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Conserved domains on  [gi|23296450|gb|AAN13061|]
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unknown protein [Arabidopsis thaliana]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 10124897)

ABC transporter ATP-binding protein with similarity to nickel import ATP-binding protein NikO, which is part of the energy-coupling factor (ECF) transporter complex NikMNQO involved in nickel import

CATH:  3.40.50.300
PubMed:  25750732|24638992
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
41-244 2.69e-80

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


:

Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 240.83  E-value: 2.69e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPK 107
Cdd:cd03225   1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkelrRKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPDHQVVMPTVEADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:cd03225  78 GLVFQNPDDQFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 188 LLDELTTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEELK-YADGAVYMENGR 244
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK---TIIIVTHDLDLLLeLADRVIVLEDGK 211
 
Name Accession Description Interval E-value
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
41-244 2.69e-80

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 240.83  E-value: 2.69e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPK 107
Cdd:cd03225   1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkelrRKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPDHQVVMPTVEADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:cd03225  78 GLVFQNPDDQFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 188 LLDELTTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEELK-YADGAVYMENGR 244
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK---TIIIVTHDLDLLLeLADRVIVLEDGK 211
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
40-254 1.43e-75

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: 229.53  E-value: 1.43e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN------- 108
Cdd:COG1122   1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNlrelrrk 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:COG1122  77 vgLVFQNPDDQLFAPTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL---NKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
40-249 3.17e-65

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 204.59  E-value: 3.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    40 VECRNLCFSVstrQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN------ 108
Cdd:TIGR04520   1 IEVENVSFSY---PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtlDEENlweirk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   109 ---FVFQNPDHQVVMPTVEADVAFGL---GkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:TIGR04520  78 kvgMVFQNPDNQFVGATVEDDVAFGLenlG----VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450   183 ACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKL-NKEEG-ITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
36-249 1.01e-52

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 172.96  E-value: 1.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   36 DNVAVECRNLCFS-VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN- 108
Cdd:PRK13633   1 MNEMIKCKNVSYKyESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsDEENl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 --------FVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIA 177
Cdd:PRK13633  81 wdirnkagMVFQNPDNQIVATIVEEDVAFGpenLG----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  178 GALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKEL-NKKYG-ITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
60-194 4.39e-35

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: 123.14  E-value: 4.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PKN--FVFQNPdhqVVMP--TVE 124
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslRKEigYVFQDP---QLFPrlTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450   125 ADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQ----TLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:pfam00005  78 ENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
56-235 1.76e-34

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 123.11  E-value: 1.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQVVMP-TVEADVAFGL- 131
Cdd:NF040873   4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggARVAYVPQRSEVPDSLPlTVRDLVAMGRw 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  132 ---GKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESdqmgVIKAV 208
Cdd:NF040873  84 arrGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE----SRERI 158
                        170       180
                 ....*....|....*....|....*...
gi 23296450  209 KDLINAKKGD-VTALWVTHRLEELKYAD 235
Cdd:NF040873 159 IALLAEEHARgATVVVVTHDLELVRRAD 186
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
69-231 1.04e-12

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: 64.32  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     69 SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFvekpknfvfqnpdhqvvmptveadvafglgkYHDMNQEEVKSRVIK 148
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------YIDGEDILEEVLDQL 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    149 ALEAVGMRDYMqrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV---KDLINAKKGDVTALWVT 225
Cdd:smart00382  50 LLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrLLLLLKSEKNLTVILTT 123

                   ....*.
gi 23296450    226 HRLEEL 231
Cdd:smart00382 124 NDEKDL 129
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
49-194 9.99e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 61.68  E-value: 9.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   49 VSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknFVF----QNPDH-QVVMPtv 123
Cdd:NF033858   7 VSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-------EVLggdmADARHrRAVCP-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  124 eaDVAF---GLGK--YHDM---------------NQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:NF033858  77 --RIAYmpqGLGKnlYPTLsvfenldffgrlfgqDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
                        170
                 ....*....|.
gi 23296450  184 CKVLLLDELTT 194
Cdd:NF033858 155 PDLLILDEPTT 165
GguA NF040905
sugar ABC transporter ATP-binding protein;
57-259 4.85e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 59.42  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSsGT-----VFVEKPKNF--VFQNPDHQVVMPTVE----- 124
Cdd:NF040905  14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PH-GSyegeiLFDGEVCRFkdIRDSEALGIVIIHQElalip 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 ----ADVAFgLG----KYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:NF040905  92 ylsiAENIF-LGneraKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  197 DESDQmgviKAVKDLINA-KKGDVTALWVTHRLEELKY-ADGAVYMENGRVV----RHGDAATISDFIK 259
Cdd:NF040905 171 NEEDS----AALLDLLLElKAQGITSIIISHKLNEIRRvADSITVLRDGRTIetldCRADEVTEDRIIR 235
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
64-193 5.34e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 56.67  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknFVFQNPdhqvvmptVEAD-------V-----AFGL 131
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-------WLFGQP--------VDAGdiatrrrVgymsqAFSL 350
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  132 gkY-----------H----DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:NF033858 351 --YgeltvrqnlelHarlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
129-249 2.41e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.19  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  129 FGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:NF000106 108 YMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 23296450  209 KDLInakKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:NF000106 188 RSMV---RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADG 226
 
Name Accession Description Interval E-value
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
41-244 2.69e-80

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


Pssm-ID: 213192 [Multi-domain]  Cd Length: 211  Bit Score: 240.83  E-value: 2.69e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPK 107
Cdd:cd03225   1 ELKNLSFSYPDGA---RPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDgkdltklslkelrRKV 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPDHQVVMPTVEADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:cd03225  78 GLVFQNPDDQFFGPTVEEEVAFGLENLG-LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDIL 156
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 188 LLDELTTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEELK-YADGAVYMENGR 244
Cdd:cd03225 157 LLDEPTAGLDPAGRRELLELLKKLKAEGK---TIIIVTHDLDLLLeLADRVIVLEDGK 211
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
40-254 1.43e-75

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: 229.53  E-value: 1.43e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN------- 108
Cdd:COG1122   1 IELENLSFSYPG----GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDgkdiTKKNlrelrrk 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:COG1122  77 vgLVFQNPDDQLFAPTVEEDVAFGP-ENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEV 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1122 156 LVLDEPTAGLDPRGRRELLELLKRL---NKEGKTVIIVTHDLDLVaELADRVIVLDDGRIVADGTPREV 221
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
40-249 3.17e-65

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


Pssm-ID: 275313 [Multi-domain]  Cd Length: 268  Bit Score: 204.59  E-value: 3.17e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    40 VECRNLCFSVstrQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN------ 108
Cdd:TIGR04520   1 IEVENVSFSY---PESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDgldtlDEENlweirk 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   109 ---FVFQNPDHQVVMPTVEADVAFGL---GkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:TIGR04520  78 kvgMVFQNPDNQFVGATVEDDVAFGLenlG----VPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAM 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450   183 ACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKL-NKEEG-ITVISITHDMEEAVLADRVIVMNKGKIVAEG 218
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
39-254 4.85e-56

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: 180.62  E-value: 4.85e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN--- 108
Cdd:COG1120   1 MLEAENLSVGYGGR-----PVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDgrdlaslSRRElar 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQnpDHQVVMP-TVEADVAFGLGKYHDMNQ---EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:COG1120  76 riaYVPQ--EPPAPFGlTVRELVALGRYPHLGLFGrpsAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALA 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 182 EACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1120 154 QEPPLLLLDEPTSHLDLAHQLEVLELLRRL--ARERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQGPPEEV 225
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
35-254 1.37e-53

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: 181.25  E-value: 1.37e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPK 107
Cdd:COG1123 256 AAEPLLEVRNLSKRYPVRGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDgkdltklSRR 335
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 N---------FVFQNPDHQVV-MPTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAI 176
Cdd:COG1123 336 SlrelrrrvqMVFQDPYSSLNpRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAI 415
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:COG1123 416 ARALALEPKLLILDEPTSALDVSVQAQILNLLRDL--QRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
36-249 1.01e-52

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 172.96  E-value: 1.01e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   36 DNVAVECRNLCFS-VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN- 108
Cdd:PRK13633   1 MNEMIKCKNVSYKyESNEESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDgldtsDEENl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 --------FVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIA 177
Cdd:PRK13633  81 wdirnkagMVFQNPDNQIVATIVEEDVAFGpenLG----IPPEEIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  178 GALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13633 157 GILAMRPECIIFDEPTAMLDPSGRREVVNTIKEL-NKKYG-ITIILITHYMEEAVEADRIIVMDSGKVVMEG 226
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
36-254 1.34e-52

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 172.10  E-value: 1.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   36 DNVAVECRNLCFSVSTRqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKNF-- 109
Cdd:PRK13632   4 KSVMIKVENVSFSYPNS---ENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDgitiSKENLke 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  110 -------VFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:PRK13632  81 irkkigiIFQNPDNQFIGATVEDDIAFGL-ENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLAL 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13632 160 NPEIIIFDESTSMLDPKGKREIKKIMVDL--RKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKEI 229
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
35-254 7.59e-51

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 166.80  E-value: 7.59e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----EKPKN- 108
Cdd:COG1121   2 MMMPAIELENLTVSYGGR-----PVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLfgkppRRARRr 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDHQVVMP-TVEaDVAfGLGKYHDMN-----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGAL 180
Cdd:COG1121  77 igYVPQRAEVDWDFPiTVR-DVV-LMGRYGRRGlfrrpSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARAL 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 181 AEACKVLLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMeNGRVVRHGDAATI 254
Cdd:COG1121 155 AQDPDLLLLDEPFAGVDAATEEALYELLREL---RREGKTILVVTHDLGAVrEYFDRVLLL-NRGLVAHGPPEEV 225
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
56-249 6.37e-49

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: 160.76  E-value: 6.37e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPdhqVVMP--T 122
Cdd:cd03259  12 SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIdgrdvtgvppeRRNIGMVFQDY---ALFPhlT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:cd03259  89 VAENIAFGL-KLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDAKLRE 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLInaKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:cd03259 168 ELREELKELQ--RELGITTIYVTHDQEEaLALADRIAVMNEGRIVQVG 213
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
39-254 1.68e-48

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: 167.77  E-value: 1.68e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLcfSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTVFVE----------- 104
Cdd:COG1123   4 LLEVRDL--SVRYPGG-DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDgrdllelseal 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 --KPKNFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:COG1123  81 rgRRIGMVFQDPMTQLNPVTVGDQIAEAL-ENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALAL 159
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1123 160 DPDLLIADEPTTALDVTTQAEILDLLREL--QRERGTTVLLITHDLGVvAEIADRVVVMDDGRIVEDGPPEEI 230
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
58-254 2.41e-48

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 161.72  E-value: 2.41e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------------EKPKNFVFQNPDHQVVMPTVE 124
Cdd:PRK13635  21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVggmvlseetvwdvRRQVGMVFQNPDNQFVGATVQ 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 ADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:PRK13635 101 DDVAFGL-ENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREV 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23296450  205 IKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13635 180 LETVRQL--KEQKGITVLSITHDLDEAAQADRVIVMNKGEILEEGTPEEI 227
cbiO PRK13650
energy-coupling factor transporter ATPase;
40-245 4.55e-48

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 160.67  E-value: 4.55e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN------- 108
Cdd:PRK13650   5 IEVKNLTFKYKEDQ--EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDgdllTEENvwdirhk 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 --FVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK13650  83 igMVFQNPDNQFVGATVEDDVAFGL-ENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  187 LLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:PRK13650 162 IILDEATSMLDPEGRLELIKTIKGI--RDDYQMTVISITHDLDEVALSDRVLVMKNGQV 218
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
40-254 4.92e-48

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 159.46  E-value: 4.92e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------EKPKN-- 108
Cdd:COG1131   1 IEVRGLTKRYG-----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVlgedvardpAEVRRri 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -FVFQNPdhqVVMP--TVEADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACK 185
Cdd:COG1131  76 gYVPQEP---ALYPdlTVRENLRF-FARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPE 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 186 VLLLDELTTFLD-ESdqmgvIKAVKDLINA-KKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1131 152 LLILDEPTSGLDpEA-----RRELWELLRElAAEGKTVLLSTHYLEEAeRLCDRVAIIDKGRIVADGTPDEL 218
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
60-267 6.93e-47

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 157.61  E-value: 6.93e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK----PKNF---------VFQNPDHQVVMPTVEAD 126
Cdd:PRK13648  25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNqaitDDNFeklrkhigiVFQNPDNQFVGSIVKYD 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  127 VAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIK 206
Cdd:PRK13648 105 VAFGL-ENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLD 183
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450  207 AVKDLINAKkgDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATISDFIKAKQSSYID 267
Cdd:PRK13648 184 LVRKVKSEH--NITIISITHDLSEAMEADHVIVMNKGTVYKEGTPTEIFDHAEELTRIGLD 242
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
37-247 8.96e-47

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 155.97  E-value: 8.96e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  37 NVAVECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN- 108
Cdd:COG1136   2 SPLLELRNLTKSYGTGEG-EVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDgqdisslSEREl 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---------FVFQnpDHQVVmP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIA 177
Cdd:COG1136  81 arlrrrhigFVFQ--FFNLL-PelTALENVALPL-LLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIA 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 178 GALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVR 247
Cdd:COG1136 157 RALVNRPKLILADEPTGNLDSKTGEEVLELLREL--NRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
41-249 1.28e-46

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: 153.75  E-value: 1.28e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknfvfQNPDHqvvM 120
Cdd:cd03214   1 EVENLSVGYGGR-----TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDG------KDLAS---L 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTVEA--DVAFglgkyhdMNQeevksrvikALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDE 198
Cdd:cd03214  67 SPKELarKIAY-------VPQ---------ALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 23296450 199 SDQMGVIKAVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHG 249
Cdd:cd03214 131 AHQIELLELLRRL--ARERGKTVVMVLHDLNlAARYADRVILLKDGRIVAQG 180
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
41-249 1.92e-46

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: 154.61  E-value: 1.92e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKN------FVFQ 112
Cdd:cd03235   1 EVEDLTVSYGGH-----PVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVfgKPLEKerkrigYVPQ 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 NPDHQVVMP-TVEADVAFGLgkYHDMN-----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:cd03235  76 RRSIDRDFPiSVRDVVLMGL--YGHKGlfrrlSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDL 153
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLEE-LKYADGAVYMeNGRVVRHG 249
Cdd:cd03235 154 LLLDEPFAGVDPKTQEDIYELLREL--RREG-MTILVVTHDLGLvLEYFDRVLLL-NRTVVASG 213
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
35-246 1.65e-45

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 153.71  E-value: 1.65e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN----- 108
Cdd:COG1116   3 AAAPALELRGVSKRFPTGGG-GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDgKPVTgpgpd 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhqVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:COG1116  82 rgVVFQEP---ALLPwlTVLDNVALGL-ELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDP 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 185 KVLLLDEltTF--LDE--SDQMGvikavKDLIN-AKKGDVTALWVTHRLEElkyadgAVYMENgRVV 246
Cdd:COG1116 158 EVLLMDE--PFgaLDAltRERLQ-----DELLRlWQETGKTVLFVTHDVDE------AVFLAD-RVV 210
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
39-254 4.09e-45

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 155.26  E-value: 4.09e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------EKPK- 107
Cdd:COG3842   5 ALELENVSKRYG-----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLdgrdvtglppEKRNv 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQNPD---HqvvMpTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:COG3842  80 GMVFQDYAlfpH---L-TVAENVAFGL-RMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEP 154
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 185 KVLLLDELTTFLDES--DQMgvIKAVKDLInaKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG3842 155 RVLLLDEPLSALDAKlrEEM--REELRRLQ--RELGITFIYVTHDQEEaLALADRIAVMNDGRIEQVGTPEEI 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
40-245 7.18e-44

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: 148.02  E-value: 7.18e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---- 108
Cdd:cd03255   1 IELKNLSKTY-GGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDgtdisklSEKElaaf 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ------FVFQnpDHQVVmP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGAL 180
Cdd:cd03255  80 rrrhigFVFQ--SFNLL-PdlTALENVELPL-LLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARAL 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 181 AEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03255 156 ANDPKIILADEPTGNLDSETGKEVMELLREL--NKEAGTTIVVVTHDPELAEYADRIIELRDGKI 218
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
40-246 8.92e-43

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: 145.31  E-value: 8.92e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN-------FVF 111
Cdd:cd03293   1 LEVRNVSKTYGGGGG-AVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDgEPVTgpgpdrgYVF 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 112 QNPdhqVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03293  80 QQD---ALLPwlTVLDNVALGL-ELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLL 155
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 190 DEltTF--LDE--SDQMGvikavKDLINA-KKGDVTALWVTHRLEElkyadgAVYMENgRVV 246
Cdd:cd03293 156 DE--PFsaLDAltREQLQ-----EELLDIwRETGKTVLLVTHDIDE------AVFLAD-RVV 203
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
40-249 9.03e-43

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 147.15  E-value: 9.03e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVStrQGISVpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF---------------VE 104
Cdd:PRK13639   2 LETRDLKYSYP--DGTEA--LKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLikgepikydkkslleVR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  105 KPKNFVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:PRK13639  78 KTVGIVFQNPDDQLFAPTVEEDVAFGplnLG----LSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  182 EACKVLLLDELTTFLDEsdqMGVIKAVKDLINAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13639 154 MKPEIIVLDEPTSGLDP---MGASQIMKLLYDLNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEG 219
cbiO PRK13640
energy-coupling factor transporter ATPase;
35-254 1.20e-42

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 146.87  E-value: 1.20e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   35 SDNvAVECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSS---------GTVFVEK 105
Cdd:PRK13640   2 KDN-IVEFKHVSF---TYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnskitvdGITLTAK 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  106 PK-------NFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAG 178
Cdd:PRK13640  78 TVwdirekvGIVFQNPDNQFVGATVGDDVAFGL-ENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAG 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  179 ALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKL--KKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVEI 230
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
59-226 3.55e-42

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: 142.95  E-value: 3.55e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF--------------VFQNPDHQVVMPTV 123
Cdd:TIGR01166   7 VLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDgEPLDYsrkgllerrqrvglVFQDPDDQLFAADV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   124 EADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:TIGR01166  87 DQDVAFGplnLG----LSEAEVERRVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTAGLDPAG 162
                         170       180
                  ....*....|....*....|....*.
gi 23296450   201 QMGVIKAVKDLINAKKGDVTAlwvTH 226
Cdd:TIGR01166 163 REQMLAILRRLRAEGMTVVIS---TH 185
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
41-245 2.07e-41

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 141.49  E-value: 2.07e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN----------- 108
Cdd:COG4619   2 ELEGLSFRVGGK-----PILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDgKPLSampppewrrqv 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -FVFQNPdhqvVM--PTVEADVAFGLGKYHDMNQEEvksRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:COG4619  77 aYVPQEP----ALwgGTVRDNLPFPFQLRERKFDRE---RALELLERLGLPpDILDKPVERLSGGERQRLALIRALLLQP 149
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 185 KVLLLDELTTFLDESDQMGVIKAVKDLINAKkgDVTALWVTHRLEELK-YADGAVYMENGRV 245
Cdd:COG4619 150 DVLLLDEPTSALDPENTRRVEELLREYLAEE--GRAVLWVSHDPEQIErVADRVLTLEAGRL 209
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
39-254 8.95e-41

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: 141.09  E-value: 8.95e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLcfSVSTRQGI-SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNF- 109
Cdd:COG1124   1 MLEVRNL--SVSYGQGGrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDgrpvtrrRRKAFr 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -----VFQ------NPDHqvvmpTVEADVAFGLgkyHDMNQEEVKSRVIKALEAVGM-RDYMQR-PIQtLSGGQKQRIAI 176
Cdd:COG1124  79 rrvqmVFQdpyaslHPRH-----TVDRILAEPL---RIHGLPDREERIAELLEQVGLpPSFLDRyPHQ-LSGGQRQRVAI 149
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKgdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:COG1124 150 ARALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERG--LTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADL 226
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
48-246 9.30e-41

