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Conserved domains on  [gi|492172462|ref|WP_005770064|]
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MULTISPECIES: Fe(3+) dicitrate ABC transporter ATP-binding protein FecE [Pseudomonas syringae group]

Protein Classification

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE( domain architecture ID 11485274)

Fe(3+) dicitrate ABC transporter ATP-binding protein FecE is the ATPase subunit of the binding-protein-dependent transport system for citrate-dependent Fe(3+), and is responsible for energy coupling to the transport system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
2-256 1.90e-172

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


:

Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 475.66  E-value: 1.90e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:PRK11231   1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11231  81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
                        250
                 ....*....|....*
gi 492172462 242 IMREPVAGTPMCIVE 256
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
 
Name Accession Description Interval E-value
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
2-256 1.90e-172

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 475.66  E-value: 1.90e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:PRK11231   1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11231  81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
                        250
                 ....*....|....*
gi 492172462 242 IMREPVAGTPMCIVE 256
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
3-254 4.02e-130

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: 368.60  E-value: 4.02e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1120   81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:COG1120  161 LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
                        250
                 ....*....|...
gi 492172462 242 IMREPVAGTPMCI 254
Cdd:COG1120  241 VIEDPVTGRPLVL 253
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
5-221 6.05e-85

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: 251.20  E-value: 6.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPq 84
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 vlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03214   80 -------------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03214  123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-212 4.61e-57

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 180.89  E-value: 4.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLsldgkgysqlsARELACKVAFLPQVLPIPEG 91
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 --VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:NF040873  70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQAcRYADHLAVM 212
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
24-238 6.86e-41

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 140.37  E-value: 6.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   24 FSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlSARELACKVAFLPQV------LPIpegvNVRQL 97
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefawdFPI----SVAHT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR03771  72 VMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462  178 LLDLMRELSAEGKTVITVLHDINQACRYADHLaVMQGGRLVTCGAPGDVLTAELVCQVFDV 238
Cdd:TIGR03771 152 LTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGV 211
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
19-168 4.96e-36

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: 125.45  E-value: 4.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462   99 AYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:pfam00005  81 RLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
13-228 3.31e-22

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 95.58  E-value: 3.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLK--AFARILtpQSGSLSLDGKGYSQLSARELAC-KVAFLPQVLpip 89
Cdd:NF033858  11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSliAGARKI--QQGRVEVLGGDMADARHRRAVCpRIAYMPQGL--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 eGVN------VRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:NF033858  86 -GKNlyptlsVFENLDF--------FGRLFGQDAAErrrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLD-ISHQV--ELLDLMRElSAEGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAPGDVLT 228
Cdd:NF033858 157 LLILDEPTTGVDpLSRRQfwELIDRIRA-ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
121-221 2.19e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.13  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 121 DQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDIN 200
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
                         90       100
                 ....*....|....*....|.
gi 492172462 201 QACRYADHLAVMQGGRLVTCG 221
Cdd:NF000106 206 EAEQLAHELTVIDRGRVIADG 226
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-200 2.27e-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: 54.69  E-value: 2.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdgkgysqlsarelackvaflpqvlpipegvnvrqlvaygrsphnsl 108
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   109 wgrLSGADQHSVDQALQRMELATlaeRPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD------LM 182
Cdd:smart00382  36 ---IDGEDILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
                          170
                   ....*....|....*...
gi 492172462   183 RELSAEGKTVITVLHDIN 200
Cdd:smart00382 110 LLKSEKNLTVILTTNDEK 127
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-232 2.73e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.44  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELAC--KVAFLPQVLPIPEGVNVRQ 96
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIATrrRVGYMSQAFSLYGELTVRQ 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  97 -LVAYGRSPHnslwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWL--AMILAQDaaIVLLDEPTTYLDI 172
Cdd:NF033858 359 nLELHARLFH------LPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLavAVIHKPE--LLILDEPTSGVDP 430
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 173 SHQVELLDLMRELSAEGKTVITV-LHDINQACRyADHLAVMQGGRLVTCGAPgdvltAELV 232
Cdd:NF033858 431 VARDMFWRLLIELSREDGVTIFIsTHFMNEAER-CDRISLMHAGRVLASDTP-----AALV 485
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-218 1.64e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.80  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  20 QDLSFSPPAGQVTALIGPNGCGKSTLLKafarILT---PQ---SGSLSLDG-----KGYSQLSAR-------ELAckvaF 81
Cdd:NF040905  18 DDVNLSVREGEIHALCGENGAGKSTLMK----VLSgvyPHgsyEGEILFDGevcrfKDIRDSEALgiviihqELA----L 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQvLPIPEGV---NVRqlvaygrsphnSLWGRLSGADQHSvdQALQRMELATLAERP---LSDLSGGQRQRAWLAMILA 155
Cdd:NF040905  90 IPY-LSIAENIflgNER-----------AKRGVIDWNETNR--RARELLAKVGLDESPdtlVTDIGVGKQQLVEIAKALS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
GguA NF040905
sugar ABC transporter ATP-binding protein;
140-193 4.78e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 4.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
 
Name Accession Description Interval E-value
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
2-256 1.90e-172

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 475.66  E-value: 1.90e-172
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:PRK11231   1 MTLRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11231  81 LPQHHLTPEGITVRELVAYGRSPWLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:PRK11231 161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTPGLLRTVFDVEAE 240
                        250
                 ....*....|....*
gi 492172462 242 IMREPVAGTPMCIVE 256
Cdd:PRK11231 241 IHPEPVSGTPMCVVR 255
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
3-254 4.02e-130

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: 368.60  E-value: 4.02e-130
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1120   81 PQEPPAPFGLTVRELVALGRYPHLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQ 241
Cdd:COG1120  161 LDEPTSHLDLAHQLEVLELLRRLARErGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLTPELLEEVYGVEAR 240
                        250
                 ....*....|...
gi 492172462 242 IMREPVAGTPMCI 254
Cdd:COG1120  241 VIEDPVTGRPLVL 253
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
13-254 1.10e-93

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 276.19  E-value: 1.10e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGV 92
Cdd:COG4604   11 YGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQENHINSRL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYGRSPHNSlwGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:COG4604   91 TVRELVAFGRFPYSK--GRLTAEDREIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDM 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 173 SHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQImrEPVAGTP 251
Cdd:COG4604  169 KHSVQMMKLLRRLADElGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEIITPEVLSDIYDTDIEV--EEIDGKR 246

                 ...
gi 492172462 252 MCI 254
Cdd:COG4604  247 ICV 249
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
4-254 1.33e-88

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 263.77  E-value: 1.33e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:PRK10253   8 LRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVARRIGLLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10253  88 QNATTPGDITVQELVARGRYPHQPLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQI 242
Cdd:PRK10253 168 DEPTTWLDISHQIDLLELLSELNREkGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEIVTAELIERIYGLRCMI 247
                        250
                 ....*....|..
gi 492172462 243 MREPVAGTPMCI 254
Cdd:PRK10253 248 IDDPVAGTPLVV 259
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
5-221 6.05e-85

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: 251.20  E-value: 6.05e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPq 84
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVP- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 vlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03214   80 -------------------------------------QALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLD 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03214  123 EPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
4-252 3.59e-83

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 249.65  E-value: 3.59e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARRRAVLP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYGRSPHnslwGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ------- 156
Cdd:COG4559   82 QHSSLAFPFTVEEVVALGRAPH----GSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAQlwepvdg 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVF 236
Cdd:COG4559  158 GPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPEEVLTDELLERVY 237
                        250
                 ....*....|....*.
gi 492172462 237 DVHVQIMREPVAGTPM 252
Cdd:COG4559  238 GADLRVLAHPEGGCPQ 253
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-245 3.73e-82

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 246.54  E-value: 3.73e-82
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARelackVA 80
Cdd:COG1121    4 MPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR-----IG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLPIPEG--VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:COG1121   79 YVPQRAEVDWDfpITVRDVVLMGRYGRRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMqGGRLVTCGAPGDVLTAELVCQVFDV 238
Cdd:COG1121  159 DLLLLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLGAVREYFDRVLLL-NRGLVAHGPPEEVLTPENLSRAYGG 237

                 ....*..
gi 492172462 239 HVQIMRE 245
Cdd:COG1121  238 PVALLAH 244
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
4-252 1.45e-77

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 235.44  E-value: 1.45e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:PRK13548   3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARRRAVLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYGRSPhnslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA---- 159
Cdd:PRK13548  83 QHSSLSFPFTVEEVVAMGRAP----HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAQLWEpdgp 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 160 --IVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVF 236
Cdd:PRK13548 159 prWLLLDEPTSALDLAHQHHVLRLARQLAHErGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLTPETLRRVY 238
                        250
                 ....*....|....*.
gi 492172462 237 DVHVQIMREPVAGTPM 252
Cdd:PRK13548 239 GADVLVQPHPETGAPL 254
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
18-255 2.54e-76

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 232.37  E-value: 2.54e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQL 97
Cdd:PRK10575  26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:PRK10575 106 VAIGRYPWHGALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 178 LLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQIMREPVAGTPMCIV 255
Cdd:PRK10575 186 VLALVHRLSQErGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAELMRGETLEQIYGIPMGILPHPAGAAPVSFV 264
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-251 5.50e-70

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 220.87  E-value: 5.50e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVA 80
Cdd:PRK09536   1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK09536  81 SVPQDTSLSFEFDVRQVVEMGRTPHRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHV 240
Cdd:PRK09536 161 LLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTADTLRAAFDART 240
                        250
                 ....*....|.
gi 492172462 241 QIMREPVAGTP 251
Cdd:PRK09536 241 AVGTDPATGAP 251
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
5-212 1.27e-68

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: 210.85  E-value: 1.27e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARelackVAFLPQ 84
Cdd:cd03235    1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR-----IGYVPQ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 VLPIPEG--VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03235   76 RRSIDRDfpISVRDVVLMGLYGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVM 212
Cdd:cd03235  156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEYFDRVLLL 205
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
4-230 4.88e-60

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: 189.47  E-value: 4.88e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG1122    1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQ------VLPIpegvnVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1122   81 FQnpddqlFAPT-----VEEDVAFG--PENL---GLPREEiRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLA 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG1122  151 MEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDY 225
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
12-212 4.61e-57

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 180.89  E-value: 4.61e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLsldgkgysqlsARELACKVAFLPQVLPIPEG 91
Cdd:NF040873   1 GYGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV-----------RRAGGARVAYVPQRSEVPDS 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 --VNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:NF040873  70 lpLTVRDLVAMGRWARRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTG 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLHDINQAcRYADHLAVM 212
Cdd:NF040873 150 LDAESRERIIALLAEEHARGATVVVVTHDLELV-RRADPCVLL 191
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-231 1.54e-56

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 181.03  E-value: 1.54e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAcKVAFLP 83
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRR-RIGYVP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:COG1131   80 QEPALYPDLTVRENLRF--------FARLYGLPRKEarerIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAEL 231
Cdd:COG1131  152 LLILDEPTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELKARLL 223
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
4-227 5.84e-55

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


Pssm-ID: 443618 [Multi-domain]  Cd Length: 243  Bit Score: 176.97  E-value: 5.84e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAcKVAFLP 83
Cdd:COG4555    2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARR-QIGVLP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYgrspHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:COG4555   81 DERGLYDRLTVRENIRY----FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4555  157 DEPTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDELR 220
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
14-216 4.60e-54

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: 173.81  E-value: 4.60e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlpiPE--- 90
Cdd:cd03225   12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVFQN---PDdqf 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 -GVNVRQLVAYGrsPHNSLwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03225   89 fGPTVEEEVAFG--LENLG---LPEEEIEErVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTA 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 492172462 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03225  164 GLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLLELADRVIVLEDGK 211
hmuV PRK13547
heme ABC transporter ATP-binding protein;
3-255 6.71e-54

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 175.40  E-value: 6.71e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ--------SGSLSLDGKGYSQLSARE 74
Cdd:PRK13547   1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  75 LACKVAFLPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13547  81 LARLRAVLPQAAQPAFAFSAREIVLLGRYPHARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 155 AQ---------DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRLVTCGAPG 224
Cdd:PRK13547 161 AQlwpphdaaqPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVHDPNLAARHADRIAMLADGAIVAHGAPA 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 492172462 225 DVLTAELVCQVFDVHVQIMREPvAGTPMCIV 255
Cdd:PRK13547 241 DVLTPAHIARCYGFAVRLVDAG-DGVPPVIV 270
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
19-256 2.45e-53

ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism];


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 173.10  E-value: 2.45e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAG-LLPGQGEILLNGRPLSDWSAAELARHRAYLSQQQSPPFAMPVFQYL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 AYGRSPHNSlwgrlSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ-------DAAIVLLDEPTTYLD 171
Cdd:COG4138   91 ALHQPAGAS-----SEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLQvwptinpEGQLLLLDEPMNSLD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQIMRepVAGTP 251
Cdd:COG4138  166 VAQQAALDRLLRELCQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPENLSEVFGVKFRRLE--VEGHR 243

                 ....*
gi 492172462 252 MCIVE 256
Cdd:COG4138  244 WLIPT 248
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
2-231 4.09e-53

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 172.55  E-value: 4.09e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA---C 77
Cdd:COG3638    1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRrlrR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQVLPIPEGVNVRQLVAYGRSPHNSLW----GRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG3638   81 RIGMIFQQFNLVPRLSVLTNVLAGRLGRTSTWrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVAIARA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 154 LAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG3638  161 LVQEPKLILADEPVASLDpkTARQV--MDLLRRIAREdGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAELTDAV 238

                 .
gi 492172462 231 L 231
Cdd:COG3638  239 L 239
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
3-229 4.27e-50

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: 171.62  E-value: 4.27e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGY-----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAc 77
Cdd:COG1123  260 LLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLR- 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 kvAFLPQVLPI---PEG-----VNVRQLVAYGRSPHnslwGRLSGADQHS-VDQALQRMEL-ATLAERPLSDLSGGQRQR 147
Cdd:COG1123  339 --ELRRRVQMVfqdPYSslnprMTVGDIIAEPLRLH----GLLSRAERRErVAELLERVGLpPDLADRYPHELSGGQRQR 412
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG1123  413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRElGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEV 492

                 ...
gi 492172462 227 LTA 229
Cdd:COG1123  493 FAN 495
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
4-221 1.26e-46

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: 154.60  E-value: 1.26e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVAFLP 83
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERR--NIGMVF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYGrsphnsLWGRLSGADQH--SVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03259   79 QDYALFPHLTVAENIAFG------LKLRGVPKAEIraRVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03259  153 LLDEPLSALDAKLREELREELKELQRElGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
3-221 1.32e-46

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: 154.97  E-value: 1.32e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC- 77
Cdd:cd03257    1 LLEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 --KVAFLPQvlpipegvnvrqlvaygrSPHNSLWGRLSGADQ----------HSVDQALQRMELATLAERPLSD------ 139
Cdd:cd03257   81 rkEIQMVFQ------------------DPMSSLNPRMTIGEQiaeplrihgkLSKKEARKEAVLLLLVGVGLPEevlnry 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 ---LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:cd03257  143 pheLSGGQRQRVAIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVAKIADRVAVMYAG 222

                 ....*.
gi 492172462 216 RLVTCG 221
Cdd:cd03257  223 KIVEEG 228
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
4-217 2.62e-46

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: 152.55  E-value: 2.62e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAFLP 83
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03230   80 EEPSLYENLTVRENL----------------------------------------KLSGGMKQRLALAQALLHDPELLIL 119
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:cd03230  120 DEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERLCDRVAILNNGRI 173
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-229 2.81e-45

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: 158.91  E-value: 2.81e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MS-ILKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSARE 74
Cdd:COG1123    1 MTpLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  75 LACKVAFLPQVlpiPE----GVNVRQLVAYGrsphnSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAW 149
Cdd:COG1123   81 RGRRIGMVFQD---PMtqlnPVTVGDQIAEA-----LENLGLSRAEARArVLELLEAVGLERRLDRYPHQLSGGQRQRVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1123  153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRErGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILA 232

                 .
gi 492172462 229 A 229
Cdd:COG1123  233 A 233
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
5-216 4.80e-45

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: 148.93  E-value: 4.80e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   5 KAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQ 84
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGYVPQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 vlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd00267   81 -------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLD 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd00267  106 EPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAADRVIVLKDGK 157
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
4-232 7.93e-45

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: 150.67  E-value: 7.93e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA-CKVA-- 80
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIArLGIGrt 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 F-LPQVLP---IPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:cd03219   81 FqIPRLFPeltVLENVMVAAQARTGSGLLLARARREEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:cd03219  161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPRV 236
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
4-236 1.27e-44

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: 150.41  E-value: 1.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGA-TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KV 79
Cdd:cd03256    1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQlrrQI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVLPIPEGVNVRQLVAYGR----SPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:cd03256   81 GMIFQQFNLIERLSVLENVLSGRlgrrSTWRSLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALM 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 156 QDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDvLTAELV 232
Cdd:cd03256  161 QQPKLILADEPVASLDpaSSRQV--MDLLKRINREeGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAE-LTDEVL 237

                 ....
gi 492172462 233 CQVF 236
Cdd:cd03256  238 DEIY 241
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
6-218 1.55e-43

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: 146.63  E-value: 1.55e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   6 AQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELACKVAFLPQ 84
Cdd:cd03226    2 IENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGK---PIKAKERRKSIGYVMQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 vlpipegvNV-RQLvaYGRSPHNSLwgRLS----GADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:cd03226   79 --------DVdYQL--FTDSVREEL--LLGlkelDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKD 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03226  147 LLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLAKVCDRVLLLANGAIV 205
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
4-218 3.75e-43

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: 146.87  E-value: 3.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGA----TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:COG1124    2 LEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVlpiPEG-VNVRQLVayGRSPHNSLWGRLSGADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:COG1124   82 QMVFQD---PYAsLHPRHTV--DRILAEPLRIHGLPDREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILE 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:COG1124  157 PELLLLDEPTSALDVSVQAEILNLLKDLREErGLTYLFVSHDLAVVAHLCDRVAVMQNGRIV 218
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
4-217 5.53e-43

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 145.34  E-value: 5.53e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLP 83
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGvNVRQLVAYGRSPHNSLWgrlsgaDQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG4619   81 QEPALWGG-TVRDNLPFPFQLRERKF------DRERALELLERLGLpPDILDKPVERLSGGERQRLALIRALLLQPDVLL 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:COG4619  154 LDEPTSALDPENTRRVEELLREYLAEeGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
4-198 8.87e-43

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: 144.54  E-value: 8.87e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGySQLSARELACKVAFLP 83
Cdd:COG4133    3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEP-IRDAREDYRRRLAYLG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAygrsphnsLWGRLSG--ADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:COG4133   82 HADGLKPELTVRENLR--------FWAALYGlrADREAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLW 153
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:COG4133  154 LLDEPFTALDAAGVALLAELIAAHLARGGAVLLTTHQ 190
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
1-227 2.43e-42

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 147.60  E-value: 2.43e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG-YSQLSARELacKV 79
Cdd:COG1118    1 MSI-EVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDlFTNLPPRER--RV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQvlpipegvN--------VRQLVAYG---RSPhnslwgrlSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQR 147
Cdd:COG1118   78 GFVFQ--------HyalfphmtVAENIAFGlrvRPP--------SKAEiRARVEELLELVQLEGLADRYPSQLSGGQRQR 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG1118  142 VALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLhDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEV 221

                 .
gi 492172462 227 L 227
Cdd:COG1118  222 Y 222
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
22-255 3.67e-42

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 144.31  E-value: 3.67e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLVAYG 101
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAWSAAELARHRAYLSQQQTPPFAMPVFQYLTLH 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPHNSLwgrlsGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ-------DAAIVLLDEPTTYLDISH 174
Cdd:PRK03695  94 QPDKTRT-----EAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLLLLDEPMNSLDVAQ 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVHVQimREPVAGTPMCI 254
Cdd:PRK03695 169 QAALDRLLSELCQQGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPENLAQVFGVNFR--RLDVEGHPMLI 246

                 .
gi 492172462 255 V 255
Cdd:PRK03695 247 S 247
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-226 3.60e-41

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 144.47  E-value: 3.60e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelacKVA 80
Cdd:COG3842    3 MPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR------------DVT 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPqvlpiPE--GVN-------------VRQLVAYG---RsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLS 141
Cdd:COG3842   71 GLP-----PEkrNVGmvfqdyalfphltVAENVAFGlrmR--------GVPKAEIRArVAELLELVGLEGLADRYPHQLS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 142 GGQRQRAWLAMILAQDAAIVLLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:COG3842  138 GGQQQRVALARALAPEPRVLLLDEPLSALDaklrEEMREELRRLQREL---GITFIYVTHDQEEALALADRIAVMNDGRI 214

                 ....*....
gi 492172462 218 VTCGAPGDV 226
Cdd:COG3842  215 EQVGTPEEI 223
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-232 4.41e-41

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: 141.71  E-value: 4.41e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA-CKV 79
Cdd:COG0411    2 DPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIArLGI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 A--FlpQVLPIPEGVNVRQ--LVAYGRSPHNSLWGRLSG---------ADQHSVDQALQRMELATLAERPLSDLSGGQRQ 146
Cdd:COG0411   82 ArtF--QNPRLFPELTVLEnvLVAAHARLGRGLLAALLRlprarreerEARERAEELLERVGLADRADEPAGNLSYGQQR 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGD 225
Cdd:COG0411  160 RLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAE 239

                 ....*..
gi 492172462 226 VLTAELV 232
Cdd:COG0411  240 VRADPRV 246
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
4-218 5.64e-41

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: 140.78  E-value: 5.64e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARIL-----TPQSGSLSLDGKGYSQLSAR--ELA 76
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDVDvlELR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 CKVAFLPQvLPIPEGVNVRQLVAYGRSPHNSLWGRLSGAdqhSVDQALQRMELATLAERPLS--DLSGGQRQRAWLAMIL 154
Cdd:cd03260   81 RRVGMVFQ-KPNPFPGSIYDNVAYGLRLHGIKLKEELDE---RVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARAL 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03260  157 ANEPEVLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMQQAARVADRTAFLLNGRLV 219
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
24-238 6.86e-41

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 140.37  E-value: 6.86e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   24 FSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlSARELACKVAFLPQV------LPIpegvNVRQL 97
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGA-----SPGKGWRHIGYVPQRhefawdFPI----SVAHT 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   98 VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR03771  72 VMSGRTGHIGWLRRPCVADFAAVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQEL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462  178 LLDLMRELSAEGKTVITVLHDINQACRYADHLaVMQGGRLVTCGAPGDVLTAELVCQVFDV 238
Cdd:TIGR03771 152 LTELFIELAGAGTAILMTTHDLAQAMATCDRV-VLLNGRVIADGTPQQLQDPAPWMTTFGV 211
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-245 1.14e-40

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 140.60  E-value: 1.14e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSG-SLSLDGKGYSQLSARELACKV 79
Cdd:COG1119    1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGEDVWELRKRI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVL--PIPEGVNVRQLVAYGRspHNS--LWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:COG1119   81 GLVSPALqlRFPRDETVLDVVLSGF--FDSigLYREPTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG-KTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:COG1119  159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGaPTLVLVTHHVEEIPPGITHVLLLKDGRVVAAGPKEEVLTSENLSE 238
                        250
                 ....*....|.
gi 492172462 235 VFDVHVQIMRE 245
Cdd:COG1119  239 AFGLPVEVERR 249
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
3-230 2.33e-40

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: 139.34  E-value: 2.33e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA---CKV 79
Cdd:COG1127    5 MIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYelrRRI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQvlpipEG-----VNVRQLVAYgrsP---HnslwGRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWL 150
Cdd:COG1127   85 GMLFQ-----GGalfdsLTVFENVAF---PlreH----TDLSEAEiRELVLEKLELVGLPGAADKMPSELSGGMRKRVAL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 151 AMILAQDAAIVLLDEPTTYLD-ISHQVeLLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1127  153 ARALALDPEILLYDEPTAGLDpITSAV-IDELIRELRDElGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLA 231

                 ..
gi 492172462 229 AE 230
Cdd:COG1127  232 SD 233
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
14-228 5.64e-40

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: 138.59  E-value: 5.64e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLpipegvn 93
Cdd:cd03295   12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYVIQQI------- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 vrqlvayGRSPHNSLWG------RLSGADQHSVDQ------ALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03295   85 -------GLFPHMTVEEnialvpKLLKWPKEKIREradellALVGLDPAEFADRYPHELSGGQQQRVGVARALAADPPLL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 162 LLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:cd03295  158 LMDEPFGALDpitrDQLQEEFKRLQQEL---GKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILR 225
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
23-230 1.18e-39

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 137.19  E-value: 1.18e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  23 SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL--SARelacKVAFLPQvlpipEG-----VNVR 95
Cdd:COG3840   19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALppAER----PVSMLFQ-----ENnlfphLTVA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVAYGRSPHnslwGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:COG3840   90 QNIGLGLRPG----LKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 176 VELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG3840  166 QEMLDLVDELCRErGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGE 221
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
4-227 1.44e-39

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: 144.13  E-value: 1.44e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:COG4988  337 IELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRRQIAWV 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGvNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAER-------PLSD----LSGGQRQRAWLA 151
Cdd:COG4988  417 PQNPYLFAG-TIRENLRLGR----------PDASDEELEAALEAAGLDEFVAAlpdgldtPLGEggrgLSGGQAQRLALA 485
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQAcRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4988  486 RALLRDAPLLLLDEPTAHLDAETEAEILQALRRL-AKGRTVILITHRLALL-AQADRILVLDDGRIVEQGTHEELL 559
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-218 1.32e-38

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 134.40  E-value: 1.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHL----DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA- 76
Cdd:COG1136    3 PLLELRNLtksyGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAr 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 ---CKVAFLPQ---VLPipeGVNVRQLVAYgrsPHnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWL 150
Cdd:COG1136   83 lrrRHIGFVFQffnLLP---ELTALENVAL---PL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAI 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRLV 218
Cdd:COG1136  156 ARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELA-ARADRVIRLRDGRIV 223
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
3-223 2.37e-38

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: 134.35  E-value: 2.37e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    3 ILKAQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL---ACK 78
Cdd:TIGR02315   1 MLEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLrklRRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   79 VAFLPQVLPIPEGVNVRQLVAYGR----SPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVLHGRlgykPTWRSLLGRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAIARAL 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462  155 AQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:TIGR02315 161 AQQPDLILADEPIASLDpkTSKQV--MDYLKRINKEdGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAP 230
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
4-217 3.32e-38

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: 133.00  E-value: 3.32e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGA----TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC-- 77
Cdd:cd03255    1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAfr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 --KVAFLPQ---VLPipeGVNVRQLVAYGrsphnSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:cd03255   81 rrHIGFVFQsfnLLP---DLTALENVELP-----LLLAGVPKKERRErAEELLERVGLGDRLNHYPSELSGGQQQRVAIA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRL 217
Cdd:cd03255  153 RALANDPKIILADEPTGNLDSETGKEVMELLRELNKEaGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
7-228 6.71e-38

