrenimlplsitklsrqeaemryqeVTEALGITEIGSKYPdEISGGQKQRTAAARALIS--KPAIVFADEPTGALDSKSA 179
Cdd:cd03238   72 -------------------------IDVGLGYLTLGQKLS-TLSGGELQRVKLASELFSepPGTLFILDEPSTGLHQQDI 125

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 180 QDLLKRLETINQQmKTTIVMVTHDPVAASYANRVIMLKDGQ 220
Cdd:cd03238  126 NQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDFGPGS 165
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 3-66 2.61e-07

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 50.89  E-value: 2.61e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEI 66
Cdd:PRK11819 324 VIEAENLSKSFGDRL----LIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI 383
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 22-221 6.36e-07

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 49.89  E-value: 6.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  22 ALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQditrmsnkqlsyfrkkdVGFIFQDYNVLHTLT 101
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGS-----------------AALIAISSGLNGQLT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 102 VRENIMLPLSITKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQD 181
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504427498 182 LLKRLETINQQMKtTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK13545 182 CLDKMNEFKEQGK-TIFFISHSlSQVKSFCTKALWLHYGQV 221
GguA NF040905
sugar ABC transporter ATP-binding protein;
3-220 6.78e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 6.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSKIYGNKKqsyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVIS------SIDnvtrGTIEINGQ-----DI 71
Cdd:NF040905   1 ILEMRGITKTFPGVK----ALDDVNLSVREGEIHALCGENGAGKSTLMKVLSgvyphgSYE----GEILFDGEvcrfkDI 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  72 tRMSnkqlsyfRKKDVGFIFQDYNVLHTLTVRENIMLPLSITK---LSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQ 148
Cdd:NF040905  73 -RDS-------EALGIVIIHQELALIPYLSIAENIFLGNERAKrgvIDWNETNRRARELLAKVGLDESPDTLVTDIGVGK 144

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504427498 149 KQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIvMVTH--DPVAAsYANRVIMLKDGQ 220
Cdd:NF040905 145 QQLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSI-IISHklNEIRR-VADSITVLRDGR 216
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
29-203 6.92e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 49.81  E-value: 6.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  29 TVEKGGFVAIMGPSGSGKTTLLNVIS--------------SIDNVT---RGTiEIngQD-ITRMSNKQLSYFRKkdVGFI 90
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILSgelipnlgdyeeepSWDEVLkrfRGT-EL--QNyFKKLYNGEIKVVHK--PQYV 169

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  91 FQDYNVLhTLTVREnimlplsitKLSRQEAEMRYQEVTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEP 170
Cdd:PRK13409 170 DLIPKVF-KGKVRE---------LLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504427498 171 TGALDSK---SAQDLLKRLetinQQMKTTIVmVTHD 203
Cdd:PRK13409 240 TSYLDIRqrlNVARLIREL----AEGKYVLV-VEHD 270
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 3-225 1.11e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 49.16  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVS---KIYGNKKQsyeaLKDIHFTVEKGGFVAIMGPSGSGKTTLLNVI-SSIDNVTRGTIEINGQDITRMSNKQ 78
Cdd:PRK13549 259 ILEVRNLTawdPVNPHIKR----VDDVSFSLRRGEILGIAGLVGAGRTELVQCLfGAYPGRWEGEIFIDGKPVKIRNPQQ 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  79 --------LSYFRKKDvGFIFQdynvlhtLTVRENIMLPL--SITKLSRQEAEMRYQEVTEALGITEIGSKYPD----EI 144
Cdd:PRK13549 335 aiaqgiamVPEDRKRD-GIVPV-------MGVGKNITLAAldRFTGGSRIDDAAELKTILESIQRLKVKTASPElaiaRL 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 145 SGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKrleTINQ--QMKTTIVMVTHD-PVAASYANRVIMLKDGQI 221
Cdd:PRK13549 407 SGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYK---LINQlvQQGVAIIVISSElPEVLGLSDRVLVMHEGKL 483