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: 139.70  E-value: 9.30e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  48 SVSTRQGISvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK----------NFVFQNPDHQ 117
Cdd:cd03226   6 SFSYKKGTE--ILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPikakerrksiGYVMQDVDYQ 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 VVMPTVEADVAFGLGKYHDMNQeevksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03226  84 LFTDSVREELLLGLKELDAGNE-----QAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLD 158
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 23296450 198 ESDQMGVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVV 246
Cdd:cd03226 159 YKNMERVGELIRELAAQGK---AVIVITHDYEFLaKVCDRVLLLANGAIV 205
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
40-254 3.46e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 140.32  E-value: 3.46e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVSTrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-------------VEKP 106
Cdd:PRK13652   4 IETRDLCYSYSG----SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLirgepitkenireVRKF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  107 KNFVFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK13652  80 VGLVFQNPDDQIFSPTVEQDIAFGpinLG----LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAME 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  184 CKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13652 156 PQVLVLDEPTAGLDPQGVKELIDFLNDL--PETYGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAYGTVEEI 225
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
56-256 5.76e-40

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: 138.84  E-value: 5.76e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------KPKNFVFQNPDhQVVMP---TV 123
Cdd:COG4555  13 KVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDgedvrkeprEARRQIGVLPD-ERGLYdrlTV 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:COG4555  92 RENIRY-FAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLDVMARRL 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23296450 204 VIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATISD 256
Cdd:COG4555 171 LREILRALKKEGK---TVLFSSHIMQEVeALCDRVVILHKGKVVAQGSLDELRE 221
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
60-256 2.87e-39

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 137.94  E-value: 2.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKN---------FVFQNPDHQVVMPTVEAD 126
Cdd:PRK13647  21 LKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMgrevNAENekwvrskvgLVFQDPDDQVFSSTVWDD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  127 VAFG---LGkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK13647 101 VAFGpvnMG----LDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRGQET 176
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23296450  204 VIKAVKDLINAKKgdvTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK13647 177 LMEILDRLHNQGK---TVIVATHDVDlAAEWADQVIVLKEGRVLAEGDKSLLTD 227
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
56-271 7.91e-39

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: 135.44  E-value: 7.91e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNpdhQVVMP--T 122
Cdd:cd03300  12 GFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLdgkditnlpphKRPVNTVFQN---YALFPhlT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD----E 198
Cdd:cd03300  89 VFENIAFGL-RLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALDlklrK 167
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 199 SDQMgvikAVKDLinAKKGDVTALWVTHRLEElkyadgavymengrvvrhgdAATISDFIKAKQSSYIDQIGS 271
Cdd:cd03300 168 DMQL----ELKRL--QKELGITFVFVTHDQEE--------------------ALTMSDRIAVMNKGKIQQIGT 214
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
41-244 1.83e-38

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: 131.98  E-value: 1.83e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkpknfvfqnpdhqvvm 120
Cdd:cd00267   1 EIENLSFRYGGR-----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILID---------------- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ptveadvafglgkyhdmNQEEVKSRVIKALEAVGMRdyMQrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:cd00267  60 -----------------GKDIAKLPLEELRRRIGYV--PQ-----LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPAS 115
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23296450 201 QMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGR 244
Cdd:cd00267 116 RERLLELLREL---AEEGRTVIIVTHDPELAeLAADRVIVLKDGK 157
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
35-254 3.24e-38

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 133.95  E-value: 3.24e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------EK 105
Cdd:COG1127   1 MSEPMIEVRNLTKSFGDR-----VVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVdgqditglsEK 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PKN-------FVFQNP---DHqvvMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIA 175
Cdd:COG1127  76 ELYelrrrigMLFQGGalfDS---L-TVFENVAFPLREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVA 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 176 IAGALAEACKVLLLDELTTFLD-ESdqMGVIkavKDLINA--KKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDA 251
Cdd:COG1127 152 LARALALDPEILLYDEPTAGLDpIT--SAVI---DELIRElrDELGLTSVVVTHDLDSAfAIADRVAVLADGKIIAEGTP 226

                ...
gi 23296450 252 ATI 254
Cdd:COG1127 227 EEL 229
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
60-254 4.79e-38

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 136.43  E-value: 4.79e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------KPKN----FVFQNPD---HqvvMpTVE 124
Cdd:COG1118  18 LDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNgrdlftnlPPRErrvgFVFQHYAlfpH---M-TVA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFGLGKyHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALA-EAcKVLLLDE----------- 191
Cdd:COG1118  94 ENIAFGLRV-RPPSKAEIRARVEELLELVQLEGLADRyPSQ-LSGGQRQRVALARALAvEP-EVLLLDEpfgaldakvrk 170
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 192 -----LTTFLDESdqmgvikavkdlinakkgDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG1118 171 elrrwLRRLHDEL------------------GGTTVFVTHDQEEaLELADRVVVMNQGRIEQVGTPDEV 221
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
35-253 5.84e-38

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: 139.89  E-value: 5.84e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNF--- 109
Cdd:COG4988 332 AGPPSIELEDVSFSYPGGR----PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILIngVDLSDLdpa 407
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 --------VFQNPdhQVVMPTVEADVAFGLgkyHDMNQEEVKsrviKALEAVGMRDYMQR-------PI----QTLSGGQ 170
Cdd:COG4988 408 swrrqiawVPQNP--YLFAGTIRENLRLGR---PDASDEELE----AALEAAGLDEFVAAlpdgldtPLgeggRGLSGGQ 478
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLD-ESDQmgvikAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG4988 479 AQRLALARALLRDAPLLLLDEPTAHLDaETEA-----EILQALRRLAKGRTVILITHRLALLAQADRILVLDDGRIVEQG 553

                ....
gi 23296450 250 DAAT 253
Cdd:COG4988 554 THEE 557
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
49-252 1.27e-37

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 132.10  E-value: 1.27e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---------FVFQ 112
Cdd:COG2884   7 VSKRYPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNgqdlsrlKRREipylrrrigVVFQ 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 npDHQVVMP-TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:COG2884  87 --DFRLLPDrTVYENVALPL-RVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADE 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 192 LTTFLDESDQMGVIKAVKDlINaKKGdVTALWVTHRLEELKYADG-AVYMENGRVVRHGDAA 252
Cdd:COG2884 164 PTGNLDPETSWEIMELLEE-IN-RRG-TTVLIATHDLELVDRMPKrVLELEDGRLVRDEARG 222
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
40-268 1.37e-37

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: 132.24  E-value: 1.37e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--------------EK 105
Cdd:cd03261   1 IELRGLTKSFGGRT-----VLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIdgedisglseaelyRL 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PKNF--VFQNP---DHqvvMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYM-QRPIQtLSGGQKQRIAIAGA 179
Cdd:cd03261  76 RRRMgmLFQSGalfDS---L-TVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAEdLYPAE-LSGGMKKRVALARA 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 180 LAEACKVLLLDELTTFLDESdQMGVIkavKDLIN--AKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGdaaTISD 256
Cdd:cd03261 151 LALDPELLLYDEPTAGLDPI-ASGVI---DDLIRslKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG---TPEE 223
                       250
                ....*....|..
gi 23296450 257 fIKAKQSSYIDQ 268
Cdd:cd03261 224 -LRASDDPLVRQ 234
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
39-254 5.69e-37

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 133.66  E-value: 5.69e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN--- 108
Cdd:COG3839   3 SLELENVSKSYG-----GVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGgrdvtdlPPKDrni 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -FVFQNPdhqVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACK 185
Cdd:COG3839  78 aMVFQSY---ALYPhmTVYENIAFPL-KLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 186 VLLLDELTTFLDES--DQM-GVIKAV-KDLinakkgDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG3839 154 VFLLDEPLSNLDAKlrVEMrAEIKRLhRRL------GTTTIYVTHDQVEaMTLADRIAVMNDGRIQQVGTPEEL 221
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
59-254 9.40e-37

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: 129.99  E-value: 9.40e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVN-----PSSGTVFVEkPKN----------------FVFQNPDhq 117
Cdd:cd03260  15 ALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDlipgaPDEGEVLLD-GKDiydldvdvlelrrrvgMVFQKPN-- 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 vVMP-TVEADVAFGLgKYHDM-NQEEVKSRVIKALEAVGMRDYMQRPIQ--TLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:cd03260  92 -PFPgSIYDNVAYGL-RLHGIkLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARALANEPEVLLLDEPT 169
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 194 TFLDESDQMgvikAVKDLINAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:cd03260 170 SALDPISTA----KIEELIAELKKEYTIVIVTHNMQQaARVADRTAFLLNGRLVEFGPTEQI 227
cbiO PRK13637
energy-coupling factor transporter ATPase;
60-249 1.09e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 131.32  E-value: 1.09e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------------KPKNFVFQNPDHQVVMPTVE 124
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDgvditdkkvklsdirKKVGLVFQYPEYQLFEETIE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 ADVAFG---LGkyhdMNQEEVKSRVIKALEAVGM--RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK13637 103 KDIAFGpinLG----LSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPK 178
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23296450  200 DQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13637 179 GRDEILNKIKEL--HKEYNMTIILVSHSMEDVaKLADRIIVMNKGKCELQG 227
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
39-256 1.60e-36

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: 129.77  E-value: 1.60e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNlcfsVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPK 107
Cdd:cd03296   2 SIEVRN----VSKRFG-DFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFggedatdvpvqERNV 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 NFVFQnpdHQVVMP--TVEADVAFGL---GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:cd03296  77 GFVFQ---HYALFRhmTVFDNVAFGLrvkPRSERPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 183 ACKVLLLDELTTFLD---ESDQMGVIKAVKDLINakkgdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:cd03296 154 EPKVLLLDEPFGALDakvRKELRRWLRRLHDELH-----VTTVFVTHDQEEaLEVADRVVVMNKGRIEQVGTPDEVYD 226
cbiO PRK13644
energy-coupling factor transporter ATPase;
58-254 3.67e-36

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 129.72  E-value: 3.67e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------------KPKNFVFQNPDHQVVMPTV 123
Cdd:PRK13644  16 PALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSgidtgdfsklqgirKLVGIVFQNPETQFVGRTV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  124 EADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK13644  96 EEDLAFGPENLC-LPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIA 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23296450  204 VIKAVKDLinAKKGDvTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13644 175 VLERIKKL--HEKGK-TIVYITHNLEELHDADRIIVMDRGKIVLEGEPENV 222
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
39-249 5.43e-36

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


Pssm-ID: 441875 [Multi-domain]  Cd Length: 711  Bit Score: 135.73  E-value: 5.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVSTRqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-------PKN--- 108
Cdd:COG2274 473 DIELENVSFRYPGD---SPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGidlrqidPASlrr 549
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQNPdhQVVMPTVEADVAFGlgkYHDMNQEEVksrvIKALEAVGMRDY-------MQRPI----QTLSGGQKQRI 174
Cdd:COG2274 550 qigVVLQDV--FLFSGTIRENITLG---DPDATDEEI----IEAARLAGLHDFiealpmgYDTVVgeggSNLSGGQRQRL 620
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG2274 621 AIARALLRNPRILILDEATSALDAETE----AIILENLRRLLKGRTVIIIAHRLSTIRLADRIIVLDKGRIVEDG 691
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
40-231 6.43e-36

ABC-type transport system involved in cytochrome c biogenesis, ATPase component [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 443308 [Multi-domain]  Cd Length: 206  Bit Score: 127.21  E-value: 6.43e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNFVFQNPDHQV 118
Cdd:COG4133   3 LEAENLSCRRGER-----LLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNgEPIRDAREDYRRRL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 --------VMP--TVEADVAFgLGKYHDMNQEEvkSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:COG4133  78 aylghadgLKPelTVRENLRF-WAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWL 154
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23296450 189 LDELTTFLDESDqmgvIKAVKDLINAKKGD-VTALWVTHRLEEL 231
Cdd:COG4133 155 LDEPFTALDAAG----VALLAELIAAHLARgGAVLLTTHQPLEL 194
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
60-249 2.11e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 128.21  E-value: 2.11e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------KPKNF---------VFQNPDHQVVMPT 122
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitagkKNKKLkplrkkvgiVFQFPEHQLFEET 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGlgkyhDMN----QEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK13634 103 VEKDICFG-----PMNfgvsEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23296450  198 ESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13634 178 PKGRKEMMEMFYKL--HKEKGLTTVLVTHSMEDAaRYADQIVVMHKGTVFLQG 228
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
60-194 4.39e-35

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: 123.14  E-value: 4.39e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PKN--FVFQNPdhqVVMP--TVE 124
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGqdltdderkslRKEigYVFQDP---QLFPrlTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450   125 ADVAFGLGKYHdMNQEEVKSRVIKALEAVGMRDYMQRPIQ----TLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:pfam00005  78 ENLRLGLLLKG-LSKREKDARAEEALEKLGLGDLADRPVGerpgTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
40-249 4.52e-35

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: 125.70  E-value: 4.52e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLcfSVS-TRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkPKN---------- 108
Cdd:cd03257   2 LEVKNL--SVSfPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFD-GKDllklsrrlrk 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 -------FVFQNPDHQV--VMpTVEADVAFGL-GKYHDMNQEEVKSRVIKALEAVGM-RDYMQR-PIQtLSGGQKQRIAI 176
Cdd:cd03257  79 irrkeiqMVFQDPMSSLnpRM-TIGEQIAEPLrIHGKLSKKEARKEAVLLLLVGVGLpEEVLNRyPHE-LSGGQRQRVAI 156
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:cd03257 157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKL--QEELGLTLLFITHDLGVVAKiADRVAVMYAGKIVEEG 228
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
40-250 8.02e-35

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


Pssm-ID: 213266 [Multi-domain]  Cd Length: 235  Bit Score: 125.14  E-value: 8.02e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQgisvpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---- 108
Cdd:cd03299   1 LKVENLSKDWKEFK------LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNgkditnlPPEKrdis 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 FVFQNpdhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:cd03299  75 YVPQN---YALFPhmTVYKNIAYGL-KKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKI 150
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLInaKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:cd03299 151 LLLDEPFSALDVRTKEKLREELKKIR--KEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGK 213
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
53-250 9.74e-35

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: 125.00  E-value: 9.74e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  53 QGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPD-----HQVVM------- 120
Cdd:cd03258  14 TGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkarRRIGMifqhfnl 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ---PTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03258  94 lssRTVFENVALPL-EIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALD 172
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23296450 198 ESDQMGVIKAVKDlINAKKGdVTALWVTHRLEELK-YADGAVYMENGRVVRHGD 250
Cdd:cd03258 173 PETTQSILALLRD-INRELG-LTIVLITHEMEVVKrICDRVAVMEKGEVVEEGT 224
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
58-249 1.68e-34

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 124.74  E-value: 1.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KP----------KNFVFQnPDHQVVmP---TV 123
Cdd:PRK11231  16 RILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGdKPismlssrqlaRRLALL-PQHHLT-PegiTV 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  124 EADVAFG----LGKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK11231  94 RELVAYGrspwLSLWGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLDIN 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23296450  200 DQMGVIKAVKDLINAKKGDVTALwvtHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK11231 173 HQVELMRLMRELNTQGKTVVTVL---HDLNQAsRYCDHLVVLANGHVMAQG 220
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
56-235 1.76e-34

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 123.11  E-value: 1.76e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQVVMP-TVEADVAFGL- 131
Cdd:NF040873   4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAggARVAYVPQRSEVPDSLPlTVRDLVAMGRw 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  132 ---GKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESdqmgVIKAV 208
Cdd:NF040873  84 arrGLWRRLTRDD-RAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAE----SRERI 158
                        170       180
                 ....*....|....*....|....*...
gi 23296450  209 KDLINAKKGD-VTALWVTHRLEELKYAD 235
Cdd:NF040873 159 IALLAEEHARgATVVVVTHDLELVRRAD 186
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
40-244 2.56e-34

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


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 121.72  E-value: 2.56e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHQvv 119
Cdd:cd03228   1 IEFKNVSFSYPGR---PKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILI-----------DGV-- 64
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 mptveaDVAfglgkyhDMNQEEVKSRVIkaleAVGmrdymQRPI---QT-----LSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:cd03228  65 ------DLR-------DLDLESLRKNIA----YVP-----QDPFlfsGTireniLSGGQRQRIAIARALLRDPPILILDE 122
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23296450 192 LTTFLD-ESDQmgvikAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGR 244
Cdd:cd03228 123 ATSALDpETEA-----LILEALRALAKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
60-249 3.85e-34

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 124.57  E-value: 3.85e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF--------------VFQNPDHQVVMPTVE 124
Cdd:PRK13636  22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDgKPIDYsrkglmklresvgmVFQDPDNQLFSASVY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 ADVAFGLgkyhdMN----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsd 200
Cdd:PRK13636 102 QDVSFGA-----VNlklpEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP-- 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 23296450  201 qMGVIKAVKDLINAKKG-DVTALWVTHRLEELK-YADGAVYMENGRVVRHG 249
Cdd:PRK13636 175 -MGVSEIMKLLVEMQKElGLTIIIATHDIDIVPlYCDNVFVMKEGRVILQG 224
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
49-256 5.67e-34

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: 123.06  E-value: 5.67e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN---------FVFQ 112
Cdd:cd03256   6 LSKTYPNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDgtdinklKGKAlrqlrrqigMIFQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 npDHQVVMP-TVEADVAFGLGKYH-------DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:cd03256  86 --QFNLIERlSVLENVLSGRLGRRstwrslfGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQP 163
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 185 KVLLLDELTTFLDESDQMGVIKAVKDlINAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:cd03256 164 KLILADEPVASLDPASSRQVMDLLKR-INREEG-ITVIVSLHQVDlAREYADRIVGLKDGRIVFDGPPAELTD 234
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
40-245 6.79e-34

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: 120.97  E-value: 6.79e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpdhqvv 119
Cdd:cd03230   1 IEVRNLSKRYGKK-----TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKV---------------- 59
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 mptveadvafgLGKYHDMNQEEVKSRVIKALEAVGMRDYMqRPIQTL--SGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03230  60 -----------LGKDIKKEPEEVKRRIGYLPEEPSLYENL-TVRENLklSGGMKQRLALAQALLHDPELLILDEPTSGLD 127
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23296450 198 ESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRV 245
Cdd:cd03230 128 PESRREFWELLREL---KKEGKTILLSSHILEEAeRLCDRVAILNNGRI 173
cbiO PRK13642
energy-coupling factor transporter ATPase;
37-249 1.40e-33

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 123.28  E-value: 1.40e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   37 NVAVECRNLCFSVSTRQGISVpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK--------- 107
Cdd:PRK13642   2 NKILEVENLVFKYEKESDVNQ--LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELltaenvwnl 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  108 ----NFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK13642  80 rrkiGMVFQNPDNQFVGATVEDDVAFGM-ENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALR 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  184 CKVLLLDELTTFLD---ESDQMGVIKAVKDlinakKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13642 159 PEIIILDESTSMLDptgRQEIMRVIHEIKE-----KYQLTVLSITHDLDEAASSDRILVMKAGEIIKEA 222
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
41-249 1.45e-33

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 122.53  E-value: 1.45e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNfvfQNPDHQV- 118
Cdd:COG4559   3 EAENLSVRLGGRT-----LLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNgRPLA---AWSPWELa 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 ----VMP---------TVEADVAFGLgkY-HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA--- 181
Cdd:COG4559  75 rrraVLPqhsslafpfTVEEVVALGR--ApHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlw 152
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 182 EAC----KVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLeEL--KYADGAVYMENGRVVRHG 249
Cdd:COG4559 153 EPVdggpRWLFLDEPTSALDLAHQHAVLRLARQL--ARRG-GGVVAVLHDL-NLaaQYADRILLLHQGRLVAQG 222
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
39-252 3.96e-33

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 120.89  E-value: 3.96e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV--------FVEKPKN-- 108
Cdd:COG4161   2 SIQLKNINCFYGSHQ-----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLniaghqfdFSQKPSEka 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---------FVFQN----PdHQVVMPT-VEADVafglgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRI 174
Cdd:COG4161  77 irllrqkvgMVFQQynlwP-HLTVMENlIEAPC-----KVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRV 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAA 252
Cdd:COG4161 151 AIARALMMEPQVLLFDEPTAALDPEITAQVVEIIREL--SQTG-ITQVIVTHEVEfARKVASQVVYMEKGRIIEQGDAS 226
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
53-254 5.43e-33