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: 133.01  E-value: 6.71e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   7 QHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL---ACKVAFLP 83
Cdd:cd03261    4 RGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGMLF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYGRSPHnslwGRLSgaDQHSVDQALQRMELATLAE----RPlSDLSGGQRQRAWLAMILAQDAA 159
Cdd:cd03261   84 QSGALFDSLTVFENVAFPLREH----TRLS--EEEIREIVLEKLEAVGLRGaedlYP-AELSGGMKKRVALARALALDPE 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 160 IVLLDEPTTYLD-ISHQVeLLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:cd03261  157 LLLYDEPTAGLDpIASGV-IDDLIRSLKKElGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRA 226
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
4-221 5.00e-37

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: 130.09  E-value: 5.00e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYsQLSARElacKVAFLP 83
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPL-DIAARN---RIGYLP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVR-QLVAYGRsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03269   77 EERGLYPKMKVIdQLVYLAQ-----LKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLI 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03269  152 LDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
14-202 1.40e-36

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


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 128.31  E-value: 1.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKVAFlpqVLPIPE- 90
Cdd:TIGR01166   3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEplDYSRKGLLERRQRVGL---VFQDPDd 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   91 ---GVNVRQLVAYGrsPHNSlwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:TIGR01166  80 qlfAADVDQDVAFG--PLNL---GLSEAEVERrVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEP 154
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 492172462  167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDINQA 202
Cdd:TIGR01166 155 TAGLDPAGREQMLAILRRLRAEGMTVVISTHDVDLA 190
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
4-216 1.55e-36

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 127.50  E-value: 1.55e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGAT--RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:cd03228    1 IEFKNVSFSYPGRpkPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQvlpipegvnvrqlvaygrSPHnslwgRLSGadqhsvdqalqrmelaTLAErplSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03228   81 VPQ------------------DPF-----LFSG----------------TIRE---NILSGGQRQRIAIARALLRDPPIL 118
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINQAcRYADHLAVMQGGR 216
Cdd:cd03228  119 ILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTI-RDADRIIVLDDGR 171
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
4-216 3.20e-36

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: 126.92  E-value: 3.20e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA--RELACKVAF 81
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDelPPLRRRIGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGVNVRQLVAYGrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03229   81 VFQDFALFPHLTVLENIALG--------------------------------------LSGGQQQRVALARALAMDPDVL 122
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:cd03229  123 LLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
4-221 3.30e-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: 127.69  E-value: 3.30e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgYSQLSAR-ELACKVAFL 82
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDG--QDVLKQPqKLRRRIGYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGVNVRQLVAYgrsphNSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03264   78 PQEFGVYPNFTVREFLDY-----IAWLKGIPSKEVKArVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSIL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03264  153 IVDEPTAGLDPEERIRFRNLLSELGED-RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
3-221 4.82e-36

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 129.84  E-value: 4.82e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARelacKVAFL 82
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRR----RIGYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 pqvlpiPE--G----VNVR-QLVAYGRsphnsLWGrLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:COG4152   77 ------PEerGlypkMKVGeQLVYLAR-----LKG-LSKAEaKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAAL 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 155 AQDAAIVLLDEPTTYLD-IShqVELL-DLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:COG4152  145 LHDPELLILDEPFSGLDpVN--VELLkDVIRELAAKGTTVIFSSHQMELVEELCDRIVIINKGRKVLSG 211
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
19-168 4.96e-36

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: 125.45  E-value: 4.96e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFPRLTVRENL 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462   99 AYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:pfam00005  81 RLGL----LLKGLSKREKDARAEEALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-232 8.46e-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: 127.41  E-value: 8.46e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-V 79
Cdd:COG0410    1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIARLgI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQ---VLPipeGVNVR---QLVAYGRSphnslwgrlsgaDQHSVDQALQRM-----ELATLAERPLSDLSGGQRQRA 148
Cdd:COG0410   81 GYVPEgrrIFP---SLTVEenlLLGAYARR------------DRAEVRADLERVyelfpRLKERRRQRAGTLSGGEQQML 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 149 WLAMILAQDAAIVLLDEPTtyLDISHQV--ELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG0410  146 AIGRALMSRPKLLLLDEPS--LGLAPLIveEIFEIIRRLNREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223

                 ....*.
gi 492172462 227 LTAELV 232
Cdd:COG0410  224 LADPEV 229
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
4-227 8.51e-36

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: 127.17  E-value: 8.51e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-VAFL 82
Cdd:cd03224    1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARAgIGYV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGVNVR---QLVAYGRSPhnslwgrlsGADQHSVDQALQRM-ELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03224   81 PEGRRIFPELTVEenlLLGAYARRR---------AKRKARLERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRP 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03224  152 KLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELL 220
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
4-218 1.91e-35

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: 126.05  E-value: 1.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYG----ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlSARELACKV 79
Cdd:cd03293    1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGE-----PVTGPGPDR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQ---VLPipeGVNVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:cd03293   76 GYVFQqdaLLP---WLTVLDNVALGL----ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAV 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 157 DAAIVLLDEPTTYLD----ISHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRLV 218
Cdd:cd03293  149 DPDVLLLDEPFSALDaltrEQLQEELLDIWRE---TGKTVLLVTHDIDEAVFLADRVVVLSArpGRIV 213
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
1-226 2.48e-35

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: 126.30  E-value: 2.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVA 80
Cdd:cd03296    1 MSI-EVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQER--NVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLPIPEGVNVRQLVAYG-RSPHNSlwGRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03296   78 FVFQHYALFRHMTVFDNVAFGlRVKPRS--ERPPEAEiRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEP 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:cd03296  156 KVLLLDEPFGALDAKVRKELRRWLRRLHDElHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEV 224
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
19-236 3.76e-35

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 126.92  E-value: 3.76e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackVAFLPQVLPIPEG--VNVRQ 96
Cdd:PRK15056  23 LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQKNL---VAYVPQSEEVDWSfpVLVED 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  97 LVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQV 176
Cdd:PRK15056 100 VVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEA 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 177 ELLDLMRELSAEGKTVITVLHDINQACRYADHlAVMQGGRLVTCGAPGDVLTAELVCQVF 236
Cdd:PRK15056 180 RIISLLRELRDEGKTMLVSTHNLGSVTEFCDY-TVMVKGTVLASGPTETTFTAENLELAF 238
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
2-221 4.50e-35

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 126.30  E-value: 4.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKG-YS-QLSARE 74
Cdd:COG1117   10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRCLNRMndLIPGarvEGEILLDGEDiYDpDVDVVE 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  75 LACKVAFLPQVL-PIPEGV--NvrqlVAYG-RsphnsLWGRLSGAD-QHSVDQALQRMEL-----ATLAERPLSdLSGGQ 144
Cdd:COG1117   90 LRRRVGMVFQKPnPFPKSIydN----VAYGlR-----LHGIKSKSElDEIVEESLRKAALwdevkDRLKKSALG-LSGGQ 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 145 RQRAWLAMILAQDAAIVLLDEPTTYLD-IS-HQVEllDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:COG1117  160 QQRLCIARALAVEPEVLLMDEPTSALDpIStAKIE--ELILELKKD-YTIVIVTHNMQQAARVSDYTAFFYLGELVEFG 235
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
13-221 4.80e-35

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: 124.91  E-value: 4.80e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFspPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL--SARelacKVAFLPQVLPIPE 90
Cdd:cd03298   10 YGEQPMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppADR----PVSMLFQENNLFA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GVNVRQLVAYGRSPhnSLwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03298   84 HLTVEQNVGLGLSP--GL--KLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAAL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 492172462 171 DISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03298  160 DPALRAEMLDLVLDLHAEtKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
21-228 6.83e-35

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: 126.03  E-value: 6.83e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---GYSQLSARELACKVAFLPQvlpIPEgvnvRQL 97
Cdd:TIGR04521  23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRditAKKKKKLKDLRKKVGLVFQ---FPE----HQL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   98 --------VAYGrsPHNslWGrLSGADQHS-VDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR04521  96 feetvykdIAFG--PKN--LG-LSEEEAEErVKEALELVGLdEEYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPT 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462  168 TYLDISHQVELLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:TIGR04521 171 AGLDPKGRKEILDLFKRLhKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFS 232
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
4-227 7.39e-35

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


Pssm-ID: 444011 [Multi-domain]  Cd Length: 569  Bit Score: 131.43  E-value: 7.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGY-GATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:COG4987  334 LELEDVSFRYpGAGRPVlDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRRIAV 413
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGvNVRQ--LVAYGRSPHNSLWgrlsgadqhsvdQALQRMELATLAERpLSD------------LSGGQRQR 147
Cdd:COG4987  414 VPQRPHLFDT-TLREnlRLARPDATDEELW------------AALERVGLGDWLAA-LPDgldtwlgeggrrLSGGERRR 479
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDInQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4987  480 LALARALLRDAPILLLDEPTEGLDAATEQALLADLLEA-LAGRTVLLITHRL-AGLERMDRILVLEDGRIVEQGTHEELL 557
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-226 8.58e-35

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 125.90  E-value: 8.58e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:PRK13635   4 EIIRVEHISFRYpdAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVWDVRRQV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFlpqVLPIPE----GVNVRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13635  84 GM---VFQNPDnqfvGATVQDDVAFGLEnigvPREEMVER--------VDQALRQVGMEDFLNREPHRLSGGQKQRVAIA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13635 153 GVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEI 227
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
14-228 8.89e-35

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: 125.83  E-value: 8.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC-----------KVAFL 82
Cdd:cd03294   35 GQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkkismvfqSFALL 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVlpipegvNVRQLVAYGRSphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03294  115 PHR-------TVLENVAFGLE----VQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILL 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 163 LDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:cd03294  184 MDEAFSALDplirREMQDELLRLQAEL---QKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILT 250
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-239 1.44e-34

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 126.07  E-value: 1.44e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAF 81
Cdd:PRK13537   6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPS-RARHARQRVGV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGVNVRQ-LVAYGRsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK13537  85 VPQFDNLDPDFTVREnLLVFGR-----YFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVH 239
Cdd:PRK13537 160 LVLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIESEIGCDVIEIY 238
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-232 1.83e-34

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 129.37  E-value: 1.83e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAF 81
Cdd:COG1129    4 LLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDaQAAGIAI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQ-VLPIPEgVNVRQLVAYGRSPHNslWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQ-----RAwlamiL 154
Cdd:COG1129   84 IHQeLNLVPN-LSVAENIFLGREPRR--GGLIDWRAMRRrARELLARLGLDIDPDTPVGDLSVAQQQlveiaRA-----L 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 155 AQDAAIVLLDEPTTYLDiSHQVE-LLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:COG1129  156 SRDARVLILDEPTASLT-EREVErLFRIIRRLKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAELTEDELV 233
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
16-234 2.38e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 124.85  E-value: 2.38e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFlpqVLPIPE----G 91
Cdd:PRK13647  18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL---VFQDPDdqvfS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 VNVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:PRK13647  95 STVWDDVAFG--PVNM---GLDKDEvERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYL 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 171 DISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:PRK13647 170 DPRGQETLMEILDRLHNQGKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTDEDIVEQ 233
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
19-221 2.74e-34

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 123.25  E-value: 2.74e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:cd03266   21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRLTARENL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 AYgrsphnslWGRLSGADQHSVDQAL----QRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03266  100 EY--------FAGLYGLKGDELTARLeelaDRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMA 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03266  172 TRALREFIRQLRALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
1-226 3.53e-34

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 126.35  E-value: 3.53e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVA 80
Cdd:PRK10851   1 MSI-EIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR--KVG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLPIPEGVNVRQLVAYGRS--PHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK10851  78 FVFQHYALFRHMTVFDNIAFGLTvlPRRE---RPNAAAiKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVE 154
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK10851 155 PQILLLDEPFGALDAQVRKELRRWLRQLHEELKfTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQV 224
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
12-223 5.09e-34

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: 122.23  E-value: 5.09e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgkGYSQLSARELACK-VAFLPQVLPIPE 90
Cdd:cd03263   11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYIN--GYSIRTDRKAARQsLGYCPQFDALFD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GVNVRQLVAYgrspHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03263   89 ELTVREHLRF----YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGL 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492172462 171 DISHQVELLDLMRELSaEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:cd03263  165 DPASRRAIWDLILEVR-KGRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
3-229 7.12e-34

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 122.41  E-value: 7.12e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKVA 80
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEdlTDSKKDINKLRRKVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQ---------VLpipEGVNVRQLVAYGRSPHNslwgrlsgADQHSVDQaLQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:COG1126   81 MVFQqfnlfphltVL---ENVTLAPIKVKKMSKAE--------AEERAMEL-LERVGLADKADAYPAQLSGGQQQRVAIA 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLD---IShqvELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1126  149 RALAMEPKVMLFDEPTSALDpelVG---EVLDVMRDLAKEGMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFE 225

                 .
gi 492172462 229 A 229
Cdd:COG1126  226 N 226
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-226 4.20e-33

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 123.26  E-value: 4.20e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVA 80
Cdd:COG3839    1 MASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDR--NIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQ---VLPipeGVNVRQLVAYG---RsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG3839   79 MVFQsyaLYP---HMTVYENIAFPlklR--------KVPKAEIDRrVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRA 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 154 LAQDAAIVLLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:COG3839  148 LVREPKVFLLDEPLSNLDaklrVEMRAEIKRLHRRL---GTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEEL 221
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
14-212 4.31e-33

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: 125.86  E-value: 4.31e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvN 93
Cdd:TIGR02857 333 GRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQIAWVPQHPFLFAG-T 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   94 VRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATL-AERPL----------SDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:TIGR02857 412 IAENIRLAR----------PDASDAEIREALERAGLDEFvAALPQgldtpigeggAGLSGGQAQRLALARAFLRDAPLLL 481
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 492172462  163 LDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQACRyADHLAVM 212
Cdd:TIGR02857 482 LDEPTAHLDAETEAEVLEALRAL-AQGRTVLLVTHRLALAAL-ADRIVVL 529
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-218 6.36e-33

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 120.58  E-value: 6.36e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARela 76
Cdd:COG1116    5 APALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPD--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 ckVAFLPQ---VLPipegvNVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMI 153
Cdd:COG1116   82 --RGVVFQepaLLPw---lTVLDNVALGL----ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARA 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 154 LAQDAAIVLLDEPTTYLD----ISHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRLV 218
Cdd:COG1116  153 LANDPEVLLMDEPFGALDaltrERLQDELLRLWQE---TGKTVLFVTHDVDEAVFLADRVVVLSArpGRIV 220
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
3-228 2.28e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 119.80  E-value: 2.28e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKV 79
Cdd:PRK13639   1 ILETRDLKYSYpDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEpiKYDKKSLLEVRKTV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQ----VLPIPegvNVRQLVAYGrsPHNSlwgRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13639  81 GIVFQnpddQLFAP---TVEEDVAFG--PLNL---GLSKEEvEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGIL 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK13639 153 AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFS 226
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
18-230 2.79e-32

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 119.33  E-value: 2.79e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlpiPE----GVN 93
Cdd:PRK13632  24 ALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEIRKKIGIIFQN---PDnqfiGAT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13632 101 VEDDIAFGlenkKVPPKKMKDI--------IDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 170 LDISHQVELLDLMRELSAEG-KTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAIL-ADKVIVFSEGKLIAQGKPKEILNNK 233
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
21-218 3.64e-32

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: 117.40  E-value: 3.64e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPaGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYsqLSARELAC------KVAFLPQVLPIPEGVNV 94
Cdd:cd03297   16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVL--FDSRKKINlppqqrKIGLVFQQYALFPHLNV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQLVAYGrsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03297   93 RENLAFG------LKRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 492172462 175 QVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03297  167 RLQLLPELKQIKKNlNIPVIFVTHDLSEAEYLADRIVVMEDGRLQ 211
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
18-230 1.11e-31

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: 123.02  E-value: 1.11e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQL 97
Cdd:COG2274  490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGVVLQDVFLFSG-TIREN 568
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGRsphnslwgrlSGADQHSVDQALQRMELATLAER-------PLSD----LSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG2274  569 ITLGD----------PDATDEEIIEAARLAGLHDFIEAlpmgydtVVGEggsnLSGGQRQRLAIARALLRNPRILILDEA 638
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 167 TTYLDISHQVELLDLMRELSAeGKTVITVLHDINQAcRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG2274  639 TSALDAETEAIILENLRRLLK-GRTVIIIAHRLSTI-RLADRIIVLDKGRIVEDGTHEELLARK 700
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-198 2.53e-31

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 120.94  E-value: 2.53e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   6 AQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQV 85
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG-----------LRIGYLPQE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  86 LPIPEGVNVRQLVAYGRSPHNSLWGRL---------SGADQHSVDQALQRME--------------LATL------AERP 136
Cdd:COG0488   70 PPLDDDLTVLDTVLDGDAELRALEAELeeleaklaePDEDLERLAELQEEFEalggweaearaeeiLSGLgfpeedLDRP 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 137 LSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIsHQVELLDlmRELSAEGKTVITVLHD 198
Cdd:COG0488  150 VSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDL-ESIEWLE--EFLKNYPGTVLVVSHD 208
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
3-218 3.62e-31

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: 117.46  E-value: 3.62e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSAREL 75
Cdd:COG0444    1 LLEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPgitSGEILFDGEDLLKLSEKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  76 ----ACKVAFLPQ--------VLPIpegvnvRQLVAYGRSPHnslwGRLSGADQHS-VDQALQRMELaTLAERPLSD--- 139
Cdd:COG0444   81 rkirGREIQMIFQdpmtslnpVMTV------GDQIAEPLRIH----GGLSKAEARErAIELLERVGL-PDPERRLDRyph 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 -LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:COG0444  150 eLSGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRElGLAILFITHDLGVVAEIADRVAVMYAGRI 229

                 .
gi 492172462 218 V 218
Cdd:COG0444  230 V 230
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
13-226 4.45e-31

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: 115.03  E-value: 4.45e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaflpQVLPIP--- 89
Cdd:cd03300   10 YGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGK------------------DITNLPphk 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 EGVN-VRQlvAYGRSPHNSLW---------GRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03300   72 RPVNtVFQ--NYALFPHLTVFeniafglrlKKLPKAEIKErVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEP 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 159 AIVLLDEPTTYLDI----SHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:cd03300  150 KVLLLDEPLGALDLklrkDMQLELKRLQKEL---GITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEI 218
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
6-225 6.09e-31

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: 114.39  E-value: 6.09e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   6 AQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdgKGYSQLS-ARELACKVAFLPQ 84
Cdd:cd03265    3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATV--AGHDVVRePREVRRRIGIVFQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 VLPIPEGVNVRQ-LVAYGRsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03265   81 DLSVDDELTGWEnLYIHAR-----LYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGD 225
Cdd:cd03265  156 DEPTIGLDPQTRAHVWEYIEKLKEEfGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEE 218
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
4-218 6.10e-31

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: 112.52  E-value: 6.10e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFL 82
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRDaRRAGIAMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQvlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03216   81 YQ-------------------------------------------------------LSVGERQMVEIARALARNARLLI 105
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03216  106 LDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
1-228 1.98e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 113.85  E-value: 1.98e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKGYSQLSAREL 75
Cdd:PRK14247   1 MNKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPEarvSGEVYLDGQDIFKMDVIEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  76 ACKVAFLPQVL-PIPEgVNVRQLVAYGRSphnslWGRLSGAD---QHSVDQALQRMEL-ATLAER---PLSDLSGGQRQR 147
Cdd:PRK14247  81 RRRVQMVFQIPnPIPN-LSIFENVALGLK-----LNRLVKSKkelQERVRWALEKAQLwDEVKDRldaPAGKLSGGQQQR 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK14247 155 LCIARALAFQPEVLLADEPTANLDPENTAKIESLFLELKKD-MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVF 233

                 .
gi 492172462 228 T 228
Cdd:PRK14247 234 T 234
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-218 1.07e-29

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 112.26  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYG----ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-- 74
Cdd:COG4525    1 MSMLTVRHVSVRYPgggqPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADRgv 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  75 LACKVAFLPQVlpipegvNVRQLVAYGRsphnslwgRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWL 150
Cdd:COG4525   81 VFQKDALLPWL-------NVLDNVAFGL--------RLRGVPKAErrarAEELLALVGLADFARRRIWQLSGGMRQRVGI 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDI----SHQVELLDLMRElsaEGKTVITVLHDINQACRYADHLAVMQG--GRLV 218
Cdd:COG4525  146 ARALAADPRFLLMDEPFGALDAltreQMQELLLDVWQR---TGKGVFLITHSVEEALFLATRLVVMSPgpGRIV 216
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
13-239 1.14e-29

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 113.77  E-value: 1.14e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVAFLPQVLPIPEGV 92
Cdd:PRK13536  51 YGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA-RARLARARIGVVPQFDNLDLEF 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQ-LVAYGRsphnslWGRLSGADQHSVDQALqrMELATL---AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK13536 130 TVREnLLVFGR------YFGMSTREIEAVIPSL--LEFARLeskADARVSDLSGGMKRRLTLARALINDPQLLILDEPTT 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQVFDVH 239
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIDEHIGCQVIEIY 272
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
19-218 1.21e-29

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: 111.14  E-value: 1.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQLV 98
Cdd:cd03245   20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYG-TLRDNI 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 AYGRSPHNSL----WGRLSGADQHSVDQA--LQRMelatLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03245   99 TLGAPLADDErilrAAELAGVTDFVNKHPngLDLQ----IGERGRG-LSGGQRQAVALARALLNDPPILLLDEPTSAMDM 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 173 SHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRLV 218
Cdd:cd03245  174 NSEERLKERLRQL-LGDKTLIIITHRPS-LLDLVDRIIVMDSGRIV 217
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
18-217 1.55e-29

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: 109.23  E-value: 1.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipegvNVrQL 97
Cdd:cd03246   17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGYLPQ--------DD-EL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 vaygrsphnslwgrLSGadqhsvdqalqrmelaTLAErplSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:cd03246   88 --------------FSG----------------SIAE---NILSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERA 134
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492172462 178 LLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRL 217
Cdd:cd03246  135 LNQAIAALKAAGATRIVIAHRPE-TLASADRILVLEDGRV 173
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
3-227 2.17e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 111.86  E-value: 2.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKV 79
Cdd:PRK13636   5 ILKVEELNYNYSdGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLMKLRESV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFlpqVLPIPE----GVNVRQLVAYG----RSPHNSLwgrlsgadQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13636  85 GM---VFQDPDnqlfSASVYQDVSFGavnlKLPEDEV--------RKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK13636 154 GVLVMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVF 230
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
12-221 3.04e-29

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 115.65  E-value: 3.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipE 90
Cdd:COG1132  348 SYPGDRPVlKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVVPQ-----D 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GV----NVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAERpLSD------------LSGGQRQRAWLAMIL 154
Cdd:COG1132  423 TFlfsgTIRENIRYGR----------PDATDEEVEEAAKAAQAHEFIEA-LPDgydtvvgergvnLSGGQRQRIAIARAL 491
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQAcRYADHLAVMQGGRLVTCG 221
Cdd:COG1132  492 LKDPPILILDEATSALDTETEALIQEALERLMK-GRTTIVIAHRLSTI-RNADRILVLDDGRIVEQG 556
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1-230 3.68e-29

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 111.05  E-value: 3.68e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckv 79
Cdd:PRK13652   1 MHLIETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVR--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVLPIPE----GVNVRQLVAYGrsPHNslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:PRK13652  78 KFVGLVFQNPDdqifSPTVEQDIAFG--PIN--LGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
18-197 4.69e-29

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 109.19  E-value: 4.69e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL--------ACKVAFlpqvlpip 89
Cdd:PRK13539  17 LFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEAchylghrnAMKPAL-------- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 egvNVRQLVAYgrsphnslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13539  89 ---TVAENLEF--------WAAFLGGEELDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAA 157
                        170       180
                 ....*....|....*....|....*...
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PRK13539 158 LDAAAVALFAELIRAHLAQGGIVIAATH 185
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
4-218 6.04e-29

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: 108.84  E-value: 6.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA--RELACKV-- 79
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEalRRIGALIea 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 -AFLPQVLpipegvnvrqlvayGRSpHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03268   81 pGFYPNLT--------------ARE-NLRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNP 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03268  146 DLLILDEPTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQKVADRIGIINKGKLI 205
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
21-228 7.48e-29

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: 112.12  E-value: 7.48e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgYSQLSARELackvaFLPqvlpiPE----GV---- 92
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGE-VLQDSARGI-----FLP-----PHrrriGYvfqe 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 -------NVRQLVAYGRsphnslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:COG4148   86 arlfphlSVRGNLLYGR------KRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG4148  160 PLAALDLARKAEILPYLERLRDELDIpILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLS 223
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
4-221 1.71e-28

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: 106.63  E-value: 1.71e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYG--ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSArELACKVAF 81
Cdd:cd03247    1 LSINNVSFSYPeqEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEK-ALSSLISV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQvlpipegvnvrqlvaygrSPHnsLWGrlsgadqhsvdqalqrmelATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03247   80 LNQ------------------RPY--LFD-------------------TTLRNNLGRRFSGGERQRLALARILLQDAPIV 120
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDInQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03247  121 LLDEPTVGLDPITERQLLSLIFEV-LKDKTLIWITHHL-TGIEHMDKILFLENGKIIMQG 178
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
23-217 2.03e-28

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: 107.64  E-value: 2.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   23 SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckVAFLPQVLPIPEGVNVRQLVAYGR 102
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRP--VSMLFQENNLFAHLTVRQNIGLGL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  103 SPhnSLwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLM 182
Cdd:TIGR01277  96 HP--GL--KLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALV 171
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 492172462  183 RELSAEGK-TVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:TIGR01277 172 KQLCSERQrTLLMVTHHLSDARAIASQIAVVSQGKI 207
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
17-221 2.23e-28

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: 107.74  E-value: 2.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKgysQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFNGQ---PRKPDQFQKCVAYVRQDDILLPGLT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAYgrSPHNSLWGRLSGA--DQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03234   98 VRETLTY--TAILRLPRKSSDAirKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLD 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLH----DInqaCRYADHLAVMQGGRLVTCG 221
Cdd:cd03234  176 SFTALNLVSTLSQLARRNRIVILTIHqprsDL---FRLFDRILLLSSGEIVYSG 226
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
1-221 3.97e-28

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 107.41  E-value: 3.97e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqlsarelackva 80
Cdd:COG4161    1 MSI-QLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFD------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 fLPQVLPIPEGVNVRQLVA-----YGRSPHNSLWGRLSGA--------DQHSVDQA---LQRMELATLAER-PLSdLSGG 143
Cdd:COG4161   68 -FSQKPSEKAIRLLRQKVGmvfqqYNLWPHLTVMENLIEApckvlglsKEQAREKAmklLARLRLTDKADRfPLH-LSGG 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 144 QRQRAWLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:COG4161  146 QQQRVAIARALMMEPQVLLFDEPTAALDpeITAQV--VEIIRELSQTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQG 223
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
4-217 5.19e-28