                 ....
gi 504427498 222 HTEL 225
Cdd:PRK13549 484 KGDL 487
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 21-233 1.21e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 48.96  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMSNKQLsyfRKKDVGFIFQDYNVLHTL 100
Cdd:PRK10982  12 KALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEA---LENGISMVHQELNLVLQR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 101 TVRENIMLPLSITKLSRQEAEMRYQE---VTEALGITEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSK 177
Cdd:PRK10982  89 SVMDNMWLGRYPTKGMFVDQDKMYRDtkaIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 178 SAQDLLKRLETINQQmKTTIVMVTHD-PVAASYANRVIMLKDGQ-IHTELFQG---DQPVS 233
Cdd:PRK10982 169 EVNHLFTIIRKLKER-GCGIVYISHKmEEIFQLCDEITILRDGQwIATQPLAGltmDKIIA 228
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 143-220 2.63e-06

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: 46.41  E-value: 2.63e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504427498 143 EISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQ 220
Cdd:cd03222   71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEGE 148
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 19-214 2.50e-05

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: 43.75  E-value: 2.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  19 SYEALKDIHFTvekGGFVAIMGPSGSGKTTLLNVISSidnVTRGTieingqdiTRMSNKQL----SYFRKKDVG----FI 90
Cdd:cd03240   11 SFHERSEIEFF---SPLTLIVGQNGAGKTTIIEALKY---ALTGE--------LPPNSKGGahdpKLIREGEVRaqvkLA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  91 FQDYNVlHTLTVRENIMLPLSITkLSRQEaemryqevtealgitEIGSKYPDEI---SGGQKQ------RTAAARALISK 161
Cdd:cd03240   77 FENANG-KKYTITRSLAILENVI-FCHQG---------------ESNWPLLDMRgrcSGGEKVlasliiRLALAETFGSN 139

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504427498 162 PAIVFADEPTGALDSKS-AQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVI 214
Cdd:cd03240  140 CGILALDEPTTNLDEENiEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIY 193
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 23-214 3.11e-05

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: 43.79  E-value: 3.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLlnvisSIDnvtrgTIEINGQditRMSNKQLS-YFR-------KKDVGFIfqdy 94
Cdd:cd03270   11 LKNVDVDIPRNKLVVITGVSGSGKSSL-----AFD-----TIYAEGQ---RRYVESLSaYARqflgqmdKPDVDSI---- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  95 nvlhtltvrENIMLPLSI-TKLSRQEAEMRYQEVTEAL----------GIT-------EIGSKY------PDEISGGQKQ 150
Cdd:cd03270   74 ---------EGLSPAIAIdQKTTSRNPRSTVGTVTEIYdylrllfarvGIRerlgflvDVGLGYltlsrsAPTLSGGEAQ 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504427498 151 RTAAARALISK--PAIVFADEPTGALDSKSAQDLLKRLETInQQMKTTIVMVTHDPVAASYANRVI 214
Cdd:cd03270  145 RIRLATQIGSGltGVLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRAADHVI 209
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 21-75 1.03e-04

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 42.47  E-value: 1.03e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504427498  21 EALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDN--VTRGTIEINGQDITRMS 75
Cdd:PRK09580  15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREDyeVTGGTVEFKGKDLLELS 71
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
18-203 3.34e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 40.76  E-value: 3.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  18 QSYEALKDIHFTvekGGFVAIMGPSGSGKTTLLNVIS-------------SIDNVTRG--------TIEINGQD--ITRM 74
Cdd:COG0419   11 RSYRDTETIDFD---DGLNLIVGPNGAGKSTILEAIRyalygkarsrsklRSDLINVGseeasvelEFEHGGKRyrIERR 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  75 SNKQLSYF------RKKDVGFIFQdynvlhtLTVRENIMLPLSITklsRQEAEMRYQEVTEALGI-TEIGSKY-----PD 142
Cdd:COG0419   88 QGEFAEFLeakpseRKEALKRLLG-------LEIYEELKERLKEL---EEALESALEELAELQKLkQEILAQLsgldpIE 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504427498 143 EISGGQKQRTAAARALiskpaIVFADepTGALDSKSAQDLLKRLEtinqqmktTIVMVTHD 203
Cdd:COG0419  158 TLSGGERLRLALADLL-----SLILD--FGSLDEERLERLLDALE--------ELAIITHV 203
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 26-222 3.60e-04