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 120.57  E-value: 5.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  53 QGISV-----PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSG---TVFVEKP---------KNFVFQNPD 115
Cdd:COG1119   7 RNVTVrrggkTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFGERRggedvwelrKRIGLVSPA 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 HQVVMP---TVEaDV----AFG-LGKYHDMNQEEVKsRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:COG1119  87 LQLRFPrdeTVL-DVvlsgFFDsIGLYREPTDEQRE-RARELLELLGLAHLADRPFGTLSQGEQRRVLIARALVKDPELL 164
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 188 LLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELkyADG---AVYMENGRVVRHGDAATI 254
Cdd:COG1119 165 ILDEPTAGLDLGARELLLALLDKL--AAEGAPTLVLVTHHVEEI--PPGithVLLLKDGRVVAAGPKEEV 230
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
38-246 1.50e-32

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 119.88  E-value: 1.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   38 VAVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNfvfQNPDH 116
Cdd:PRK13548   1 AMLEARNLSVRLGGRT-----LLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNgRPLA---DWSPA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  117 QV-----VMP---------TVEADVAFGLGKyHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA- 181
Cdd:PRK13548  73 ELarrraVLPqhsslsfpfTVEEVVAMGRAP-HGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAq 151
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  182 -----EACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLeEL--KYADGAVYMENGRVV 246
Cdd:PRK13548 152 lwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQL--AHERGLAVIVVLHDL-NLaaRYADRIVLLHQGRLV 220
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
58-245 2.68e-32

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 121.98  E-value: 2.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------KPKNFVFQN----PdHqvvMpT 122
Cdd:PRK09452  28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDgqdithvpaenRHVNTVFQSyalfP-H---M-T 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES--D 200
Cdd:PRK09452 103 VFENVAFGL-RMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDESLSALDYKlrK 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  201 QMGV-IKAVKdlinaKKGDVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK09452 182 QMQNeLKALQ-----RKLGITFVFVTHDQEEaLTMSDRIVVMRDGRI 223
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
40-254 4.18e-32

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 121.48  E-value: 4.18e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLcfsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------KPKN 108
Cdd:PRK11607  20 LEIRNL-----TKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDgvdlshvppyqRPIN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 FVFQNpdhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK11607  95 MMFQS---YALFPhmTVEQNIAFGL-KQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKL 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450  187 LLLDELTTFLDES--DQMGVikAVKDLInaKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11607 171 LLLDEPMGALDKKlrDRMQL--EVVDIL--ERVGVTCVMVTHDQEEaMTMAGRIAIMNRGKFVQIGEPEEI 237
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
40-244 1.04e-31

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 116.03  E-value: 1.04e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPdhqVV 119
Cdd:cd03250   1 ISVEDASFTWDSGEQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGSIAYVSQEP---WI 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 MP-TVEADVAFGlgkyHDMNQEEVKsRVIKA------LEAVGMRDYM---QRPIqTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03250  78 QNgTIRENILFG----KPFDEERYE-KVIKAcalepdLEILPDGDLTeigEKGI-NLSGGQKQRISLARAVYSDADIYLL 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 190 DElttfldesdqmgVIKAV---------KDLINAK-KGDVTALWVTHRLEELKYADGAVYMENGR 244
Cdd:cd03250 152 DD------------PLSAVdahvgrhifENCILGLlLNNKTRILVTHQLQLLPHADQIVVLDNGR 204
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
58-235 2.31e-31

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 115.97  E-value: 2.31e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPD--HQVVMPTVEADVAFGLGKYH 135
Cdd:PRK10247  21 KILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEG-EDISTLKPEiyRQQVSYCAQTPTLFGDTVYD 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  136 DM-------NQEEVKSRVIKALEAVGMRDYM-QRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQmgviKA 207
Cdd:PRK10247 100 NLifpwqirNQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNK----HN 175
                        170       180       190
                 ....*....|....*....|....*....|
gi 23296450  208 VKDLIN--AKKGDVTALWVTHRLEELKYAD 235
Cdd:PRK10247 176 VNEIIHryVREQNIAVLWVTHDKDEINHAD 205
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
56-249 2.40e-31

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: 115.43  E-value: 2.40e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN----FVFQNpdhQVVMP--T 122
Cdd:cd03301  12 NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGgrdvtdlPPKDrdiaMVFQN---YALYPhmT 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:cd03301  89 VYDNIAFGL-KLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNLDAKLRV 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLinAKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03301 168 QMRAELKRL--QQRLGTTTIYVTHdQVEAMTMADRIAVMNDGQIQQIG 213
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
40-245 3.01e-31

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: 115.32  E-value: 3.01e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKN------ 108
Cdd:cd03262   1 IEIKNLHKSFGDFH-----VLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDglkltDDKKninelr 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ----FVFQNPD---HQvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:cd03262  76 qkvgMVFQQFNlfpHL----TVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALA 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 182 EACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRV 245
Cdd:cd03262 152 MNPKVMLFDEPTSALDPELVGEVLDVMKDL--AEEG-MTMVVVTHEMGfAREVADRVIFMDDGRI 213
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
64-256 3.96e-31

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 115.24  E-value: 3.96e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQnpDHQVVMP-TVEADVAFGL 131
Cdd:COG3840  19 DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWngqdltalppaERPVSMLFQ--ENNLFPHlTVAQNIGLGL 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKyhDMN-QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES--DQMgvIKAV 208
Cdd:COG3840  97 RP--GLKlTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPAlrQEM--LDLV 172
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23296450 209 KDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:COG3840 173 DEL--CRERGLTVLMVTHDPEDaARIADRVLLVADGRIAADGPTAALLD 219
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
62-249 4.58e-31

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: 114.70  E-value: 4.58e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  62 DCSFRIPsGQLWMILGPNGCGKSTLLKILAGVVNPSSG------TVFVEKPKN-----------FVFQNpdhQVVMP--T 122
Cdd:cd03297  16 KIDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGtivlngTVLFDSRKKinlppqqrkigLVFQQ---YALFPhlN 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYHDMnqeEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:cd03297  92 VRENLAFGLKRKRNR---EDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRL 168
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 23296450 203 GVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:cd03297 169 QLLPELKQI--KKNLNIPVIFVTHDLSEAEYlADRIVVMEDGRLQYIG 214
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
35-250 9.59e-31

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 116.49  E-value: 9.59e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   35 SDNVAVECRNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------- 104
Cdd:PRK13631  17 SDDIILRVKNLYCVFDEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyigdkknn 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  105 ----------KPKNF---------VFQNPDHQVVMPTVEADVAFG---LGkyhdMNQEEVKSRVIKALEAVGMRD-YMQR 161
Cdd:PRK13631  97 helitnpyskKIKNFkelrrrvsmVFQFPEYQLFKDTIEKDIMFGpvaLG----VKKSEAKKLAKFYLNKMGLDDsYLER 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  162 PIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD---ESDQMGVIKavkdliNAKKGDVTALWVTHRLEE-LKYADGA 237
Cdd:PRK13631 173 SPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDpkgEHEMMQLIL------DAKANNKTVFVITHTMEHvLEVADEV 246
                        250
                 ....*....|...
gi 23296450  238 VYMENGRVVRHGD 250
Cdd:PRK13631 247 IVMDKGKILKTGT 259
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
56-246 1.16e-30

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: 112.14  E-value: 1.16e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPDHqvvmptveadvafglgkyh 135
Cdd:cd03216  12 GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDG-KEVSFASPRD------------------- 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 136 dmnqeevksrvikALEA-VGMrdymqrpIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinA 214
Cdd:cd03216  72 -------------ARRAgIAM-------VYQLSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRL--R 129
                       170       180       190
                ....*....|....*....|....*....|...
gi 23296450 215 KKGdVTALWVTHRLEE-LKYADGAVYMENGRVV 246
Cdd:cd03216 130 AQG-VAVIFISHRLDEvFEIADRVTVLRDGRVV 161
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
56-249 1.62e-30

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: 113.14  E-value: 1.62e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNFVFQN------------PDHQVVmpt 122
Cdd:cd03269  12 RVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDgKPLDIAARNrigylpeerglyPKMKVI--- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 veaDVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQm 202
Cdd:cd03269  89 ---DQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSGLDPVNV- 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23296450 203 gviKAVKDLINAKKGD-VTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:cd03269 165 ---ELLKDVIRELARAgKTVILSTHQMELVeELCDRVLLLNKGRAVLYG 210
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
58-254 2.48e-30

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 114.33  E-value: 2.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF--------------VFQNPDHQVVMPT 122
Cdd:PRK13638  15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQgKPLDYskrgllalrqqvatVFQDPEQQIFYTD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:PRK13638  95 IDSDIAFSL-RNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRT 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23296450  203 GVIKAVKDLINAKKGDVTAlwvTHRLEELKYADGAVY-MENGRVVRHGDAATI 254
Cdd:PRK13638 174 QMIAIIRRIVAQGNHVIIS---SHDIDLIYEISDAVYvLRQGQILTHGAPGEV 223
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
59-249 2.70e-30

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: 112.67  E-value: 2.70e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  59 ILRDCSFRIPSGqLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKNFvfqnpdHQVV--MP--------- 121
Cdd:cd03264  15 ALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIdgqdvlKQPQKL------RRRIgyLPqefgvypnf 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:cd03264  88 TVREFLDY-IAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEER 166
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23296450 202 MGVIKAVKDLinakKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:cd03264 167 IRFRNLLSEL----GEDRIVILSTHIVEDVESlCNQVAVLNKGKLVFEG 211
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
35-253 2.96e-30

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: 118.72  E-value: 2.96e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSvstRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPK------ 107
Cdd:COG4987 329 PGGPSLELEDVSFR---YPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLgGVDLrdlded 405
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 108 ------NFVFQNPDhqVVMPTVEADVAFGLGkyhDMNQEEVksrvIKALEAVGMRDYMQRPIQ-----------TLSGGQ 170
Cdd:COG4987 406 dlrrriAVVPQRPH--LFDTTLRENLRLARP---DATDEEL----WAALERVGLGDWLAALPDgldtwlgeggrRLSGGE 476
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIkavKDLINAKKGDvTALWVTHRLEELKYADGAVYMENGRVVRHGD 250
Cdd:COG4987 477 RRRLALARALLRDAPILLLDEPTEGLDAATEQALL---ADLLEALAGR-TVLLITHRLAGLERMDRILVLEDGRIVEQGT 552

                ...
gi 23296450 251 AAT 253
Cdd:COG4987 553 HEE 555
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
53-255 4.57e-30

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 117.43  E-value: 4.57e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  53 QGIS-----VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPknFVFQNP----DHQVVM-- 120
Cdd:COG1129   8 RGISksfggVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDgEP--VRFRSPrdaqAAGIAIih 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ------P--TVEADVAFG--LGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:COG1129  86 qelnlvPnlSVAENIFLGrePRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDARVLILD 165
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 191 ELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATIS 255
Cdd:COG1129 166 EPTASLTEREVERLFRIIRRL---KAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVGTGPVAELT 228
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
40-250 5.30e-30

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: 112.63  E-value: 5.30e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQGisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNF-------- 109
Cdd:cd03249   1 IEFKNVSFRYPSRPD--VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLdgVDIRDLnlrwlrsq 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ---VFQNPdhqVVMP-TVEADVAFGLgkyHDMNQEEVKsRVIKALEA--------------VGmrdymQRPIQtLSGGQK 171
Cdd:cd03249  79 iglVSQEP---VLFDgTIAENIRYGK---PDATDEEVE-EAAKKANIhdfimslpdgydtlVG-----ERGSQ-LSGGQK 145
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 172 QRIAIAGALAEACKVLLLDELTTFLD-ESDqmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGD 250
Cdd:cd03249 146 QRIAIARALLRNPKILLLDEATSALDaESE-----KLVQEALDRAMKGRTTIVIAHRLSTIRNADLIAVLQNGQVVEQGT 220
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
59-251 9.96e-30

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 112.03  E-value: 9.96e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV--------FVEKPK-----------NFVFQN----Pd 115
Cdd:PRK11124  17 ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLniagnhfdFSKTPSdkairelrrnvGMVFQQynlwP- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  116 HQVVMPT-VEADV-AFGLGKyhdmnqEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK11124  96 HLTVQQNlIEAPCrVLGLSK------DQALARAEKLLERLRLKPYADRfPLH-LSGGQQQRVAIARALMMEPQVLLFDEP 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  193 TTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDA 251
Cdd:PRK11124 169 TAALDPEITAQIVSIIREL--AETG-ITQVIVTHEVEvARKTASRVVYMENGHIVEQGDA 225
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
41-245 1.99e-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: 1.99e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVStrqGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHqvvm 120
Cdd:cd03246   2 EVENVSFRYP---GAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRL-----------DG---- 63
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ptveADV-AFGLGKYHDMnqeevksrvikaleaVGmrdYMQRPIQ---------TLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:cd03246  64 ----ADIsQWDPNELGDH---------------VG---YLPQDDElfsgsiaenILSGGQRQRLGLARALYGNPRILVLD 121
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 191 ELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03246 122 EPNSHLDVEGERALNQAIAAL---KAAGATRIVIAHRPETLASADRILVLEDGRV 173
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
58-248 2.04e-29

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 111.72  E-value: 2.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-----VEKP---KNFVFQnpdHQVVMP--TVEADV 127
Cdd:PRK11248  15 PALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITldgkpVEGPgaeRGVVFQ---NEGLLPwrNVQDNV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  128 AFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE----LTTFLDESDQMG 203
Cdd:PRK11248  92 AFGL-QLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEpfgaLDAFTREQMQTL 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23296450  204 VIKAVKDliNAKKgdvtALWVTHRLEElkyadgAVYMEN---------GRVVRH 248
Cdd:PRK11248 171 LLKLWQE--TGKQ----VLLITHDIEE------AVFMATelvllspgpGRVVER 212
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
39-249 3.98e-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: 3.98e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKN---- 108
Cdd:COG1132 339 EIEFENVSFSYPGDR----PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIdgvdirDLTLEslrr 414
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ---FVFQnpDHQVVMPTVEADVAFGLGKYHDmnqEEVksrvIKALEAVGMRDYMQR-------PI----QTLSGGQKQRI 174
Cdd:COG1132 415 qigVVPQ--DTFLFSGTIRENIRYGRPDATD---EEV----EEAAKAAQAHEFIEAlpdgydtVVgergVNLSGGQRQRI 485
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 175 AIAGALAEACKVLLLDELTTFLD-ESDQMgVIKAVKDLInakkGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG1132 486 AIARALLKDPPILILDEATSALDtETEAL-IQEALERLM----KGRTTIVIAHRLSTIRNADRILVLDDGRIVEQG 556
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
60-249 6.04e-29

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: 109.38  E-value: 6.04e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKNFVFQN----PDHQVVMP--TVEADVA 128
Cdd:cd03266  21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDgfdvvKEPAEARRRlgfvSDSTGLYDrlTARENLE 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 129 FgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:cd03266 101 Y-FAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALREFI 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 23296450 209 KDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:cd03266 180 RQLRALGK---CILFSTHIMQEVeRLCDRVVVLHRGRVVYEG 218
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
40-249 6.15e-29

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC transporter that is expressed in the mitochondria. Although the specific function of ATM1 is unknown, its disruption results in the accumulation of excess mitochondrial iron, loss of mitochondrial cytochromes, oxidative damage to mitochondrial DNA, and decreased levels of cytosolic heme proteins. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 109.63  E-value: 6.15e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-------------- 105
Cdd:cd03253   1 IEFENVTFAYDPGR----PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGqdirevtldslrra 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 ----PKNFVFQNPdhqvvmpTVEADVAFGlgkYHDMNQEEVksrvIKALEA-----------------VGMRDYMqrpiq 164
Cdd:cd03253  77 igvvPQDTVLFND-------TIGYNIRYG---RPDATDEEV----IEAAKAaqihdkimrfpdgydtiVGERGLK----- 137
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 165 tLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGR 244
Cdd:cd03253 138 -LSGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRDVSKGR----TTIVIAHRLSTIVNADKIIVLKDGR 212

                ....*
gi 23296450 245 VVRHG 249
Cdd:cd03253 213 IVERG 217
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
56-246 6.64e-29

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: 109.13  E-value: 6.64e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPKNFVFQN----PDHQVVMP--TVE 124
Cdd:cd03263  14 TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINgysirTDRKAARQSlgycPQFDALFDelTVR 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdqmgV 204
Cdd:cd03263  94 EHLRF-YARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDP-----A 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23296450 205 IK-AVKDLINAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVV 246
Cdd:cd03263 168 SRrAIWDLILEVRKGRSIILTTHSMDEAEAlCDRIAIMSDGKLR 211
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
60-249 8.60e-29

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: 109.00  E-value: 8.60e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKN------FVFQNPDHQVVMPTVEADV 127
Cdd:cd03265  16 VRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVaghdvvREPREvrrrigIVFQDLSVDDELTGWENLY 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 128 AFglGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKA 207
Cdd:cd03265  96 IH--ARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQTRAHVWEY 173
                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 23296450 208 VKDLInaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:cd03265 174 IEKLK--EEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEG 214
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
58-252 1.75e-28

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: 109.51  E-value: 1.75e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------VEKPKNFVFQNPdHQVVMP 121
Cdd:TIGR02769  25 PVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSfrgqdlyqldrkqrraFRRDVQLVFQDS-PSAVNP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   122 --TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDE 198
Cdd:TIGR02769 104 rmTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRsEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDM 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 23296450   199 SDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAA 252
Cdd:TIGR02769 184 VLQAVILELLRKL--QQAFGTAYLFITHDLRLVqSFCQRVAVMDKGQIVEECDVA 236
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
40-250 2.67e-28

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: 108.09  E-value: 2.67e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQ 117
Cdd:cd03251   1 VEFKNVTF---RYPGDGPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDghDVRDYTLASLRRQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 V-VMP--------TVEADVAFGLgkyHDMNQEEVksrvIKALEAVGMRDY-MQRPIQ----------TLSGGQKQRIAIA 177
Cdd:cd03251  78 IgLVSqdvflfndTVAENIAYGR---PGATREEV----EEAARAANAHEFiMELPEGydtvigergvKLSGGQRQRIAIA 150
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450 178 GALAEACKVLLLDELTTFLD-ESDqmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGD 250
Cdd:cd03251 151 RALLKDPPILILDEATSALDtESE-----RLVQAALERLMKNRTTFVIAHRLSTIENADRIVVLEDGKIVERGT 219
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
57-244 2.75e-28

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: 106.50  E-value: 2.75e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------------EKPKNFVFQNPdhqVVMP 121
Cdd:cd03229  13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIdgedltdledelpplRRRIGMVFQDF---ALFP 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 --TVEADVAFGLgkyhdmnqeevksrvikaleavgmrdymqrpiqtlSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:cd03229  90 hlTVLENIALGL-----------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDPI 134
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23296450 200 DQMGVIKAVKDLiNAKKGdVTALWVTHRLEEL-KYADGAVYMENGR 244
Cdd:cd03229 135 TRREVRALLKSL-QAQLG-ITVVLVTHDLDEAaRLADRVVVLRDGK 178
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
40-254 3.02e-28

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 110.58  E-value: 3.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNlcfsVSTRQGISVPIlRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNFVFQNPDHQ 117
Cdd:PRK11432   7 VVLKN----ITKRFGSNTVI-DNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIdgEDVTHRSIQQRDIC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 VV---------MPTVEaDVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:PRK11432  82 MVfqsyalfphMSLGE-NVGYGL-KMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLL 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  189 LDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11432 160 FDEPLSNLDANLRRSMREKIREL--QQQFNITSLYVTHdQSEAFAVSDTVIVMNKGKIMQIGSPQEL 224
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
58-249 5.02e-28

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: 106.81  E-value: 5.02e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFriPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPDhqvVMP--TVE 124
Cdd:cd03298  14 PMHFDLTF--AQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLIngvdvtaappaDRPVSMLFQENN---LFAhlTVE 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVAFGLGKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:cd03298  89 QNVGLGLSPGLKLTAED-RQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEM 167
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*.
gi 23296450 205 IKAVKDLINAKKgdVTALWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:cd03298 168 LDLVLDLHAETK--MTVLMVTHQPEDaKRLAQRVVFLDNGRIAAQG 211
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
59-245 5.02e-28

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 110.17  E-value: 5.02e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPDHQVVMpTVEADV 127
Cdd:PRK10851  17 VLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFhgtdvsrlharDRKVGFVFQHYALFRHM-TVFDNI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  128 AFGLG---KYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK10851  96 AFGLTvlpRRERPNAAAIKAKVTQLLEMVQLAHLADRyPAQ-LSGGQKQRVALARALAVEPQILLLDEPFGALDAQVRKE 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23296450  204 VIKAVKDLINAKKgdVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK10851 175 LRRWLRQLHEELK--FTSVFVTHDQEEaMEVADRVVVMSQGNI 215
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
39-249 9.59e-28