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: 106.46  E-value: 5.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA--RELACKVAF 81
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKniNELRQKVGM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQ---------VLpipEGVNVRQLVAYGRSPHNslwgrlsgADQHSVdQALQRMELATLAERPLSDLSGGQRQRAWLAM 152
Cdd:cd03262   81 VFQqfnlfphltVL---ENITLAPIKVKGMSKAE--------AEERAL-ELLEKVGLADKADAYPAQLSGGQQQRVAIAR 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:cd03262  149 ALAMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREVADRVIFMDDGRI 213
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
3-218 6.25e-28

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 111.31  E-value: 6.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKGysqlsarelaCKVAFL 82
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GET----------VKIGYF 383
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVL-PIPEGVNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMelatL-----AERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:COG0488  384 DQHQeELDPDKTVLDELRDGA----------PGGTEQEVRGYLGRF----LfsgddAFKPVGVLSGGEKARLALAKLLLS 449
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELsaEGkTVITVLHDinqacRY-----ADHLAVMQGGRLV 218
Cdd:COG0488  450 PPNVLLLDEPTNHLDIETLEALEEALDDF--PG-TVLLVSHD-----RYfldrvATRILEFEDGGVR 508
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
14-227 8.20e-28

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


Pssm-ID: 443660 [Multi-domain]  Cd Length: 563  Bit Score: 111.38  E-value: 8.20e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGv 92
Cdd:COG4618  342 GSKRpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRHIGYLPQDVELFDG- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAygrsphnslwgRLSGADQHSVDQAlqrmelATLA-------------ERPLSD----LSGGQRQRAWLAMILA 155
Cdd:COG4618  421 TIAENIA-----------RFGDADPEKVVAA------AKLAgvhemilrlpdgyDTRIGEggarLSGGQRQRIGLARALY 483
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG4618  484 GDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEVL 554
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
19-227 1.39e-27

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: 105.88  E-value: 1.39e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELacKVAFLPQVLPIPEGVNVRQLV 98
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKR--DISYVPQNYALFPHMTVYKNI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 AYGRSphNSLWGRLSgaDQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVEL 178
Cdd:cd03299   93 AYGLK--KRKVDKKE--IERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKL 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492172462 179 LDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03299  169 REELKKIRKEfGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVF 218
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
13-228 1.72e-27

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 105.95  E-value: 1.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysqLSARELACKVAFLPQvlpiPEGV 92
Cdd:PRK09493  11 FGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG-----LKVNDPKVDERLIRQ----EAGM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYgrsPH-----NSLWG--RLSGAD-QHSVDQALQRMELATLAER----PlSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK09493  82 VFQQFYLF---PHltaleNVMFGplRVRGASkEEAEKQARELLAKVGLAERahhyP-SELSGGQQQRVAIARALAVKPKL 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK09493 158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIK 225
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
4-226 1.82e-27

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: 105.68  E-value: 1.82e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-VAFL 82
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARAgIAYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   83 PQvlpipeGvnvRQLVAYGRSPHNSLWG--RLSGADQHSVDQALQRME-LATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:TIGR03410  81 PQ------G---REIFPRLTVEENLLTGlaALPRRSRKIPDEIYELFPvLKEMLGRRGGDLSGGQQQQLAIARALVTRPK 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462  160 IVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGmAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
8-227 1.94e-27

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: 105.78  E-value: 1.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   8 HLDIGYGATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---KGYSQLSARElacKVAFLP 83
Cdd:cd03253    5 NVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdiREVTLDSLRR---AIGVVP 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 Q--VLpipegVN--VRqlvaygrspHNSLWGRLSGADQHSVDQA--------LQRMELA---TLAERPLSdLSGGQRQRA 148
Cdd:cd03253   82 QdtVL-----FNdtIG---------YNIRYGRPDATDEEVIEAAkaaqihdkIMRFPDGydtIVGERGLK-LSGGEKQRV 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03253  147 AIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK-GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGTHEELL 223
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
26-199 2.00e-27

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: 110.26  E-value: 2.00e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  26 PPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---------KG------YSQLSARELacKVAFLPQ-VLPIP 89
Cdd:COG1245   96 PKKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPswdevlkrfRGtelqdyFKKLANGEI--KVAHKPQyVDLIP 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 EGV--NVRQLvaygrsphnslwgrLSGADQH-SVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:COG1245  174 KVFkgTVREL--------------LEKVDERgKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
                        170       180       190
                 ....*....|....*....|....*....|...
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDI 199
Cdd:COG1245  240 SSYLDIYQRLNVARLIRELAEEGKYVLVVEHDL 272
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-229 2.59e-27

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: 109.77  E-value: 2.59e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGA----TRIVQDLSFSPPAGQVTALIGPNGCGKS----TLLKAFARILTPQSGSLSLDGKGYSQLSA 72
Cdd:COG4172    4 MPLLSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGLSE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  73 RELaCKV-----AFLPQ--------VLPIpegvnVRQlVAYGRSPHnslwGRLSGAdqhsvdQALQRM-ELATL-----A 133
Cdd:COG4172   84 REL-RRIrgnriAMIFQepmtslnpLHTI-----GKQ-IAEVLRLH----RGLSGA------AARARAlELLERvgipdP 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 134 ERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADH 208
Cdd:COG4172  147 ERRLDAyphqLSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRElGMALLLITHDLGVVRRFADR 226
                        250       260
                 ....*....|....*....|.
gi 492172462 209 LAVMQGGRLVTCGAPGDVLTA 229
Cdd:COG4172  227 VAVMRQGEIVEQGPTAELFAA 247
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
7-230 3.27e-27

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: 105.01  E-value: 3.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   7 QHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQ 84
Cdd:cd03251    4 KNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGLVSQ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 VLPIPEGvNVRQLVAYGRsphnslwgrlSGADQHSVDQALQR-------MEL-----ATLAERPlSDLSGGQRQRAWLAM 152
Cdd:cd03251   84 DVFLFND-TVAENIAYGR----------PGATREEVEEAARAanahefiMELpegydTVIGERG-VKLSGGQRQRIAIAR 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:cd03251  152 ALLKDPPILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLS-TIENADRIVVLEDGKIVERGTHEELLAQG 227
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
1-221 4.77e-27

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 104.71  E-value: 4.77e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSIlKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqLSARELACKVA 80
Cdd:PRK11124   1 MSI-QLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFD-FSKTPSDKAIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLpipeGVNVRQlvaYGRSPHNSLWGRLSGA--------DQHSVDQA---LQRMELATLAER-PLSdLSGGQRQRA 148
Cdd:PRK11124  79 ELRRNV----GMVFQQ---YNLWPHLTVQQNLIEApcrvlglsKDQALARAeklLERLRLKPYADRfPLH-LSGGQQQRV 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11124 151 AIARALMMEPQVLLFDEPTAALDpeITAQI--VSIIRELAETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
23-234 4.97e-27

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 104.28  E-value: 4.97e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  23 SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS-ARElacKVAFLPQVLPIPEGVNVRQLVAYG 101
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPpSRR---PVSMLFQENNLFSHLTVAQNIGLG 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 102 RSPhnSLwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDL 181
Cdd:PRK10771  96 LNP--GL--KLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 182 MRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVTCGApgdvlTAELVCQ 234
Cdd:PRK10771 172 VSQVCQERQlTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP-----TDELLSG 220
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-226 6.63e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 105.27  E-value: 6.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGS---LSLDGKGYSQLSARELA 76
Cdd:PRK13640   4 NIVEFKHVSFTYPDSKkpALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPnskITVDGITLTAKTVWDIR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 CKVAFlpqVLPIPE----GVNVRQLVAYG----RSPHNSLwgrlsgadQHSVDQALQRMELATLAERPLSDLSGGQRQRA 148
Cdd:PRK13640  84 EKVGI---VFQNPDnqfvGATVGDDVAFGlenrAVPRPEM--------IKIVRDVLADVGMLDYIDSEPANLSGGQKQRV 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQAcRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13640 153 AIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKnNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEI 230
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
3-224 7.51e-27

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 103.59  E-value: 7.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElackVAF 81
Cdd:COG2884    1 MIRFENVSKRYPGGReALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRRE----IPY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLpipeGV---------------NVR-QLVAYGRSPHnslwgrlsgADQHSVDQALQRMELATLAERPLSDLSGGQR 145
Cdd:COG2884   77 LRRRI----GVvfqdfrllpdrtvyeNVAlPLRVTGKSRK---------EIRRRVREVLDLVGLSDKAKALPHELSGGEQ 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPG 224
Cdd:COG2884  144 QRVAIARALVNRPELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARG 222
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
17-218 9.30e-27

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 108.07  E-value: 9.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQVLP-IPEgVNV 94
Cdd:PRK11288  18 KALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAaLAAGVAIIYQELHlVPE-MTV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQLVAYGRSPHNSLWGRLSGADQHSVDQaLQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK11288  97 AENLYLGQLPHKGGIVNRRLLNYEAREQ-LEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPTSSLSARE 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK11288 176 IEQLFRVIRELRAEGRVILYVSHRMEEIFALCDAITVFKDGRYV 219
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
19-229 1.47e-26

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: 108.03  E-value: 1.47e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQLV 98
Cdd:TIGR03375 481 LDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRNIGYVPQDPRLFYG-TLRDNI 559
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   99 AYGRsPHnslwgrlsgADQHSVDQALQRMELATLA-------ERPLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:TIGR03375 560 ALGA-PY---------ADDEEILRAAELAGVTEFVrrhpdglDMQIGErgrsLSGGQRQAVALARALLRDPPILLLDEPT 629
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462  168 TYLDISHQVELLDLMRELSAeGKTVITVLHDiNQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR03375 630 SAMDNRSEERFKDRLKRWLA-GKTLVLVTHR-TSLLDLVDRIIVMDNGRIVADGPKDQVLEA 689
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
12-229 1.93e-26

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: 103.04  E-value: 1.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackVAFLPQVLPIPEG 91
Cdd:cd03258   14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKEL---RKARRRIGMIFQH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 VN------VRQLVAYgrsPHnSLWGrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:cd03258   91 FNllssrtVFENVAL---PL-EIAG-VPKAEIEErVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCD 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:cd03258  166 EATSALDPETTQSILALLRDINRElGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFAN 231
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
2-226 2.06e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 103.68  E-value: 2.06e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:PRK13648   6 SIIVFKNVSFQYqsDASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKLRKHI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFlpqVLPIPE----GVNVRQLVAYGRSPHNslwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK13648  86 GI---VFQNPDnqfvGSIVKYDVAFGLENHA-----VPYDEMHRrVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVL 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13648 158 ALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEI 229
cbiO PRK13643
energy-coupling factor transporter ATPase;
15-227 2.83e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 104.05  E-value: 2.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL-DGKGYSQLSARELACKVAFLPQVLPIPEGV- 92
Cdd:PRK13643  18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgDIVVSSTSKQKEIKPVRKKVGVVFQFPESQl 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 ---NVRQLVAYGrsPHNslwgrLSGADQHSVDQALQRMELATLA----ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK13643  98 feeTVLKDVAFG--PQN-----FGIPKEKAEKIAAEKLEMVGLAdefwEKSPFELSGGQMRRVAIAGILAMEPEVLVLDE 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK13643 171 PTAGLDPKARIEMMQLFESIHQSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVF 232
cbiO PRK13641
energy-coupling factor transporter ATPase;
21-228 3.02e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 103.76  E-value: 3.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGY----SQLSARELACKVAFlpqVLPIPEGV---- 92
Cdd:PRK13641  25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSL---VFQFPEAQlfen 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYGrsPHNslwgrLSGADQHSVDQALQRMELATLAERPLS----DLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK13641 102 TVLKDVEFG--PKN-----FGFSEDEAKEKALKWLKKVGLSEDLISkspfELSGGQMRRVAIAGVMAYEPEILCLDEPAA 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 169 YLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK13641 175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFS 234
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
14-229 3.23e-26

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 106.66  E-value: 3.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQWDRETFGKHIGYLPQDVELFPGTV 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   94 VRQLVAYGRSPHNS---LWGRLSGAdqHSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:TIGR01842 409 AENIARFGENADPEkiiEAAKLAGV--HELILRLPDGYDTVIGPGG-ATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462  171 DISHQVELLDLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR01842 486 DEEGEQALANAIKALKARGITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEVLAK 543
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
26-199 4.30e-26

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 106.43  E-value: 4.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  26 PPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---------KG------YSQLSARELacKVAFLPQ-VLPIP 89
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEEEPswdevlkrfRGtelqnyFKKLYNGEI--KVVHKPQyVDLIP 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 EGV--NVRQLvaygrsphnslwgrLSGADQHSV-DQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK13409 174 KVFkgKVREL--------------LKKVDERGKlDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
                        170       180       190
                 ....*....|....*....|....*....|...
gi 492172462 167 TTYLDISHQVELLDLMRELsAEGKTVITVLHDI 199
Cdd:PRK13409 240 TSYLDIRQRLNVARLIREL-AEGKYVLVVEHDL 271
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
4-198 5.48e-26

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family transporter in which each gene contains an N-terminal membrane-spanning domain (pfam00664) and a C-terminal ATP-binding domain (pfam00005). In E. coli these genes were discovered as mutants which caused the terminal heme-copper oxidase complex cytochrome bd to fail to assemble. Recent work has shown that the transporter is involved in export of redox-active thiol compounds such as cysteine and glutathione. The linkage to assembly of the cytochrome bd complex is further supported by the conserved operon structure found outside the gammaproteobacteria (cydABCD) containing both the transporter and oxidase genes components. The genes used as the seed members for this model are all either found in the gammproteobacterial context or the CydABCD context. All members of this family scoring above trusted at the time of its creation were from genomes which encode a cytochrome bd complex.


Pssm-ID: 274331 [Multi-domain]  Cd Length: 530  Bit Score: 105.91  E-value: 5.48e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:TIGR02868 335 LELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   83 PQVlPIPEGVNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAERpLSD------------LSGGQRQRAWL 150
Cdd:TIGR02868 415 AQD-AHLFDTTVRENLRLAR----------PDATDEELWAALERVGLADWLRA-LPDgldtvlgeggarLSGGERQRLAL 482
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 492172462  151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHD 198
Cdd:TIGR02868 483 ARALLADAPILLLDEPTEHLDAETADELLEDLLAAL-SGRTVVLITHH 529
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
3-210 5.68e-26

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 102.55  E-value: 5.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKGY--SQLSAREL 75
Cdd:PRK14243  10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPVEV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  76 ACKVAFLPQVlPIPEGVNVRQLVAYGrSPHNSLWGRLSGADQHSVDQALQRMELA-TLAERPLSdLSGGQRQRAWLAMIL 154
Cdd:PRK14243  90 RRRIGMVFQK-PNPFPKSIYDNIAYG-ARINGYKGDMDELVERSLRQAALWDEVKdKLKQSGLS-LSGGQQQRLCIARAI 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINQACRYADHLA 210
Cdd:PRK14243 167 AVQPEVILMDEPCSALDPISTLRIEELMHELK-EQYTIIIVTHNMQQAARVSDMTA 221
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
4-221 6.05e-26

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 106.06  E-value: 6.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGY--GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:PRK11160 339 LTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALRQAISV 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQvlpipegvnvrqlvaygrSPH---NSLWGRLSGADQHSVD----QALQRMELATLAE-------------RPlsdLS 141
Cdd:PRK11160 419 VSQ------------------RVHlfsATLRDNLLLAAPNASDealiEVLQQVGLEKLLEddkglnawlgeggRQ---LS 477
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 142 GGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11160 478 GGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEH-AQNKTVLMITHRLT-GLEQFDRICVMDNGQIIEQG 555
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
13-232 6.30e-26

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 105.88  E-value: 6.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQVLPIPEG 91
Cdd:COG3845   15 FGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPRDaIALGIGMVHQHFMLVPN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 VNVRQLVAYGRSPHNSLWGRLSGADQHsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:COG3845   95 LTVAENIVLGLEPTKGGRLDRKAARAR-IRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLT 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:COG3845  174 PQEADELFEILRRLAAEGKSIIFITHKLREVMAIADRVTVLRRGKVVGTVDTAETSEEELA 234
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
25-199 9.84e-26

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: 101.67  E-value: 9.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  25 SPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLS--------LDGKGYSQL-----SARELACKVAFLPQ-VLPIPE 90
Cdd:cd03236   22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeiLDEFRGSELqnyftKLLEGDVKVIVKPQyVDLIPK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GV--NVRQLvaygrsphnslwgrLSGADQ-HSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:cd03236  102 AVkgKVGEL--------------LKKKDErGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPS 167
                        170       180       190
                 ....*....|....*....|....*....|..
gi 492172462 168 TYLDISHQVELLDLMRELSAEGKTVITVLHDI 199
Cdd:cd03236  168 SYLDIKQRLNAARLIRELAEDDNYVLVVEHDL 199
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
21-227 1.14e-25

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: 103.27  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqlSARELAC------KVAFLPQVLPIPEGVNV 94
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLF--DSRKGIFlppekrRIGYVFQEARLFPHLSV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   95 RQLVAYGRSphnslwgRLSGADQHSVDQALQRM-ELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:TIGR02142  93 RGNLRYGMK-------RARPSERRISFERVIELlGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDP 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 492172462  174 HQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:TIGR02142 166 RKYEILPYLERLHAEfGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVW 220
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
34-223 1.30e-25

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: 102.57  E-value: 1.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   34 LIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLpIPEgVNVRQLVAYGRsphnslwgRLS 113
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYAL-FPH-MTVEENVAFGL--------KMR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  114 GADQHSVD----QALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS----HQVELLDLMREL 185
Cdd:TIGR01187  71 KVPRAEIKprvlEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL 150
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 492172462  186 saeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:TIGR01187 151 ---GITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTP 185
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
13-221 1.43e-25

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: 100.02  E-value: 1.43e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFlpQVLPIPEGV 92
Cdd:cd03301   10 FGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVF--QNYALYPHM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYGRsphnslwgRLSGADQHSVDQALQR----MELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03301   88 TVYDNIAFGL--------KLRKVPKDEIDERVREvaelLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLS 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 169 YLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03301  160 NLDaklrVQMRAELKRLQQRL---GTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
17-229 1.53e-25

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 100.93  E-value: 1.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---------GY-SQLSARElackvaflpqvl 86
Cdd:COG1134   40 WALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRvsallelgaGFhPELTGRE------------ 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 pipegvNVRqlvaygrsphnsLWGRLSGADQHSVDQALQRM-ELATLAE---RPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1134  108 ------NIY------------LNGRLLGLSRKEIDEKFDEIvEFAELGDfidQPVKTYSSGMRARLAFAVATAVDPDILL 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:COG1134  170 VDEVLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEVIAA 236
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
3-226 1.85e-25

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 103.38  E-value: 1.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:PRK11607  19 LLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMFQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLpIPEgVNVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK11607  99 SYAL-FPH-MTVEQNIAFGlkqdKLPKAEIASR--------VNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRP 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 159 AIVLLDEPTTYLDIS----HQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK11607 169 KLLLLDEPMGALDKKlrdrMQLEVVDILERV---GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEI 237
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
3-227 2.09e-25

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 100.54  E-value: 2.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElacKVAFL 82
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---GVVFQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLpIPeGVNVRQLVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK11248  78 NEGL-LP-WRNVQDNVAFGL----QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLL 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGrlvtcgaPGDVL 227
Cdd:PRK11248 152 LDEPFGALDAFTREQMQTLLLKLWQEtGKQVLLITHDIEEAVFMATELVLLSPG-------PGRVV 210
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
15-217 2.13e-25

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


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 99.85  E-value: 2.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNV 94
Cdd:cd03248   26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQE-PVLFARSL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQLVAYG--RSPHNSLWGRLSGADQHSVDQALQRmELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:cd03248  105 QDNIAYGlqSCSFECVKEAAQKAHAHSFISELAS-GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDA 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 492172462 173 SHQVELLDLMRElSAEGKTVITVLHDINQACRyADHLAVMQGGRL 217
Cdd:cd03248  184 ESEQQVQQALYD-WPERRTVLVIAHRLSTVER-ADQILVLDGGRI 226
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
22-256 2.51e-25

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 100.85  E-value: 2.51e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  22 LSFSPPAgqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG--YSQLSARELACKVAflpQVLPIPEG----VNVR 95
Cdd:PRK13638  22 LDFSLSP--VTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPldYSKRGLLALRQQVA---TVFQDPEQqifyTDID 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVAYgrSPHNslWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:PRK13638  97 SDIAF--SLRN--LGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 176 VELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT-AELVCQ-------VFDVHVQImrepv 247
Cdd:PRK13638 173 TQMIAIIRRIVAQGNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFAcTEAMEQagltqpwLVKLHTQL----- 247

                 ....*....
gi 492172462 248 aGTPMCIVE 256
Cdd:PRK13638 248 -GLPLCKTE 255
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
12-227 2.64e-25

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: 99.61  E-value: 2.64e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPE 90
Cdd:cd03254   11 SYDEKKPVlKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVLQDTFLFS 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GvNVRQLVAYGRsphnslwgrlSGADQHSVDQALQRMELATLAERpL------------SDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03254   91 G-TIMENIRLGR----------PNATDEEVIEAAKEAGAHDFIMK-LpngydtvlgengGNLSQGERQLLAIARAMLRDP 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:cd03254  159 KILILDEATSNIDTETEKLIQEALEKLM-KGRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDELL 225
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
3-227 4.13e-25

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 100.00  E-value: 4.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlsaRELACkvafl 82
Cdd:PRK11701   6 LLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQL---RDLYA----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 pqvLPIPE---------GVnVRQLVAYGRSPHNSLWG----RLSGA-DQH------SVDQALQRMELAtlAERpLSDL-- 140
Cdd:PRK11701  78 ---LSEAErrrllrtewGF-VHQHPRDGLRMQVSAGGnigeRLMAVgARHygdiraTAGDWLERVEID--AAR-IDDLpt 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 --SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK11701 151 tfSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRElGLAVVIVTHDLAVARLLAHRLLVMKQGRV 230
                        250
                 ....*....|
gi 492172462 218 VTCGAPGDVL 227
Cdd:PRK11701 231 VESGLTDQVL 240
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
3-229 5.68e-25

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: 103.23  E-value: 5.68e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGY-----------GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGKGYSQLS 71
Cdd:COG4172  275 LLEARDLKVWFpikrglfrrtvGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLR-LIPSEGEIRFDGQDLDGLS 353
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  72 ARELackvafLP-----QVlpipegV------------NVRQLVAYGRSPHNSlwgRLSGADQHS-VDQALQRMEL-ATL 132
Cdd:COG4172  354 RRAL------RPlrrrmQV------VfqdpfgslsprmTVGQIIAEGLRVHGP---GLSAAERRArVAEALEEVGLdPAA 418
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 133 AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDInQACRY-ADHLA 210
Cdd:COG4172  419 RHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREhGLAYLFISHDL-AVVRAlAHRVM 497
                        250
                 ....*....|....*....
gi 492172462 211 VMQGGRLVTCGAPGDVLTA 229
Cdd:COG4172  498 VMKDGKVVEQGPTEQVFDA 516
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
4-225 6.10e-25

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 98.32  E-value: 6.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSARELacKVA 80
Cdd:COG4136    2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAfsaSGEVLLNGRRLTALPAEQR--RIG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLPIPEGVNVRQLVAYGrsphnsLWGRLSGAD-QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLA-MILAQDA 158
Cdd:COG4136   80 ILFQDDLLFPHLSVGENLAFA------LPPTIGRAQrRARVEQALEEAGLAGFADRDPATLSGGQRARVALLrALLAEPR 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 159 AiVLLDEPTTYLDISHQVELLDLMRE-LSAEGKTVITVLHDINqacryadhlAVMQGGRLVTCGAPGD 225
Cdd:COG4136  154 A-LLLDEPFSKLDAALRAQFREFVFEqIRQRGIPALLVTHDEE---------DAPAAGRVLDLGNWQH 211
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
19-218 8.38e-25

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: 98.56  E-value: 8.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK-GYSQlsARELACKVAFL----PQV---LPIPE 90
Cdd:cd03267   37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLvPWKR--RKKFLRRIGVVfgqkTQLwwdLPVID 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GVNVRQLVaYGRSPhnslwgrlsGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:cd03267  115 SFYLLAAI-YDLPP---------ARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGL 184
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 492172462 171 DISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:cd03267  185 DVVAQENIRNFLKEYNRErGTTVLLTSHYMKDIEALARRVLVIDKGRLL 233
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
18-218 1.19e-24

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: 98.38  E-value: 1.19e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQL 97
Cdd:cd03249   18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQE-PVLFDGTIAEN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGRSPhnslwgrlsgADQHSVDQALQR-------MELA----TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:cd03249   97 IRYGKPD----------ATDEEVEEAAKKanihdfiMSLPdgydTLVGERGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 167 TTYLD-ISHQV--ELLDLMRelsaEGKTVITVLHDINqACRYADHLAVMQGGRLV 218
Cdd:cd03249  167 TSALDaESEKLvqEALDRAM----KGRTTIVIAHRLS-TIRNADLIAVLQNGQVV 216
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
4-203 1.51e-24

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is a cytosolic protein required by fungal ribosomes for in vitro protein synthesis and for in vivo growth. EF-3 stimulates the binding of the EF-1: GTP: aa-tRNA ternary complex to the ribosomal A site by facilitated release of the deacylated tRNA from the E site. The reaction requires ATP hydrolysis. EF-3 contains two ATP nucleotide binding sequence (NBS) motifs. NBSI is sufficient for the intrinsic ATPase activity. NBSII is essential for the ribosome-stimulated functions.