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 41.32  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  26 IHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRmsnKQLSYFRKKdvgF--IFQDYNVLHTLTVR 103
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTA---DNREAYRQL---FsaVFSDFHLFDRLLGL 424

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 104 ENIMLPLSITKLsrqEAEMRYQEVTE----ALGITeigskypdEISGGQKQRTAAARALI-SKPAIVFaDEptGALDsks 178
Cdd:COG4615  425 DGEADPARAREL---LERLELDHKVSvedgRFSTT--------DLSQGQRKRLALLVALLeDRPILVF-DE--WAAD--- 487

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504427498 179 aQD----------LLKRLEtinQQMKTTIVmVTHDPVAASYANRVIMLKDGQIH 222
Cdd:COG4615  488 -QDpefrrvfyteLLPELK---ARGKTVIA-ISHDDRYFDLADRVLKMDYGKLV 536
PLN03073 PLN03073
ABC transporter F family; Provisional
 120-229 4.09e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.38  E-value: 4.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 120 AEMRYQEVTEALGIT-EIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTGALDSKSaqdlLKRLETINQQMKTTIV 198
Cdd:PLN03073 320 AEARAASILAGLSFTpEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHA----VLWLETYLLKWPKTFI 395

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 504427498 199 MVTHdpvAASYANRV----IMLKDGQIHTelFQGD 229
Cdd:PLN03073 396 VVSH---AREFLNTVvtdiLHLHGQKLVT--YKGD 425
VirB11 COG0630
Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell ...
 30-55 4.68e-04

Type IV secretory pathway ATPase VirB11/Archaellum biosynthesis ATPase ArlI/FlaI [Cell motility, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 440395 [Multi-domain]  Cd Length: 462  Bit Score: 40.83  E-value: 4.68e-04
                         10        20
                 ....*....|....*....|....*.
gi 504427498  30 VEKGGFVAIMGPSGSGKTTLLNVISS 55
Cdd:COG0630  287 LENGKSVLVAGGTASGKTTLLNALLS 312
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 40-203 5.54e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 40.65  E-value: 5.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  40 GPSGSGKTTLLNVISSIDNVTRGTIEINgqditrmSNKQLSYFRKKDvgFIFQDYNVLHTLTV-----------RENI-M 107
Cdd:PRK15064  34 GANGCGKSTFMKILGGDLEPSAGNVSLD-------PNERLGKLRQDQ--FAFEEFTVLDTVIMghtelwevkqeRDRIyA 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 108 LP-------LSITKLSRQEAEM-------RYQEVTEALGI-TEIGSKYPDEISGGQKQRTAAARALISKPAIVFADEPTG 172
Cdd:PRK15064 105 LPemseedgMKVADLEVKFAEMdgytaeaRAGELLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTN 184

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504427498 173 ALDSksaqDLLKRLETINQQMKTTIVMVTHD 203
Cdd:PRK15064 185 NLDI----NTIRWLEDVLNERNSTMIIISHD 211
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 23-51 8.09e-04

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 40.38  E-value: 8.09e-04
                          10        20
                  ....*....|....*....|....*....
gi 504427498   23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLN 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
 21-50 8.14e-04

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 39.77  E-value: 8.14e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 504427498  21 EALKDIHFTVEKG-GFVAIMGPSGSGKTTLL 50
Cdd:COG3267   30 EALARLEYALAQGgGFVVLTGEVGTGKTTLL 60
PhnN COG3709
Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];
31-51 8.36e-04

Ribose 1,5-bisphosphate kinase PhnN [Carbohydrate transport and metabolism];


Pssm-ID: 442923  Cd Length: 188  Bit Score: 39.41  E-value: 8.36e-04
                         10        20
                 ....*....|....*....|.
gi 504427498  31 EKGGFVAIMGPSGSGKTTLLN 51
Cdd:COG3709    3 GPGRLIYVVGPSGAGKDSLLA 23
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 3-221 9.09e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 40.10  E-value: 9.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498   3 ILKVSHVSkiygNKKQSyeALKDIHFTVEKGGFVAIMGPSGSGKTTLLNVISSIDNVTRGTIEINGQDITRMS------- 75
Cdd:PRK10982 250 ILEVRNLT----SLRQP--SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNaneainh 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  76 --------NKQLSYFRKKDVGFIFQDYNVLHTLTvrenimlplSITKLSRQEAEMRYQEVTEALGI------TEIGSkyp 141
Cdd:PRK10982 324 gfalvteeRRSTGIYAYLDIGFNSLISNIRNYKN---------KVGLLDNSRMKSDTQWVIDSMRVktpghrTQIGS--- 391