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: 106.13  E-value: 9.59e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  39 AVECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkpkNFVFQNPDHQV 118
Cdd:cd03245   2 RIEFRNVSFSYPNQE---IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLD---GTDIRQLDPAD 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMP--------------TVEADVAFGLGKYHDmnqeevkSRVIKALEAVGMRDYMQR-------PI----QTLSGGQKQR 173
Cdd:cd03245  76 LRRnigyvpqdvtlfygTLRDNITLGAPLADD-------ERILRAAELAGVTDFVNKhpngldlQIgergRGLSGGQRQA 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLInakkGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03245 149 VALARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLL----GDKTLIIITHRPSLLDLVDRIIVMDSGRIVADG 220
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
60-254 1.15e-27

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: 106.37  E-value: 1.15e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNFV-------FQNP---DHQVVMPT 122
Cdd:cd03219  16 LDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDgeditglPPHEIArlgigrtFQIPrlfPELTVLEN 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 123 VEADVAFGLGKYHDM-----NQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL- 196
Cdd:cd03219  96 VMVAAQARTGSGLLLararrEEREARERAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLn 175
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 197 -DESDQMG-VIKAVKDlinakkGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:cd03219 176 pEETEELAeLIRELRE------RGITVLLVEHDMDVvMSLADRVTVLDQGRVIAEGTPDEV 230
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
56-254 1.65e-27

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: 106.96  E-value: 1.65e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------------KPKNFVFQnpdHQV 118
Cdd:cd03294  36 QTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDgqdiaamsrkelrelrrKKISMVFQ---SFA 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:cd03294 113 LLPhrTVLENVAFGL-EVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSAL 191
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 197 DEsdqmgVIKavKDL------INAKKGDvTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:cd03294 192 DP-----LIR--REMqdellrLQAELQK-TIVFITHDLDEaLRLGDRIAIMKDGRLVQVGTPEEI 248
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
43-254 1.95e-27

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: 107.83  E-value: 1.95e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  43 RNLCFSVSTRQGIsVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---SSGTVFVE-------KPKNF--- 109
Cdd:COG0444   5 RNLKVYFPTRRGV-VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDgedllklSEKELrki 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -------VFQ------NPdhqvVMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGGQKQ 172
Cdd:COG0444  84 rgreiqmIFQdpmtslNP----VM-TVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRldryPHE-LSGGMRQ 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 173 RIAIAGALaeAC--KVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHG 249
Cdd:COG0444 158 RVMIARAL--ALepKLLIADEPTTALDVTIQAQILNLLKDL--QRELGLAILFITHDLGVVAEiADRVAVMYAGRIVEEG 233

                ....*
gi 23296450 250 DAATI 254
Cdd:COG0444 234 PVEEL 238
cbiO PRK13649
energy-coupling factor transporter ATPase;
58-262 4.22e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 105.98  E-value: 4.22e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK------PKN-----------FVFQNPDHQVVM 120
Cdd:PRK13649  21 RALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDtlitstSKNkdikqirkkvgLVFQFPESQLFE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  121 PTVEADVAFGLGKYhDMNQEEVKSRVIKALEAVGMRD--YMQRPIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDE 198
Cdd:PRK13649 101 ETVLKDVAFGPQNF-GVSQEEAEALAREKLALVGISEslFEKNPFE-LSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  199 SDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI---SDFIKAKQ 262
Cdd:PRK13649 179 KGRKELMTLFKKL---HQSGMTIVLVTHLMDDVaNYADFVYVLEKGKLVLSGKPKDIfqdVDFLEEKQ 243
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
64-255 4.48e-27

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 109.55  E-value: 4.48e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFVE-------------KPKNFVFQNPdhQVVMPTVEADVAfg 130
Cdd:PRK11174 370 NFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINgielreldpeswrKHLSWVGQNP--QLPHGTLRDNVL-- 444
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  131 LGKyHDMNQEEVKSrvikALEAVGMRDYMQR-------PIQ----TLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK11174 445 LGN-PDASDEQLQQ----ALENAWVSEFLPLlpqgldtPIGdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAH 519
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  200 DQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHGDAATIS 255
Cdd:PRK11174 520 SEQLVMQALNAASRRQ----TTLMVTHQLEDLAQWDQIWVMQDGQIVQQGDYAELS 571
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
43-250 7.33e-27

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 106.70  E-value: 7.33e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  43 RNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN------- 108
Cdd:COG1135   5 ENLSKTFPTKGG-PVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDgvdltalSERElraarrk 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPDhqvVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEA 183
Cdd:COG1135  84 igMIFQHFN---LLSsrTVAENVALPL-EIAGVPKAEIRKRVAELLELVGLSDKADAyPSQ-LSGGQKQRVGIARALANN 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 184 CKVLLLDELTTFLD-ESdqmgvIKAVKDL---INAKKGdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:COG1135 159 PKVLLCDEATSALDpET-----TRSILDLlkdINRELG-LTIVLITHEMDVVRRiCDRVAVLENGRIVEQGP 224
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
56-245 1.33e-26

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 106.85  E-value: 1.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNFVFQNPDHQVVMPTVEADVAFG--- 130
Cdd:PRK09536  15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVagDDVEALSARAASRRVASVPQDTSLSFEfdv 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  131 -----------LGKYHDMNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK09536  95 rqvvemgrtphRSRFDTWTETD-RAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDIN 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  200 DQMGVIKAVKDLINAKKGDVTALwvtHRLE-ELKYADGAVYMENGRV 245
Cdd:PRK09536 174 HQVRTLELVRRLVDDGKTAVAAI---HDLDlAARYCDELVLLADGRV 217
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
35-252 2.10e-26

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: 102.90  E-value: 2.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------EK 105
Cdd:COG4181   4 SSAPIIELRGLTKTVGTGAG-ELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLagqdlfaldED 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 PK--------NFVFQNpdHQ----------VVMPTVEADVAfglgkyhdmnqeEVKSRVIKALEAVGMRDYMQ-RPIQtL 166
Cdd:COG4181  83 ARarlrarhvGFVFQS--FQllptltalenVMLPLELAGRR------------DARARARALLERVGLGHRLDhYPAQ-L 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdQMGviKAVKDLI---NAKKGdVTALWVTHRLEELKYADGAVYMENG 243
Cdd:COG4181 148 SGGEQQRVALARAFATEPAILFADEPTGNLDA--ATG--EQIIDLLfelNRERG-TTLVLVTHDPALAARCDRVLRLRAG 222

                ....*....
gi 23296450 244 RVVRHGDAA 252
Cdd:COG4181 223 RLVEDTAAT 231
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
57-256 2.21e-26

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: 102.51  E-value: 2.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknfVFQN------PDHQVVmptvEADVAF- 129
Cdd:cd03224  13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSI--------RFDGrditglPPHERA----RAGIGYv 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 130 --GLGKYHDMNQEE---------VKSRVIKALEAV-GM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:cd03224  81 peGRRIFPELTVEEnlllgayarRRAKRKARLERVyELfprlKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPS 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 194 tfldesdqMG----VIKAVKDLINA-KKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:cd03224 161 --------EGlapkIVEEIFEAIRElRDEGVTILLVEQNARFaLEIADRAYVLERGRVVLEGTAAELLA 221
cbiO PRK13641
energy-coupling factor transporter ATPase;
60-248 2.22e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 104.14  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------------EKPKNFVFQNPDHQVVMPT 122
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIagyhitpetgnknlkklRKKVSLVFQFPEAQLFENT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGlGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:PRK13641 103 VLKDVEFG-PKNFGFSEDEAKEKALKWLKKVGLSeDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGR 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 23296450  202 MGVIKAVKDLinaKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRH 248
Cdd:PRK13641 182 KEMMQLFKDY---QKAGHTVILVTHNMDDVaEYADDVLVLEHGKLIKH 226
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
59-249 2.72e-26

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 103.53  E-value: 2.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--EKPKNFVFQNPDHQV-------VMP---TVEAD 126
Cdd:PRK10253  22 VAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLdgEHIQHYASKEVARRIgllaqnaTTPgdiTVQEL 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  127 VAFGLGKYHDMN---QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK10253 102 VARGRYPHQPLFtrwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQID 181
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  204 VIKAVKDLiNAKKGDVTALwVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:PRK10253 182 LLELLSEL-NREKGYTLAA-VLHDLNQaCRYASHLIALREGKIVAQG 226
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
60-243 2.84e-26

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: 102.54  E-value: 2.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPDHQVV------MP--TVEADVAFGL 131
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEG-KQITEPGPDRMVVfqnyslLPwlTVRENIALAV 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   132 GKY-HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD----ESDQMGVIK 206
Cdd:TIGR01184  80 DRVlPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDaltrGNLQEELMQ 159
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 23296450   207 AVKDlinakkGDVTALWVTHRLEE-LKYADGAVYMENG 243
Cdd:TIGR01184 160 IWEE------HRVTVLMVTHDVDEaLLLSDRVVMLTNG 191
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
58-246 3.02e-26

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily represents ABC transporters involved in peptide antibiotic resistance. Bacitracin is a dodecapeptide antibiotic produced by B. licheniformis and B. subtilis. The synthesis of bacitracin is non-ribosomally catalyzed by a multi-enzyme complex BcrABC. Bacitracin has potent antibiotic activity against gram-positive bacteria. The inhibition of peptidoglycan biosynthesis is the best characterized bacterial effect of bacitracin. The bacitracin resistance of B. licheniformis is mediated by the ABC transporter Bcr which is composed of two identical BcrA ATP-binding subunits and one each of the integral membrane proteins, BcrB and BcrC. B. subtilis cells carrying bcr genes on high-copy number plasmids develop collateral detergent sensitivity, a similar phenomenon in human cells with overexpressed multi-drug resistance P-glycoprotein.


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 101.91  E-value: 3.02e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVeKPKNFVFQNPDHQVVMPTVEADVAFG------- 130
Cdd:cd03268  14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITF-DGKSYQKNIEALRRIGALIEAPGFYPnltaren 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 131 ---LGKYHDMNqeevKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDqmgvIKA 207
Cdd:cd03268  93 lrlLARLLGIR----KKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLDPDG----IKE 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23296450 208 VKDLI-NAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVV 246
Cdd:cd03268 165 LRELIlSLRDQGITVLISSHLLSEIqKVADRIGIINKGKLI 205
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
60-250 4.68e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 103.63  E-value: 4.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV--------FVEKPKNF---------------------- 109
Cdd:PRK13651  23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewifkdekNKKKTKEKekvleklviqktrfkkikkike 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  110 -------VFQNPDHQVVMPTVEADVAFGLGKYhDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:PRK13651 103 irrrvgvVFQFAEYQLFEQTIEKDIIFGPVSM-GVSKEEAKKRAAKYIELVGLdESYLQRSPFELSGGQKRRVALAGILA 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  182 EACKVLLLDELTTFLDESdqmGVIKAVKDLINAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGD 250
Cdd:PRK13651 182 MEPDFLVFDEPTAGLDPQ---GVKEILEIFDNLNKQGKTIILVTHDLDNvLEWTKRTIFFKDGKIIKDGD 248
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
56-254 5.78e-26

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 103.26  E-value: 5.78e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPknfvFQNPDHQVV--MP---------TV 123
Cdd:COG4152  13 DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDgEP----LDPEDRRRIgyLPeerglypkmKV 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDeSDQMG 203
Cdd:COG4152  89 GEQLVY-LARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDEPFSGLD-PVNVE 166
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 204 VIK-AVKDLinAKKGdVTALWVTHRL---EELkyADGAVYMENGRVVRHGDAATI 254
Cdd:COG4152 167 LLKdVIREL--AAKG-TTVIFSSHQMelvEEL--CDRIVIINKGRKVLSGSVDEI 216
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
48-259 9.16e-26

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: 101.61  E-value: 9.16e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  48 SVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKN------------FVFQnp 114
Cdd:cd03295   5 NVTKRYGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDgEDIReqdpvelrrkigYVIQ-- 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 dhQV-VMP--TVEADVAFgLGKYHDMNQEEVKSRVIKALEAVGM--RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03295  83 --QIgLFPhmTVEENIAL-VPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLM 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 190 DELTTFLD----ESDQMGVIKAVKDLinaKKgdvTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI-----SDFIK 259
Cdd:cd03295 160 DEPFGALDpitrDQLQEEFKRLQQEL---GK---TIVFVTHDIDEaFRLADRIAIMKNGEIVQVGTPDEIlrspaNDFVA 233
cbiO PRK13643
energy-coupling factor transporter ATPase;
60-269 1.27e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 102.50  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------------EKPKNFVFQNPDHQVVMPT 122
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVgdivvsstskqkeikpvRKKVGVVFQFPESQLFEET 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGLGKYhDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:PRK13643 102 VLKDVAFGPQNF-GIPKEKAEKIAAEKLEMVGLaDEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKAR 180
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  202 MGVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI---SDFIKA------KQSSYIDQI 269
Cdd:PRK13643 181 IEMMQLFESIHQSGQ---TVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSDVfqeVDFLKAhelgvpKATHFADQL 255
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
47-254 1.37e-25

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 103.34  E-value: 1.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   47 FSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPD-----HQVVM- 120
Cdd:PRK11153  11 FPQGGRT---IHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKElrkarRQIGMi 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  121 ---------PTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:PRK11153  88 fqhfnllssRTVFDNVALPL-ELAGTPKAEIKARVTELLELVGLSDKADRyPAQ-LSGGQKQRVAIARALASNPKVLLCD 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450  191 ELTTFLDESDQMGVIKAVKDlINAKKGdVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11153 166 EATSALDPATTRSILELLKD-INRELG-LTIVLITHEMDVVKrICDRVAVIDAGRLVEQGTVSEV 228
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
57-254 2.21e-25

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: 100.88  E-value: 2.21e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNFV-------FQNP-------- 114
Cdd:COG0411  17 LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDgrditglPPHRIArlgiartFQNPrlfpeltv 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 -DH-----QVVMPTVEADVAFGLGKYHDmNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:COG0411  97 lENvlvaaHARLGRGLLAALLRLPRARR-EEREARERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLL 175
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 189 LDE----LTTflDESDQM-GVIKAVKDlinakKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG0411 176 LDEpaagLNP--EETEELaELIRRLRD-----ERGITILLIEHDMDLVmGLADRIVVLDFGRVIAEGTPAEV 240
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
57-249 3.09e-25

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: 99.53  E-value: 3.09e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknfvfqnpdhQVVMP-----------TVEA 125
Cdd:cd03220  35 FWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG-----------RVSSLlglgggfnpelTGRE 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAFgLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQmgvI 205
Cdd:cd03220 104 NIYL-NGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQ---E 179
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23296450 206 KAVKDLINAKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHG 249
Cdd:cd03220 180 KCQRRLRELLKQGKTVILVSHDPSSIKrLCDRALVLEKGKIRFDG 224
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
41-254 3.12e-25

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 100.68  E-value: 3.12e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQGI----SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----KPKNF--- 109
Cdd:COG4167   6 EVRNLSKTFKYRTGLfrrqQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINghklEYGDYkyr 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ------VFQNPD-----HQVVMPTVEADVAFGLgkyhDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIA 177
Cdd:COG4167  86 ckhirmIFQDPNtslnpRLNIGQILEEPLRLNT----DLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALA 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 178 GALAEACKVLLLDELTTFLDESdqmgvIKAvkDLIN------AKKGdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:COG4167 162 RALILQPKIIIADEALAALDMS-----VRS--QIINlmlelqEKLG-ISYIYVSQHLGIVKHiSDKVLVMHQGEVVEYGK 233

                ....
gi 23296450 251 AATI 254
Cdd:COG4167 234 TAEV 237
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
40-249 3.17e-25

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: 104.41  E-value: 3.17e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    40 VECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQ 117
Cdd:TIGR02203 331 VEFRNVTF---RYPGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDghDLADYTLASLRRQ 407
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   118 V------VM---PTVEADVAFGLGKYHDMNQEEVKSRVIKALEAV-GMRDYMQRPI----QTLSGGQKQRIAIAGALAEA 183
Cdd:TIGR02203 408 ValvsqdVVlfnDTIANNIAYGRTEQADRAEIERALAAAYAQDFVdKLPLGLDTPIgengVLLSGGQRQRLAIARALLKD 487
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450   184 CKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR02203 488 APILILDEATSALDNESERLVQAALERLMQGR----TTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
59-246 3.21e-25

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 100.92  E-value: 3.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------EKPKNF------VFQ------NPDH 116
Cdd:PRK10419  27 VLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWrgeplaklnrAQRKAFrrdiqmVFQdsisavNPRK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  117 qvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRD-YMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK10419 107 -----TVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDsVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSN 181
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23296450  196 LDESDQMGVIKAVKDLinAKKGDVTALWVTH--RLEElKYADGAVYMENGRVV 246
Cdd:PRK10419 182 LDLVLQAGVIRLLKKL--QQQFGTACLFITHdlRLVE-RFCQRVMVMDNGQIV 231
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
40-254 4.54e-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: 103.61  E-value: 4.54e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQGI------SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFVE-------KP 106
Cdd:COG4172 276 LEARDLKVWFPIKRGLfrrtvgHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLALLRLI-PSEGEIRFDgqdldglSR 354
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 107 KNF---------VFQ------NPDHqvvmpTVEADVAFGLGKYH-DMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGG 169
Cdd:COG4172 355 RALrplrrrmqvVFQdpfgslSPRM-----TVGQIIAEGLRVHGpGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGG 429
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 170 QKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRH 248
Cdd:COG4172 430 QRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDL--QREHGLAYLFISHDLAVVRAlAHRVMVMKDGKVVEQ 507

                ....*.
gi 23296450 249 GDAATI 254
Cdd:COG4172 508 GPTEQV 513
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
40-249 4.62e-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: 99.22  E-value: 4.62e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRqgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKN----- 108
Cdd:cd03254   3 IEFENVNFSYDEK----KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIdgidirDISRKslrsm 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhqVVMP-TVEADVAFGlgkyHDMNQEEVksrVIKALEAVGMRDY-MQRPI----------QTLSGGQKQRI 174
Cdd:cd03254  79 igVVLQDT---FLFSgTIMENIRLG----RPNATDEE---VIEAAKEAGAHDFiMKLPNgydtvlgengGNLSQGERQLL 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 175 AIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03254 149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMKGR----TSIIIAHRLSTIKNADKILVLDDGKIIEEG 219
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
42-197 4.81e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 103.61  E-value: 4.81e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  42 CRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekPKN----FVFQNP--- 114
Cdd:COG0488   1 LENLSKSFGGR-----PLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI--PKGlrigYLPQEPpld 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 115 DHQVVMPTV-----------------EADVAFG----------LGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTL 166
Cdd:COG0488  74 DDLTVLDTVldgdaelraleaeleelEAKLAEPdedlerlaelQEEFEALGGWEAEARAEEILSGLGFpEEDLDRPVSEL 153
                       170       180       190
                ....*....|....*....|....*....|.
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:COG0488 154 SGGWRRRVALARALLSEPDLLLLDEPTNHLD 184
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
35-254 4.87e-25

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 100.11  E-value: 4.87e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  35 SDNVAVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLK------------------------IL 90
Cdd:COG1117   7 TLEPKIEVRNLNVYYGDKQ-----ALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndlipgarvegeilldgedIY 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  91 AGVVNPSS-----GTVFvEKPKNF---VFQNpdhqvvmptveadVAFGLgKYHDM-NQEEVKSRVIKALEAVGM----RD 157
Cdd:COG1117  82 DPDVDVVElrrrvGMVF-QKPNPFpksIYDN-------------VAYGL-RLHGIkSKSELDEIVEESLRKAALwdevKD 146
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 158 YMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDesdqmgVI--KAVKDLINAKKGDVTALWVTH------RLe 229
Cdd:COG1117 147 RLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALD------PIstAKIEELILELKKDYTIVIVTHnmqqaaRV- 219
                       250       260
                ....*....|....*....|....*
gi 23296450 230 elkyADGAVYMENGRVVRHGDAATI 254
Cdd:COG1117 220 ----SDYTAFFYLGELVEFGPTEQI 240
cbiO PRK13645
energy-coupling factor transporter ATPase;
34-249 5.39e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 100.47  E-value: 5.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   34 FSDNVAVEcrNLCFSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---------- 103
Cdd:PRK13645   3 FSKDIILD--NVSYTYAKKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipanlk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  104 --------EKPKNFVFQNPDHQVVMPTVEADVAFG---LGKyhdmNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQK 171
Cdd:PRK13645  81 kikevkrlRKEIGLVFQFPEYQLFQETIEKDIAFGpvnLGE----NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQK 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  172 QRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVtaLWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:PRK13645 157 RRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRI--IMVTHNMDQvLRIADEVIVMHEGKVISIG 233
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
40-249 8.59e-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: 98.94  E-value: 8.59e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQG----------------ISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV 103
Cdd:cd03267   1 IEVSNLSKSYRVYSKepgligslkslfkrkyREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 104 ------EKPKNFVFQnpdHQVVM----------PTVEadvAFGLGKY-HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTL 166
Cdd:cd03267  81 aglvpwKRRKKFLRR---IGVVFgqktqlwwdlPVID---SFYLLAAiYDLPPARFKKRLDELSELLDLEELLDTPVRQL 154
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEEL-KYADGAVYMENGRV 245
Cdd:cd03267 155 SLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEY-NRERG-TTVLLTSHYMKDIeALARRVLVIDKGRL 232

                ....
gi 23296450 246 VRHG 249
Cdd:cd03267 233 LYDG 236
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
40-245 1.09e-24

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: 98.31  E-value: 1.09e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKN---------- 108
Cdd:cd03248  12 VKFQNVTFAYPTRP--DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLdGKPISqyehkylhsk 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhQVVMPTVEADVAFGLGkyhDMNQEEVKSRVIKAlEAVGMRDYMQRPIQT--------LSGGQKQRIAIAG 178
Cdd:cd03248  90 vsLVGQEP--VLFARSLQDNIAYGLQ---SCSFECVKEAAQKA-HAHSFISELASGYDTevgekgsqLSGGQKQRVAIAR 163
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 179 ALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03248 164 ALIRNPQVLILDEATSALDaESEQQ-----VQQALYDWPERRTVLVIAHRLSTVERADQILVLDGGRI 226
cbiO PRK13646
energy-coupling factor transporter ATPase;
60-246 1.37e-24

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 99.47  E-value: 1.37e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE------KPKN-----------FVFQNPDHQVVMPT 122
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDditithKTKDkyirpvrkrigMVFQFPESQLFEDT 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGlGKYHDMNQEEVKSRVIKALEAVGM-RDYM-QRPIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:PRK13646 103 VEREIIFG-PKNFKMNLDEVKNYAHRLLMDLGFsRDVMsQSPFQ-MSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQS 180
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  201 QMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVV 246
Cdd:PRK13646 181 KRQVMRLLKSL--QTDENKTIILVSHDMNEVaRYADEVIVMKEGSIV 225
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
57-249 2.39e-24

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ATP transporter that exports lipid A and to eukaryotic P-glycoproteins.