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 95.21  E-value: 1.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLP 83
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-----------VKIGYFE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QvlpipegvnvrqlvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03221   70 Q-------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLL 94
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSaegKTVITVLHD---INQAC 203
Cdd:cd03221   95 DEPTNHLDLESIEALEEALKEYP---GTVILVSHDryfLDQVA 134
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
12-221 1.99e-24

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 96.47  E-value: 1.99e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKgysQLSARELACKVAFLPQvlpip 89
Cdd:cd03213   18 SKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGR---PLDKRSFRKIIGYVPQ----- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 egvnvrqlvaygrspHNSLWGRLSgadqhsVDQALQrmeLAtlAErpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:cd03213   90 ---------------DDILHPTLT------VRETLM---FA--AK--LRGLSGGERKRVSIALELVSNPSLLFLDEPTSG 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 170 LDISHQVELLDLMRELSAEGKTVITVLH----DINQACryaDHLAVMQGGRLVTCG 221
Cdd:cd03213  142 LDSSSALQVMSLLRRLADTGRTIICSIHqpssEIFELF---DKLLLLSQGRVIYFG 194
cbiO PRK13649
energy-coupling factor transporter ATPase;
17-226 2.39e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 98.28  E-value: 2.39e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSA----RELACKVAFlpqVLPIPEGV 92
Cdd:PRK13649  21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQIRKKVGL---VFQFPESQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 ----NVRQLVAYGrsPHNSlwgrlsGADQHSVdQALQRMELA------TLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13649  98 lfeeTVLKDVAFG--PQNF------GVSQEEA-EALAREKLAlvgiseSLFEKNPFELSGGQMRRVAIAGILAMEPKILV 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13649 169 LDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDI 232
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
3-221 2.41e-24

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 97.92  E-value: 2.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQ---SGSLSLDGKG-YS-QLSAREL 75
Cdd:PRK14239   5 ILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPEvtiTGSIVYNGHNiYSpRTDTVDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  76 ACKVAFLPQvLPIPEGVNVRQLVAYGRsphnslwgRLSGA-DQHSVDQALQR-MELATLAER---PLSD----LSGGQRQ 146
Cdd:PRK14239  85 RKEIGMVFQ-QPNPFPMSIYENVVYGL--------RLKGIkDKQVLDEAVEKsLKGASIWDEvkdRLHDsalgLSGGQQQ 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLD-ISH-QVE--LLDLMRELsaegkTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK14239 156 RVCIARVLATSPKIILLDEPTSALDpISAgKIEetLLGLKDDY-----TMLLVTRSMQQASRISDRTGFFLDGDLIEYN 229
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
15-218 3.64e-24

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: 96.65  E-value: 3.64e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC----KVAFLPQVLPIPE 90
Cdd:TIGR02211  17 DTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKlrnkKLGFIYQFHHLLP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   91 GVNVRQLVAYgrsPhnSLWGRLSGADQHSVDQA-LQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:TIGR02211  97 DFTALENVAM---P--LLIGKKSVKEAKERAYEmLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPSLVLADEPTGN 171
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 492172462  170 LDISHQVELLDLMRELSAEGKT-VITVLHDINQACRyADHLAVMQGGRLV 218
Cdd:TIGR02211 172 LDNNNAKIIFDLMLELNRELNTsFLVVTHDLELAKK-LDRVLEMKDGQLF 220
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
15-226 3.98e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 98.17  E-value: 3.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL------DGKGYSQLsaRELACKVAFlpqVLPI 88
Cdd:PRK13634  19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKL--KPLRKKVGI---VFQF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  89 PEgvnvRQL--------VAYGrsPHNSlwgrlsGAdqhSVDQALQR----MELATLAERPLS----DLSGGQRQRAWLAM 152
Cdd:PRK13634  94 PE----HQLfeetvekdICFG--PMNF------GV---SEEDAKQKaremIELVGLPEELLArspfELSGGQMRRVAIAG 158
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13634 159 VLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEkGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREI 233
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
29-199 5.09e-24

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 100.65  E-value: 5.09e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgkgysqlsarelaCKVAFLPQVLPIPEGVNVRQL-----VAYGRS 103
Cdd:PRK13409 365 GEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-------------LKISYKPQYIKPDYDGTVEDLlrsitDDLGSS 431
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 104 PHNSlwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMR 183
Cdd:PRK13409 432 YYKS--------------EIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIR 497
                        170
                 ....*....|....*..
gi 492172462 184 ELSAE-GKTVITVLHDI 199
Cdd:PRK13409 498 RIAEErEATALVVDHDI 514
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
18-229 5.96e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 97.04  E-value: 5.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK------GYSQLSARELACKVAFL-PQVLPIPE 90
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAIKLRKEVGMVfQQPNPFPH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 gVNVRQLVAYGRSPHNSLWGRlsgADQHSVDQALQRM----ELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK14246 105 -LSIYDNIAYPLKSHGIKEKR---EIKKIVEECLRKVglwkEVYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEP 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 167 TTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:PRK14246 181 TSMIDIVNSQAIEKLITELKNE-IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTS 242
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
18-221 7.94e-24

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 100.18  E-value: 7.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQL 97
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQE-PVLFSGSVREN 574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   98 VAYG--RSPHNSLwgrLSGADQHSVDQALQRME--LATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:TIGR00958 575 IAYGltDTPDEEI---MAAAKAANAHDFIMEFPngYDTEVGEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAE 651
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 492172462  174 HQVELLDLMrelSAEGKTVITVLHDInQACRYADHLAVMQGGRLVTCG 221
Cdd:TIGR00958 652 CEQLLQESR---SRASRTVLLIAHRL-STVERADQILVLKKGSVVEMG 695
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
13-232 1.66e-23

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 99.09  E-value: 1.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS---ARELACKVAFlpQVLPIP 89
Cdd:PRK09700  15 FGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDhklAAQLGIGIIY--QELSVI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 EGVNVRQLVAYGRSPHNSLWGrLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK09700  93 DELTVLENLYIGRHLTKKVCG-VNIIDwremRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDE 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:PRK09700 172 PTSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDVSNDDIV 238
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
4-221 4.19e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 94.52  E-value: 4.19e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ-----SGSLSLDGKG-YS-QLSARELA 76
Cdd:PRK14267   5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNiYSpDVDPIEVR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 CKVAFLPQVL-PIPEgVNVRQLVAYGRSPHNSLWGRlsGADQHSVDQALQRMELATLAERPLSD----LSGGQRQRAWLA 151
Cdd:PRK14267  85 REVGMVFQYPnPFPH-LTIYDNVAIGVKLNGLVKSK--KELDERVEWALKKAALWDEVKDRLNDypsnLSGGQRQRLVIA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEgKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK14267 162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPAQAARVSDYVAFLYLGKLIEVG 230
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
3-202 4.71e-23

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 93.63  E-value: 4.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:PRK10247   7 LLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYRQQVSYC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVlPIPEGVNVRQLVAYgrsPhnslWG-RLSGADQHSVDQALQRMELA-TLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK10247  87 AQT-PTLFGDTVYDNLIF---P----WQiRNQQPDPAIFLDDLERFALPdTILTKNIAELSGGEKQRISLIRNLQFMPKV 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHD---INQA 202
Cdd:PRK10247 159 LLLDEITSALDESNKHNVNEIIHRYVREqNIAVLWVTHDkdeINHA 204
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
29-214 5.07e-23

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: 94.01  E-value: 5.07e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelacKVAFLPQVLPIPEGVNVRQLvaygrsphnsL 108
Cdd:cd03237   25 SEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELD------------TVSYKPQYIKADYEGTVRDL----------L 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 WGRLSGADQHS--VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS 186
Cdd:cd03237   83 SSITKDFYTHPyfKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
                        170       180
                 ....*....|....*....|....*....
gi 492172462 187 AEG-KTVITVLHDINQACRYADHLAVMQG 214
Cdd:cd03237  163 ENNeKTAFVVEHDIIMIDYLADRLIVFEG 191
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
29-199 6.72e-23

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: 97.55  E-value: 6.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgkgysqlsarelaCKVAFLPQVLPIPEGVNVRQLV--AYGRSPHN 106
Cdd:COG1245  366 GEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED-------------LKISYKPQYISPDYDGTVEEFLrsANTDDFGS 432
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 107 SLWgrlsgadQHSVdqaLQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS 186
Cdd:COG1245  433 SYY-------KTEI---IKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFA 502
                        170
                 ....*....|....
gi 492172462 187 AE-GKTVITVLHDI 199
Cdd:COG1245  503 ENrGKTAMVVDHDI 516
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
19-227 7.78e-23

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 96.26  E-value: 7.78e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELA----CKVAFLPQVLPIPEGVNV 94
Cdd:PRK10070  44 VKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELRevrrKKIAMVFQSFALMPHMTV 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQLVAYGRSphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK10070 124 LDNTAFGME----LAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLI 199
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 175 QVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK10070 200 RTEMQDELVKLQAKhQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEIL 253
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
13-223 9.77e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 95.48  E-value: 9.77e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaFLPQVLPIPEGV 92
Cdd:PRK11000  13 YGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEK---------------RMNDVPPAERGV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 N-VRQlvAYGRSPHNSL-----WG-RLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK11000  78 GmVFQ--SYALYPHLSVaenmsFGlKLAGAKkeeiNQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVF 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 162 LLDEPTTYLD----ISHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:PRK11000 156 LLDEPLSNLDaalrVQMRIEISRLHKRL---GRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKP 218
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
4-227 1.09e-22

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: 97.12  E-value: 1.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYG-ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   83 PQVLPIPEGVNVRQLvaygrsphnsLWGRLSGADQHSVDQALQRMELATLAER-PL----------SDLSGGQRQRAWLA 151
Cdd:TIGR01193 554 PQEPYIFSGSILENL----------LLGAKENVSQDEIWAACEIAEIKDDIENmPLgyqtelseegSSISGGQKQRIALA 623
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462  152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMreLSAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVL 227
Cdd:TIGR01193 624 RALLTDSKVLILDESTSNLDTITEKKIVNNL--LNLQDKTIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELL 696
cbiO PRK13637
energy-coupling factor transporter ATPase;
1-226 1.21e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 93.96  E-value: 1.21e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSIlKAQHLDIGYG-----ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYS--QLSAR 73
Cdd:PRK13637   1 MSI-KIENLTHIYMegtpfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  74 ELACKVAFlpqVLPIPEgvnvRQL--------VAYGrsPHNslwgrLSGADQHSVDQALQRMELA-----TLAERPLSDL 140
Cdd:PRK13637  80 DIRKKVGL---VFQYPE----YQLfeetiekdIAFG--PIN-----LGLSEEEIENRVKRAMNIVgldyeDYKDKSPFEL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLVT 219
Cdd:PRK13637 146 SGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNmTIILVSHSMEDVAKLADRIIVMNKGKCEL 225

                 ....*..
gi 492172462 220 CGAPGDV 226
Cdd:PRK13637 226 QGTPREV 232
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
4-236 1.31e-22

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: 92.61  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-VAFL 82
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLgIGYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGVNVRQ---LVAYGRsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:cd03218   81 PQEASIFRKLTVEEnilAVLEIR--------GLSKKEREEkLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLD-ISHQvELLDLMRELSAEGktvITVL---HDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:cd03218  153 KFLLLDEPFAGVDpIAVQ-DIQKIIKILKDRG---IGVLitdHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVRK 228

                 ..
gi 492172462 235 VF 236
Cdd:cd03218  229 VY 230
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
17-221 3.01e-22

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: 91.44  E-value: 3.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---------GY-SQLSARElackvaflpqvl 86
Cdd:cd03220   36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRvssllglggGFnPELTGRE------------ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 pipegvNVRqlvaygrsphnsLWGRLSGADQHSVDQALQRM-ELATLAE---RPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:cd03220  104 ------NIY------------LNGRLLGLSRKEIDEKIDEIiEFSELGDfidLPVKTYSSGMKARLAFAIATALEPDILL 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:cd03220  166 IDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-226 3.05e-22

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 94.24  E-value: 3.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVA 80
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLpIPEgVNVRQLVAYG----RSPHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK09452  92 FQSYAL-FPH-MTVFENVAFGlrmqKTPAAEITPR--------VMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVN 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 157 DAAIVLLDEPTTYLDI----SHQVELLDLMRELsaeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK09452 162 KPKVLLLDESLSALDYklrkQMQNELKALQRKL---GITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREI 232
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
13-228 3.31e-22

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 95.58  E-value: 3.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLK--AFARILtpQSGSLSLDGKGYSQLSARELAC-KVAFLPQVLpip 89
Cdd:NF033858  11 YGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSliAGARKI--QQGRVEVLGGDMADARHRRAVCpRIAYMPQGL--- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 eGVN------VRQLVAYgrsphnslWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:NF033858  86 -GKNlyptlsVFENLDF--------FGRLFGQDAAErrrrIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLD-ISHQV--ELLDLMRElSAEGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAPGDVLT 228
Cdd:NF033858 157 LLILDEPTTGVDpLSRRQfwELIDRIRA-ERPGMSVLVATAYMEEAERF-DWLVAMDAGRVLATGTPAELLA 226
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
13-225 3.42e-22

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 93.63  E-value: 3.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS--ARELaCKV----AFLPQvL 86
Cdd:PRK11432  16 FGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSiqQRDI-CMVfqsyALFPH-M 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 PIPEGvnvrqlVAYGRsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK11432  94 SLGEN------VGYGL----KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEP 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 167 TTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGD 225
Cdd:PRK11432 164 LSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQE 223
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-228 5.02e-22

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 92.06  E-value: 5.02e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGY---------GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS 71
Cdd:PRK10419   1 MTLLNVSGLSHHYahgglsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  72 ARElacKVAFLPQVLPI----PEGVNVRQLV-AYGRSPHNSLWGrLSGADQ-HSVDQALQRMELA-TLAERPLSDLSGGQ 144
Cdd:PRK10419  81 RAQ---RKAFRRDIQMVfqdsISAVNPRKTVrEIIREPLRHLLS-LDKAERlARASEMLRAVDLDdSVLDKRPPQLSGGQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 145 RQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTV-ITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:PRK10419 157 LQRVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTAcLFITHDLRLVERFCQRVMVMDNGQIVETQPV 236

                 ....*
gi 492172462 224 GDVLT 228
Cdd:PRK10419 237 GDKLT 241
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
21-198 1.04e-21

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: 89.77  E-value: 1.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KVAFLPQVLPIPEGVNVRQL 97
Cdd:cd03292   19 GINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYlrrKIGVVFQDFRLLPDRNVYEN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGRsphnslwgRLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIS 173
Cdd:cd03292   99 VAFAL--------EVTGVPpreiRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170
                        170       180
                 ....*....|....*....|....*
gi 492172462 174 HQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03292  171 TTWEIMNLLKKINKAGTTVVVATHA 195
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1-236 1.07e-21

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 90.34  E-value: 1.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK-V 79
Cdd:PRK10895   1 MATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARRgI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQvlpipEGVNVRQLVAYgrsphNSLWGRLS-----GADQHSvDQALQRME---LATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK10895  81 GYLPQ-----EASIFRRLSVY-----DNLMAVLQirddlSAEQRE-DRANELMEefhIEHLRDSMGQSLSGGERRRVEIA 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAEL 231
Cdd:PRK10895 150 RALAANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEH 229

                 ....*
gi 492172462 232 VCQVF 236
Cdd:PRK10895 230 VKRVY 234
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
18-218 1.09e-21

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 91.02  E-value: 1.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL---SARELACKVAFLPQvlPIPEGVNV 94
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLdrkQRRAFRRDVQLVFQ--DSPSAVNP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   95 RQLV-AYGRSPHNSLwGRLSGADQHSVDQALQRM-EL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:TIGR02769 104 RMTVrQIIGEPLRHL-TSLDESEQKARIAELLDMvGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLD 182
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 492172462  172 ISHQVELLDLMRELSAEGKTV-ITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:TIGR02769 183 MVLQAVILELLRKLQQAFGTAyLFITHDLRLVQSFCQRVAVMDKGQIV 230
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
4-229 1.10e-21

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


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 94.01  E-value: 1.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYGATRI--VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRpaLDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASLRRQVAL 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   82 LPQVLPIPEGvNVRQLVAYGRsphnslwgrLSGADQHSVDQALQRMELATLAER-PL----------SDLSGGQRQRAWL 150
Cdd:TIGR02203 411 VSQDVVLFND-TIANNIAYGR---------TEQADRAEIERALAAAYAQDFVDKlPLgldtpigengVLLSGGQRQRLAI 480
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462  151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERL-MQGRTTLVIAHRLS-TIEKADRIVVMDDGRIVERGTHNELLAR 557
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
18-216 1.78e-21

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: 89.07  E-value: 1.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIPEGvNVRQL 97
Cdd:cd03250   20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNG-TIREN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGrSPHNSLWGRlsgadqhSV------DQALQRME---LATLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03250   86 ILFG-KPFDEERYE-------KVikacalEPDLEILPdgdLTEIGEKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLS 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 492172462 169 YLDiSHQVELL--DLMRELSAEGKTVITVLHDInQACRYADHLAVMQGGR 216
Cdd:cd03250  157 AVD-AHVGRHIfeNCILGLLLNNKTRILVTHQL-QLLPHADQIVVLDNGR 204
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
4-197 2.51e-21

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 88.57  E-value: 2.51e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLsARELACKVAFLP 83
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQ-RDEPHENILYLG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   84 QVLPIPEGVNVRQLVaygrsphnSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:TIGR01189  80 HLPGLKPELSALENL--------HFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWIL 151
                         170       180       190
                  ....*....|....*....|....*....|....
gi 492172462  164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:TIGR01189 152 DEPTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
13-227 2.94e-21

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 89.64  E-value: 2.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlpipEGV 92
Cdd:PRK10619  15 YGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQLKVADKNQL----RLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYgrsPHNSLWGRLSG--------------ADQHSVDQALQRMELATLAERPL----SDLSGGQRQRAWLAMIL 154
Cdd:PRK10619  91 RTRLTMVF---QHFNLWSHMTVlenvmeapiqvlglSKQEARERAVKYLAKVGIDERAQgkypVHLSGGQQQRVSIARAL 167
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK10619 168 AMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLF 240
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
18-229 7.04e-21

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 88.60  E-value: 7.04e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTP----QSGSLSLDGKGY--SQLSARELAC-----KVAFLPqvl 86
Cdd:PRK10418  18 LVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAgvrqTAGRVLLDGKPVapCALRGRKIATimqnpRSAFNP--- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 pipegvnVRQLVAYGRSPHNSLwGRLSgadqhSVDQALQRMELATLAE--RPLS----DLSGGQRQRAWLAMILAQDAAI 160
Cdd:PRK10418  95 -------LHTMHTHARETCLAL-GKPA-----DDATLTAALEAVGLENaaRVLKlypfEMSGGMLQRMMIALALLCEAPF 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 161 VLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:PRK10418 162 IIADEPTTDLDVVAQARILDLLESIVQKrALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNA 231
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
19-226 1.08e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 88.61  E-value: 1.08e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYS---------------------QLSARELAC 77
Cdd:PRK13633  26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSdeenlwdirnkagmvfqnpdnQIVATIVEE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQVLPI-PEGVNVRqlvaygrsphnslwgrlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK13633 106 DVAFGPENLGIpPEEIRER------------------------VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAM 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13633 162 RPECIIFDEPTAMLDPSGRREVVNTIKELNKKyGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEI 231
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
3-217 1.36e-20

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 85.95  E-value: 1.36e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGatriVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAF 81
Cdd:cd03215    4 VLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDaIRAGIAY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LP---------QVLPIPEGVNVRQLvaygrsphnslwgrlsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAM 152
Cdd:cd03215   80 VPedrkreglvLDLSVAENIALSSL------------------------------------------LSGGNQQKVVLAR 117
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:cd03215  118 WLARDPRVLILDEPTRGVDVGAKAEIYRLIRELADAGKAVLLISSELDELLGLCDRILVMYEGRI 182
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
7-230 1.39e-20

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: 87.54  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   7 QHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSqlsareLACKVAFLPQ 84
Cdd:cd03252    4 EHVRFRYKPDGpvILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLA------LADPAWLRRQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 VlpipeGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQR-------MEL-----ATLAERPLSdLSGGQRQRAWLAM 152
Cdd:cd03252   78 V-----GVVLQENVLFNRSIRDNIALADPGMSMERVIEAAKLagahdfiSELpegydTIVGEQGAG-LSGGQRQRIAIAR 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:cd03252  152 ALIHNPRILIFDEATSALDYESEHAIMRNMHDICA-GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDELLAEN 227
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
14-228 1.42e-20

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 88.98  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KVAFlpqvlpIPE 90
Cdd:COG1135   16 GPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAarrKIGM------IFQ 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GVN------VRQLVAYgrsphnSLwgRLSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAI 160
Cdd:COG1135   90 HFNllssrtVAENVAL------PL--EIAGVPkaeiRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 161 VLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHD---INQACryaDHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG1135  162 LLCDEATSALDpeTTRSI--LDLLKDINRElGLTIVLITHEmdvVRRIC---DRVAVLENGRIVEQGPVLDVFA 230
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-218 1.65e-20

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 90.08  E-value: 1.65e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLdigyGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAF 81
Cdd:COG1129  256 VLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRDaIRAGIAY 331
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LP---------QVLPIPEGVNVRQLVAYGRsphnslWGRLSGADQHS-VDQALQRMELATL-AERPLSDLSGGQRQRAWL 150
Cdd:COG1129  332 VPedrkgeglvLDLSIRENITLASLDRLSR------GGLLDRRRERAlAEEYIKRLRIKTPsPEQPVGNLSGGNQQKVVL 405
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:COG1129  406 AKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVISSELPELLGLSDRILVMREGRIV 473
cbiO PRK13646
energy-coupling factor transporter ATPase;
19-226 1.69e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 88.30  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG-KGYSQLSARELACKVAFLPQVLPIPEGV----N 93
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDiTITHKTKDKYIRPVRKRIGMVFQFPESQlfedT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAYGrsPHNSlwgrlsGADQHSV-DQALQR-MELA----TLAERPLSdLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PRK13646 103 VEREIIFG--PKNF------KMNLDEVkNYAHRLlMDLGfsrdVMSQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPT 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 168 TYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDeNKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKEL 233
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
14-223 2.13e-20

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 87.51  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC---KVAFLPQVLPIPE 90
Cdd:PRK11831  18 GNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTvrkRMSMLFQSGALFT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 GVNVRQLVAYGRSPHNslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK11831  98 DMNVFDNVAYPLREHT----QLPAPLLHStVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVG 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 170 LD-ISHQVeLLDLMREL-SAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:PRK11831 174 QDpITMGV-LVKLISELnSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSA 228
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
4-221 3.51e-20

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 89.52  E-value: 3.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDI-GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILtPQSGSLSLDGKGYSQLSARELACKVAFL 82
Cdd:PRK11174 350 IEAEDLEIlSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWV 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGvNVRQLVAYGRSphnslwgrlsGADQHSVDQALQRMELATLAER-------PLSD----LSGGQRQRAWLA 151
Cdd:PRK11174 429 GQNPQLPHG-TLRDNVLLGNP----------DASDEQLQQALENAWVSEFLPLlpqgldtPIGDqaagLSVGQAQRLALA 497
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 152 MILAQDAAIVLLDEPTTYLDiSHQVELldLMRELS--AEGKTVITVLHDINQACRYaDHLAVMQGGRLVTCG 221
Cdd:PRK11174 498 RALLQPCQLLLLDEPTASLD-AHSEQL--VMQALNaaSRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQG 565
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
14-218 5.89e-20

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 87.09  E-value: 5.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckvAFLPQVLPI---PE 90
Cdd:COG4608   29 GVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRELR---PLRRRMQMVfqdPY 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 G-VN----VRQLVAYGRSPHnslwGRLSGAD-QHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:COG4608  106 AsLNprmtVGDIIAEPLRIH----GLASKAErRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVC 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINqACRY-ADHLAVMQGGRLV 218
Cdd:COG4608  182 DEPVSALDVSIQAQVLNLLEDLQDElGLTYLFISHDLS-VVRHiSDRVAVMYLGKIV 237
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
18-221 6.45e-20

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


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 88.65  E-value: 6.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipEGV----N 93
Cdd:TIGR01846 472 VLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWLRRQMGVVLQ-----ENVlfsrS 546
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   94 VRQLVAYGRS----PHNSLWGRLSGAdqHSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:TIGR01846 547 IRDNIALCNPgapfEHVIHAAKLAGA--HDFISELPQGYNTEVGEKG-ANLSGGQRQRIAIARALVGNPRILIFDEATSA 623
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 492172462  170 LDISHQVELLDLMRELSAeGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:TIGR01846 624 LDYESEALIMRNMREICR-GRTVIIIAHRLS-TVRACDRIIVLEKGQIAESG 673
cbiO PRK13650
energy-coupling factor transporter ATPase;
18-223 7.88e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 86.32  E-value: 7.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFlpqVLPIPE----GVN 93
Cdd:PRK13650  22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGM---VFQNPDnqfvGAT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTY 169
Cdd:PRK13650  99 VEDDVAFGLEnkgiPHEEMKER--------VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSM 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 170 LDISHQVELLDLMRELSAE-GKTVITVLHDINQACrYADHLAVMQGGRLVTCGAP 223
Cdd:PRK13650 171 LDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTP 224
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
2-222 1.07e-19

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 85.45  E-value: 1.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLS--------LDGKGYSQLSAR 73
Cdd:PRK09984   3 TIIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGShiellgrtVQREGRLARDIR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  74 ELACKVAFLPQVLPIPEGVNVRQLVAYGRSPHNSLWGR----LSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAW 149
Cdd:PRK09984  83 KSRANTGYIFQQFNLVNRLSVLENVLIGALGSTPFWRTcfswFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVA 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 150 LAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA-EGKTVITVLHDINQACRYADHLAVMQGGRLVTCGA 222
Cdd:PRK09984 163 IARALMQQAKVILADEPIASLDPESARIVMDTLRDINQnDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGS 236
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
16-197 1.95e-19

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 87.17  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGysqlsarelacKVAFLPQVLPIPEGvNVR 95
Cdd:COG4178  376 RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA-----------RVLFLPQRPYLPLG-TLR 443
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVAYgrsPHnslwgrlsGADQHS---VDQALQRMELATLAERpLSD-------LSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:COG4178  444 EALLY---PA--------TAEAFSdaeLREALEAVGLGHLAER-LDEeadwdqvLSLGEQQRLAFARLLLHKPDWLFLDE 511
                        170       180       190
                 ....*....|....*....|....*....|..
gi 492172462 166 PTTYLDISHQVELLDLMRELSAEGkTVITVLH 197
Cdd:COG4178  512 ATSALDEENEAALYQLLREELPGT-TVISVGH 542
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
3-230 1.97e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 85.67  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGAT-----RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKGYSQLSARELAC 77
Cdd:PRK13631  21 ILRVKNLYCVFDEKqenelVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQV-GDIYIGDKKNNHEL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQvlPIPEGVNVRQLVAY-GRSPHNSLWGRLSGAD---------QHSVDQA------LQRMEL-ATLAERPLSDL 140
Cdd:PRK13631 100 ITNPYSK--KIKNFKELRRRVSMvFQFPEYQLFKDTIEKDimfgpvalgVKKSEAKklakfyLNKMGLdDSYLERSPFGL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTC 220
Cdd:PRK13631 178 SGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
                        250
                 ....*....|
gi 492172462 221 GAPGDVLTAE 230
Cdd:PRK13631 258 GTPYEIFTDQ 267
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
13-248 1.98e-19

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 84.73  E-value: 1.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSldgKGYSQLS-ARE---LACKVAFLpqvLPI 88
Cdd:PRK11247  22 YGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELL---AGTAPLAeAREdtrLMFQDARL---LPW 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  89 PEgvnVRQLVAYGrsphnslwgrLSGadqHSVDQALQRMELATLAER----PLSdLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:PRK11247  96 KK---VIDNVGLG----------LKG---QWRDAALQALAAVGLADRanewPAA-LSGGQKQRVALARALIHRPGLLLLD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 165 EPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRL---VTCGAP-----GDVLTAELVCQV 235
Cdd:PRK11247 159 EPLGALDALTRIEMQDLIESLWQQhGFTVLLVTHDVSEAVAMADRVLLIEEGKIgldLTVDLPrprrrGSARLAELEAEV 238
                        250
                 ....*....|...
gi 492172462 236 FDvhvQIMREPVA 248
Cdd:PRK11247 239 LQ---RVMSRGES 248
cbiO PRK13642
energy-coupling factor transporter ATPase;
3-235 2.38e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 84.76  E-value: 2.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDL---SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKV 79
Cdd:PRK13642   4 ILEVENLVFKYEKESDVNQLngvSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFlpqVLPIPE----GVNVRQLVAYGRS----PHNSLWGRlsgadqhsVDQALQRMELATLAERPLSDLSGGQRQRAWLA 151
Cdd:PRK13642  84 GM---VFQNPDnqfvGATVEDDVAFGMEnqgiPREEMIKR--------VDEALLAVNMLDFKTREPARLSGGQKQRVAVA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 152 MILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGK-TVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVL-TA 229
Cdd:PRK13642 153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQlTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFaTS 231