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498 142 deISGGQKQRTAAARALISKPAIVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVMVTHDPVAASYANRVIMLKDGQI 221
Cdd:PRK10982 392 --LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLV 469
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 144-204 5.34e-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: 36.57  E-value: 5.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498 144 ISGGQKQRTAAARALIS---KPA-IVFADEPTGALDSKSAQDLLKRLETINQQMKTTIVmVTHDP 204
Cdd:cd03227   78 LSGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLP 141
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-175 5.36e-03

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 37.85  E-value: 5.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLNVI---SSIDNVTrGTIEINGQDItRMSN------KQLSYFR--KKDVGFIF 91
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgrSYGRNIS-GTVFKDGKEV-DVSTvsdaidAGLAYVTedRKGYGLNL 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504427498  92 QDynvlhtlTVRENIMLPlSITKLSR-----QEAEMRY-QEVTEALGIteigsKYPD------EISGGQKQRTAAARALI 159
Cdd:NF040905 354 ID-------DIKRNITLA-NLGKVSRrgvidENEEIKVaEEYRKKMNI-----KTPSvfqkvgNLSGGNQQKVVLSKWLF 420

                        170
                 ....*....|....*.
gi 504427498 160 SKPAIVFADEPTGALD 175
Cdd:NF040905 421 TDPDVLILDEPTRGID 436
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 142-214 5.36e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 37.89  E-value: 5.36e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504427498  142 DEISGGQKQRTAAARALISKPAIV--FADEPTGALDSKSAQDLLKRLETINQQmKTTIVMVTHDPVAASYANRVI 214
Cdd:PRK00635  475 ATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQ-GNTVLLVEHDEQMISLADRII 548
uvrA PRK00349
excinuclease ABC subunit UvrA;
23-51 5.79e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 37.74  E-value: 5.79e-03
                         10        20
                 ....*....|....*....|....*....
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLN 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
23-51 6.14e-03

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 37.70  E-value: 6.14e-03
                         10        20
                 ....*....|....*....|....*....
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLN 51
Cdd:COG0178  621 LKNVDVEIPLGVLTCVTGVSGSGKSTLVN 649
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 23-51 7.59e-03

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: 36.82  E-value: 7.59e-03
                         10        20
                 ....*....|....*....|....*....
gi 504427498  23 LKDIHFTVEKGGFVAIMGPSGSGKTTLLN 51
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN 39
PRK10246 PRK10246
exonuclease subunit SbcC; Provisional
 26-53 8.48e-03

exonuclease subunit SbcC; Provisional


Pssm-ID: 182330 [Multi-domain]  Cd Length: 1047  Bit Score: 37.47  E-value: 8.48e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 504427498   26 IHFTVE---KGGFVAIMGPSGSGKTTLLNVI 53
Cdd:PRK10246   20 IDFTAEpfaSNGLFAITGPTGAGKTTLLDAI 50
MMR_HSR1 pfam01926
50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete ...
 35-72 8.78e-03

50S ribosome-binding GTPase; The full-length GTPase protein is required for the complete activity of the protein of interacting with the 50S ribosome and binding of both adenine and guanine nucleotides, with a preference for guanine nucleotide.


Pssm-ID: 460387 [Multi-domain]  Cd Length: 113  Bit Score: 35.29  E-value: 8.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 504427498   35 FVAIMGPSGSGKTTLLNVI-------SSIDNVTR----GTIEINGQDIT 72
Cdd:pfam01926   1 RVALVGRPNVGKSTLINALtgakaivSDYPGTTRdpneGRLELKGKQII 49
AAA_22 pfam13401
AAA domain;
34-67 8.88e-03

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 35.40  E-value: 8.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 504427498   34 GFVAIMGPSGSGKTTLL-NVISSIDNVTRGTIEIN 67
Cdd:pfam13401   6 GILVLTGESGTGKTTLLrRLLEQLPEVRDSVVFVD 40
 
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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