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 101.70  E-value: 2.39e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKNF------VFQNPdhQVVMPTV 123
Cdd:TIGR02204 353 QPALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDgvdlrqlDPAELrarmalVPQDP--VLFAASV 430
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   124 EADVAFGlgkYHDMNQEEVKSRVIKA-----LEAV--GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:TIGR02204 431 MENIRYG---RPDATDEEVEAAARAAhahefISALpeGYDTYLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSAL 507
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23296450   197 D-ESDQMgVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR02204 508 DaESEQL-VQQALETLMKGR----TTLIIAHRLATVLKADRIVVMDQGRIVAQG 556
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
59-245 3.20e-24

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 97.83  E-value: 3.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF--------VEKPKNFVFQNPDhqvVMP--TVEADVA 128
Cdd:PRK11247  27 VLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGELLagtaplaeAREDTRLMFQDAR---LLPwkKVIDNVG 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  129 FGL-GKYHDmnqeevksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMgvikA 207
Cdd:PRK11247 104 LGLkGQWRD--------AALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLLDEPLGALDALTRI----E 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 23296450  208 VKDLINA--KKGDVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK11247 172 MQDLIESlwQQHGFTVLLVTHDVSEaVAMADRVLLIEEGKI 212
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
57-254 3.64e-24

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 97.46  E-value: 3.64e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQ-----NPDHqvvmpTVEADVAFGl 131
Cdd:COG1134  39 FWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGRVSALLElgagfHPEL-----TGRENIYLN- 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 132 GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDL 211
Cdd:COG1134 113 GRLLGLSRKEIDEKFDEIVEFAELGDFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL 192
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 23296450 212 inaKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATI 254
Cdd:COG1134 193 ---RESGRTVIFVSHSMGAVRrLCDRAIWLEKGRLVMDGDPEEV 233
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
49-240 4.18e-24

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: 100.82  E-value: 4.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN------FVFQNPd 115
Cdd:TIGR02857 327 VSVAYPGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNgvpladaDADSwrdqiaWVPQHP- 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   116 hQVVMPTVEADVAFGLGkyhDMNQEEVKsrviKALEAVGMRDYMQ-RP--IQT--------LSGGQKQRIAIAGALAEAC 184
Cdd:TIGR02857 406 -FLFAGTIAENIRLARP---DASDAEIR----EALERAGLDEFVAaLPqgLDTpigeggagLSGGQAQRLALARAFLRDA 477
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450   185 KVLLLDELTTFLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYM 240
Cdd:TIGR02857 478 PLLLLDEPTAHLDAETEAEVLEALRALAQGR----TVLLVTHRLALAALADRIVVL 529
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
62-254 5.73e-24

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: 99.02  E-value: 5.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  62 DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV--------EKPKN---------FVFQNP---DHQvvmp 121
Cdd:COG4148  17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsARGIFlpphrrrigYVFQEArlfPHL---- 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEADVAFGlgkYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:COG4148  93 SVRGNLLYG---RKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 23296450 202 MGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG4148 170 AEILPYLERL--RDELDIPILYVSHSLDEvARLADHVVLLEQGRVVASGPLAEV 221
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
58-251 7.00e-24

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: 100.50  E-value: 7.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------EKPKNFVFQNP-DHQVVMPTVEAD 126
Cdd:TIGR01842 332 PTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLdgadlkqwdrETFGKHIGYLPqDVELFPGTVAEN 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   127 VA-FGlgkyhdmnqEEVKSR-VIKALEAVGMRDYMQRPIQ-----------TLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:TIGR01842 412 IArFG---------ENADPEkIIEAAKLAGVHELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKLVVLDEPN 482
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450   194 TFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDA 251
Cdd:TIGR01842 483 SNLDEEGEQALANAIKAL---KARGITVVVITHRPSLLGCVDKILVLQDGRIARFGER 537
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
40-256 8.87e-24

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 96.32  E-value: 8.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNlcfsVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLK-------------ILAG--VVNPSSGTVFVE 104
Cdd:PRK09493   2 IEFKN----VSKHFG-PTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRcinkleeitsgdlIVDGlkVNDPKVDERLIR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  105 KPKNFVFQNPDhqvVMPTVEA--DVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:PRK09493  77 QEAGMVFQQFY---LFPHLTAleNVMFGPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAV 153
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450  183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK09493 154 KPKLMLFDEPTSALDPELRHEVLKVMQDL--AEEG-MTMVIVTHEIGfAEKVASRLIFIDKGRIAEDGDPQVLIK 225
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
57-256 2.96e-23

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: 94.66  E-value: 2.96e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknfVFQN------PDHQVV------MP--- 121
Cdd:COG0410  16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSI--------RFDGeditglPPHRIArlgigyVPegr 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 ------TVEADVAfgLGKYHDMNQEEVKSRvikaLEAVG-----MRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:COG0410  88 rifpslTVEENLL--LGAYARRDRAEVRAD----LERVYelfprLKERRRQRAGTLSGGEQQMLAIGRALMSRPKLLLLD 161
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 191 ELTtfldesdqMG----VIKAVKDLINA-KKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISD 256
Cdd:COG0410 162 EPS--------LGlaplIVEEIFEIIRRlNREGVTILLVEQNARFaLEIADRAYVLERGRIVLEGTAAELLA 225
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
54-252 3.82e-23

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: 98.28  E-value: 3.82e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF---VEkpknfVFQ-NPDH--QVV--MP---- 121
Cdd:COG4618 342 GSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRldgAD-----LSQwDREElgRHIgyLPqdve 416
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 ----TVEADVA-FGlgkyhDMNQEEVksrvIKALEAVGMRDYMQR-------PI----QTLSGGQKQRIAIAGALAEACK 185
Cdd:COG4618 417 lfdgTIAENIArFG-----DADPEKV----VAAAKLAGVHEMILRlpdgydtRIgeggARLSGGQRQRIGLARALYGDPR 487
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 186 VLLLDELTTFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAA 252
Cdd:COG4618 488 LVVLDEPNSNLDDEGEAALAAAIRAL---KARGATVVVITHRPSLLAAVDKLLVLRDGRVQAFGPRD 551
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
48-253 7.23e-23

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 94.56  E-value: 7.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   48 SVSTRQGISVpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKP------KNFVFQNPDHQVV- 119
Cdd:PRK15056  13 TVTWRNGHTA--LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISIlGQPtrqalqKNLVAYVPQSEEVd 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  120 --MPTVEADVAFgLGKYHDMN-----QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK15056  91 wsFPVLVEDVVM-MGRYGHMGwlrraKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEP 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  193 TTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVyMENGRVVRHGDAAT 253
Cdd:PRK15056 170 FTGVDVKTEARIISLLRELRDEGK---TMLVSTHNLGSVtEFCDYTV-MVKGTVLASGPTET 227
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
58-249 1.11e-22

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 91.61  E-value: 1.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNFVFQNPDHQVVMptveadvafglgkyhd 136
Cdd:cd03247  16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEItLDGVPVSDLEKALSSLISV---------------- 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 MNQEevksrviKALEAVGMRDYMQRPiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKk 216
Cdd:cd03247  80 LNQR-------PYLFDTTLRNNLGRR---FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKDK- 148
                       170       180       190
                ....*....|....*....|....*....|...
gi 23296450 217 gdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03247 149 ---TLIWITHHLTGIEHMDKILFLENGKIIMQG 178
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
40-254 1.22e-22

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 94.80  E-value: 1.22e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLC--FSVST----RQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--------- 104
Cdd:COG4608   8 LEVRDLKkhFPVRGglfgRTVGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDgqditglsg 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 105 ---KPKN----FVFQNPdHQVVMP--TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQR-PIQtLSGGQKQR 173
Cdd:COG4608  88 relRPLRrrmqMVFQDP-YASLNPrmTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRpEHADRyPHE-FSGGQRQR 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 174 IAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAA 252
Cdd:COG4608 166 IGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDL--QDELGLTYLFISHDLSVVRHiSDRVAVMYLGKIVEIAPRD 243

                ..
gi 23296450 253 TI 254
Cdd:COG4608 244 EL 245
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
59-254 2.23e-22

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 92.80  E-value: 2.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------------KPKNFVFQNPDHqvv 119
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDgkvlyfgkdifqidaiklrKEVGMVFQQPNP--- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  120 MP--TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK14246 102 FPhlSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPT 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  194 TFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK14246 182 SMIDIVNS----QAIEKLITELKNEIAIVIVSHNPQQVaRVADYVAFLYNGELVEWGSSNEI 239
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
40-254 3.10e-22

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 92.55  E-value: 3.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVSTRQGI----SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF----- 109
Cdd:PRK15112   5 LEVRNLSKTFRYRTGWfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDdHPLHFgdysy 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  110 -------VFQNPD-----HQVVMPTVEadvaFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAI 176
Cdd:PRK15112  85 rsqrirmIFQDPStslnpRQRISQILD----FPLRLNTDLEPEQREKQIIETLRQVGLLpDHASYYPHMLAPGQKQRLGL 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  177 AGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:PRK15112 161 ARALILRPKVIIADEALASLDMSMRSQLINLMLEL-QEKQG-ISYIYVTQHLGMMKHiSDQVLVMHQGEVVERGSTADV 237
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
49-228 6.19e-22

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: 94.73  E-value: 6.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------EKPKNFVFQNPDHQ 117
Cdd:TIGR02868 340 LSAGYPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLdgvpvssldqdEVRRRVSVCAQDAH 419
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   118 VVMPTVEADVAFGLGkyhDMNQEEvksrVIKALEAVGMRDYMQRPI-----------QTLSGGQKQRIAIAGALAEACKV 186
Cdd:TIGR02868 420 LFDTTVRENLRLARP---DATDEE----LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPI 492
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 23296450   187 LLLDELTTFLD--ESDQMgvikaVKDLINAKKGDVTaLWVTHRL 228
Cdd:TIGR02868 493 LLLDEPTEHLDaeTADEL-----LEDLLAALSGRTV-VLITHHL 530
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
58-254 6.74e-22

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 91.30  E-value: 6.74e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNfVFQNPD--------------HQVVMPTV 123
Cdd:COG4604  15 VVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDG-LD-VATTPSrelakrlailrqenHINSRLTV 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFGLGKYHD--MNQEEvKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD--ES 199
Cdd:COG4604  93 RELVAFGRFPYSKgrLTAED-REIIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDYVLLDEPLNNLDmkHS 171
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 200 DQMgvIKAVKDLinAKKGDVTALWVTHrleEL----KYADGAVYMENGRVVRHGDAATI 254
Cdd:COG4604 172 VQM--MKLLRRL--ADELGKTVVIVLH---DInfasCYADHIVAMKDGRVVAQGTPEEI 223
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
35-245 7.30e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 91.03  E-value: 7.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   35 SDNVAVECRNLCFSVSTRQgISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKN----- 108
Cdd:PRK11629   1 MNKILLQCDNLCKRYQEGS-VQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDViFNGQPMSklssa 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 -----------FVFQN----PD----HQVVMPTVeadvafgLGKyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGG 169
Cdd:PRK11629  80 akaelrnqklgFIYQFhhllPDftalENVAMPLL-------IGK---KKPAEINSRALEMLAAVGLEHRANHRPSELSGG 149
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  170 QKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdvTA-LWVTHRLEELKYADGAVYMENGRV 245
Cdd:PRK11629 150 ERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGEL-NRLQG--TAfLVVTHDLQLAKRMSRQLEMRDGRL 223
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
59-256 8.52e-22

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: 90.66  E-value: 8.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN-------FVfqnPDHQVVMP--T 122
Cdd:TIGR03410  15 ILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDgeditklPPHEraragiaYV---PQGREIFPrlT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   123 VEADVAFGLGKYHDMNQEEVKSrvIKALEAVgMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTtfldESDQM 202
Cdd:TIGR03410  92 VEENLLTGLAALPRRSRKIPDE--IYELFPV-LKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLLLDEPT----EGIQP 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450   203 GVIK----AVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATISD 256
Cdd:TIGR03410 165 SIIKdigrVIRRL--RAEGGMAILLVEQYLDfARELADRYYVMERGRVVASGAGDELDE 221
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
57-245 9.04e-22

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 92.98  E-value: 9.04e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------EKPKN----FVFQN----PdHqvvMp 121
Cdd:PRK11650  17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIggrvvneLEPADrdiaMVFQNyalyP-H---M- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  122 TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES-- 199
Cdd:PRK11650  92 SVRENMAYGL-KIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFLFDEPLSNLDAKlr 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 23296450  200 DQMGV-IKAVKDLINakkgdVTALWVTH-RLEELKYADGAVYMENGRV 245
Cdd:PRK11650 171 VQMRLeIQRLHRRLK-----TTSLYVTHdQVEAMTLADRVVVMNGGVA 213
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
40-249 9.37e-22

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 94.40  E-value: 9.37e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    40 VECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KP-KNF-------- 109
Cdd:TIGR00958 479 IEFQDVSFSYPNRP--DVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDgVPlVQYdhhylhrq 556
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   110 ---VFQNPdhqVVM-PTVEADVAFGLGKYHDmnqEEVKSrvikALEAVGMRDYMQRPIQT-----------LSGGQKQRI 174
Cdd:TIGR00958 557 valVGQEP---VLFsGSVRENIAYGLTDTPD---EEIMA----AAKAANAHDFIMEFPNGydtevgekgsqLSGGQKQRI 626
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450   175 AIAGALAEACKVLLLDELTTFLD-ESDQmgvikAVKDLinAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR00958 627 AIARALVRKPRVLILDEATSALDaECEQ-----LLQES--RSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMG 695
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
40-269 1.43e-21

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 90.98  E-value: 1.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------V 103
Cdd:PRK11831   8 VDMRGVSFTRGNR-----CIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILfdgenipamsrsrlytV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  104 EKPKNFVFQNPDHQVVMpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK11831  83 RKRMSMLFQSGALFTDM-NVFDNVAYPLREHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  184 CKVLLLDEltTFLDESD-QMGVIKAVKDLINAKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATISDFIKAK 261
Cdd:PRK11831 162 PDLIMFDE--PFVGQDPiTMGVLVKLISELNSALG-VTCVVVSHDVPEvLSIADHAYIVADKKIVAHGSAQALQANPDPR 238

                 ....*...
gi 23296450  262 QSSYIDQI 269
Cdd:PRK11831 239 VRQFLDGI 246
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
54-251 1.66e-21

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 93.44  E-value: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   54 GIS-----VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKNFvfqnpdhQVVMPTVEADV 127
Cdd:PRK11288   9 GIGktfpgVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIdGQEMRF-------ASTTAALAAGV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  128 A--------------------------FGLgkyhdMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALA 181
Cdd:PRK11288  82 AiiyqelhlvpemtvaenlylgqlphkGGI-----VNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALA 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450  182 EACKVLLLDELTTFLD--ESDQ-MGVIKAVKDlinakKGDVTaLWVTHRLEELkYA--DGAVYMENGRVVRHGDA 251
Cdd:PRK11288 157 RNARVIAFDEPTSSLSarEIEQlFRVIRELRA-----EGRVI-LYVSHRMEEI-FAlcDAITVFKDGRYVATFDD 224
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
31-246 1.88e-21

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 93.21  E-value: 1.88e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  31 RIKFSD-----NVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvek 105
Cdd:COG0488 302 EIRFPPperlgKKVLELEGLSKSYGDK-----TLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTV---- 372
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 106 pknfvfqnpdhqvvmpTVEADVAFGlgkYHDMNQEEVKS--RVIKALEAVG-------MRDYMQR----------PIQTL 166
Cdd:COG0488 373 ----------------KLGETVKIG---YFDQHQEELDPdkTVLDELRDGApggteqeVRGYLGRflfsgddafkPVGVL 433
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 167 SGGQKQRIAIAGALAEACKVLLLDELTTFLD-ESdqmgvIKAVKDLINAKKGdvTALWVTH-R--LEELkyADGAVYMEN 242
Cdd:COG0488 434 SGGEKARLALAKLLLSPPNVLLLDEPTNHLDiET-----LEALEEALDDFPG--TVLLVSHdRyfLDRV--ATRILEFED 504

                ....
gi 23296450 243 GRVV 246
Cdd:COG0488 505 GGVR 508
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
56-191 1.99e-21

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 89.08  E-value: 1.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---SSGTVF----------VEKPK-NFVFQNP---DHqv 118
Cdd:COG4136  13 GRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLlngrrltalpAEQRRiGILFQDDllfPH-- 90
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 119 vMpTVEADVAFGLGkyHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:COG4136  91 -L-SVGENLAFALP--PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDE 159
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
59-249 1.99e-21

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: 89.85  E-value: 1.99e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPKNFVFQnpDHQVVMPTVEA 125
Cdd:cd03252  17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDghdlaladpawlrRQVGVVLQ--ENVLFNRSIRD 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 DVAFGlgkyhdmNQEEVKSRVIKALEAVGMRDY-MQRPI----------QTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:cd03252  95 NIALA-------DPGMSMERVIEAAKLAGAHDFiSELPEgydtivgeqgAGLSGGQRQRIAIARALIHNPRILIFDEATS 167
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 195 FLDESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03252 168 ALDYESEHAIMRNMHDICAGR----TVIIIAHRLSTVKNADRIIVMEKGRIVEQG 218
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
75-226 2.03e-21

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: 93.31  E-value: 2.03e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPknfvfqnpdhQVVMPTVEADVAFGLGKYH--DMNQEEVKSRVI 147
Cdd:COG1245 371 IVGPNGIGKTTFAKILAGVLKPDEGEVDEDlkisyKP----------QYISPDYDGTVEEFLRSANtdDFGSSYYKTEII 440
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 148 KALeavGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTH 226
Cdd:COG1245 441 KPL---GLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF--AENRGKTAMVVDH 514
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
60-255 2.39e-21