                 ....*.
gi 492172462 230 ELVCQV 235
Cdd:PRK13642 232 EDMVEI 237
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-199 3.87e-19

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 83.62  E-value: 3.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKA-QHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSldgkgysqlsaRELACKV 79
Cdd:PRK09544   1 MTSLVSlENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK-----------RNGKLRI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVL----PIPEGVnvrqlvaygrsphnSLWGRLS-GADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMIL 154
Cdd:PRK09544  70 GYVPQKLyldtTLPLTV--------------NRFLRLRpGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARAL 135
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDI 199
Cdd:PRK09544 136 LNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRElDCAVLMVSHDL 181
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
7-221 3.94e-19

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: 86.41  E-value: 3.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   7 QHLDIGYGATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---KGYSQLSARElacKVAFL 82
Cdd:COG5265  361 ENVSFGYDPERpILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGqdiRDVTQASLRA---AIGIV 437
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQ--VLpipegVN--VRQLVAYGRSphnslwgrlsGADQHSVDQALQRMEL-----------ATL-AERPLSdLSGGQRQ 146
Cdd:COG5265  438 PQdtVL-----FNdtIAYNIAYGRP----------DASEEEVEAAARAAQIhdfieslpdgyDTRvGERGLK-LSGGEKQ 501
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHdinqacR-----YADHLAVMQGGRLVTCG 221
Cdd:COG5265  502 RVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAH------RlstivDADEILVLEAGRIVERG 574
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
4-221 4.17e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 84.38  E-value: 4.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTP-----QSGSLSLDGKG-YSQLSARELAC 77
Cdd:PRK14271  22 MAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKvsgyrYSGDVLLGGRSiFNYRDVLEFRR 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQvLPIPEGVNVRQLVAYGRSPHNslwgRLSGADQHSVDQA-LQRMELATLAERPLSD----LSGGQRQRAWLAM 152
Cdd:PRK14271 102 RVGMLFQ-RPNPFPMSIMDNVLAGVRAHK----LVPRKEFRGVAQArLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLAR 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELsAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK14271 177 TLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSL-ADRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
17-218 4.55e-19

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 83.60  E-value: 4.55e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckvAFLPQV----------- 85
Cdd:COG1101   20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEYKRA---KYIGRVfqdpmmgtaps 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  86 LPIPEgvNVrqLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELAtLAER---PLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:COG1101   97 MTIEE--NL--ALAYRRGKRRGLRRGLTKKRRELFRELLATLGLG-LENRldtKVGLLSGGQRQALSLLMATLTKPKLLL 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 163 LDEPTTYLD--ISHQVelLDLMRELSAEGK-TVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:COG1101  172 LDEHTAALDpkTAALV--LELTEKIVEENNlTTLMVTHNMEQALDYGNRLIMMHEGRII 228
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
3-232 4.70e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 85.87  E-value: 4.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS---ARELAckV 79
Cdd:PRK15439  11 LLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTpakAHQLG--I 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVLPIPEGVNVRQLVAYGRSPHNslwgrlsgADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK15439  89 YLVPQEPLLFPNLSVKENILFGLPKRQ--------ASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELV 232
Cdd:PRK15439 161 ILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADLSTDDII 233
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
4-197 7.48e-19

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the bacterial CcmAB transporter. The CCM family is involved in bacterial cytochrome c biogenesis. Cytochrome c maturation in E. coli requires the ccm operon, which encodes eight membrane proteins (CcmABCDEFGH). CcmE is a periplasmic heme chaperon that binds heme covalently and transfers it onto apocytochrome c in the presence of CcmF, CcmG, and CcmH. The CcmAB proteins represent an ABC transporter and the CcmCD proteins participate in heme transfer to CcmE.


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 81.77  E-value: 7.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSArELACKVAFLP 83
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIARGLLYLG 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVLPIPEGVNVRQLVAYgrsphnslWGRLSGADQhsVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03231   80 HAPGIKTTLSVLENLRF--------WHADHSDEQ--VEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWIL 149
                        170       180       190
                 ....*....|....*....|....*....|....
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:cd03231  150 DEPTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
14-226 1.68e-18

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 83.35  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLpIPEgVN 93
Cdd:PRK11650  15 GKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVFQNYAL-YPH-MS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAYGRsphnslwgRLSGADQHSVDQ----ALQRMELATLAERPLSDLSGGQRQRawLAMILA--QDAAIVLLDEPT 167
Cdd:PRK11650  93 VRENMAYGL--------KIRGMPKAEIEErvaeAARILELEPLLDRKPRELSGGQRQR--VAMGRAivREPAVFLFDEPL 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 168 TYLD----ISHQVELLDLMRELSAegkTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK11650 163 SNLDaklrVQMRLEIQRLHRRLKT---TSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEV 222
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
13-221 1.92e-18

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 83.09  E-value: 1.92e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDL---SFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---GYSQLSARELACKVaflpqvl 86
Cdd:PRK11308  22 FKPERLVKALdgvSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQdllKADPEAQKLLRQKI------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 pipegvnvrQLVAygRSPHNSLWGR----------------LSGADQhsVDQALQRMELATL----AERPLSDLSGGQRQ 146
Cdd:PRK11308  95 ---------QIVF--QNPYGSLNPRkkvgqileepllintsLSAAER--REKALAMMAKVGLrpehYDRYPHMFSGGQRQ 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQElGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKG 237
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
19-200 1.99e-18

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 82.83  E-value: 1.99e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaflpqvlpIP---EGVNVR 95
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGY----------------------VPfkrRKEFAR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QL-VAYG-RSphnSLWGRLSGAD----------------QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:COG4586   96 RIgVVFGqRS---QLWWDLPAIDsfrllkaiyripdaeyKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHR 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTviTVL---HDIN 200
Cdd:COG4586  173 PKILFLDEPTIGLDVVSKEAIREFLKEYNRERGT--TILltsHDMD 216
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
13-229 2.53e-18

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 81.77  E-value: 2.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  13 YGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAflpqvlpipegv 92
Cdd:COG4598   18 FGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGELVPA------------ 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYgRS------PHNSLWGRLS------GADQH----SVDQALQRMElATLAERPLSD--------LSGGQRQRA 148
Cdd:COG4598   86 DRRQLQRI-RTrlgmvfQSFNLWSHMTvlenviEAPVHvlgrPKAEAIERAE-ALLAKVGLADkrdaypahLSGGQQQRA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG4598  164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFG 243

                 .
gi 492172462 229 A 229
Cdd:COG4598  244 N 244
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
21-227 3.52e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 82.06  E-value: 3.52e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL---DGKGYSQLSARELAC--------KVAFLPQVLPIP 89
Cdd:PRK13651  25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEKVLeklviqktRFKKIKKIKEIR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  90 EGVNV------RQL-------------VAYGRSPhnslwgrlsgadQHSVDQALQRMELATLAERPLS----DLSGGQRQ 146
Cdd:PRK13651 105 RRVGVvfqfaeYQLfeqtiekdiifgpVSMGVSK------------EEAKKRAAKYIELVGLDESYLQrspfELSGGQKR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDI 252

                 .
gi 492172462 227 L 227
Cdd:PRK13651 253 L 253
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
10-218 3.71e-18

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes a multidomain ABC transporter subunit that is one of three protein families associated with some regularity with a distinctive family of putative bacteriocins. It includes a bacteriocin-processing peptidase domain at the N-terminus. Model TIGR03793 describes a conserved propeptide region for this bacteriocin family, unusual because it shows obvious homology a region of the enzyme nitrile hydratase up to the classic Gly-Gly cleavage motif. This family is therefore predicted to be a subunit of a bacteriocin processing and export system characteristic to this system that we designate NHLM, Nitrile Hydratase Leader Microcin. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 83.45  E-value: 3.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   10 DIGYGATRI----VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQV 85
Cdd:TIGR03796 482 NITFGYSPLepplIENFSLTLQPGQRVALVGGSGSGKSTIAKLVAGLYQPWSGEILFDGIPREEIPREVLANSVAMVDQD 561
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   86 LPIPEGvNVRQLVaygrsphnSLWGR------LSGADQ----HSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILA 155
Cdd:TIGR03796 562 IFLFEG-TVRDNL--------TLWDPtipdadLVRACKdaaiHDVITSRPGGYDAELAEGG-ANLSGGQRQRLEIARALV 631
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462  156 QDAAIVLLDEPTTYLDIshQVELLdLMRELSAEGKTVITVLHDINqACRYADHLAVMQGGRLV 218
Cdd:TIGR03796 632 RNPSILILDEATSALDP--ETEKI-IDDNLRRRGCTCIIVAHRLS-TIRDCDEIIVLERGKVV 690
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
19-240 3.83e-18

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 82.54  E-value: 3.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAckvAFLPQVLPIPEGVN----- 93
Cdd:PRK11153  21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELR---KARRQIGMIFQHFNllssr 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 -VRQLVAygrsphnsLWGRLSGADQHS----VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK11153  98 tVFDNVA--------LPLELAGTPKAEikarVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 169 YLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDV-------LTAELVCQVFDVHV 240
Cdd:PRK11153 170 ALDPATTRSILELLKDINRElGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVfshpkhpLTREFIQSTLHLDL 249
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
4-228 4.10e-18

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 81.24  E-value: 4.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiLTPQSGSLSLDGK----GYS----QLSAREL 75
Cdd:PRK14258   8 IKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNR-MNELESEVRVEGRveffNQNiyerRVNLNRL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  76 ACKVAFL---PQVLPIpegvNVRQLVAYGRS-----PHNSLWGRLSGA--DQHSVDQALQRMELATLaerplsDLSGGQR 145
Cdd:PRK14258  87 RRQVSMVhpkPNLFPM----SVYDNVAYGVKivgwrPKLEIDDIVESAlkDADLWDEIKHKIHKSAL------DLSGGQQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLD------ISHQVELLDLMRELsaegkTVITVLHDINQACRYADHLAVMQG----- 214
Cdd:PRK14258 157 QRLCIARALAVKPKVLLMDEPCFGLDpiasmkVESLIQSLRLRSEL-----TMVIVSHNLHQVSRLSDFTAFFKGnenri 231
                        250
                 ....*....|....
gi 492172462 215 GRLVTCGAPGDVLT 228
Cdd:PRK14258 232 GQLVEFGLTKKIFN 245
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
4-230 5.01e-18

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


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 83.08  E-value: 5.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYG--ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLkafaRIL----TPQSGSLSLDGKGYSQLSARELAc 77
Cdd:TIGR03797 452 IEVDRVTFRYRpdGPLILDDVSLQIEPGEFVAIVGPSGSGKSTLL----RLLlgfeTPESGSVFYDGQDLAGLDVQAVR- 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   78 kvaflpqvlpipegvnvRQL---VAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLAE----RPL----------SDL 140
Cdd:TIGR03797 527 -----------------RQLgvvLQNGRLMSGSIFENIAGGAPLTLDEAWEAARMAGLAEdiraMPMgmhtviseggGTL 589
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAegkTVITVLHDINqACRYADHLAVMQGGRLVTC 220
Cdd:TIGR03797 590 SGGQRQRLLIARALVRKPRILLFDEATSALDNRTQAIVSESLERLKV---TRIVIAHRLS-TIRNADRIYVLDAGRVVQQ 665
                         250
                  ....*....|
gi 492172462  221 GAPGDVLTAE 230
Cdd:TIGR03797 666 GTYDELMARE 675
cbiO PRK13644
energy-coupling factor transporter ATPase;
29-228 5.07e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 81.19  E-value: 5.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSL---SLDGKGYSQLSA-RELACKVAFLPQVLPIpeGVNVRQLVAYGrsP 104
Cdd:PRK13644  28 GEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVlvsGIDTGDFSKLQGiRKLVGIVFQNPETQFV--GRTVEEDLAFG--P 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 105 HNSLWGRLSgaDQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRE 184
Cdd:PRK13644 104 ENLCLPPIE--IRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 492172462 185 LSAEGKTVITVLHDINQaCRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:PRK13644 182 LHEKGKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLS 224
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
14-216 6.07e-18

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: 80.17  E-value: 6.07e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRI--VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG----YSQLSARELackVA------- 80
Cdd:COG4778   20 GGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGgwvdLAQASPREI---LAlrrrtig 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 ----FLpQVLPipeGVNVRQLVAygrsphNSLwgRLSGADQhsvDQALQRME--LATL--AERpLSDL-----SGGQRQR 147
Cdd:COG4778   97 yvsqFL-RVIP---RVSALDVVA------EPL--LERGVDR---EEARARARelLARLnlPER-LWDLppatfSGGEQQR 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:COG4778  161 VNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREAVADRVVDVTPFS 229
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
19-215 7.10e-18

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: 79.82  E-value: 7.10e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackVAFlpQVLPIPEGVNVRQLV 98
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM---VVF--QNYSLLPWLTVRENI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   99 AYGRsphNSLWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVE 177
Cdd:TIGR01184  76 ALAV---DRVLPDLSKSERRAiVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 492172462  178 LLD-LMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:TIGR01184 153 LQEeLMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNG 191
cbiO PRK13645
energy-coupling factor transporter ATPase;
21-235 1.04e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 80.44  E-value: 1.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSppAGQVTALIGPNGCGKSTLLKAFARILTPQSG-SLSLDGKGYSQL----SARELACKVAFlpqVLPIPE----G 91
Cdd:PRK13645  31 SLTFK--KNKVTCVIGTTGSGKSTMIQLTNGLIISETGqTIVGDYAIPANLkkikEVKRLRKEIGL---VFQFPEyqlfQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 VNVRQLVAYGrsPHNSlwgrlsGADQHSVDQAL-QRMELATL----AERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK13645 106 ETIEKDIAFG--PVNL------GENKQEAYKKVpELLKLVQLpedyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEP 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 167 TTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT-AELVCQV 235
Cdd:PRK13645 178 TGGLDPKGEEDFINLFERLNKEyKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSnQELLTKI 248
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1-218 2.12e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 81.29  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGY---GATR-IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARIL-TPQ----SGSLSLDGKGYSQLS 71
Cdd:PRK15134   3 QPLLAIENLSVAFrqqQTVRtVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLpSPPvvypSGDIRFHGESLLHAS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  72 AREL----ACKVAF------------------LPQVLPIPEGVnvRQLVAYGRSphnslwgrLSGADQHSVDQALQRmel 129
Cdd:PRK15134  83 EQTLrgvrGNKIAMifqepmvslnplhtlekqLYEVLSLHRGM--RREAARGEI--------LNCLDRVGIRQAAKR--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 130 atLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADH 208
Cdd:PRK15134 150 --LTDYP-HQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQElNMGLLFITHNLSIVRKLADR 226
                        250
                 ....*....|
gi 492172462 209 LAVMQGGRLV 218
Cdd:PRK15134 227 VAVMQNGRCV 236
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
16-217 2.86e-17

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 78.32  E-value: 2.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC----KVAFLPQ---VLP- 87
Cdd:PRK11629  22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAElrnqKLGFIYQfhhLLPd 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  88 --IPEGVNVRQLVAyGRSPHNSlwgrlsgadQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:PRK11629 102 ftALENVAMPLLIG-KKKPAEI---------NSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADE 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492172462 166 PTTYLDISHQVELLDLMRELSA-EGKTVITVLHDINQACRYADHLAvMQGGRL 217
Cdd:PRK11629 172 PTGNLDARNADSIFQLLGELNRlQGTAFLVVTHDLQLAKRMSRQLE-MRDGRL 223
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
4-223 3.33e-17

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 77.45  E-value: 3.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGA--TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:cd03369    7 IEVENLSVRYAPdlPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQVLPIPEGVNVRQLVAYGRSPHNSLWGRLSGADQHsvdqalqrmelatlaerplSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:cd03369   87 IPQDPTLFSGTIRSNLDPFDEYSDEEIYGALRVSEGG-------------------LNLSQGQRQLLCLARALLKRPRVL 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 162 LLDEPTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAP 223
Cdd:cd03369  148 VLDEATASIDYATDALIQKTIREEFT-NSTILTIAHRLRTIIDY-DKILVMDAGEVKEYDHP 207
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-236 3.49e-17

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 78.15  E-value: 3.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS----AREla 76
Cdd:COG1137    1 MMTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhkrARL-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 cKVAFLPQVLPIPEGVNVRQ---LVAYGRsphnslwgRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAM 152
Cdd:COG1137   79 -GIGYLPQEASIFRKLTVEDnilAVLELR--------KLSKKEREErLEELLEEFGITHLRKSKAYSLSGGERRRVEIAR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 153 ILAQDAAIVLLDEPTTYLD-IShqV-ELLDLMRELSAEGktvITVL---HDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:COG1137  150 ALATNPKFILLDEPFAGVDpIA--VaDIQKIIRHLKERG---IGVLitdHNVRETLGICDRAYIISEGKVLAEGTPEEIL 224

                 ....*....
gi 492172462 228 TAELVCQVF 236
Cdd:COG1137  225 NNPLVRKVY 233
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-219 3.52e-17

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: 77.86  E-value: 3.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHL----DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS----AR 73
Cdd:COG4181    7 PIIELRGLtktvGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDedarAR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  74 ELACKVAFLPQ--------------VLPIpEGVNVRQlvAYGRSphnslwgrlsgadqhsvDQALQRMELATLAE-RPlS 138
Cdd:COG4181   87 LRARHVGFVFQsfqllptltalenvMLPL-ELAGRRD--ARARA-----------------RALLERVGLGHRLDhYP-A 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 139 DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--ISHQVelLDLMRELSAE-GKTVITVLHDINQACRyADHLAVMQGG 215
Cdd:COG4181  146 QLSGGEQQRVALARAFATEPAILFADEPTGNLDaaTGEQI--IDLLFELNRErGTTLVLVTHDPALAAR-CDRVLRLRAG 222

                 ....
gi 492172462 216 RLVT 219
Cdd:COG4181  223 RLVE 226
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
3-172 4.73e-17

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: 80.36  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKgysqlsarelACKVAFL 82
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GE----------TVKLAYV 390
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   83 PQvlpipegvnvrqlvayGRS---PHNSLWGRLSGADQHSVdqaLQRMELATLA------------ERPLSDLSGGQRQR 147
Cdd:TIGR03719 391 DQ----------------SRDaldPNKTVWEEISGGLDIIK---LGKREIPSRAyvgrfnfkgsdqQKKVGQLSGGERNR 451
                         170       180
                  ....*....|....*....|....*
gi 492172462  148 AWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:TIGR03719 452 VHLAKTLKSGGNVLLLDEPTNDLDV 476
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
21-218 5.47e-17

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: 79.84  E-value: 5.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELAckvAFlpqvlpipegvnvRQLVA- 99
Cdd:COG4615  352 DLTIRR--GELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ---PVTADNRE---AY-------------RQLFSa 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 100 ----YgrspH--NSLWGRLSGADQHSVDQALQRMELA---TLAERPLS--DLSGGQRQRawLAMILA--QDAAIVLLDE- 165
Cdd:COG4615  411 vfsdF----HlfDRLLGLDGEADPARARELLERLELDhkvSVEDGRFSttDLSQGQRKR--LALLVAllEDRPILVFDEw 484
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 166 -----PtTYLDISHQvELLDLMRelsAEGKTVITVLHDInqacRY---ADHLAVMQGGRLV 218
Cdd:COG4615  485 aadqdP-EFRRVFYT-ELLPELK---ARGKTVIAISHDD----RYfdlADRVLKMDYGKLV 536
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
21-221 5.49e-17

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 77.87  E-value: 5.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQSGSL-----SLDGK---GYSQLSARELACKVAFLPQ---VLP-- 87
Cdd:PRK11264  23 DLEVKP--GEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTArslSQQKGLIRQLRQHVGFVFQnfnLFPhr 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  88 -----IPEG-VNVR-----QLVAYGRsphnslwgrlsgadqhsvdQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:PRK11264 101 tvlenIIEGpVIVKgepkeEATARAR-------------------ELLAKVGLAGKETSYPRRLSGGQQQRVAIARALAM 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11264 162 RPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFARDVADRAIFMDQGRIVEQG 226
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
18-223 6.38e-17

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: 77.15  E-value: 6.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQ- 96
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIPQD-PVLFSGTIRSn 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  97 LVAYGRSPHNSLWgrlsgadqhsvdQALQRMELATLAERPL-----------SDLSGGQRQRAWLAMILAQDAAIVLLDE 165
Cdd:cd03244   98 LDPFGEYSDEELW------------QALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLARALLRKSKILVLDE 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 166 PTTYLDISHQVELLDLMRELSAeGKTVITVLHDINQACRYaDHLAVMQGGRLVTCGAP 223
Cdd:cd03244  166 ATASVDPETDALIQKTIREAFK-DCTVLTIAHRLDTIIDS-DRILVLDKGRVVEFDSP 221
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
3-226 6.81e-17

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 77.72  E-value: 6.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKvafl 82
Cdd:PRK11300   5 LLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARM---- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 pqvlpipeGV-----NVR----------QLVAYGRSPHNSLwgrLSG---------ADQHSVDQA---LQRMELATLAER 135
Cdd:PRK11300  81 --------GVvrtfqHVRlfremtvienLLVAQHQQLKTGL---FSGllktpafrrAESEALDRAatwLERVGLLEHANR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 136 PLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQG 214
Cdd:PRK11300 150 QAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLVMGISDRIYVVNQ 229
                        250
                 ....*....|..
gi 492172462 215 GRLVTCGAPGDV 226
Cdd:PRK11300 230 GTPLANGTPEEI 241
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
19-230 7.97e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 79.44  E-value: 7.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK---------------GYSQLSARElackVAFLP 83
Cdd:PRK09700 279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKdisprspldavkkgmAYITESRRD----NGFFP 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 QVlpipegvNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMELATLA------ERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK09700 355 NF-------SIAQNMAISRSLKDGGYKGAMGLFHEVDEQRTAENQRELLAlkchsvNQNITELSGGNQQKVLISKWLCCC 427
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK09700 428 PEVIIFDEPTRGIDVGAKAEIYKVMRQLADDGKVILMVSSELPEIITVCDRIAVFCEGRLTQILTNRDDMSEE 500
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
19-221 1.19e-16

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 79.13  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIP-EGVNVRQL 97
Cdd:PRK10261 340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDPyASLDPRQT 419
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGRSPHNSLWGRLSG-ADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:PRK10261 420 VGDSIMEPLRVHGLLPGkAAAARVAWLLERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIR 499
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492172462 176 VELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK10261 500 GQIINLLLDLQRDfGIAYLFISHDMAVVERISHRVAVMYLGQIVEIG 546
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
14-221 1.54e-16

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 78.85  E-value: 1.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL--ACKVAFLPQVLpipeg 91
Cdd:PRK13657 346 NSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLrrNIAVVFQDAGL----- 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 vnvrqlvaYGRSPHNSLW-GRLSGADQHSVD-----QALQRME-----LATLA-ERPLSdLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK13657 421 --------FNRSIEDNIRvGRPDATDEEMRAaaeraQAHDFIErkpdgYDTVVgERGRQ-LSGGERQRLAIARALLKDPP 491
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLS-TVRNADRILVFDNGRVVESG 551
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
17-218 3.32e-16

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 75.49  E-value: 3.32e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARI--LTPQSGSLSLDGKGYSQLSARELACK---VAFlPQVLPIPeG 91
Cdd:COG0396   14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHpkYEVTSGSILLDGEDILELSPDERARAgifLAF-QYPVEIP-G 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 VNVRQLVaygRSPHNSLWG-RLSGADQHS-VDQALQRMEL-ATLAERPL-SDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:COG0396   92 VSVSNFL---RTALNARRGeELSAREFLKlLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEILQMLLLEPKLAILDETD 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 168 TYLDI-SHQVeLLDLMRELSAEGKT--VIT----VLHDINqacryADHLAVMQGGRLV 218
Cdd:COG0396  169 SGLDIdALRI-VAEGVNKLRSPDRGilIIThyqrILDYIK-----PDFVHVLVDGRIV 220
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
30-223 3.96e-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: 78.13  E-value: 3.96e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    30 QVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGY-SQLSArelackvaflpqvlpipegvnVRQlvAYGRSP-HNS 107
Cdd:TIGR01257  957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA---------------------VRQ--SLGMCPqHNI 1013
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   108 LWGRLSGADQ---------HSVDQALQRMElATLAERPL--------SDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:TIGR01257 1014 LFHHLTVAEHilfyaqlkgRSWEEAQLEME-AMLEDTGLhhkrneeaQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGV 1092
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 492172462   171 DISHQVELLDLMRELSAeGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAP 223
Cdd:TIGR01257 1093 DPYSRRSIWDLLLKYRS-GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
12-198 8.53e-16

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 76.69  E-value: 8.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELAC----KVAFLPQ--- 84
Cdd:PRK10535  17 GEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQlrreHFGFIFQryh 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 VLP-IPEGVNVRQLVAYGRSPHNSlwgRLSGADQhsvdqALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10535  97 LLShLTAAQNVEVPAVYAGLERKQ---RLLRAQE-----LLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILA 168
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHD 203
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
4-227 1.85e-15

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: 75.61  E-value: 1.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLD-GKGYSQLSARELACK---- 78
Cdd:TIGR03269 285 VSKRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvGDEWVDMTKPGPDGRgrak 364
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   79 --VAFLPQvlpipegvnvrqlvAYGRSPHNSLWGRLSGA------DQHSVDQALQRMELATLAE--------RPLSDLSG 142
Cdd:TIGR03269 365 ryIGILHQ--------------EYDLYPHRTVLDNLTEAiglelpDELARMKAVITLKMVGFDEekaeeildKYPDELSE 430
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  143 GQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD-LMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:TIGR03269 431 GERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHsILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIG 510

                  ....*.
gi 492172462  222 APGDVL 227
Cdd:TIGR03269 511 DPEEIV 516
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
4-223 2.90e-15

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 73.06  E-value: 2.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA-----RIltpQSGSLSLDGKGYSQLSARELACK 78
Cdd:TIGR01978   1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAghpsyEV---TSGTILFKGQDLLELEPDERARA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   79 VAFLPQVLP--IPeGVNVRQLVaygRSPHNSlwgRLSGADQHSVD---------QALQRMEL-ATLAERPLSD-LSGGQR 145
Cdd:TIGR01978  78 GLFLAFQYPeeIP-GVSNLEFL---RSALNA---RRSARGEEPLDlldfekllkEKLALLDMdEEFLNRSVNEgFSGGEK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  146 QRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRY--ADHLAVMQGGRLVTCGAP 223
Cdd:TIGR01978 151 KRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGINRLREPDRSFLIITHY-QRLLNYikPDYVHVLLDGRIVKSGDV 229
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
3-217 3.20e-15

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: 74.86  E-value: 3.20e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    3 ILKAQHL---DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKA-FARILTPQSGSLSLDGKGYSQLS-ARELAC 77
Cdd:TIGR02633 257 ILEARNLtcwDVINPHRKRVDDVSFSLRRGEILGVAGLVGAGRTELVQAlFGAYPGKFEGNVFINGKPVDIRNpAQAIRA 336
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   78 KVAFLPQ---------VLPIPEGVNVRQLVAYgrsphnSLWGRL-SGADQHSVDQALQRMELATLA-ERPLSDLSGGQRQ 146
Cdd:TIGR02633 337 GIAMVPEdrkrhgivpILGVGKNITLSVLKSF------CFKMRIdAAAELQIIGSAIQRLKVKTASpFLPIGRLSGGNQQ 410
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462  147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:TIGR02633 411 KAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQEGVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
18-198 3.51e-15

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 74.99  E-value: 3.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPI--PEGvNVR 95
Cdd:PRK11147 334 LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----------LEVAYFDQHRAEldPEK-TVM 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVAYGRSPHNslwgrLSGADQHsVDQALQ-------RmelatlAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK11147 402 DNLAEGKQEVM-----VNGRPRH-VLGYLQdflfhpkR------AMTPVKALSGGERNRLLLARLFLKPSNLLILDEPTN 469
                        170       180       190
                 ....*....|....*....|....*....|.
gi 492172462 169 YLDIshqvELLDLMRELSAEGK-TVITVLHD 198
Cdd:PRK11147 470 DLDV----ETLELLEELLDSYQgTVLLVSHD 496
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
16-197 3.74e-15

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


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 71.03  E-value: 3.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPIPEGvNVR 95
Cdd:cd03223   14 RVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMPEG-----------EDLLFLPQRPYLPLG-TLR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVAYgrsPhnslWGRLsgadqhsvdqalqrmelatlaerplsdLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQ 175
Cdd:cd03223   82 EQLIY---P----WDDV---------------------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESE 127
                        170       180
                 ....*....|....*....|..
gi 492172462 176 VELLDLMRELSAegkTVITVLH 197
Cdd:cd03223  128 DRLYQLLKELGI---TVISVGH 146
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
29-224 6.99e-15

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 73.93  E-value: 6.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   29 GQVTALIGPNGCGKSTLLKAFARILTP---QSGSLSLDGKgysQLSARELACKVAFLPQV-LPIP-----EGVNVRQLVA 99
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGM---PIDAKEMRAISAYVQQDdLFIPtltvrEHLMFQAHLR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  100 YGRSPHNSlwGRlsgadQHSVDQALQRMELATLA------ERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD-- 171
Cdd:TIGR00955 128 MPRRVTKK--EK-----RERVDEVLQALGLRKCAntrigvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDsf 200
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 492172462  172 ISHQVelLDLMRELSAEGKTVITVLHD-INQACRYADHLAVMQGGRLVTCGAPG 224
Cdd:TIGR00955 201 MAYSV--VQVLKGLAQKGKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPD 252
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
3-172 1.04e-14

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 73.23  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL-------------------- 62
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgetvklayvdqsrdaldpnk 403
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  63 -------DGKGYSQLSARElackvaflpqvlpipegVNVRqlvAY-GRspHNslwgrLSGADQhsvdqalqrmelatlaE 134
Cdd:PRK11819 404 tvweeisGGLDIIKVGNRE-----------------IPSR---AYvGR--FN-----FKGGDQ----------------Q 440
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492172462 135 RPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:PRK11819 441 KKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLDV 478
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
29-214 1.10e-14

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: 69.91  E-value: 1.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysqlsarelaCKVAFLPQVLpipegvnvrqlvaygrsphnsl 108
Cdd:cd03222   25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDG------------ITPVYKPQYI---------------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 wgrlsgadqhsvdqalqrmelatlaerplsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE 188
Cdd:cd03222   71 ------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEE 120
                        170       180
                 ....*....|....*....|....*..
gi 492172462 189 G-KTVITVLHDINQACRYADHLAVMQG 214
Cdd:cd03222  121 GkKTALVVEHDLAVLDYLSDRIHVFEG 147
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
4-221 1.18e-14

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: 70.63  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKGYSQLSARELACKVAF 81
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEERARLGIF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 L-PQVLPIPEGVNVRQLVaygrsphnslwgrlsgadqhsvdqalqrmelatlaeRPLSD-LSGGQRQRAWLAMILAQDAA 159
Cdd:cd03217   81 LaFQYPPEIPGVKNADFL------------------------------------RYVNEgFSGGEKKRNEILQLLLLEPD 124
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH-----DINQacryADHLAVMQGGRLVTCG 221
Cdd:cd03217  125 LAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHyqrllDYIK----PDRVHVLYDGRIVKSG 187
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
14-176 1.27e-14

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 73.41  E-value: 1.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQsGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:TIGR01271 1230 AGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLSTE-GEIQIDGVSWNSVTLQTWRKAFGVIPQKVFIFSGTF 1308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    94 VRQLVAYGRSPHNSLWGRLSGADQHSV-DQALQRMELAtlaerpLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:TIGR01271 1309 RKNLDPYEQWSDEEIWKVAEEVGLKSViEQFPDKLDFV------LVDggyvLSNGHKQLMCLARSILSKAKILLLDEPSA 1382

                   ....*....
gi 492172462   169 YLD-ISHQV 176
Cdd:TIGR01271 1383 HLDpVTLQI 1391
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
19-231 1.99e-14

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 70.97  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK--GYSQLSARELACKVAF------------LPQ 84
Cdd:PRK15112  29 VKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHplHFGDYSYRSQRIRMIFqdpstslnprqrISQ 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  85 VLPIPEGVNVrQLVAYGRsphnslwgrlsgadQHSVDQALQRMELatlaerpLSD--------LSGGQRQRAWLAMILAQ 156
Cdd:PRK15112 109 ILDFPLRLNT-DLEPEQR--------------EKQIIETLRQVGL-------LPDhasyyphmLAPGQKQRLGLARALIL 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462 157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAEL 231
Cdd:PRK15112 167 RPKVIIADEALASLDMSMRSQLINLMLELQEKqGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-218 2.17e-14

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 70.68  E-value: 2.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQL-SARELACKV 79
Cdd:PRK11614   3 KVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVLPIPEGVNVRQLVAYGrsphnslwGRLsgADQHSVDQALQRME--LATLAERPLS---DLSGGQRQRAWLAMIL 154
Cdd:PRK11614  83 AIVPEGRRVFSRMTVEENLAMG--------GFF--AERDQFQERIKWVYelFPRLHERRIQragTMSGGEQQMLAIGRAL 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK11614 153 MSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANQALKLADRGYVLENGHVV 216
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
1-226 4.36e-14

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 70.91  E-value: 4.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKST-------LLKAFARIltpqSGSLSLDGKGYSQ 69
Cdd:PRK09473  10 DALLDVKDLRVTFstpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQtafalmgLLAANGRI----GGSATFNGREILN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  70 LSAREL----ACKVAFLPQ------------------VLPIPEGVNVRQlvAYGRSphnslwgrLSGADQHSVDQALQRM 127
Cdd:PRK09473  86 LPEKELnklrAEQISMIFQdpmtslnpymrvgeqlmeVLMLHKGMSKAE--AFEES--------VRMLDAVKMPEARKRM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 128 ELATlaerplSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKT-VITVLHDINQACRYA 206
Cdd:PRK09473 156 KMYP------HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTaIIMITHDLGVVAGIC 229
                        250       260
                 ....*....|....*....|
gi 492172462 207 DHLAVMQGGRLVTCGAPGDV 226
Cdd:PRK09473 230 DKVLVMYAGRTMEYGNARDV 249
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
4-230 4.68e-14

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 71.48  E-value: 4.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDigygATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFL 82
Cdd:PRK11288 258 LRLDGLK----GPGLREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRDaIRAGIMLC 333
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 P---------QVLPIPEGVNVrqlvayGRSPHNSLWGRL--SGADQHSVDQALQRMELATL-AERPLSDLSGGQRQRAWL 150
Cdd:PRK11288 334 PedrkaegiiPVHSVADNINI------SARRHHLRAGCLinNRWEAENADRFIRSLNIKTPsREQLIMNLSGGNQQKAIL 407
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 151 AMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVtcgapGDVLTAE 230
Cdd:PRK11288 408 GRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPEVLGVADRIVVMREGRIA-----GELAREQ 482
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
3-216 5.20e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 71.11  E-value: 5.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILtPQ---SGSLSLDGKGYSQLSARELACK- 78
Cdd:PRK13549   5 LLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEGEELQASNIRDTERAg 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  79 VAFLPQVLPIPEGVNVRQLVAYGRSPHNSlwGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQD 157
Cdd:PRK13549  84 IAIIHQELALVKELSVLENIFLGNEITPG--GIMDYDAMYLrAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGR 216
Cdd:PRK13549 162 ARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVKAISDTICVIRDGR 220
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
18-185 5.80e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 71.27  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQsGSLSLDGKGYSQLSAREL-----ACKVAFLPQVLPIPEGV 92
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINSQ-GEIWFDGQPLHNLNRRQLlpvrhRIQVVFQDPNSSLNPRL 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVAYGRSPHNSlwgRLSGADQHS-VDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL 170
Cdd:PRK15134 380 NVLQIIEEGLRVHQP---TLSAAQREQqVIAVMEEVGLdPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTSSL 456
                        170
                 ....*....|....*
gi 492172462 171 DISHQVELLDLMREL 185
Cdd:PRK15134 457 DKTVQAQILALLKSL 471
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
28-218 7.48e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 70.80  E-value: 7.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  28 AGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGY-------SQLSA-----RELAckvaFLPQvLPIPEGVNVr 95
Cdd:PRK10762  29 PGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfngpksSQEAGigiihQELN----LIPQ-LTIAENIFL- 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 qlvayGRSPHNSlWGRLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PRK10762 103 -----GREFVNR-FGRIDWKKMYAeADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDALTDTE 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492172462 175 QVELLDLMRELSAEGKTVITVLH---DINQACryaDHLAVMQGGRLV 218
Cdd:PRK10762 177 TESLFRVIRELKSQGRGIVYISHrlkEIFEIC---DDVTVFRDGQFI 220
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
21-217 7.96e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 70.85  E-value: 7.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQ-------VLPIPEGV 92
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrLARGLVYLPEdrqssglYLDAPLAW 360
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  93 NVRQLVaYGRsphNSLWGRlSGADQHSVDQALQRMELA-TLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK15439 361 NVCALT-HNR---RGFWIK-PARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVD 435
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK15439 436 VSARNDIYQLIRSIAAQNVAVLFISSDLEEIEQMADRVLVMHQGEI 481
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
3-218 1.06e-13

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 68.36  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElackVAF 81
Cdd:PRK10908   1 MIRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNRE----VPF 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LpqvlpipegvnvRQLVAYGRSPHNSLWGR-----------LSGAD----QHSVDQALQRMELATLAERPLSDLSGGQRQ 146
Cdd:PRK10908  77 L------------RRQIGMIFQDHHLLMDRtvydnvaipliIAGASgddiRRRVSAALDKVGLLDKAKNFPIQLSGGEQQ 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 147 RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK10908 145 RVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLH 216
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
20-227 1.32e-13

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 70.05  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  20 QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDG---KGYSQLSARElacKVAFLPQvlpipegvNVRQ 96
Cdd:PRK11176 360 RNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGhdlRDYTLASLRN---QVALVSQ--------NVHL 428
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  97 L-------VAYGRSPHNSLWGRLSGADQ-HSVDqALQRME--LATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK11176 429 FndtiannIAYARTEQYSREQIEEAARMaYAMD-FINKMDngLDTVIGENGVLLSGGQRQRIAIARALLRDSPILILDEA 507
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 167 TTYLDISHQVELLDLMRELSAEgKTVITVLHDINqACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK11176 508 TSALDTESERAIQAALDELQKN-RTSLVIAHRLS-TIEKADEILVVEDGEIVERGTHAELL 566
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
17-198 1.40e-13

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: 66.61  E-value: 1.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPagQVTALIGPNGCGKSTLLKAFARILTPQSgslsldgkgysqlsarelackvaflpQVLPIPEGVNVRQ 96
Cdd:cd03227   11 FVPNDVTFGEG--SLTIITGPNGSGKSTILDAIGLALGGAQ--------------------------SATRRRSGVKAGC 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  97 LVAYgrsphnslwgrlsgadqhsvdqalQRMELATLaerpLSDLSGGQRQRAWLAMILA----QDAAIVLLDEPTTYLDI 172
Cdd:cd03227   63 IVAA------------------------VSAELIFT----RLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDP 114
                        170       180
                 ....*....|....*....|....*.
gi 492172462 173 SHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03227  115 RDGQALAEAILEHLVKGAQVIVITHL 140
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
19-215 1.55e-13

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: 67.74  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACK----VAFLPQVlPIPEGVNV 94
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRnrysVAYAAQK-PWLLNATV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQLVAYGrSPHNSLWGRL---SGADQHSVDqALQRMELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03290   96 EENITFG-SPFNKQRYKAvtdACSLQPDID-LLPFGDQTEIGERGI-NLSGGQRQRICVARALYQNTNIVFLDDPFSALD 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 172 ISHQVELLD--LMRELSAEGKTVITVLHDInQACRYADHLAVMQGG 215
Cdd:cd03290  173 IHLSDHLMQegILKFLQDDKRTLVLVTHKL-QYLPHADWIIAMKDG 217
cyc_pep_trnsptr TIGR01194
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...
28-219 1.72e-13

cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. Bacteria have elaborate pathways for the production of toxins and secondary metabolites. Many such compounds, including syringomycin and pyoverdine are synthesized on non-ribosomal templates consisting of a multienzyme complex. On several occasions the proteins of the complex and transporter protein are present on the same operon. Often times these compounds cross the biological membrane by specific transporters. Syringomycin is an amphipathic, cylclic lipodepsipeptide when inserted into host causes formation of channels, permeable to variety of cations. On the other hand, pyoverdine is a cyclic octa-peptidyl dihydroxyquinoline, which is efficient in sequestering iron for uptake. [Transport and binding proteins, Amino acids, peptides and amines, Transport and binding proteins, Other]


Pssm-ID: 130262 [Multi-domain]  Cd Length: 555  Bit Score: 69.60  E-value: 1.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   28 AGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackvaflpqvlpipegvnvRQLVAYGRSPHNs 107
Cdd:TIGR01194 367 QGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDY-------------------RDLFSAIFADFH- 426
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  108 LWGRLSGAD---QHSVDQA---LQRMELA------TLAERPLSDLSGGQRQRawLAMILA--QDAAIVLLDEPTTYLDIS 173
Cdd:TIGR01194 427 LFDDLIGPDegeHASLDNAqqyLQRLEIAdkvkieDGGFSTTTALSTGQQKR--LALICAwlEDRPILLFDEWAADQDPA 504
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 492172462  174 -HQVELLDLMRELSAEGKTVITVLHDiNQACRYADHLAVMQGGRLVT 219
Cdd:TIGR01194 505 fKRFFYEELLPDLKRQGKTIIIISHD-DQYFELADQIIKLAAGCIVK 550
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
3-217 1.79e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 69.57  E-value: 1.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHL---DIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKA-FARILTPQSGSLSLDGKGYSQLSARE-LAC 77
Cdd:PRK13549 259 ILEVRNLtawDPVNPHIKRVDDVSFSLRRGEILGIAGLVGAGRTELVQClFGAYPGRWEGEIFIDGKPVKIRNPQQaIAQ 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQ-------VLPIPEGVNVrQLVAYGRSphnSLWGRL-SGADQHSVDQALQRMELATL-AERPLSDLSGGQRQRA 148
Cdd:PRK13549 339 GIAMVPEdrkrdgiVPVMGVGKNI-TLAALDRF---TGGSRIdDAAELKTILESIQRLKVKTAsPELAIARLSGGNQQKA 414
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK13549 415 VLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
2-214 2.10e-13

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 67.50  E-value: 2.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLD--IGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLS----AR 73
Cdd:PRK10584   5 NIVEVHHLKksVGQGEHElsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDeearAK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  74 ELACKVAFLPQVLPIPEGVNVRQLVaygrsphnSLWGRLSG-ADQHSVDQALQRMELATLAER----PlSDLSGGQRQRA 148
Cdd:PRK10584  85 LRAKHVGFVFQSFMLIPTLNALENV--------ELPALLRGeSSRQSRNGAKALLEQLGLGKRldhlP-AQLSGGEQQRV 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQG 214
Cdd:PRK10584 156 ALARAFNGRPDVLFADEPTGNLDRQTGDKIADLLFSLNREhGTTLILVTHDLQLAARCDRRLRLVNG 222
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
22-205 2.96e-13

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of the ABC transporter ATP-binding cassette, but are found outside the common ABC transporter operon structure that features integral membrane permease proteins and substrate-binding proteins encoded next to the ATP-binding cassette (ABC domain) protein. The member protein ChvD from Agrobacterium tumefaciens was identified as both a candidate to interact with VirB8, based on yeast two-hybrid analysis, and as an apparent regulator of VirG. The general function of this protein family is unknown.


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 69.19  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   22 LSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDgKGYsqlsarelacKVAFLPQVLPIPEGVNVRQLVAYG 101
Cdd:TIGR03719  26 LSFFP--GAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARPQ-PGI----------KVGYLPQEPQLDPTKTVRENVEEG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  102 RSPHNSLWGRLS----------------------------GADQHSVDQalqRMELATLAER------PLSDLSGGQRQR 147
Cdd:TIGR03719  93 VAEIKDALDRFNeisakyaepdadfdklaaeqaelqeiidAADAWDLDS---QLEIAMDALRcppwdaDVTKLSGGERRR 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462  148 AWLAMILAQDAAIVLLDEPTTYLDiSHQVELLDlmRELSAEGKTVITVLHDinqacRY 205
Cdd:TIGR03719 170 VALCRLLLSKPDMLLLDEPTNHLD-AESVAWLE--RHLQEYPGTVVAVTHD-----RY 219
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
18-229 3.38e-13

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 69.20  E-value: 3.38e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVNVRQL 97
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVLFSGSLRMNL 1380
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    98 VAYGRSPHNSLWGRLSGADQHSVDQALQ---RMELATLAErplsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:TIGR00957 1381 DPFSQYSDEEVWWALELAHLKTFVSALPdklDHECAEGGE----NLSVGQRQLVCLARALLRKTKILVLDEATAAVDLET 1456
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 492172462   175 QvELLDLMRELSAEGKTVITVLHDINQACRYAdHLAVMQGGRLVTCGAPGDVLTA 229
Cdd:TIGR00957 1457 D-NLIQSTIRTQFEDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPSNLLQQ 1509
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
14-176 7.43e-13

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 66.80  E-value: 7.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  14 GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQsGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVN 93
Cdd:cd03289   15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTE-GDIQIDGVSWNSVPLQKWRKAFGVIPQKVFIFSGTF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAYGRSPHNSLWGRLSGADQHSV-DQALQRMELAtlaerpLSD----LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:cd03289   94 RKNLDPYGKWSDEEIWKVAEEVGLKSViEQFPGQLDFV------LVDggcvLSHGHKQLMCLARSVLSKAKILLLDEPSA 167

                 ....*....
gi 492172462 169 YLD-ISHQV 176
Cdd:cd03289  168 HLDpITYQV 176
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
3-197 7.54e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 65.36  E-value: 7.54e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysQLSARELAC---KV 79
Cdd:PRK13540   1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER----QSIKKDLCTyqkQL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVLPIPEGVNVRQlvaygrsphNSLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK13540  77 CFVGHRSGINPYLTLRE---------NCLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAK 147
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PRK13540 148 LWLLDEPLVALDELSLLTIITKIQEHRAKGGAVLLTSH 185
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
19-222 8.70e-13

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 67.57  E-value: 8.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTpQSGSLSLDGKGYSQLSARELackVAFLPQVLPIPEGVNVRQLV 98
Cdd:PRK10261  32 VRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLE-QAGGLVQCDKMLLRRRSRQV---IELSEQSAAQMRHVRGADMA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 AYGRSPHNSLWGRLSGADQHS----VDQALQRMELATLAERPLS----------------DLSGGQRQRAWLAMILAQDA 158
Cdd:PRK10261 108 MIFQEPMTSLNPVFTVGEQIAesirLHQGASREEAMVEAKRMLDqvripeaqtilsryphQLSGGMRQRVMIAMALSCRP 187
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 159 AIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCGA 222
Cdd:PRK10261 188 AVLIADEPTTALDVTIQAQILQLIKVLQKEmSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGS 252
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
3-218 1.27e-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: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILtPQ---SGSLSLDGKGYSQLSARELACK- 78
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVY-PHgtwDGEIYWSGSPLKASNIRDTERAg 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   79 VAFLPQVLPIPEGVNVRQLVAYGRS-PHNSlwGRLSGADQ-HSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILA 155
Cdd:TIGR02633  80 IVIIHQELTLVPELSVAENIFLGNEiTLPG--GRMAYNAMyLRAKNLLRELQLdADNVTRPVGDYGGGQQQLVEIAKALN 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462  156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
29-217 1.89e-12

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 66.53  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTllkaFARILT----PQSGSLSLDGkgysqlsarelackvaflpqvlpipEGVNVRQLVAYgRSP 104
Cdd:PRK10522 349 GELLFLIGGNGSGKST----LAMLLTglyqPQSGEILLDG-------------------------KPVTAEQPEDY-RKL 398
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 105 HNS------LWGRLSGADQHSVDQA-----LQRMELA---TLAERPLSD--LSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK10522 399 FSAvftdfhLFDQLLGPEGKPANPAlvekwLERLKMAhklELEDGRISNlkLSKGQKKRLALLLALAEERDILLLDEWAA 478
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 169 YLD-----ISHQvELLDLMRELsaeGKTVITVLHDiNQACRYADHLAVMQGGRL 217
Cdd:PRK10522 479 DQDphfrrEFYQ-VLLPLLQEM---GKTIFAISHD-DHYFIHADRLLEMRNGQL 527
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
20-193 1.89e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 64.44  E-value: 1.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  20 QDLSFSPPAGQVTALIGPNGCGKSTLLkafaRILT----PQSGSLSLDGKGYSQLsaRElackvAFLPQVLPI--PEGVN 93
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLL----RILAglarPDAGEVLWQGEPIRRQ--RD-----EYHQDLLYLghQPGIK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 vRQLVAYgrspHNSLW-GRLSG-ADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK13538  87 -TELTAL----ENLRFyQRLHGpGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
                        170       180
                 ....*....|....*....|...
gi 492172462 172 iSHQVELL-DLMRELSAEGKTVI 193
Cdd:PRK13538 162 -KQGVARLeALLAQHAEQGGMVI 183
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
7-171 2.42e-12

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 66.28  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   7 QHLDIGYGATRIV-QDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQV 85
Cdd:PRK10790 344 DNVSFAYRDDNLVlQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQGVAMVQQD 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  86 lPIPEGVNVRQLVAYGRSphnslwgrlsgADQHSVDQALQRMELATLAeRPLSD------------LSGGQRQRAWLAMI 153
Cdd:PRK10790 424 -PVVLADTFLANVTLGRD-----------ISEEQVWQALETVQLAELA-RSLPDglytplgeqgnnLSVGQKQLLALARV 490
                        170
                 ....*....|....*...
gi 492172462 154 LAQDAAIVLLDEPTTYLD 171
Cdd:PRK10790 491 LVQTPQILILDEATANID 508
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
27-221 2.76e-12

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 65.67  E-value: 2.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  27 PAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARElacKVAFLPqvlpiPEGVNVRQLVAYGR-SPH 105
Cdd:PRK11144  22 PAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGR---VLFDAE---KGICLP-----PEKRRIGYVFQDARlFPH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 106 NSLWGRL----SGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDL 181
Cdd:PRK11144  91 YKVRGNLrygmAKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492172462 182 MRELSAEGKT-VITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK11144 171 LERLAREINIpILYVSHSLDEILRLADRVVVLEQGKVKAFG 211
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
16-194 3.48e-12

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis fibrosis transmembrane conductor regulator (CFTR) in eukaryotes. The principal role of this protein is chloride ion conductance. The protein is predicted to consist of 12 transmembrane domains. Mutations or lesions in the genetic loci have been linked to the aetiology of asthma, bronchiectasis, chronic obstructive pulmonary disease etc. Disease-causing mutations have been studied by 36Cl efflux assays in vitro cell cultures and electrophysiology, all of which point to the impairment of chloride channel stability and not the biosynthetic processing per se. [Transport and binding proteins, Anions]


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 66.09  E-value: 3.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIPEGVnVR 95
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGT-IK 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    96 QLVAYGRSphnslwgrlsgADQH---SVDQALQRME-LATLAER---PLSD----LSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:TIGR01271  505 DNIIFGLS-----------YDEYrytSVIKACQLEEdIALFPEKdktVLGEggitLSGGQRARISLARAVYKDADLYLLD 573
                          170       180       190
                   ....*....|....*....|....*....|..
gi 492172462   165 EPTTYLDISHQVELLD--LMRELSAEGKTVIT 194
Cdd:TIGR01271  574 SPFTHLDVVTEKEIFEscLCKLMSNKTRILVT 605
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
3-215 5.14e-12

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: 65.81  E-value: 5.14e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462     3 ILKAQHLDIGYGATR--IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQlSARELACKVA 80
Cdd:TIGR01257 1937 ILRLNELTKVYSGTSspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILT-NISDVHQNMG 2015
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    81 FLPQVLPIPEGVNVRQlvaygrspHNSLWGRLSGADQHSVDQ----ALQRMELATLAERPLSDLSGGQRQRAWLAMILAQ 156
Cdd:TIGR01257 2016 YCPQFDAIDDLLTGRE--------HLYLYARLRGVPAEEIEKvanwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIG 2087
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462   157 DAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGG 215
Cdd:TIGR01257 2088 CPPLVLLDEPTTGMDPQARRMLWNTIVSIIREGRAVVLTSHSMEECEALCTRLAIMVKG 2146
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
15-215 6.36e-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: 64.11  E-value: 6.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  15 ATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIPEGVnV 94
Cdd:cd03291   49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGT-I 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQLVAYGRSphnslwgrlsgADQH---SVDQALQRME-LATLAER---PLSD----LSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:cd03291  115 KENIIFGVS-----------YDEYrykSVVKACQLEEdITKFPEKdntVLGEggitLSGGQRARISLARAVYKDADLYLL 183
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 492172462 164 DEPTTYLDISHQVELLD-LMRELSAEgKTVITVLHDINQaCRYADHLAVMQGG 215
Cdd:cd03291  184 DSPFGYLDVFTEKEIFEsCVCKLMAN-KTRILVTSKMEH-LKKADKILILHEG 234
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
4-198 1.37e-11