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 92.78  E-value: 2.39e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF-------------VFQnpdHQVVMP--TV 123
Cdd:COG3845  21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDgKPVRIrsprdaialgigmVHQ---HFMLVPnlTV 97
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFGL--GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL--DES 199
Cdd:COG3845  98 AENIVLGLepTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRGARILILDEPTAVLtpQEA 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450 200 DQmgVIKAVKDLinAKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATIS 255
Cdd:COG3845 178 DE--LFEILRRL--AAEG-KSIIFITHKLREvMAIADRVTVLRRGKVVGTVDTAETS 229
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
58-197 3.99e-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: 88.18  E-value: 3.99e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNFVFQNPDHQVV----MPTVEAD--VAFG 130
Cdd:TIGR01189  14 MLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVrWNGTPLAEQRDEPHENILylghLPGLKPElsALEN 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450   131 LGKYHDMNQEEVKSrVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:TIGR01189  94 LHFWAAIHGGAQRT-IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALD 159
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
75-226 4.51e-21

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 92.18  E-value: 4.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----KPknfvfqnpdhQVVMPTVEADVAFGLGKYHDM-NQEEVKSRVIK 148
Cdd:PRK13409 370 IVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisyKP----------QYIKPDYDGTVEDLLRSITDDlGSSYYKSEIIK 439
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  149 ALeavGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKkgDVTALWVTH 226
Cdd:PRK13409 440 PL---QLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEER--EATALVVDH 512
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
57-246 6.09e-21

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 88.99  E-value: 6.09e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE----------KPKNF---VFQNPdhqvVM--- 120
Cdd:COG1101  19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDgkdvtklpeyKRAKYigrVFQDP----MMgta 94
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 P--TVEADVA--------FGLGKYHDMNQ-EEVKSRvIKALEaVGMRDYMQRPIQTLSGGQKQriaiAGALAEAC----K 185
Cdd:COG1101  95 PsmTIEENLAlayrrgkrRGLRRGLTKKRrELFREL-LATLG-LGLENRLDTKVGLLSGGQRQ----ALSLLMATltkpK 168
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450 186 VLLLDELTTFLDESDQMGVIKAVKDLINAKKgdVTALWVTHRLEE-LKYADGAVYMENGRVV 246
Cdd:COG1101 169 LLLLDEHTAALDPKTAALVLELTEKIVEENN--LTTLMVTHNMEQaLDYGNRLIMMHEGRII 228
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
62-226 1.04e-20

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: 88.23  E-value: 1.04e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  62 DCSFR-------IPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKnfVFQNPdhQVVMPTVEADV-AFGLGK 133
Cdd:cd03237  10 LGEFTleveggsISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDT--VSYKP--QYIKADYEGTVrDLLSSI 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 134 YHDM-NQEEVKSRVIKALeavGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLI 212
Cdd:cd03237  86 TKDFyTHPYFKTEIAKPL---QIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIRRFA 162
                       170
                ....*....|....*
gi 23296450 213 -NAKKgdvTALWVTH 226
Cdd:cd03237 163 eNNEK---TAFVVEH 174
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
45-254 1.07e-20

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: 89.79  E-value: 1.07e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    45 LCFSVSTRQGisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV----------------EKPK- 107
Cdd:TIGR02142   1 LSARFSKRLG---DFSLDADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLngrtlfdsrkgiflppEKRRi 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   108 NFVFQNPD---HQVVMPTVEADVAFGLGKYHDMNQEEVksrvikaLEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:TIGR02142  78 GYVFQEARlfpHLSVRGNLRYGMKRARPSERRISFERV-------IELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSP 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450   185 KVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:TIGR02142 151 RLLLMDEPLAALDDPRKYEILPYLERL--HAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPIAEV 219
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
43-254 1.24e-20

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 88.31  E-value: 1.24e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   43 RNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKP------KNFVFQNPD 115
Cdd:PRK10575  15 RNVSFRVPGRT-----LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLdAQPleswssKAFARKVAY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  116 HQVVMP-----TVEADVAFG-------LGKYHDMNQEevksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:PRK10575  90 LPQQLPaaegmTVRELVAIGrypwhgaLGRFGAADRE----KVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQD 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  184 CKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK10575 166 SRCLLLDEPTSALDIAHQVDVLALVHRL--SQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAEL 235
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
49-249 1.39e-20

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The amino terminal domain (pfam03412) processes the N-terminal leader peptide from the bacteriocin while C-terminal domains resemble ABC transporter membrane protein and ATP-binding cassette domain. In general, bacteriocins are agents which are responsible for killing or inhibiting the closely related species or even different strains of the same species. Bacteriocins are usually encoded by bacterial plasmids. Bacteriocins are named after the species and hence in literature one encounters various names e.g., leucocin from Leuconostic geldium; pedicocin from Pedicoccus acidilactici; sakacin from Lactobacillus sake etc. [Protein fate, Protein and peptide secretion and trafficking, Protein fate, Protein modification and repair, Transport and binding proteins, Other]


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 90.95  E-value: 1.39e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------------EKPKNFVFQNPd 115
Cdd:TIGR01193 479 VSYSYGYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLngfslkdidrhtlRQFINYLPQEP- 557
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   116 hqvVMPTVEADVAFGLGKYHDMNQEEVKsrviKALEAVGMRD---YMQRPIQT--------LSGGQKQRIAIAGALAEAC 184
Cdd:TIGR01193 558 ---YIFSGSILENLLLGAKENVSQDEIW----AACEIAEIKDdieNMPLGYQTelseegssISGGQKQRIALARALLTDS 630
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450   185 KVLLLDELTTFLDESDQMgviKAVKDLINAKkgDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR01193 631 KVLILDESTSNLDTITEK---KIVNNLLNLQ--DKTIIFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
49-226 1.61e-20

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: 87.08  E-value: 1.61e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  49 VSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PK-----NFVFQ 112
Cdd:cd03292   6 VTKTYPNGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGqdvsdlrgraiPYlrrkiGVVFQ 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 N----PDHqvvmpTVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:cd03292  86 DfrllPDR-----NVYENVAFAL-EVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILI 159
                       170       180       190
                ....*....|....*....|....*....|....*...
gi 23296450 189 LDELTTFLDESDQMGVIKAVKDlINakKGDVTALWVTH 226
Cdd:cd03292 160 ADEPTGNLDPDTTWEIMNLLKK-IN--KAGTTVVVATH 194
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
40-249 1.97e-20

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 89.32  E-value: 1.97e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVSTrqgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKN---------- 108
Cdd:PRK11000   4 VTLRNVTKAYGD-----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIgEKRMNdvppaergvg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 FVFQNpdhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK11000  79 MVFQS---YALYPhlSVAENMSFGL-KLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  187 LLLDELTTFLDES--DQMGV-IKAVKdlinaKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK11000 155 FLLDEPLSNLDAAlrVQMRIeISRLH-----KRLGRTMIYVTHdQVEAMTLADKIVVLDAGRVAQVG 216
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
64-254 2.11e-20

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 86.94  E-value: 2.11e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------KPKNFVFQNPD---HQvvmpTVEADVAF 129
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNgqdhtttppsrRPVSMLFQENNlfsHL----TVAQNIGL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  130 GLGKYHDMNQEEvKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:PRK10771  95 GLNPGLKLNAAQ-REKLHAIARQMGIEDLLARlPGQ-LSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLV 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  209 KDLINAKkgDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK10771 173 SQVCQER--QLTLLMVSHSLEDaARIAPRSLVVADGRIAWDGPTDEL 217
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
40-249 2.23e-20

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 90.08  E-value: 2.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE--KPKNFVFQNPDHQ 117
Cdd:PRK11176 342 IEFRNVTF---TYPGKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDghDLRDYTLASLRNQ 418
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 VVM---------PTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVgmrDYMQRPIQT--------LSGGQKQRIAIAGAL 180
Cdd:PRK11176 419 VALvsqnvhlfnDTIANNIAYARTEQYSREQIEEAARMAYAMDFI---NKMDNGLDTvigengvlLSGGQRQRIAIARAL 495
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  181 AEACKVLLLDELTTFLD-ESDqmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK11176 496 LRDSPILILDEATSALDtESE-----RAIQAALDELQKNRTSLVIAHRLSTIEKADEILVVEDGEIVERG 560
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
31-235 3.17e-20

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 89.87  E-value: 3.17e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  31 RIKFSDNVAVECRNLcfSVSTRQGisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFV 110
Cdd:COG4178 354 RIETSEDGALALEDL--TLRTPDG--RPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGARVL 429
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 F--QNP-------DHQVVMPTVEadvafglgkyHDMNQEEVKsrviKALEAVGMRDYMQRP------IQTLSGGQKQRIA 175
Cdd:COG4178 430 FlpQRPylplgtlREALLYPATA----------EAFSDAELR----EALEAVGLGHLAERLdeeadwDQVLSLGEQQRLA 495
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 176 IAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYAD 235
Cdd:COG4178 496 FARLLLHKPDWLFLDEATSALDEENE----AALYQLLREELPGTTVISVGHRSTLAAFHD 551
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
43-254 3.68e-20

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: 89.36  E-value: 3.68e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  43 RNLcfSVSTRQG-ISVPILRDCSFRIPSGQLWMILGPNGCGKS----TLLKILAGVVNPSSGTVFVE------KPKN--- 108
Cdd:COG4172  10 EDL--SVAFGQGgGTVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDgqdllgLSERelr 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --------FVFQ------NPDHqvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGGQ 170
Cdd:COG4172  88 rirgnriaMIFQepmtslNPLH-----TIGKQIAEVLRLHRGLSGAAARARALELLERVGIPDPERRldayPHQ-LSGGQ 161
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLiNAKKGdvTALW-VTH-----RleelKYADGAVYMENGR 244
Cdd:COG4172 162 RQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDL-QRELG--MALLlITHdlgvvR----RFADRVAVMRQGE 234
                       250
                ....*....|
gi 23296450 245 VVRHGDAATI 254
Cdd:COG4172 235 IVEQGPTAEL 244
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
40-226 3.79e-20

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 84.04  E-value: 3.79e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTvfVEKPKNFVFQnpdhqvv 119
Cdd:cd03221   1 IELENLSKTYGGK-----LLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGI--VTWGSTVKIG------- 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 mptveadvafglgkyhdmnqeevksrvikaleavgmrdYMQRpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLD-E 198
Cdd:cd03221  67 --------------------------------------YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDlE 104
                       170       180
                ....*....|....*....|....*...
gi 23296450 199 SdqmgvIKAVKDLINAKKGDVtaLWVTH 226
Cdd:cd03221 105 S-----IEALEEALKEYPGTV--ILVSH 125
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
47-254 4.97e-20

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 86.43  E-value: 4.97e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  47 FSVSTRQGisvPIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFV-EKP------------KNFVFQN 113
Cdd:COG4138   6 VAVAGRLG---PI----SAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLnGRPlsdwsaaelarhRAYLSQQ 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 114 PDHQVVMPtveadvAF---GLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGAL--------AE 182
Cdd:COG4138  78 QSPPFAMP------VFqylALHQPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwptinPE 151
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 183 AcKVLLLDELTTFLDESDQmgviKAVKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:COG4138 152 G-QLLLLDEPMNSLDVAQQ----AALDRLLRelCQQG-ITVVMSSHDLNHtLRHADRVWLLKQGKLVASGETAEV 220
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
33-229 1.68e-19

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 84.24  E-value: 1.68e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  33 KFSDNVAVECRNLC--FSVSTRQgISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFV 110
Cdd:COG2401  18 SSVLDLSERVAIVLeaFGVELRV-VERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQF 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 111 FQNpdhqvvMPTVEAdvafgLGKYHDMNQeevksrVIKALEAVGMRD--YMQRPIQTLSGGQKQRIAIAGALAEACKVLL 188
Cdd:COG2401  97 GRE------ASLIDA-----IGRKGDFKD------AVELLNAVGLSDavLWLRRFKELSTGQKFRFRLALLLAERPKLLV 159
                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 23296450 189 LDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLE 229
Cdd:COG2401 160 IDEFCSHLDRQTAKRVARNLQKL--ARRAGITLVVATHHYD 198
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
40-254 1.78e-19

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 86.17  E-value: 1.78e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVSTRQGI-----SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF------VEKPK- 107
Cdd:PRK11308   6 LQAIDLKKHYPVKRGLfkperLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYyqgqdlLKADPe 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  108 ---------NFVFQNPdHQVVMP--TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIA 175
Cdd:PRK11308  86 aqkllrqkiQIVFQNP-YGSLNPrkKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIA 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  176 IAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11308 165 IARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDL--QQELGLSYVFISHDLSVVEHiADEVMVMYLGRCVEKGTKEQI 242
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
60-226 2.56e-19

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 85.52  E-value: 2.56e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV------EKPKNFVfqnpdHQ--VVM----------P 121
Cdd:COG4586  38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVlgyvpfKRRKEFA-----RRigVVFgqrsqlwwdlP 112
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 TVEadvAFGL-GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESD 200
Cdd:COG4586 113 AID---SFRLlKAIYRIPDAEYKKRLDELVELLDLGELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVS 189
                       170       180
                ....*....|....*....|....*.
gi 23296450 201 QMGVIKAVKDlINAKKGdVTALWVTH 226
Cdd:COG4586 190 KEAIREFLKE-YNRERG-TTILLTSH 213
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
39-254 2.97e-19

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 84.42  E-value: 2.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   39 AVECRNLcfsvsTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-------EKPKN--- 108
Cdd:PRK11264   3 AIEVKNL-----VKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVgditidtARSLSqqk 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 -----------FVFQN----PDHQVVMPTVEADVAFglgkyHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQR 173
Cdd:PRK11264  78 glirqlrqhvgFVFQNfnlfPHRTVLENIIEGPVIV-----KGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  174 IAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKgdvTALWVTHRLEELK-YADGAVYMENGRVVRHGDAA 252
Cdd:PRK11264 153 VAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKR---TMVIVTHEMSFARdVADRAIFMDQGRIVEQGPAK 229

                 ..
gi 23296450  253 TI 254
Cdd:PRK11264 230 AL 231
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
43-251 3.04e-19

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 83.96  E-value: 3.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  43 RNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG--VVNPSSGTVFVEKpKN------------ 108
Cdd:COG0396   4 KNLHVSVEGK-----EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpKYEVTSGSILLDG-EDilelspderara 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FV-FQNPdhqVVMPTV-------EADVAFGLGKyhdMNQEEVKSRVIKALEAVGM-RDYMQRPI-QTLSGGQKQRIAI 176
Cdd:COG0396  78 giFLaFQYP---VEIPGVsvsnflrTALNARRGEE---LSAREFLKLLKEKMKELGLdEDFLDRYVnEGFSGGEKKRNEI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 177 AGALAEACKVLLLDELTTFLDeSDqmgVIKAVKDLINA-KKGDVTALWVTH--RLeeLKY--ADGAVYMENGRVVRHGDA 251
Cdd:COG0396 152 LQMLLLEPKLAILDETDSGLD-ID---ALRIVAEGVNKlRSPDRGILIITHyqRI--LDYikPDFVHVLVDGRIVKSGGK 225
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
64-197 3.07e-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: 83.31  E-value: 3.07e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkPKNFVFQNPD---------HQVVMPT---VEADVAFgl 131
Cdd:cd03231  20 SFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLN-GGPLDFQRDSiargllylgHAPGIKTtlsVLENLRF-- 96
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 132 gkYHDMNQEEvksRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:cd03231  97 --WHADHSDE---QVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALD 157
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
54-243 4.59e-19

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: 83.15  E-value: 4.59e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF--VEKPKNFVFQNPDHQ-------------V 118
Cdd:cd03290  11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHwsNKNESEPSFEATRSRnrysvayaaqkpwL 90
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 119 VMPTVEADVAFGlgkyHDMNQEEVKSrVIKALEAVGMRDYMQRPIQT--------LSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:cd03290  91 LNATVEENITFG----SPFNKQRYKA-VTDACSLQPDIDLLPFGDQTeigerginLSGGQRQRICVARALYQNTNIVFLD 165
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450 191 ELTTFLD--ESD---QMGVIKAVKDlinAKKgdvTALWVTHRLEELKYADGAVYMENG 243
Cdd:cd03290 166 DPFSALDihLSDhlmQEGILKFLQD---DKR---TLVLVTHKLQYLPHADWIIAMKDG 217
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
60-226 5.38e-19

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 83.00  E-value: 5.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-----VEKPKN-----------FVFQnpDHQVVMP-T 122
Cdd:PRK10908  18 LQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWfsghdITRLKNrevpflrrqigMIFQ--DHHLLMDrT 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQR-PIQtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQ 201
Cdd:PRK10908  96 VYDNVAIPL-IIAGASGDDIRRRVSAALDKVGLLDKAKNfPIQ-LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALS 173
                        170       180
                 ....*....|....*....|....*
gi 23296450  202 MGVIKAVKDLinaKKGDVTALWVTH 226
Cdd:PRK10908 174 EGILRLFEEF---NRVGVTVLMATH 195
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
35-250 2.02e-18

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 84.49  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   35 SDNVAVECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKN----- 108
Cdd:PRK11160 334 ADQVSLTLNNVSFTYPDQP---QPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLnGQPIAdysea 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 -------FVFQNPDhqVVMPTVEADVAFGLGKYHDmnqeevkSRVIKALEAVGMRDYMQ-------------RPiqtLSG 168
Cdd:PRK11160 411 alrqaisVVSQRVH--LFSATLRDNLLLAAPNASD-------EALIEVLQQVGLEKLLEddkglnawlgeggRQ---LSG 478
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  169 GQKQRIAIAGALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVR 247
Cdd:PRK11160 479 GEQRRLGIARALLHDAPLLLLDEPTEGLDaETERQ-----ILELLAEHAQNKTVLMITHRLTGLEQFDRICVMDNGQIIE 553

                 ...
gi 23296450  248 HGD 250
Cdd:PRK11160 554 QGT 556
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
51-246 5.82e-18

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: 80.39  E-value: 5.82e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  51 TRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTVFV--EKPKNFVFQN-----PDHQVVM 120
Cdd:cd03234  14 KNWNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGgttSGQILFngQPRKPDQFQKcvayvRQDDILL 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 P--TVEADVAFGLgkyHDMNQEEVKSRVIKALEA-VGMRDYMQRPI-----QTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:cd03234  94 PglTVRETLTYTA---ILRLPRKSSDAIRKKRVEdVLLRDLALTRIggnlvKGISGGERRRVSIAVQLLWDPKVLILDEP 170
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 193 TTFLDESDQMGVIKAVKDLinAKKGDvTALWVTH--RLEELKYADGAVYMENGRVV 246
Cdd:cd03234 171 TSGLDSFTALNLVSTLSQL--ARRNR-IVILTIHqpRSDLFRLFDRILLLSSGEIV 223
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
39-249 6.78e-18

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 83.09  E-value: 6.78e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   39 AVECRNLCFSV-STRQGISvpilrDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE------------- 104
Cdd:PRK13657 334 AVEFDDVSFSYdNSRQGVE-----DVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDgtdirtvtraslr 408
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  105 KPKNFVFQNPdhQVVMPTVEADVAfgLGKyHDMNQEEVKsrviKALEAVGMRDYMQRPIQ-----------TLSGGQKQR 173
Cdd:PRK13657 409 RNIAVVFQDA--GLFNRSIEDNIR--VGR-PDATDEEMR----AAAERAQAHDFIERKPDgydtvvgergrQLSGGERQR 479
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  174 IAIAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK13657 480 LAIARALLKDPPILILDEATSALDVETE----AKVKAALDELMKGRTTFIIAHRLSTVRNADRILVFDNGRVVESG 551
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
38-249 8.13e-18

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: 79.13  E-value: 8.13e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  38 VAVECRNLCFSVSTRQGISV-PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS--SGTVFV----EKPKN-- 108
Cdd:cd03213   2 VTLSFRNLTVTVKSSPSKSGkQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLIngrpLDKRSfr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 ----FVFQnpdHQVVMP--TVEadvafglgkyhdmnqeevksrvikalEAVgmrdYMQRPIQTLSGGQKQRIAIAGALAE 182
Cdd:cd03213  82 kiigYVPQ---DDILHPtlTVR--------------------------ETL----MFAAKLRGLSGGERKRVSIALELVS 128
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRL--EELKYADGAVYMENGRVVRHG 249
Cdd:cd03213 129 NPSLLFLDEPTSGLDSSSALQVMSLLRRL--ADTG-RTIICSIHQPssEIFELFDKLLLLSQGRVIYFG 194
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
58-249 1.13e-17