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 64.14  E-value: 1.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   4 LKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG----YSQLSARELAckv 79
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENAnigyYAQDHAYDFE--- 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 aflpqvlpipEGVNVRQLVAYGRSPhnslwgrlsGADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQRAWLAMILAQDA 158
Cdd:PRK15064 397 ----------NDLTLFDWMSQWRQE---------GDDEQAVRGTLGRLLFsQDDIKKSVKVLSGGEKGRMLFGKLMMQKP 457
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492172462 159 AIVLLDEPTTYLDIsHQVELLDLMRELsAEGkTVITVLHD 198
Cdd:PRK15064 458 NVLVMDEPTNHMDM-ESIESLNMALEK-YEG-TLIFVSHD 494
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
6-197 1.83e-11

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction only];


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 61.90  E-value: 1.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   6 AQHLDIGYGA--TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARiltpqsgslsldgkgysQLSARELACKVAFlp 83
Cdd:COG2401   31 LEAFGVELRVveRYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAG-----------------ALKGTPVAGCVDV-- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  84 qvlpipegvnvrqlvaygrsPHNSLWGRLSGADQ----HSVDQALQRMELATLAE-----RPLSDLSGGQRQRAWLAMIL 154
Cdd:COG2401   92 --------------------PDNQFGREASLIDAigrkGDFKDAVELLNAVGLSDavlwlRRFKELSTGQKFRFRLALLL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 492172462 155 AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAE-GKTVITVLH 197
Cdd:COG2401  152 AERPKLLVIDEFCSHLDRQTAKRVARNLQKLARRaGITLVVATH 195
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
22-233 2.03e-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: 63.81  E-value: 2.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackVAFLPQVLPIpEGVNVRQLVAYG 101
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGS-------------VAYVPQQAWI-QNDSLRENILFG 722
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   102 RSPHNSLWGRLSGADQHSVD-QALQRMELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:TIGR00957  723 KALNEKYYQQVLEACALLPDlEILPSGDRTEIGEKGV-NLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGKHIFE 801
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   181 --LMRELSAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLT-----AELVC 233
Cdd:TIGR00957  802 hvIGPEGVLKNKTRILVTHGISYLPQ-VDVIIVMSGGKISEMGSYQELLQrdgafAEFLR 860
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
3-231 2.32e-11

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 63.12  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDI-GYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSAREL-ACKVA 80
Cdd:COG3845  257 VLEVENLSVrDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERrRLGVA 336
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQ-------VLPIPEGVNVrqLVAYGRSPHNSLWGRLsgaDQHSV-DQALQRME----LATLAERPLSDLSGGQRQRA 148
Cdd:COG3845  337 YIPEdrlgrglVPDMSVAENL--ILGRYRRPPFSRGGFL---DRKAIrAFAEELIEefdvRTPGPDTPARSLSGGNQQKV 411
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 149 WLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLT 228
Cdd:COG3845  412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGEVPAAEATR 491

                 ...
gi 492172462 229 AEL 231
Cdd:COG3845  492 EEI 494
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
8-217 2.68e-11

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 63.10  E-value: 2.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   8 HLDIGYGATRI---------VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LAC 77
Cdd:PRK10762 248 RLDKAPGEVRLkvdnlsgpgVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDgLAN 327
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQ-------VLpipeGVNVRQ---LVAYGRspHNSLWGRLSGADQH-SVDQALQRMELATLA-ERPLSDLSGGQR 145
Cdd:PRK10762 328 GIVYISEdrkrdglVL----GMSVKEnmsLTALRY--FSRAGGSLKHADEQqAVSDFIRLFNIKTPSmEQAIGLLSGGNQ 401
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PRK10762 402 QKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAEGLSIILVSSEMPEVLGMSDRILVMHEGRI 473
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
19-208 3.09e-11

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: 61.08  E-value: 3.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPagqVTALIGPNGCGKSTLLKAFARILTpqsGSLSLDGKGYSQLsaRELACKVAFLPQVLPIPEGVNVRQLV 98
Cdd:cd03240   15 RSEIEFFSP---LTLIVGQNGAGKTTIIEALKYALT---GELPPNSKGGAHD--PKLIREGEVRAQVKLAFENANGKKYT 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 AYgRSPH---NSLWgrlsgadqhsVDQAlqrmELATLAERPLSDLSGGQRQ------RAWLAMILAQDAAIVLLDEPTTY 169
Cdd:cd03240   87 IT-RSLAileNVIF----------CHQG----ESNWPLLDMRGRCSGGEKVlasliiRLALAETFGSNCGILALDEPTTN 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492172462 170 LDISH-QVELLDLMRE-LSAEGKTVITVLHDINQAcRYADH 208
Cdd:cd03240  152 LDEENiEESLAEIIEErKSQKNFQLIVITHDEELV-DAADH 191
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
22-205 3.69e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.83  E-value: 3.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  22 LSFSPPA--GqvtaLIGPNGCGKSTLLKAFARILTPQSGSLSLDgKGYsqlsarelacKVAFLPQVLPIPEGVNVRQLV- 98
Cdd:PRK11819  28 LSFFPGAkiG----VLGLNGAGKSTLLRIMAGVDKEFEGEARPA-PGI----------KVGYLPQEPQLDPEKTVRENVe 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 ------------------AYGRSPHNS---------LWGRLSGADQHSVDQalqRMELATLAER------PLSDLSGGQR 145
Cdd:PRK11819  93 egvaevkaaldrfneiyaAYAEPDADFdalaaeqgeLQEIIDAADAWDLDS---QLEIAMDALRcppwdaKVTKLSGGER 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 146 QRAWLAMILAQDAAIVLLDEPTTYLDiSHQVELLDlmRELSAEGKTVITVLHDinqacRY 205
Cdd:PRK11819 170 RRVALCRLLLEKPDMLLLDEPTNHLD-AESVAWLE--QFLHDYPGTVVAVTHD-----RY 221
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
19-227 3.81e-11

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 61.76  E-value: 3.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelackvaflPQVLPIPEGVNvrqlv 98
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE-----------------VSVIAISAGLS----- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 aygrsphnslwGRLSGAD----------------QHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13546  98 -----------GQLTGIEniefkmlcmgfkrkeiKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILV 166
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVL 227
Cdd:PRK13546 167 IDEALSVGDQTFAQKCLDKIYEFKEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVL 231
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1-229 4.04e-11

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 62.07  E-value: 4.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGAT----RIVQDLSFSPPAGQVTALIGPNGCGKS-TLLKAFARILTP---QSGSLSLDGKGYSQLSA 72
Cdd:PRK11022   1 MALLNVDKLSVHFGDEsapfRAVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  73 RE----LACKVAFLPQV------------LPIPEGVNVRQlvaygrsphnslwgrlSGADQHSVDQALQRMELATLAErP 136
Cdd:PRK11022  81 KErrnlVGAEVAMIFQDpmtslnpcytvgFQIMEAIKVHQ----------------GGNKKTRRQRAIDLLNQVGIPD-P 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 137 LS-------DLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELS-AEGKTVITVLHDINQACRYADH 208
Cdd:PRK11022 144 ASrldvyphQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQqKENMALVLITHDLALVAEAAHK 223
                        250       260
                 ....*....|....*....|.
gi 492172462 209 LAVMQGGRLVTCGAPGDVLTA 229
Cdd:PRK11022 224 IIVMYAGQVVETGKAHDIFRA 244
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
17-218 7.91e-11

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding cassette transporters; The pleiotropic drug resistance (PDR) is a well-described phenomenon occurring in fungi and shares several similarities with processes in bacteria and higher eukaryotes. This PDR subfamily represents domain I of its (ABC-IM)2 organization. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds including sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 59.56  E-value: 7.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKGYSQLSARElackVAFLPQVLPIPEGVNV 94
Cdd:cd03232   21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrKTAGVITGEILINGRPLDKNFQRS----TGYVEQQDVHSPNLTV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  95 RQlvaygrsphnSLwgRLSGAdqhsvdqalqrmelatlaerpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:cd03232   97 RE----------AL--RFSAL---------------------LRGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQA 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 175 QVELLDLMRELSAEGKTVITVLHDINQAC-RYADHLAVMQ-GGRLV 218
Cdd:cd03232  144 AYNIVRFLKKLADSGQAILCTIHQPSASIfEKFDRLLLLKrGGKTV 189
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
19-218 1.23e-10

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213205 [Multi-domain]  Cd Length: 176  Bit Score: 58.87  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFariltpqsgslsldgkGYSQLSARELACKVAFLPQVLpipegVNVRQLv 98
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVNEG----------------LYASGKARLISFLPKFSRNKL-----IFIDQL- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  99 aygrsphnslwgrlsgadQHSVDQALQRMELatlaERPLSDLSGGQRQRAWLAMILAQDA--AIVLLDEPTTYLDISHQV 176
Cdd:cd03238   69 ------------------QFLIDVGLGYLTL----GQKLSTLSGGELQRVKLASELFSEPpgTLFILDEPSTGLHQQDIN 126
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 492172462 177 ELLDLMRELSAEGKTVITVLHDINQACrYADHLAVM------QGGRLV 218
Cdd:cd03238  127 QLLEVIKGLIDLGNTVILIEHNLDVLS-SADWIIDFgpgsgkSGGKVV 173
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
19-221 1.75e-10

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 60.11  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEG-----VN 93
Cdd:PRK15079  37 VDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLAslnprMT 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  94 VRQLVAygrSPHNSLWGRLSGADqhsVDQALQRME-----LATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:PRK15079 117 IGEIIA---EPLRTYHPKLSRQE---VKDRVKAMMlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 169 YLDISHQVELLDLMRELSAE-GKTVITVLHDINQACRYADHLAVMQGGRLVTCG 221
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREmGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELG 244
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
121-221 2.19e-10

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 60.13  E-value: 2.19e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 121 DQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDIN 200
Cdd:NF000106 126 DELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYME 205
                         90       100
                 ....*....|....*....|.
gi 492172462 201 QACRYADHLAVMQGGRLVTCG 221
Cdd:NF000106 206 EAEQLAHELTVIDRGRVIADG 226
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
29-218 2.58e-10

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 60.13  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARE-LACKVAFLPQVLPIPEGVNVRQLVAYGRSPHNS 107
Cdd:PRK10982  24 HSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEaLENGISMVHQELNLVLQRSVMDNMWLGRYPTKG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 108 LWgrlsgadqhsVDQA-LQRMELATLAE--------RPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYL---DISHq 175
Cdd:PRK10982 104 MF----------VDQDkMYRDTKAIFDEldididprAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLtekEVNH- 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 492172462 176 veLLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:PRK10982 173 --LFTIIRKLKERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
PLN03211 PLN03211
ABC transporter G-25; Provisional
29-197 2.98e-10

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 60.28  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFA----------------RILTPQ----SGSLSLDGKGYSQLSARE--LACKVAFLPQVL 86
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNALAgriqgnnftgtilannRKPTKQilkrTGFVTQDDILYPHLTVREtlVFCSLLRLPKSL 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 PIPEgvnvrqlvaygrsphnslwgRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PLN03211 174 TKQE--------------------KILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEP 233
                        170       180       190
                 ....*....|....*....|....*....|.
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:PLN03211 234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMH 264
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
18-197 3.52e-10

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 273360 [Multi-domain]  Cd Length: 659  Bit Score: 59.76  E-value: 3.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPIPEGvNVRQL 97
Cdd:TIGR00954 467 LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK-----------GKLFYVPQRPYMTLG-TLRDQ 534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   98 VAYGRSPHNSLWGRLSGADqhsVDQALQRMELATLAERPLS---------DLSGGQRQRAWLAMILAQDAAIVLLDEPTT 168
Cdd:TIGR00954 535 IIYPDSSEDMKRRGLSDKD---LEQILDNVQLTHILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAILDECTS 611
                         170       180       190
                  ....*....|....*....|....*....|
gi 492172462  169 ylDISHQVEllDLMRELSAE-GKTVITVLH 197
Cdd:TIGR00954 612 --AVSVDVE--GYMYRLCREfGITLFSVSH 637
PLN03232 PLN03232
ABC transporter C family member; Provisional
19-194 7.63e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 59.22  E-value: 7.63e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSlSLDGKGysqlsarelacKVAFLPQVlPIPEGVNVRQLV 98
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS-SVVIRG-----------SVAYVPQV-SWIFNATVRENI 699
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   99 AYGRSPHNSLWGRL--SGADQHSVDQALQRmELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--ISH 174
Cdd:PLN03232  700 LFGSDFESERYWRAidVTALQHDLDLLPGR-DLTEIGERGV-NISGGQKQRVSMARAVYSNSDIYIFDDPLSALDahVAH 777
                         170       180
                  ....*....|....*....|
gi 492172462  175 QVELLDLMRELSAEGKTVIT 194
Cdd:PLN03232  778 QVFDSCMKDELKGKTRVLVT 797
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
3-194 1.57e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.40  E-value: 1.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELACKVAFL 82
Cdd:PRK13543  11 LLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGK---TATRGDRSRFMAYL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  83 PQVLPIPEGVNVRQLVAYgrspHNSLWGRLSgadQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVL 162
Cdd:PRK13543  88 GHLPGLKADLSTLENLHF----LCGLHGRRA---KQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWL 160
                        170       180       190
                 ....*....|....*....|....*....|....
gi 492172462 163 LDEPTTYLDIShQVELLDLM--RELSAEGKTVIT 194
Cdd:PRK13543 161 LDEPYANLDLE-GITLVNRMisAHLRGGGAALVT 193
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
1-172 1.66e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.04  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKafarILtpqSGSLSLDgKGYSQLsARELacKVA 80
Cdd:PRK11147   1 MSLISIHGAWLSFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMK----IL---NGEVLLD-DGRIIY-EQDL--IVA 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLP----------IPEGVN-----------VRQLVAYGRSP--------------HNSLWgRLsgadQHSVDQALQ 125
Cdd:PRK11147  70 RLQQDPPrnvegtvydfVAEGIEeqaeylkryhdISHLVETDPSEknlnelaklqeqldHHNLW-QL----ENRINEVLA 144
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 492172462 126 RMELAtlAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDI 172
Cdd:PRK11147 145 QLGLD--PDAALSSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDI 189
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
29-200 2.27e-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: 54.69  E-value: 2.27e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdgkgysqlsarelackvaflpqvlpipegvnvrqlvaygrsphnsl 108
Cdd:smart00382   2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIY---------------------------------------------- 35
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   109 wgrLSGADQHSVDQALQRMELATlaeRPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD------LM 182
Cdd:smart00382  36 ---IDGEDILEEVLDQLLLIIVG---GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrlLL 109
                          170
                   ....*....|....*...
gi 492172462   183 RELSAEGKTVITVLHDIN 200
Cdd:smart00382 110 LLKSEKNLTVILTTNDEK 127
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
3-198 2.34e-09

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 57.49  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLdGKG-----YSQLSARELAC 77
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGiklgyFAQHQLEFLRA 390
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  78 KVAFLPQVLPIPEGVNVRQLVAYgrsphnsLWGRLSGADQhsVDQALQRmelatlaerplsdLSGGQRQRAWLAMILAQD 157
Cdd:PRK10636 391 DESPLQHLARLAPQELEQKLRDY-------LGGFGFQGDK--VTEETRR-------------FSGGEKARLVLALIVWQR 448
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 492172462 158 AAIVLLDEPTTYLDISHQVELLDLMRELsaEGKTVItVLHD 198
Cdd:PRK10636 449 PNLLLLDEPTNHLDLDMRQALTEALIDF--EGALVV-VSHD 486
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
19-232 2.73e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 57.44  E-value: 2.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysQLSARELAC--KVAFLPQVLPIPEGVNVRQ 96
Cdd:NF033858 282 VDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQ---PVDAGDIATrrRVGYMSQAFSLYGELTVRQ 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  97 -LVAYGRSPHnslwgrLSGADQHS-VDQALQRMELATLAERPLSDLSGGQRQRAWL--AMILAQDaaIVLLDEPTTYLDI 172
Cdd:NF033858 359 nLELHARLFH------LPAAEIAArVAEMLERFDLADVADALPDSLPLGIRQRLSLavAVIHKPE--LLILDEPTSGVDP 430
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462 173 SHQVELLDLMRELSAEGKTVITV-LHDINQACRyADHLAVMQGGRLVTCGAPgdvltAELV 232
Cdd:NF033858 431 VARDMFWRLLIELSREDGVTIFIsTHFMNEAER-CDRISLMHAGRVLASDTP-----AALV 485
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
29-224 3.00e-09

Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 57.43  E-value: 3.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    29 GQVTALIGPNGCGKSTLLKAFARILTP---QSGSLSLDGKGYSQLSARELA-CKvaflPQVLPIPEgVNVR---QLVAYG 101
Cdd:TIGR00956  789 GTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDSSFQRSIGyVQ----QQDLHLPT-STVReslRFSAYL 863
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   102 RSPHNslwgrLSGADQHS-VDQALQRMELATLAER----PLSDLSGGQRQRAWLAMIL-AQDAAIVLLDEPTTYLDISHQ 175
Cdd:TIGR00956  864 RQPKS-----VSKSEKMEyVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELvAKPKLLLFLDEPTSGLDSQTA 938
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 492172462   176 VELLDLMRELSAEGKTVITVLH----DINQAcryADHLAVMQ-GGRLVTCGAPG 224
Cdd:TIGR00956  939 WSICKLMRKLADHGQAILCTIHqpsaILFEE---FDRLLLLQkGGQTVYFGDLG 989
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
17-197 3.23e-09

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 56.55  E-value: 3.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFsPPAGQVTALIGPNGCGKSTLLKAFARILTPQSG-SLSL-DGKGYSQLSARELACKVAF-------LPQVLP 87
Cdd:COG3593   12 RSIKDLSI-ELSDDLTVLVGENNSGKSSILEALRLLLGPSSSrKFDEeDFYLGDDPDLPEIEIELTFgsllsrlLRLLLK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  88 IPEGVNVRQLVAYGRSPHNSLWGRLS---------GADQHSVDQALQRMELATLA-----------ERPLSDLSGGQRQR 147
Cdd:COG3593   91 EEDKEELEEALEELNEELKEALKALNellseylkeLLDGLDLELELSLDELEDLLkslslriedgkELPLDRLGSGFQRL 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 148 AWLAMILA-------QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:COG3593  171 ILLALLSAlaelkraPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTH 227
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
134-227 3.63e-09

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of proteins of which all members for which functions are known except the UvrA proteins are involved in the transport of material through membranes. UvrA orthologs are involved in the recognition of DNA damage as a step in nucleotide excision repair. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 56.95  E-value: 3.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  134 ERPLSDLSGGQRQRAWLAMILAQDAAIVL--LDEPTTYLdisHQVE---LLDLMRELSAEGKTVITVLHDiNQACRYADH 208
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGL---HQRDnrrLINTLKRLRDLGNTLIVVEHD-EDTIRAADY 558
                          90       100
                  ....*....|....*....|....*
gi 492172462  209 L------AVMQGGRLVTCGAPGDVL 227
Cdd:TIGR00630 559 VidigpgAGEHGGEVVASGTPEEIL 583
PLN03130 PLN03130
ABC transporter C family member; Provisional
22-230 4.86e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 56.67  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGVnvrqlVAYG 101
Cdd:PLN03130 1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIPQAPVLFSGT-----VRFN 1332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  102 RSP---HN--SLWGRLSGAdqHSVDqALQRMELATLAE--RPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISH 174
Cdd:PLN03130 1333 LDPfneHNdaDLWESLERA--HLKD-VIRRNSLGLDAEvsEAGENFSVGQRQLLSLARALLRRSKILVLDEATAAVDVRT 1409
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  175 QVELLDLMRElsaEGK--TVITVLHDINQA--CryaDHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PLN03130 1410 DALIQKTIRE---EFKscTMLIIAHRLNTIidC---DRILVLDAGRVVEFDTPENLLSNE 1463
PLN03073 PLN03073
ABC transporter F family; Provisional
12-217 4.89e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.41  E-value: 4.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GY-GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKG----YSQLSARELACKVAFLPQVL 86
Cdd:PLN03073 517 GYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVrmavFSQHHVDGLDLSSNPLLYMM 596
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  87 PIPEGVNVRQLVAygrspHNSLWGrLSGadqhsvdqalqrmelaTLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PLN03073 597 RCFPGVPEQKLRA-----HLGSFG-VTG----------------NLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEP 654
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492172462 167 TTYLDIShQVELldLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRL 217
Cdd:PLN03073 655 SNHLDLD-AVEA--LIQGLVLFQGGVLMVSHDEHLISGSVDELWVVSEGKV 702
PLN03232 PLN03232
ABC transporter C family member; Provisional
8-230 6.63e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 56.14  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462    8 HLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLP 87
Cdd:PLN03232 1241 HLRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIPQSPV 1320
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   88 IPEGVNVRQLVAYgrSPHN--SLWGRLSGAdqhSVDQALQRMELATLAE--RPLSDLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PLN03232 1321 LFSGTVRFNIDPF--SEHNdaDLWEALERA---HIKDVIDRNPFGLDAEvsEGGENFSVGQRQLLSLARALLRRSKILVL 1395
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462  164 DEPTTYLDISHQVELLDLMRElSAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:PLN03232 1396 DEATASVDVRTDSLIQRTIRE-EFKSCTMLVIAHRLNTIID-CDKILVLSSGQVLEYDSPQELLSRD 1460
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
21-185 7.53e-09

Predicted ATP-binding protein involved in virulence [General function prediction only];


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 55.00  E-value: 7.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK------------------GYS---QLSARELACKV 79
Cdd:COG3950   18 EIDFDNPPR-LTVLVGENGSGKTTLLEAIALALSGLLSRLDDVKFrkllirngefgdsaklilYYGtsrLLLDGPLKKLE 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  80 AFLPQVLP--------IPEGVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQ--------------RMELATL----- 132
Cdd:COG3950   97 RLKEEYFSrldgydslLDEDSNLREFLEWLREYLEDLENKLSDELDEKLEAVREalnkllpdfkdiriDRDPGRLvildk 176
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 133 --AERPLSDLSGGQRQR-AWLAMILAQDA-------------AIVLLDEPTTYLDISHQVELLDLMREL 185
Cdd:COG3950  177 ngEELPLNQLSDGERSLlALVGDLARRLAelnpalenplegeGIVLIDEIDLHLHPKWQRRILPDLRKI 245
PTZ00243 PTZ00243
ABC transporter; Provisional
22-223 1.06e-08

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 55.56  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   22 LSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVLPIPEGvNVRQLVayg 101
Cdd:PTZ00243 1329 VSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSMIPQDPVLFDG-TVRQNV--- 1404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  102 rSPhnslwgrLSGADQHSVDQALqrmELATLAERPLSDLSG--------------GQRQRAWLA-MILAQDAAIVLLDEP 166
Cdd:PTZ00243 1405 -DP-------FLEASSAEVWAAL---ELVGLRERVASESEGidsrvleggsnysvGQRQLMCMArALLKKGSGFILMDEA 1473
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462  167 TTYLD--ISHQVElLDLMRELSAEgkTVITVLHDINQACRYaDHLAVMQGGRLVTCGAP 223
Cdd:PTZ00243 1474 TANIDpaLDRQIQ-ATVMSAFSAY--TVITIAHRLHTVAQY-DKIIVMDHGAVAEMGSP 1528
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
34-217 1.07e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 55.28  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  34 LIGPNGCGKSTLLKAFARILTPQSGSLSLDgkgysqlsareLACKVAFLPQVLPIPEGVNVRQLVAYGrspHNSLWGRLS 113
Cdd:PRK15064  32 LIGANGCGKSTFMKILGGDLEPSAGNVSLD-----------PNERLGKLRQDQFAFEEFTVLDTVIMG---HTELWEVKQ 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 114 GAD------QHSVDQALQRMEL-ATLAE--------R-----------------PLSDLSGGQRQRAWLAMILAQDAAIV 161
Cdd:PRK15064  98 ERDriyalpEMSEEDGMKVADLeVKFAEmdgytaeaRagelllgvgipeeqhygLMSEVAPGWKLRVLLAQALFSNPDIL 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 492172462 162 LLDEPTTYLDIsHQVELLDlmRELSAEGKTVITVLHD---INQACryaDHLAVMQGGRL 217
Cdd:PRK15064 178 LLDEPTNNLDI-NTIRWLE--DVLNERNSTMIIISHDrhfLNSVC---THMADLDYGEL 230
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
29-230 1.43e-08

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: 54.14  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVR-QLVAYGRSPHNS 107
Cdd:cd03288   47 GQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSIILQD-PILFSGSIRfNLDPECKCTDDR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 108 LWGRLSGADQHSVDQALQRMELATLAERPlSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA 187
Cdd:cd03288  126 LWEALEIAQLKNMVKSLPGGLDAVVTEGG-ENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENILQKVVMTAFA 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 492172462 188 EgKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGDVLTAE 230
Cdd:cd03288  205 D-RTVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQE 245
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
19-223 1.53e-08

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: 54.16  E-value: 1.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLL-----KAFARIL--------------------------------TPQSGSLS 61
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIndtlyPALARRLhlkkeqpgnhdrieglehidkvividqspigrTPRSNPAT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  62 ldgkgYSQL--SARELACKVA----FLPQVLPipegvnvrqlVAY-GRSPHNSLwgrlsgadQHSVDQALQRME------ 128
Cdd:cd03271   91 -----YTGVfdEIRELFCEVCkgkrYNRETLE----------VRYkGKSIADVL--------DMTVEEALEFFEnipkia 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 129 --LATLAE---------RPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKT 191
Cdd:cd03271  148 rkLQTLCDvglgyiklgQPATTLSGGEAQRIKLAKELSKRStgkTLYILDEPTTGLhfhDVKK---LLEVLQRLVDKGNT 224
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 492172462 192 VITVLHDINQAcRYADHLAVM------QGGRLVTCGAP 223
Cdd:cd03271  225 VVVIEHNLDVI-KCADWIIDLgpeggdGGGQVVASGTP 261
GguA NF040905
sugar ABC transporter ATP-binding protein;
20-218 1.64e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 54.80  E-value: 1.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  20 QDLSFSPPAGQVTALIGPNGCGKSTLLKafarILT---PQ---SGSLSLDG-----KGYSQLSAR-------ELAckvaF 81
Cdd:NF040905  18 DDVNLSVREGEIHALCGENGAGKSTLMK----VLSgvyPHgsyEGEILFDGevcrfKDIRDSEALgiviihqELA----L 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  82 LPQvLPIPEGV---NVRqlvaygrsphnSLWGRLSGADQHSvdQALQRMELATLAERP---LSDLSGGQRQRAWLAMILA 155
Cdd:NF040905  90 IPY-LSIAENIflgNER-----------AKRGVIDWNETNR--RARELLAKVGLDESPdtlVTDIGVGKQQLVEIAKALS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 492172462 156 QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLV 218
Cdd:NF040905 156 KDVKLLILDEPTAALNEEDSAALLDLLLELKAQGITSIIISHKLNEIRRVADSITVLRDGRTI 218
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
16-234 2.95e-08