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: 82.18  E-value: 1.13e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHQ---------------VVmP- 121
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILI-----------DGQdirdvtqaslraaigIV-Pq 439
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 122 -------TVEADVAFGLgkyHDMNQEEVksrvIKALEAVGMRDYMQR-P--IQT--------LSGGQKQRIAIAGALAEA 183
Cdd:COG5265 440 dtvlfndTIAYNIAYGR---PDASEEEV----EAAARAAQIHDFIESlPdgYDTrvgerglkLSGGEKQRVAIARTLLKN 512
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 184 CKVLLLDELTTFLD---ESDQMGVIKAVkdlinAKkgDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:COG5265 513 PPILIFDEATSALDsrtERAIQAALREV-----AR--GRTTLVIAHRLSTIVDADEILVLEAGRIVERG 574
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
41-197 1.54e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 78.76  E-value: 1.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   41 ECRNLCfsvSTRQGisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfVEKPKNFVFQNPD----- 115
Cdd:PRK13539   4 EGEDLA---CVRGG--RVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTI-KLDGGDIDDPDVAeachy 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  116 --HQVVMP---TVEADVAFGLGKYhdmNQEEvkSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:PRK13539  78 lgHRNAMKpalTVAENLEFWAAFL---GGEE--LDIAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILD 152

                 ....*..
gi 23296450  191 ELTTFLD 197
Cdd:PRK13539 153 EPTAALD 159
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
59-249 2.06e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 80.23  E-value: 2.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKP---------------KNFVFQNPDHQVVmpt 122
Cdd:PRK13537  22 VVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSIsLCGEPvpsrarharqrvgvvPQFDNLDPDFTVR--- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 vEADVAFGlgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQM 202
Cdd:PRK13537  99 -ENLLVFG--RYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQARH 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 23296450  203 GVIKAVKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13537 176 LMWERLRSLLARGK---TILLTTHFMEEAeRLCDRLCVIEEGRKIAEG 220
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
56-249 2.57e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 78.80  E-value: 2.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVN--PS---SGTVFVEKPKNF-------------VFQNPDHq 117
Cdd:PRK14247  15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIElyPEarvSGEVYLDGQDIFkmdvielrrrvqmVFQIPNP- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 vvMPTVE--ADVAFGLgKYHDM--NQEEVKSRVIKALEAVGM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:PRK14247  94 --IPNLSifENVALGL-KLNRLvkSKKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLA 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450  190 DELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTH-RLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK14247 171 DEPTANLDPENT----AKIESLFLELKKDMTIVLVTHfPQQAARISDYVAFLYKGQIVEWG 227
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
61-211 2.90e-17

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 77.92  E-value: 2.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   61 RDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF-----VEKpknfvfQNPD---------HQV-VMP--TV 123
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLwqgepIRR------QRDEyhqdllylgHQPgIKTelTA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  124 EADVAFglgkYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdqmg 203
Cdd:PRK13538  92 LENLRF----YQRLHGPGDDEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDK----- 162

                 ....*...
gi 23296450  204 viKAVKDL 211
Cdd:PRK13538 163 --QGVARL 168
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
65-233 3.73e-17

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: 78.56  E-value: 3.73e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  65 FRIP---SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTvFVEKP------KNF---VFQNPDHQVVMPTVEADVAfglG 132
Cdd:cd03236  18 HRLPvprEGQVLGLVGPNGIGKSTALKILAGKLKPNLGK-FDDPPdwdeilDEFrgsELQNYFTKLLEGDVKVIVK---P 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 133 KYHDMNQEEVKSRVIKALEAV---GMRDY----------MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:cd03236  94 QYVDLIPKAVKGKVGELLKKKderGKLDElvdqlelrhvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
                       170       180       190
                ....*....|....*....|....*....|....
gi 23296450 200 DQMGVIKAVKDLINAKKgdvTALWVTHRLEELKY 233
Cdd:cd03236 174 QRLNAARLIRELAEDDN---YVLVVEHDLAVLDY 204
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
52-249 3.89e-17

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 80.46  E-value: 3.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   52 RQGISVPIlRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-----------------KPKNFVFQNp 114
Cdd:PRK10070  37 KTGLSLGV-KDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDgvdiakisdaelrevrrKKIAMVFQS- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  115 dhQVVMP--TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK10070 115 --FALMPhmTVLDNTAFGM-ELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEA 191
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450  193 TTFLDE------SDQMGVIKAvkdlinakKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHG 249
Cdd:PRK10070 192 FSALDPlirtemQDELVKLQA--------KHQRTIVFISHDLDEaMRIGDRIAIMQNGEVVQVG 247
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
37-226 3.98e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 78.35  E-value: 3.98e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   37 NVAVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKIL--------------------AGVVNP 96
Cdd:PRK14267   2 KFAIETVNLRVYYGSNH-----VIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFnrllelneearvegevrlfgRNIYSP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   97 SSGTVFVEKPKNFVFQNPDHQVVMpTVEADVAFGLgKYHDM--NQEEVKSRVIKALEAVGMRDYMQRPIQ----TLSGGQ 170
Cdd:PRK14267  77 DVDPIEVRREVGMVFQYPNPFPHL-TIYDNVAIGV-KLNGLvkSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQ 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  171 KQRIAIAGALAEACKVLLLDELTTFLDEsdqMGVIKaVKDLINAKKGDVTALWVTH 226
Cdd:PRK14267 155 RQRLVIARALAMKPKILLMDEPTANIDP---VGTAK-IEELLFELKKEYTIVLVTH 206
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
58-249 4.13e-17

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 79.87  E-value: 4.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV---EKPKNFVFQNPDHQVVMPTVEADVAFGL--- 131
Cdd:PRK13536  55 AVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVlgvPVPARARLARARIGVVPQFDNLDLEFTVren 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  132 ----GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKA 207
Cdd:PRK13536 135 llvfGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHLIWER 214
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23296450  208 VKDLINAKKgdvTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:PRK13536 215 LRSLLARGK---TILLTTHFMEEAeRLCDRLCVLEAGRKIAEG 254
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
43-269 6.35e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 80.13  E-value: 6.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   43 RNLcfSVSTRQGISV-PILRDCSFRIPSGQLWMILGPNGCGKS-TLLKIL-----AGVVNPSSGTVF-------VEKPK- 107
Cdd:PRK15134   9 ENL--SVAFRQQQTVrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILrllpsPPVVYPSGDIRFhgesllhASEQTl 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  108 --------NFVFQ------NPDHqvvmpTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGG 169
Cdd:PRK15134  87 rgvrgnkiAMIFQepmvslNPLH-----TLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdyPHQ-LSGG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  170 QKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRH 248
Cdd:PRK15134 161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLREL--QQELNMGLLFITHNLSIVrKLADRVAVMQNGRCVEQ 238
                        250       260
                 ....*....|....*....|.
gi 23296450  249 GDAATIsdfIKAKQSSYIDQI 269
Cdd:PRK15134 239 NRAATL---FSAPTHPYTQKL 256
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
56-249 7.04e-17

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: 80.17  E-value: 7.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPKNFVFQnpDHQVVMPT 122
Cdd:TIGR01846 469 SPEVLSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDgvdlaiadpawlrRQMGVVLQ--ENVLFSRS 546
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   123 VEADVAFGlgkyhdmNQEEVKSRVIKALEAVGMRDYMQRPIQ-----------TLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:TIGR01846 547 IRDNIALC-------NPGAPFEHVIHAAKLAGAHDFISELPQgyntevgekgaNLSGGQRQRIAIARALVGNPRILIFDE 619
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450   192 LTTFLD-ESDQmgVIKAVKDLINAKKgdvTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR01846 620 ATSALDyESEA--LIMRNMREICRGR---TVIIIAHRLSTVRACDRIIVLEKGQIAESG 673
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
37-222 7.92e-17

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: 77.09  E-value: 7.92e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  37 NVAVECRNLC--FSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFV--FQ 112
Cdd:COG4778   2 TTLLEVENLSktFTLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDGGWVdlAQ 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 113 NPDHQV----------------VMPTVEA-DVafglgkyhdmnqeevksrVIKALEAVGM---------RDYMQR----- 161
Cdd:COG4778  82 ASPREIlalrrrtigyvsqflrVIPRVSAlDV------------------VAEPLLERGVdreeararaRELLARlnlpe 143
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 162 -----PIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMgvikAVKDLINAKKGDVTAL 222
Cdd:COG4778 144 rlwdlPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRA----VVVELIEEAKARGTAI 205
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
39-231 8.89e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 77.77  E-value: 8.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   39 AVECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILaGVVNPSSGTVFVEKPKNFVFQN----- 113
Cdd:PRK14258   7 AIKVNNLSFYYDTQK-----ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCL-NRMNELESEVRVEGRVEFFNQNiyerr 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  114 --------------PDHQVVMPTVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQT----LSGGQKQRIA 175
Cdd:PRK14258  81 vnlnrlrrqvsmvhPKPNLFPMSVYDNVAYGVKIVGWRPKLEIDDIVESALKDADLWDEIKHKIHKsaldLSGGQQQRLC 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  176 IAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL 231
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSL--RLRSELTMVIVSHNLHQV 214
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
41-261 9.87e-17

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 76.41  E-value: 9.87e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGvvnpssgtvfvekpknfvfqNPDHQVvm 120
Cdd:cd03217   2 EIKDLHVSVGGKE-----ILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG--------------------HPKYEV-- 54
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 ptVEADVAFglgKYHDMNQEEVKSRvikALEAVGMRdyMQRPIQ---------------TLSGGQKQRIAIAGALAEACK 185
Cdd:cd03217  55 --TEGEILF---KGEDITDLPPEER---ARLGIFLA--FQYPPEipgvknadflryvneGFSGGEKKRNEILQLLLLEPD 124
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450 186 VLLLDELTTFLDesdqMGVIKAVKDLINA-KKGDVTALWVTHRLEELKY--ADGAVYMENGRVVRHGDaATISDFIKAK 261
Cdd:cd03217 125 LAILDEPDSGLD----IDALRLVAEVINKlREEGKSVLIITHYQRLLDYikPDRVHVLYDGRIVKSGD-KELALEIEKK 198
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
59-228 1.77e-16

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 76.69  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfVEKPKNFVFQNPDHQVVMPTVEADVafglGKYHDMN 138
Cdd:PRK09544  19 VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI-KRNGKLRIGYVPQKLYLDTTLPLTV----NRFLRLR 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  139 QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMgvikAVKDLINA--KK 216
Cdd:PRK09544  94 PGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQV----ALYDLIDQlrRE 169
                        170
                 ....*....|..
gi 23296450  217 GDVTALWVTHRL 228
Cdd:PRK09544 170 LDCAVLMVSHDL 181
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
67-249 3.16e-16

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 76.20  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   67 IPSGQLWMILGPNGCGKSTLLKILAGVVN----PSSGTVF--------------VEKPK---NFVFQNPDhQVVMPTVEA 125
Cdd:PRK09984  27 IHHGEMVALLGPSGSGKSTLLRHLSGLITgdksAGSHIELlgrtvqregrlardIRKSRantGYIFQQFN-LVNRLSVLE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  126 DVAFG-LG---------KYHDMNQeevKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK09984 106 NVLIGaLGstpfwrtcfSWFTREQ---KQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILADEPIAS 182
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 23296450  196 LDESDQMGVIKAVKDlINAKKGdVTALWVTHRLE-ELKYADGAVYMENGRVVRHG 249
Cdd:PRK09984 183 LDPESARIVMDTLRD-INQNDG-ITVVVTLHQVDyALRYCERIVALRQGHVFYDG 235
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
58-243 5.64e-16

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: 75.66  E-value: 5.64e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfveKPKNFVFQNPDHQVVMP-TVEADVAFGLgkyhD 136
Cdd:cd03291  51 PVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI---KHSGRISFSSQFSWIMPgTIKENIIFGV----S 123
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 137 MNQEEVKSrVIKA------LEAVGMRDY--MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:cd03291 124 YDEYRYKS-VVKAcqleedITKFPEKDNtvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTEKEIFESC 202
                       170       180       190
                ....*....|....*....|....*....|....*
gi 23296450 209 KDLINAKKgdvTALWVTHRLEELKYADGAVYMENG 243
Cdd:cd03291 203 VCKLMANK---TRILVTSKMEHLKKADKILILHEG 234
PTZ00243 PTZ00243
ABC transporter; Provisional
59-259 1.33e-15

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 76.36  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPdhQVVMPTVEADVAFglgkyhdmN 138
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAERSIAYVPQQA--WIMNATVRGNILF--------F 744
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   139 QEEVKSRVIKA-----LEAvgmrDYMQRP--IQT--------LSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdQMG 203
Cdd:PTZ00243  745 DEEDAARLADAvrvsqLEA----DLAQLGggLETeigekgvnLSGGQKARVSLARAVYANRDVYLLDDPLSALDA--HVG 818
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450   204 ViKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAAtisDFIK 259
Cdd:PTZ00243  819 E-RVVEECFLGALAGKTRVLATHQVHVVPRADYVVALGDGRVEFSGSSA---DFMR 870
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
39-249 2.42e-15

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 75.52  E-value: 2.42e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   39 AVECRNLCFSVSTRQgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPknfvFQNPDHQ 117
Cdd:PRK10790 340 RIDIDNVSFAYRDDN----LVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDgRP----LSSLSHS 411
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 VV-----M----PTVEADVAFG---LGKyhDMNQEevksRVIKALEAV-------GMRDYMQRPI----QTLSGGQKQRI 174
Cdd:PRK10790 412 VLrqgvaMvqqdPVVLADTFLAnvtLGR--DISEE----QVWQALETVqlaelarSLPDGLYTPLgeqgNNLSVGQKQLL 485
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450  175 AIAGALAEACKVLLLDELTTFLDEsdqmGVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:PRK10790 486 ALARVLVQTPQILILDEATANIDS----GTEQAIQQALAAVREHTTLVVIAHRLSTIVEADTILVLHRGQAVEQG 556
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
57-255 2.44e-15

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 75.35  E-value: 2.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPS---SGTVFVE-KPKnfVFQN-PD---------HQVVMPT 122
Cdd:PRK13549  18 VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVY-PHgtyEGEIIFEgEEL--QASNiRDteragiaiiHQELALV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVA---FgLG----KYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK13549  95 KELSVLeniF-LGneitPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450  196 LDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATIS 255
Cdd:PRK13549 174 LTESETAVLLDIIRDL---KAHGIACIYISHKLNEVKaISDTICVIRDGRHIGTRPAAGMT 231
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
56-247 2.46e-15

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 75.53  E-value: 2.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK-----------------NFVFQ------ 112
Cdd:PRK10535  20 QVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDvatldadalaqlrrehfGFIFQryhlls 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  113 --NPDHQVVMPTVEAdvafGLGKyhdmnqEEVKSRVIKALEAVGMRDYMQ-RPIQtLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:PRK10535 100 hlTAAQNVEVPAVYA----GLER------KQRLLRAQELLQRLGLEDRVEyQPSQ-LSGGQQQRVSIARALMNGGQVILA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  190 DELTTFLDESDQMGVIKAVKDLinAKKGDvTALWVTHRLEELKYADGAVYMENGRVVR 247
Cdd:PRK10535 169 DEPTGALDSHSGEEVMAILHQL--RDRGH-TVIIVTHDPQVAAQAERVIEIRDGEIVR 223
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
40-235 3.01e-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: 71.42  E-value: 3.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLcfSVSTRQGIsvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTvfVEKPKN----FVFQNPd 115
Cdd:cd03223   1 IELENL--SLATPDGR--VLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGR--IGMPEGedllFLPQRP- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 116 hqvvmptveadvafglgkYhdMNQEEVKSRVIKALEavgmrdymqrpiQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:cd03223  74 ------------------Y--LPLGTLREQLIYPWD------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSA 121
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 23296450 196 LDESDQMGVIKAVKDLInakkgdVTALWVTHRLEELKYAD 235
Cdd:cd03223 122 LDEESEDRLYQLLKELG------ITVISVGHRPSLWKFHD 155
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
40-246 3.85e-15

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: 72.53  E-value: 3.85e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLcfSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK------PKN----- 108
Cdd:cd03244   3 IEFKNV--SLRYRPN-LPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGvdiskiGLHdlrsr 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 109 --FVFQNPdhqVVMP-TVEADVAFgLGKYHDmnqeevkSRVIKALEAVGMRDY-MQRPIQ----------TLSGGQKQRI 174
Cdd:cd03244  80 isIIPQDP---VLFSgTIRSNLDP-FGEYSD-------EELWQALERVGLKEFvESLPGGldtvveeggeNLSVGQRQLL 148
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450 175 AIAGALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVV 246
Cdd:cd03244 149 CLARALLRKSKILVLDEATASVDpETDAL-----IQKTIREAFKDCTVLTIAHRLDTIIDSDRILVLDKGRVV 216
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
33-242 3.91e-15

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 75.07  E-value: 3.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    33 KFSDNVAVECRNLCFSVSTRQgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNF--- 109
Cdd:PTZ00265  376 KLKDIKKIQFKNVRFHYDTRK--DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSHNLkdi 453
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   110 -----------VFQNP---------------------------------DHQVVMPTVEADVAFGLGKYHDMNQE----- 140
Cdd:PTZ00265  454 nlkwwrskigvVSQDPllfsnsiknnikyslyslkdlealsnyynedgnDSQENKNKRNSCRAKCAGDLNDMSNTtdsne 533
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   141 --EVK--------SRVIKALEAVGMRDYMQ-----------RPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PTZ00265  534 liEMRknyqtikdSEVVDVSKKVLIHDFVSalpdkyetlvgSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNK 613
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 23296450   200 DQMGVIKAVKDLiNAKKGDVTALwVTHRLEELKYADGAVYMEN 242
Cdd:PTZ00265  614 SEYLVQKTINNL-KGNENRITII-IAHRLSTIRYANTIFVLSN 654
hmuV PRK13547
heme ABC transporter ATP-binding protein;
59-254 4.23e-15

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 73.32  E-value: 4.23e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG----VVNPSSGTVFVEKPKNfvfQNPDHQV----------VMPTvE 124
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdltgGGAPRGARVTGDVTLN---GEPLAAIdaprlarlraVLPQ-A 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 ADVAFG--------LGKY-HDMNQEEVKSR----VIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE--------- 182
Cdd:PRK13547  92 AQPAFAfsareivlLGRYpHARRAGALTHRdgeiAWQALALAGATALVGRDVTTLSGGELARVQFARVLAQlwpphdaaq 171
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450  183 ACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13547 172 PPRYLLLDEPTAALDLAHQHRLLDTVRRL--ARDWNLGVLAIVHDPNlAARHADRIAMLADGAIVAHGAPADV 242
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
58-243 4.59e-15

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: 74.95  E-value: 4.59e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfveKPKNFVFQNPDHQVVMP-TVEADVAFGLgkyhd 136
Cdd:TIGR01271  440 PVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI---KHSGRISFSPQTSWIMPgTIKDNIIFGL----- 511
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    137 mNQEEVKSR-VIKA--LEavgmRDYMQRPIQ----------TLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:TIGR01271  512 -SYDEYRYTsVIKAcqLE----EDIALFPEKdktvlgeggiTLSGGQRARISLARAVYKDADLYLLDSPFTHLDVVTEKE 586
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 23296450    204 VIKA-VKDLINAKkgdvTALWVTHRLEELKYADGAVYMENG 243
Cdd:TIGR01271  587 IFEScLCKLMSNK----TRILVTSKLEHLKKADKILLLHEG 623
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
59-254 4.77e-15

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 72.69  E-value: 4.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK--------------------------NFVFQ 112
Cdd:PRK10619  20 VLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTinlvrdkdgqlkvadknqlrllrtrlTMVFQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  113 NPD---HQVVMPTV-EADV-AFGLGKyhdmnqEEVKSRVIKALEAVGMRDYMQR--PIQtLSGGQKQRIAIAGALAEACK 185
Cdd:PRK10619 100 HFNlwsHMTVLENVmEAPIqVLGLSK------QEARERAVKYLAKVGIDERAQGkyPVH-LSGGQQQRVSIARALAMEPE 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  186 VLLLDELTTFLDESDQMGVIKAVKDLinAKKGDvTALWVTHRLEELKYADGAV-YMENGRVVRHGDAATI 254
Cdd:PRK10619 173 VLLFDEPTSALDPELVGEVLRIMQQL--AEEGK-TMVVVTHEMGFARHVSSHViFLHQGKIEEEGAPEQL 239
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
65-216 9.01e-15