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 53.87  E-value: 2.95e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  16 TRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELackvaflpqvlpipegvnvR 95
Cdd:PRK10938  16 TKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGERQSQFSHITRLSFEQL-------------------Q 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVA--YGR------SPHNSLWGRlSGAD--QHSVDQALQRMELAT------LAERPLSDLSGGQRQRAWLAMILAQDAA 159
Cdd:PRK10938  77 KLVSdeWQRnntdmlSPGEDDTGR-TTAEiiQDEVKDPARCEQLAQqfgitaLLDRRFKYLSTGETRKTLLCQALMSEPD 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462 160 IVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVTCGAPGDVLTAELVCQ 234
Cdd:PRK10938 156 LLILDEPFDGLDVASRQQLAELLASLHQSGITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQALVAQ 230
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
18-221 3.19e-08

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 53.95  E-value: 3.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQL 97
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQT-PFLFSDTVANN 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  98 VAYGRsphnslwgrlSGADQHSVDQALQrmeLATLAERPLS--------------DLSGGQRQRAWLAMILAQDAAIVLL 163
Cdd:PRK10789 409 IALGR----------PDATQQEIEHVAR---LASVHDDILRlpqgydtevgergvMLSGGQKQRISIARALLLNAEILIL 475
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462 164 DEPTTYLDISHQVELLDLMRELSaEGKTVITVLHDINqACRYADHLAVMQGGRLVTCG 221
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWG-EGRTVIISAHRLS-ALTEASEILVMQHGHIAQRG 531
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
21-201 4.08e-08

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 53.74  E-value: 4.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGkgysqlSARELACKVAFLPQVLPIpEGVNVRQLvay 100
Cdd:PRK13545  42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG------SAALIAISSGLNGQLTGI-ENIELKGL--- 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 101 grsphnsLWGRLSGADQHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLD 180
Cdd:PRK13545 112 -------MMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLD 184
                        170       180
                 ....*....|....*....|.
gi 492172462 181 LMRELSAEGKTVITVLHDINQ 201
Cdd:PRK13545 185 KMNEFKEQGKTIFFISHSLSQ 205
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
19-230 5.04e-08

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 53.19  E-value: 5.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARElACKVAFlpqVLPIPE-------- 90
Cdd:PRK10982 264 IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANE-AINHGF---ALVTEErrstgiya 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 --GVNVRQLVAYGRSPHNSlWGRLSGADQHSVDQ-ALQRMELATLAER-PLSDLSGGQRQRAWLAMILAQDAAIVLLDEP 166
Cdd:PRK10982 340 ylDIGFNSLISNIRNYKNK-VGLLDNSRMKSDTQwVIDSMRVKTPGHRtQIGSLSGGNQQKVIIGRWLLTQPEILMLDEP 418
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 492172462 167 TTYLDISHQVELLDLMRELSAEGKTVITVLHDINQACRYADHLAVMQGGRLVtcgapGDVLTAE 230
Cdd:PRK10982 419 TRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMPELLGITDRILVMSNGLVA-----GIVDTKT 477
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
29-198 5.41e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 53.25  E-value: 5.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKgysqlsarelaCKVAFLPQVLPIPEgVNVRQLVAYGRSPHNSL 108
Cdd:PRK10636  27 GQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGN-----------WQLAWVNQETPALP-QPALEYVIDGDREYRQL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 109 WGRLSGADQHSVDQALQ--------------RMELATLA----------ERPLSDLSGGQRQRAWLAMILAQDAAIVLLD 164
Cdd:PRK10636  95 EAQLHDANERNDGHAIAtihgkldaidawtiRSRAASLLhglgfsneqlERPVSDFSGGWRMRLNLAQALICRSDLLLLD 174
                        170       180       190
                 ....*....|....*....|....*....|....
gi 492172462 165 EPTTYLDIShqvELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK10636 175 EPTNHLDLD---AVIWLEKWLKSYQGTLILISHD 205
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
18-218 1.36e-07

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: 50.72  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQ---SGSLSLDGKGYSQLSARelaCK--VAFLPQV-LPIPEg 91
Cdd:cd03233   22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFAEK---YPgeIIYVSEEdVHFPT- 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 VNVRQLVAYGRsphnslwgRLSGADQhsvdqalqrmelatlaerpLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:cd03233   98 LTVRETLDFAL--------RCKGNEF-------------------VRGISGGERKRVSIAEALVSRASVLCWDNSTRGLD 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 492172462 172 ISHQVELLDLMRELSAEGKTVITVlhDINQACR--YA--DHLAVMQGGRLV 218
Cdd:cd03233  151 SSTALEILKCIRTMADVLKTTTFV--SLYQASDeiYDlfDKVLVLYEGRQI 199
ycf16 CHL00131
sulfate ABC transporter protein; Validated
2-221 1.37e-07

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 51.18  E-value: 1.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   2 SILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA-----RILtpqSGSLSLDGKGYSQLSARELA 76
Cdd:CHL00131   6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAghpayKIL---EGDILFKGESILDLEPEERA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  77 CKVAFLPQVLP--IPeGVNVRQL--VAYgRSPHNSLwgRLSGADQHSVDQAL-QRMELATLAERPLS-----DLSGGQRQ 146
Cdd:CHL00131  83 HLGIFLAFQYPieIP-GVSNADFlrLAY-NSKRKFQ--GLPELDPLEFLEIInEKLKLVGMDPSFLSrnvneGFSGGEKK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 147 R-AWLAMILAqDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHdinqacrYA--------DHLAVMQGGRL 217
Cdd:CHL00131 159 RnEILQMALL-DSELAILDETDSGLDIDALKIIAEGINKLMTSENSIILITH-------YQrlldyikpDYVHVMQNGKI 230

                 ....
gi 492172462 218 VTCG 221
Cdd:CHL00131 231 IKTG 234
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
134-221 1.75e-07

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 50.72  E-value: 1.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 134 ERPLSDLSGGQRQRAWLAMILAQDAAIVL--LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRYADHL-- 209
Cdd:cd03270  132 SRSAPTLSGGEAQRIRLATQIGSGLTGVLyvLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHD-EDTIRAADHVid 210
                         90
                 ....*....|....*.
gi 492172462 210 ----AVMQGGRLVTCG 221
Cdd:cd03270  211 igpgAGVHGGEIVAQG 226
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
18-212 2.15e-07

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 51.57  E-value: 2.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSL-DGKGYSQLSARELACKVAFLPQVlPIPEGVNVRQ 96
Cdd:PTZ00265  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQD-PLLFSNSIKN 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   97 LVAY------------------------GRSPHNSLWGRLSGaDQHSVDQALQRMEL----------------------- 129
Cdd:PTZ00265  479 NIKYslyslkdlealsnyynedgndsqeNKNKRNSCRAKCAG-DLNDMSNTTDSNELiemrknyqtikdsevvdvskkvl 557
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  130 ------------ATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSA-EGKTVITVL 196
Cdd:PTZ00265  558 ihdfvsalpdkyETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGnENRITIIIA 637
                         250
                  ....*....|....*.
gi 492172462  197 HDINqACRYADHLAVM 212
Cdd:PTZ00265  638 HRLS-TIRYANTIFVL 652
PTZ00243 PTZ00243
ABC transporter; Provisional
18-225 3.28e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 51.32  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   18 IVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLsldgkgysqLSARElackVAFLPQVLPIpegvnvrqL 97
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRV---------WAERS----IAYVPQQAWI--------M 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   98 VAYGRSphNSLW------GRLSGA---DQHSVDQALQRMELAT-LAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPT 167
Cdd:PTZ00243  734 NATVRG--NILFfdeedaARLADAvrvSQLEADLAQLGGGLETeIGEKGV-NLSGGQKARVSLARAVYANRDVYLLDDPL 810
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462  168 TYLDiSHQVELldLMREL---SAEGKTVITVLHDINQACRyADHLAVMQGGRLVTCGAPGD 225
Cdd:PTZ00243  811 SALD-AHVGER--VVEECflgALAGKTRVLATHQVHVVPR-ADYVVALGDGRVEFSGSSAD 867
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
119-226 4.01e-07

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 50.80  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 119 SVDQALQRME--------LATLAE---------RPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHq 175
Cdd:COG0178  789 TVEEALEFFEnipkiarkLQTLQDvglgyiklgQPATTLSGGEAQRVKLASELSKRStgkTLYILDEPTTGLhfhDIRK- 867
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 176 veLLDLMRELSAEGKTVITVLHD---InqacRYADHLAVM------QGGRLVTCGAPGDV 226
Cdd:COG0178  868 --LLEVLHRLVDKGNTVVVIEHNldvI----KTADWIIDLgpeggdGGGEIVAEGTPEEV 921
COG3910 COG3910
Predicted ATPase [General function prediction only];
19-197 5.43e-07

Predicted ATPase [General function prediction only];


Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 49.38  E-value: 5.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  19 VQDLSFSPPagqVTALIGPNGCGKSTLLKAFARiltpqsgSLSLDGKGYSQL-------SARELAckvaflpQVLpipeg 91
Cdd:COG3910   30 LEGLEFHPP---VTFFVGENGSGKSTLLEAIAV-------AAGFNPEGGSKNfrfstreSESALG-------EYL----- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  92 vnvrQLVaygRSPHNSLWGR-LSGADQHSVDQALQRMELATLA------ERPLSDLSGGQrqrAWLAMILA--QDAAIVL 162
Cdd:COG3910   88 ----RLS---RGLPKPRDGFfLRAESFFNVATYLDELAAEGPGildsygGRSLHEQSHGE---SFLALFENrfRGNGLYL 157
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 492172462 163 LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH 197
Cdd:COG3910  158 LDEPEAALSPSRQLALLALIHDLVREGSQFIIATH 192
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
120-226 6.09e-07

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: 50.40  E-value: 6.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  120 VDQALQRMELAtlaeRPLSDLSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVI 193
Cdd:TIGR00630 814 CDVGLGYIRLG----QPATTLSGGEAQRIKLAKELSKRStgrTLYILDEPTTGLhfdDIKK---LLEVLQRLVDKGNTVV 886
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 492172462  194 TVLHDINqACRYADHLAVM------QGGRLVTCGAPGDV 226
Cdd:TIGR00630 887 VIEHNLD-VIKTADYIIDLgpeggdGGGTVVASGTPEEV 924
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
11-171 8.25e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 49.63  E-value: 8.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  11 IGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKafarILT---PQ--SGSLSLDGK---------------GY--S 68
Cdd:PRK10938 268 VSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLS----LITgdhPQgySNDLTLFGRrrgsgetiwdikkhiGYvsS 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  69 QLsarELACKVAflpqvlpipegVNVRQLVAYGRSPHNSLWGRLSGADQHSVDQALQRMEL-ATLAERPLSDLSGGQRQR 147
Cdd:PRK10938 344 SL---HLDYRVS-----------TSVRNVILSGFFDSIGIYQAVSDRQQKLAQQWLDILGIdKRTADAPFHSLSWGQQRL 409
                        170       180
                 ....*....|....*....|....
gi 492172462 148 AWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK10938 410 ALIVRALVKHPTLLILDEPLQGLD 433
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
3-221 1.07e-06

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 48.63  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   3 ILKAQHLDIGYGATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFA--RILTPQSGSLSLDGKGYSQLSARELACKVA 80
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAgrEDYEVTGGTVEFKGKDLLELSPEDRAGEGI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  81 FLPQVLP--IPegvnvrqlvayGRSPHNSLWGRLSGADQHSVDQALQRMELATLAERPLSDL---------------SGG 143
Cdd:PRK09580  81 FMAFQYPveIP-----------GVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 144 QRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHdINQACRY--ADHLAVMQGGRLVTCG 221
Cdd:PRK09580 150 EKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSLRDGKRSFIIVTH-YQRILDYikPDYVHVLYQGRIVKSG 228
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
1-229 2.28e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 47.87  E-value: 2.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   1 MSILKAQHLDIGY----GATRIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARIlTPQSGSLSLDGKGYS-----QLS 71
Cdd:PRK15093   1 MPLLDIRNLTIEFktsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGV-TKDNWRVTADRMRFDdidllRLS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  72 ARE----LACKVAFL---PQVLPIPEGVNVRQLV-AYGRSPHNSLWGRLSGADQHSVDQALQRMEL----ATLAERPLsD 139
Cdd:PRK15093  80 PRErrklVGHNVSMIfqePQSCLDPSERVGRQLMqNIPGWTYKGRWWQRFGWRKRRAIELLHRVGIkdhkDAMRSFPY-E 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVL-HDINQACRYADHLAVMQGGRLV 218
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLIsHDLQMLSQWADKINVLYCGQTV 238
                        250
                 ....*....|.
gi 492172462 219 TCGAPGDVLTA 229
Cdd:PRK15093 239 ETAPSKELVTT 249
PLN03140 PLN03140
ABC transporter G family member; Provisional
23-224 3.51e-06

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 47.92  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   23 SFSPpaGQVTALIGPNGCGKSTLL-------------------------KAFARIltpqSGSLSLDGKGYSQLSARELAC 77
Cdd:PLN03140  902 AFRP--GVLTALMGVSGAGKTTLMdvlagrktggyiegdirisgfpkkqETFARI----SGYCEQNDIHSPQVTVRESLI 975
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   78 KVAFLPqvlpIPEGVNVRQLVAYgrsphnslwgrlsgadqhsVDQALQRMELATLAER-----PLSDLSGGQRQRAWLAM 152
Cdd:PLN03140  976 YSAFLR----LPKEVSKEEKMMF-------------------VDEVMELVELDNLKDAivglpGVTGLSTEQRKRLTIAV 1032
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462  153 ILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLH----DINQAcryADHLAVMQ-GGRLVTCGAPG 224
Cdd:PLN03140 1033 ELVANPSIIFMDEPTSGLDARAAAIVMRTVRNTVDTGRTVVCTIHqpsiDIFEA---FDELLLMKrGGQVIYSGPLG 1106
PLN03130 PLN03130
ABC transporter C family member; Provisional
21-201 4.34e-06

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 47.81  E-value: 4.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   21 DLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQS-GSLSLDGKgysqlsarelackVAFLPQVLPIPEGvNVRQLVA 99
Cdd:PLN03130  635 NINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSdASVVIRGT-------------VAYVPQVSWIFNA-TVRDNIL 700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  100 YGrSPHNSlwGRLSGA-DQHSVDQALQRM---ELATLAERPLsDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD--IS 173
Cdd:PLN03130  701 FG-SPFDP--ERYERAiDVTALQHDLDLLpggDLTEIGERGV-NISGGQKQRVSMARAVYSNSDVYIFDDPLSALDahVG 776
                         170       180       190
                  ....*....|....*....|....*....|.
gi 492172462  174 HQVELLDLMRELSaeGKTVITV---LHDINQ 201
Cdd:PLN03130  777 RQVFDKCIKDELR--GKTRVLVtnqLHFLSQ 805
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
134-227 5.15e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 47.52  E-value: 5.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  134 ERPLSDLSGGQRQRAWLAMILAQDAAIV--LLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDiNQACRYADHL-- 209
Cdd:PRK00635  471 ERALATLSGGEQERTALAKHLGAELIGItyILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHD-EQMISLADRIid 549
                          90       100
                  ....*....|....*....|..
gi 492172462  210 ----AVMQGGRLVTCGAPGDVL 227
Cdd:PRK00635  550 igpgAGIFGGEVLFNGSPREFL 571
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
133-198 5.54e-06

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 5.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 492172462 133 AERPLSDLSGGQRQ------RAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:PRK03918 782 KERPLTFLSGGERIalglafRLALSLYLAGNIPLLILDEPTPFLDEERRRKLVDIMERYLRKIPQVIIVSHD 853
AAA_23 pfam13476
AAA domain;
20-68 7.12e-06

AAA domain;


Pssm-ID: 463890 [Multi-domain]  Cd Length: 190  Bit Score: 45.56  E-value: 7.12e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 492172462   20 QDLSFSPPagqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYS 68
Cdd:pfam13476  12 QTIDFSKG---LTLITGPNGSGKTTILDAIKLALYGKTSRLKRKSGGGF 57
uvrA PRK00349
excinuclease ABC subunit UvrA;
131-230 7.69e-06

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 46.99  E-value: 7.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 131 TLAeRPLSDLSGGQRQRAWLAmilAQdaaI------VL--LDEPTTYLdisHQ------VELLDLMRELsaeGKTVITVL 196
Cdd:PRK00349 482 TLS-RSAGTLSGGEAQRIRLA---TQ---IgsgltgVLyvLDEPSIGL---HQrdndrlIETLKHLRDL---GNTLIVVE 548
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 492172462 197 HDiNQACRYADHL------AVMQGGRLVTCGAPGDVLTAE 230
Cdd:PRK00349 549 HD-EDTIRAADYIvdigpgAGVHGGEVVASGTPEEIMKNP 587
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
81-217 8.38e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 46.75  E-value: 8.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462   81 FLPQVLPIP-EGVNVRQLVAYGRSPHNSLWgrLSGADQHSVDQALQRMELATLA-ERPLSDLSGGQRQRAWLAMIL---A 155
Cdd:PRK00635  751 FLPQVLEVRyKGKNIADILEMTAYEAEKFF--LDEPSIHEKIHALCSLGLDYLPlGRPLSSLSGGEIQRLKLAYELlapS 828
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462  156 QDAAIVLLDEPTTYLDiSHQVE-LLDLMRELSAEGKTVITVLHDINqACRYADHLAVM--QGGRL 217
Cdd:PRK00635  829 KKPTLYVLDEPTTGLH-THDIKaLIYVLQSLTHQGHTVVIIEHNMH-VVKVADYVLELgpEGGNL 891
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
137-230 9.76e-06

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 46.75  E-value: 9.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  137 LSDLSGGQRQRAWLAMIL---AQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHDInQACRYADHLAVM- 212
Cdd:PRK00635 1697 LSSLSLSEKIAIKIAKFLylpPKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDP-ALLKQADYLIEMg 1775
                          90       100
                  ....*....|....*....|...
gi 492172462  213 -----QGGRLVTCGAPGDVLTAE 230
Cdd:PRK00635 1776 pgsgkTGGKILFSGPPKDISASK 1798
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
131-230 2.47e-05

Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 45.40  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 131 TLAeRPLSDLSGGQRQRAWLAmilaqdAAI------VL--LDEPTTYLdisHQ---VELLDLMRELSAEGKTVITVLHDi 199
Cdd:COG0178  478 TLD-RSAGTLSGGEAQRIRLA------TQIgsglvgVLyvLDEPSIGL---HQrdnDRLIETLKRLRDLGNTVIVVEHD- 546
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 492172462 200 NQACRYADHL------AVMQGGRLVTCGAPGDVLTAE 230
Cdd:COG0178  547 EDTIRAADYIidigpgAGEHGGEVVAQGTPEEILKNP 583
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
119-171 3.36e-05

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: 44.79  E-value: 3.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 492172462  119 SVDQALQRMELATLAERPL---SDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:TIGR03269 145 AVGRAVDLIEMVQLSHRIThiaRDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLD 200
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
12-198 3.60e-05

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 43.80  E-value: 3.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  12 GYGATRIVQDLSFSPPAGQVTALI-GPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFLPQvlpipe 90
Cdd:cd03279   10 NFGPFREEQVIDFTGLDNNGLFLIcGPTGAGKSTILDAITYALYGKTPRYGRQENLRSVFAPGEDTAEVSFTFQ------ 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  91 gvnvrqlvaygRSPHNSLWGRLSGADQHSVDQA--LQRMELATLAERPLSDLSGGQRQRAWLAM------ILAQDAAIVL 162
Cdd:cd03279   84 -----------LGGKKYRVERSRGLDYDQFTRIvlLPQGEFDRFLARPVSTLSGGETFLASLSLalalseVLQNRGGARL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 492172462 163 ----LDEPTTYLDISHQVELLDLMRELSAEGKTVITVLHD 198
Cdd:cd03279  153 ealfIDEGFGTLDPEALEAVATALELIRTENRMVGVISHV 192
AAA_29 pfam13555
P-loop containing region of AAA domain;
20-57 4.24e-05

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 40.28  E-value: 4.24e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 492172462   20 QDLSFSPpaGQVTALIGPNGCGKSTLLKAFARILTPQS 57
Cdd:pfam13555  15 HTIPIDP--RGNTLLTGPSGSGKSTLLDAIQTLLVPAK 50
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
134-193 7.79e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 43.15  E-value: 7.79e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492172462  134 ERPLSDLSGGQRQraWLAMILA-----QDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:pfam13304 231 ELPAFELSDGTKR--LLALLAAllsalPKGGLLLIDEPESGLHPKLLRRLLELLKELSRNGAQLI 293
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
31-65 9.52e-05

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 42.76  E-value: 9.52e-05
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 492172462   31 VTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGK 65
Cdd:pfam13304   1 INVLIGPNGSGKSNLLEALRFLADFDALVIGLTDE 35
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
20-199 1.22e-04

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 41.92  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  20 QDLSFSPPagqVTALIGPNGCGKSTLLKAFARILTPQSGSLSLDGKGYSQLSARELACKVAFL----PQVLPIPEGvNVR 95
Cdd:COG0419   17 ETIDFDDG---LNLIVGPNGAGKSTILEAIRYALYGKARSRSKLRSDLINVGSEEASVELEFEhggkRYRIERRQG-EFA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  96 QLVAYGRSPHNSLWGRLSGAD------------QHSVDQALQRMELATLAER----------PLSDLSGGQRQRAWLAMI 153
Cdd:COG0419   93 EFLEAKPSERKEALKRLLGLEiyeelkerlkelEEALESALEELAELQKLKQeilaqlsgldPIETLSGGERLRLALADL 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 492172462 154 LAqdaaiVLLDepTTYLDISHQVELLDLMRELSaegktVITvlHDI 199
Cdd:COG0419  173 LS-----LILD--FGSLDEERLERLLDALEELA-----IIT--HVI 204
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
140-199 1.88e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 42.71  E-value: 1.88e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492172462  140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEG-KTVITVLHDI 199
Cdd:PTZ00265 1359 LSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKAdKTIITIAHRI 1419
COG4637 COG4637
Predicted ATPase [General function prediction only];
29-50 2.05e-04

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 42.23  E-value: 2.05e-04
                         10        20
                 ....*....|....*....|..
gi 492172462  29 GQVTALIGPNGCGKSTLLKAFA 50
Cdd:COG4637   21 GPLTVLIGANGSGKSNLLDALR 42
uvrA PRK00349
excinuclease ABC subunit UvrA;
140-226 2.25e-04

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 42.37  E-value: 2.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 LSGGQRQRAWLAMILAQDA---AIVLLDEPTTYL---DISHqveLLDLMRELSAEGKTVITVLH--DInqaCRYADHLAV 211
Cdd:PRK00349 831 LSGGEAQRVKLAKELSKRStgkTLYILDEPTTGLhfeDIRK---LLEVLHRLVDKGNTVVVIEHnlDV---IKTADWIID 904
                         90       100
                 ....*....|....*....|.
gi 492172462 212 M------QGGRLVTCGAPGDV 226
Cdd:PRK00349 905 LgpeggdGGGEIVATGTPEEV 925
GguA NF040905
sugar ABC transporter ATP-binding protein;
140-193 4.78e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 4.78e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 492172462 140 LSGGQRQRAWLAMILAQDAAIVLLDEPTTYLDISHQVELLDLMRELSAEGKTVI 193
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVI 458
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
140-209 5.37e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 41.18  E-value: 5.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462 140 LSGGQRQ------RAWLAMILAQ----DAAI--VLLDEPTTYLD---ISHQVELLDLMRELSAEgkTVITVLHDiNQACR 204
Cdd:PRK02224 782 LSGGERAlfnlslRCAIYRLLAEgiegDAPLppLILDEPTVFLDsghVSQLVDLVESMRRLGVE--QIVVVSHD-DELVG 858

                 ....*
gi 492172462 205 YADHL 209
Cdd:PRK02224 859 AADDL 863
COG1106 COG1106
ATPase/GTPase, AAA15 family [General function prediction only];
20-50 6.32e-04

ATPase/GTPase, AAA15 family [General function prediction only];


Pssm-ID: 440723 [Multi-domain]  Cd Length: 330  Bit Score: 40.41  E-value: 6.32e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 492172462  20 QDLSFSPPA---GQVTALIGPNGCGKSTLLKAFA 50
Cdd:COG1106   17 LTLSMVASGlrlLRVNLIYGANASGKSNLLEALY 50
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
26-55 1.62e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 1.62e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 492172462   26 PPAGQVTALIGPNGCGKSTLLKAFARILTP 55
Cdd:COG4913    21 DFDGRGTLLTGDNGSGKSTLLDAIQTLLVP 50
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
17-171 1.69e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 38.70  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492172462  17 RIVQDLSFSPPAGQVTALIGPNGCGKSTLLKAFARILTPQSGSLSldgkgYSQLSARELA---CkvAFLPQVLPIPEGVN 93
Cdd:PRK13541  14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIY-----YKNCNINNIAkpyC--TYIGHNLGLKLEMT 86
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492172462  94 VRQLVAYGRSPHNSLwgrlsgadqHSVDQALQRMELATLAERPLSDLSGGQRQRAWLAMILAQDAAIVLLDEPTTYLD 171
Cdd:PRK13541  87 VFENLKFWSEIYNSA---------ETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLS 155
AAA_15 pfam13175
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
30-49 4.32e-03

AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the AAA superfamily.


Pssm-ID: 433011 [Multi-domain]  Cd Length: 392  Bit Score: 37.96  E-value: 4.32e-03
                          10        20
                  ....*....|....*....|
gi 492172462   30 QVTALIGPNGCGKSTLLKAF 49
Cdd:pfam13175  24 DLTVLIGKNNSGKSSILEAL 43
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
137-174 6.62e-03

ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of chromosomes (SMC) proteins are large (approximately 110 to 170 kDa), and each is arranged into five recognizable domains. Amino-acid sequence homology of SMC proteins between species is largely confined to the amino- and carboxy-terminal globular domains. The amino-terminal domain contains a 'Walker A' nucleotide-binding domain (GxxGxGKS/T, in the single-letter amino-acid code), which by mutational studies has been shown to be essential in several proteins. The carboxy-terminal domain contains a sequence (the DA-box) that resembles a 'Walker B' motif, and a motif with homology to the signature sequence of the ATP-binding cassette (ABC) family of ATPases. The sequence homology within the carboxy-terminal domain is relatively high within the SMC1-SMC4 group, whereas SMC5 and SMC6 show some divergence in both of these sequences. In eukaryotic cells, the proteins are found as heterodimers of SMC1 paired with SMC3, SMC2 with SMC4, and SMC5 with SMC6 (formerly known as Rad18).


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 36.89  E-value: 6.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 492172462 137 LSDLSGGQRQRAWLAMILA----QDAAIVLLDEPTTYLDISH 174
Cdd:cd03273  164 LTELSGGQRSLVALSLILAlllfKPAPMYILDEVDAALDLSH 205
PLN03073 PLN03073
ABC transporter F family; Provisional
141-197 6.90e-03

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 37.53  E-value: 6.90e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 492172462 141 SGGQRQRAWLAMILAQDAAIVLLDEPTTYLDIsHQVelLDLMRELSAEGKTVITVLH 197
Cdd:PLN03073 346 SGGWRMRIALARALFIEPDLLLLDEPTNHLDL-HAV--LWLETYLLKWPKTFIVVSH 399
 
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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