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ribosomal structure and biogenesis];


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 73.67  E-value: 9.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  65 FRIP---SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQ---------------NPDHQVVM-Ptvea 125
Cdd:COG1245  91 YGLPvpkKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEPSWDEVLKrfrgtelqdyfkklaNGEIKVAHkP---- 166
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 126 dvafglgKYHDMNQEEVKSRVIKALEAV-------------GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:COG1245 167 -------QYVDLIPKVFKGTVRELLEKVdergkldelaeklGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
                       170       180
                ....*....|....*....|....
gi 23296450 193 TTFLDESDQMGVIKAVKDLINAKK 216
Cdd:COG1245 240 SSYLDIYQRLNVARLIRELAEEGK 263
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
37-197 9.38e-15

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 73.82  E-value: 9.38e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    37 NVAVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPK-NFVFQNP 114
Cdd:TIGR03719 320 DKVIEAENLTKAFGDK-----LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIgETVKlAYVDQSR 394
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   115 DHQVVMPTVEADVAFGLgKYHDMNQEEVKSRVIkaleaVGMRDYM----QRPIQTLSGGQKQRIAIAGALAEACKVLLLD 190
Cdd:TIGR03719 395 DALDPNKTVWEEISGGL-DIIKLGKREIPSRAY-----VGRFNFKgsdqQKKVGQLSGGERNRVHLAKTLKSGGNVLLLD 468

                  ....*..
gi 23296450   191 ELTTFLD 197
Cdd:TIGR03719 469 EPTNDLD 475
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
41-269 9.74e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 73.59  E-value: 9.74e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   41 ECRNLCFSVSTRQGISVPI------LRDCSFRIPSGQLWMILGPNGCGKST----LLKILAgvvnpSSGTV-FVEKP-KN 108
Cdd:PRK15134 277 DVEQLQVAFPIRKGILKRTvdhnvvVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIwFDGQPlHN 351
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 F--------------VFQNPdHQVVMP--TVEADVAFGLGKYH-DMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQ 170
Cdd:PRK15134 352 LnrrqllpvrhriqvVFQDP-NSSLNPrlNVLQIIEEGLRVHQpTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQ 430
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHG 249
Cdd:PRK15134 431 RQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSL--QQKHQLAYLFISHDLHVVRaLCHQVIVLRQGEVVEQG 508
                        250       260
                 ....*....|....*....|
gi 23296450  250 DAATIsdfIKAKQSSYIDQI 269
Cdd:PRK15134 509 DCERV---FAAPQQEYTRQL 525
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
57-255 1.08e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 73.28  E-value: 1.08e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpKNFVFQNPDHQVVMP--------------- 121
Cdd:PRK09700  18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITI---NNINYNKLDHKLAAQlgigiiyqelsvide 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  122 -TVEADVAFG---LGKYHDMN---QEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:PRK09700  95 lTVLENLYIGrhlTKKVCGVNiidWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTS 174
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23296450  195 FL--DESDQMGVIkavkdlINAKKGDVTAL-WVTHRLEELK-YADGAVYMENGRVVRHGDAATIS 255
Cdd:PRK09700 175 SLtnKEVDYLFLI------MNQLRKEGTAIvYISHKLAEIRrICDRYTVMKDGSSVCSGMVSDVS 233
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
75-261 1.19e-14

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 71.73  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   75 ILGPNGCGKSTLLKIL--------------------AGVVNPSSGTVFVEKPKNFVFQNPDHqvvMP-TVEADVAFGLGK 133
Cdd:PRK14239  36 LIGPSGSGKSTLLRSInrmndlnpevtitgsivyngHNIYSPRTDTVDLRKEIGMVFQQPNP---FPmSIYENVVYGLRL 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  134 YHDMNQEEVKSRVIKALEAVGM----RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsdqmgvIKA-- 207
Cdd:PRK14239 113 KGIKDKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTSALDP------ISAgk 186
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23296450  208 VKDLINAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI---------SDFIKAK 261
Cdd:PRK14239 187 IEETLLGLKDDYTMLLVTRSMQQAsRISDRTGFFLDGDLIEYNDTKQMfmnpkhketEDYISGK 250
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
40-256 2.11e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 72.39  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVStrqgiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNFVFQNPDHQV 118
Cdd:PRK15439  12 LCARSISKQYS-----GVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGgNPCARLTPAKAHQL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  119 ---VMP---------TVEADVAFGLGKyhdmnQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK15439  87 giyLVPqepllfpnlSVKENILFGLPK-----RQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSRI 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450  187 LLLDELTTFLDESDQMGVIKAVKDLINakKGdVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK15439 162 LILDEPTASLTPAETERLFSRIRELLA--QG-VGIVFISHKLPEIrQLADRISVMRDGTIALSGKTADLST 229
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
65-235 2.25e-14

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 72.53  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   65 FRIPS---GQLWMILGPNGCGKSTLLKILAGVVNPSSGTvFVEKP------KNF---VFQNPDHQVVMPTVEADVafglg 132
Cdd:PRK13409  91 YGLPIpkeGKVTGILGPNGIGKTTAVKILSGELIPNLGD-YEEEPswdevlKRFrgtELQNYFKKLYNGEIKVVH----- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  133 K--YHDMNQEEVKSRVIKALEAV-------------GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK13409 165 KpqYVDLIPKVFKGKVRELLKKVdergkldevverlGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 23296450  198 ESDQMGVIKAVKDLINAKkgdvTALWVTHRLEELKY-AD 235
Cdd:PRK13409 245 IRQRLNVARLIRELAEGK----YVLVVEHDLAVLDYlAD 279
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
43-252 2.38e-14

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: 70.75  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    43 RNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGvvNPS----SGTVFV-----------EKPK 107
Cdd:TIGR01978   4 KDLHVSVEDK-----EILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSyevtSGTILFkgqdllelepdERAR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   108 NFVFQNPDHQVVMPTVEADV-----------AFGLGKYHDMN-QEEVKsrviKALEAVGM-RDYMQRPIQT-LSGGQKQR 173
Cdd:TIGR01978  77 AGLFLAFQYPEEIPGVSNLEflrsalnarrsARGEEPLDLLDfEKLLK----EKLALLDMdEEFLNRSVNEgFSGGEKKR 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   174 IAIAGALAEACKVLLLDELTTFLDesdqMGVIKAVKDLINAKKGDVTA-LWVTHRLEELKY--ADGAVYMENGRVVRHGD 250
Cdd:TIGR01978 153 NEILQMALLEPKLAILDEIDSGLD----IDALKIVAEGINRLREPDRSfLIITHYQRLLNYikPDYVHVLLDGRIVKSGD 228

                  ..
gi 23296450   251 AA 252
Cdd:TIGR01978 229 VE 230
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
62-241 2.60e-14

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: 72.47  E-value: 2.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    62 DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKN--FVFQNPdhqvvmptveadvAFGLGKYHD--- 136
Cdd:TIGR00954 470 SLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAKGKlfYVPQRP-------------YMTLGTLRDqii 536
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   137 --MNQEEVKSR------VIKALEAVGMRDYMQRPI---------QTLSGGQKQRIAIAGALAEACKVLLLDELTTfldes 199
Cdd:TIGR00954 537 ypDSSEDMKRRglsdkdLEQILDNVQLTHILEREGgwsavqdwmDVLSGGEKQRIAMARLFYHKPQFAILDECTS----- 611
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 23296450   200 dqmGVIKAVKDLI--NAKKGDVTALWVTHRLEELKYADGAVYME 241
Cdd:TIGR00954 612 ---AVSVDVEGYMyrLCREFGITLFSVSHRKSLWKYHEYLLYMD 652
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
48-254 3.41e-14

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 70.35  E-value: 3.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   48 SVSTRQGisvPIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSSGTVFV-EKPknfVFQNPDH---------- 116
Cdd:PRK03695   7 AVSTRLG---PL----SAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFaGQP---LEAWSAAelarhrayls 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  117 QVVMPTVEADVAFGLGKY-HDMNQEEVKSRVIKAL-EAVGMRDYMQRPIQTLSGGQKQRIAIAGALAE-------ACKVL 187
Cdd:PRK03695  76 QQQTPPFAMPVFQYLTLHqPDKTRTEAVASALNEVaEALGLDDKLGRSVNQLSGGEWQRVRLAAVVLQvwpdinpAGQLL 155
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  188 LLDELTTFLDESDQmgviKAVKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK03695 156 LLDEPMNSLDVAQQ----AALDRLLSelCQQG-IAVVMSSHDLNHtLRHADRVWLLKQGKLLASGRRDEV 220
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
64-250 4.49e-14

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 70.89  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------VEKPKNFVFQNPDHQV--VMpTVEA 125
Cdd:PRK15079  41 TLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAwlgkdllgmkddewraVRSDIQMIFQDPLASLnpRM-TIGE 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  126 DVAFGLGKYH-DMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK15079 120 IIAEPLRTYHpKLSRQEVKDRVKAMMLKVGLLpNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQ 199
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 23296450  204 VIKAVKDLinAKKGDVTALWVTHRLEELKY-ADGAVYMENGRVVRHGD 250
Cdd:PRK15079 200 VVNLLQQL--QREMGLSLIFIAHDLAVVKHiSDRVLVMYLGHAVELGT 245
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
40-254 1.41e-13

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: 68.34  E-value: 1.41e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  40 VECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEkpKNFVFQNPDHQ-- 117
Cdd:cd03218   1 LRAENLSKRYGKRK-----VVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLD--GQDITKLPMHKra 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 118 ----VVMP---------TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEAC 184
Cdd:cd03218  74 rlgiGYLPqeasifrklTVEENILAVL-EIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNP 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 185 KVLLLDELTTFLDE---SDQMGVIKAVKD-----LI---NAKkgdvtalwvthrlEELKYADGAVYMENGRVVRHGDAAT 253
Cdd:cd03218 153 KFLLLDEPFAGVDPiavQDIQKIIKILKDrgigvLItdhNVR-------------ETLSITDRAYIIYEGKVLAEGTPEE 219

                .
gi 23296450 254 I 254
Cdd:cd03218 220 I 220
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
58-239 1.52e-13

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 67.67  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknfvfQNPDHQvvMPTVEADVAF-----GLG 132
Cdd:PRK13540  15 PLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFER------QSIKKD--LCTYQKQLCFvghrsGIN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  133 K--------YHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:PRK13540  87 PyltlrencLYDIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTI 166
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 23296450  205 IKAVKDliNAKKGDVTALwVTHRLEELKYADGAVY 239
Cdd:PRK13540 167 ITKIQE--HRAKGGAVLL-TSHQDLPLNKADYEEY 198
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
60-230 1.78e-13

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 68.66  E-value: 1.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLK------------------------ILAGVVNPssgtVFVEKPKNFVFQNPD 115
Cdd:PRK14243  26 VKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndlipgfrvegkvtfhgknLYAPDVDP----VEVRRRIGMVFQKPN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  116 hqvvmP---TVEADVAFG---LGKYHDMNqEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:PRK14243 102 -----PfpkSIYDNIAYGariNGYKGDMD-ELVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILM 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 23296450  190 DELTTFLDESDQMgvikAVKDLINAKKGDVTALWVTHRLEE 230
Cdd:PRK14243 176 DEPCSALDPISTL----RIEELMHELKEQYTIIIVTHNMQQ 212
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
54-235 2.28e-13

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: 66.58  E-value: 2.28e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLK-ILAgvvnPSSGTVFVEKPKNFvfqnPDHQVVMptveadvafgLG 132
Cdd:cd03238   5 GANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY----ASGKARLISFLPKF----SRNKLIF----------ID 66
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 133 KyhdmnqeevksrvIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK--VLLLDELTTFLDESDQMGVIKAV 208
Cdd:cd03238  67 Q-------------LQFLIDVGL-GYLTlgQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132
                       170       180
                ....*....|....*....|....*..
gi 23296450 209 KDLINAKkgdVTALWVTHRLEELKYAD 235
Cdd:cd03238 133 KGLIDLG---NTVILIEHNLDVLSSAD 156
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
58-197 2.47e-13

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 67.18  E-value: 2.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVV---MPTVEADVAfGLGKY 134
Cdd:PRK13543  25 PVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYlghLPGLKADLS-TLENL 103
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  135 HDMNQ---EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK13543 104 HFLCGlhgRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
58-217 2.58e-13

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 66.90  E-value: 2.58e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTV---------FVEKPKNFVFQNPDHQVVMP--TV 123
Cdd:cd03233  21 PILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIhyngipykeFAEKYPGEIIYVSEEDVHFPtlTV 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 124 EADVAFglgkyhdmnqeevksrvikALEAVGmrDYMQRPIqtlSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:cd03233 101 RETLDF-------------------ALRCKG--NEFVRGI---SGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTALE 156
                       170
                ....*....|....
gi 23296450 204 VIKAVKDLINAKKG 217
Cdd:cd03233 157 ILKCIRTMADVLKT 170
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
64-254 3.32e-13

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: 69.06  E-value: 3.32e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE---------KPK-----------NFVFQNPD---HQVVM 120
Cdd:TIGR03269 304 SLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVRvgdewvdmtKPGpdgrgrakryiGILHQEYDlypHRTVL 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   121 PTVEAdvAFGLgkyhDMNQEEVKSRVIKALEAVGMRDYMQRPI-----QTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:TIGR03269 384 DNLTE--AIGL----ELPDELARMKAVITLKMVGFDEEKAEEIldkypDELSEGERHRVALAQVLIKEPRIVILDEPTGT 457
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450   196 LDESDQMGVIKAVkdlINAKKG-DVTALWVTHRLE-ELKYADGAVYMENGRVVRHGDAATI 254
Cdd:TIGR03269 458 MDPITKVDVTHSI---LKAREEmEQTFIIVSHDMDfVLDVCDRAALMRDGKIVKIGDPEEI 515
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
60-256 5.11e-13

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 68.38  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTVEADVAFGLgkYHDMNQ 139
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTGIENIELKGL--MMGLTK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  140 EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELttfLDESDQMGVIKAVKDLINAKKGDV 219
Cdd:PRK13545 118 EKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEA---LSVGDQTFTKKCLDKMNEFKEQGK 194
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 23296450  220 TALWVTHRLEELK-YADGAVYMENGRVVRHGDAATISD 256
Cdd:PRK13545 195 TIFFISHSLSQVKsFCTKALWLHYGQVKEYGDIKEVVD 232
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
56-255 5.86e-13

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: 68.31  E-value: 5.86e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    56 SVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVV---NPSSGTVFVEKPknFVFQNPD----------HQVVMPT 122
Cdd:TIGR02633  13 GVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYphgTWDGEIYWSGSP--LKASNIRdteragiviiHQELTLV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   123 VEADVAFGLGKYHD-------MNQEEVKSRVIKALEAVGMRDY-MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:TIGR02633  91 PELSVAENIFLGNEitlpggrMAYNAMYLRAKNLLRELQLDADnVTRPVGDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450   195 FLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATIS 255
Cdd:TIGR02633 171 SLTEKETEILLDIIRDL---KAHGVACVYISHKLNEVKaVCDTICVIRDGQHVATKDMSTMS 229
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
71-230 6.58e-13

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 68.50  E-value: 6.58e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     71 QLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----EKPKNFVFQN----PDHQVVMP--TVEADVAFgLGKYHDMNQ 139
Cdd:TIGR01257  957 QITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVggkdiETNLDAVRQSlgmcPQHNILFHhlTVAEHILF-YAQLKGRSW 1035
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    140 EEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQmgviKAVKDLINAKKGDV 219
Cdd:TIGR01257 1036 EEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSR----RSIWDLLLKYRSGR 1111
                          170
                   ....*....|.
gi 23296450    220 TALWVTHRLEE 230
Cdd:TIGR01257 1112 TIIMSTHHMDE 1122
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
59-254 8.32e-13

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 66.07  E-value: 8.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFqnPDHQVVMPTV-----EADVAFGLGK 133
Cdd:PRK10895  18 VVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLL--PLHARARRGIgylpqEASIFRRLSV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  134 Y----------HDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:PRK10895  96 YdnlmavlqirDDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISVID 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 23296450  204 VIKAVKDLINAKKGdvtALWVTHRLEE-LKYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK10895 176 IKRIIEHLRDSGLG---VLITDHNVREtLAVCERAYIVSQGHLIAHGTPTEI 224
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
59-255 8.81e-13

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: 67.91  E-value: 8.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGV--VNPSSGTV-----------FVEKPKNFVFQNPDHQVVMPTVEA 125
Cdd:TIGR03269  15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIiyhvalcekcgYVERPSKVGEPCPVCGGTLEPEEV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   126 D---------------VAFGLGKYHDMNQEE-VKSRVIKALEAVGM--RDYMQRPIQ----------------TLSGGQK 171
Cdd:TIGR03269  95 DfwnlsdklrrrirkrIAIMLQRTFALYGDDtVLDNVLEALEEIGYegKEAVGRAVDliemvqlshrithiarDLSGGEK 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   172 QRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGD 250
Cdd:TIGR03269 175 QRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEA--VKASGISMVLTSHWPEVIeDLSDKAIWLENGEIKEEGT 252

                  ....*
gi 23296450   251 AATIS 255
Cdd:TIGR03269 253 PDEVV 257
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
59-249 9.58e-13

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 67.76  E-value: 9.58e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG------VVNPS---SGTVfVEKPK-----NFVFQNpDHQVVMPTVE 124
Cdd:TIGR00955  40 LLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFrspkgvKGSGSvllNGMP-IDAKEmraisAYVQQD-DLFIPTLTVR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   125 ADVAFG----LGKyhDMNQEEVKSRVIKALEAVGMRDYMQRPIQT------LSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:TIGR00955 118 EHLMFQahlrMPR--RVTKKEKRERVDEVLQALGLRKCANTRIGVpgrvkgLSGGERKRLAFASELLTDPPLLFCDEPTS 195
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450   195 FLDESDQMGVIKAVKDLinAKKGDvTALWVTH----RLEELkyADGAVYMENGRVVRHG 249
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGL--AQKGK-TIICTIHqpssELFEL--FDKIILMAEGRVAYLG 249
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
69-231 1.04e-12

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: 64.32  E-value: 1.04e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     69 SGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFvekpknfvfqnpdhqvvmptveadvafglgkYHDMNQEEVKSRVIK 148
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVI-------------------------------YIDGEDILEEVLDQL 49
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    149 ALEAVGMRDYMqrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV---KDLINAKKGDVTALWVT 225
Cdd:smart00382  50 LLIIVGGKKAS------GSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEelrLLLLLKSEKNLTVILTT 123

                   ....*.
gi 23296450    226 HRLEEL 231
Cdd:smart00382 124 NDEKDL 129
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
62-197 1.06e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.45  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   62 DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPK-NFVFQNPDHQVVMPTVEADVAFGLgKYHDMNQ 139
Cdd:PRK11819 342 DLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIgETVKlAYVDQSRDALDPNKTVWEEISGGL-DIIKVGN 420
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  140 EEVKSRVikaleavgmrdYM----------QRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK11819 421 REIPSRA-----------YVgrfnfkggdqQKKVGVLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD 477
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
40-254 1.25e-12

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 65.88  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   40 VECRNLCFSVStrqgisVPILRDCSFRIPSGQLWMILGPNGCGKS----TLLKILAGVVNPSSGTVFVE----------- 104
Cdd:PRK10418   5 IELRNIALQAA------QPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDgkpvapcalrg 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  105 KPKNFVFQNPD------HQVVMPTVEADVAFGlgkyhdmnQEEVKSRVIKALEAVGMRDyMQRPIQT----LSGGQKQRI 174
Cdd:PRK10418  79 RKIATIMQNPRsafnplHTMHTHARETCLALG--------KPADDATLTAALEAVGLEN-AARVLKLypfeMSGGMLQRM 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  175 AIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLInaKKGDVTALWVTH------RLeelkyADGAVYMENGRVVRH 248
Cdd:PRK10418 150 MIALALLCEAPFIIADEPTTDLDVVAQARILDLLESIV--QKRALGMLLVTHdmgvvaRL-----ADDVAVMSHGRIVEQ 222

                 ....*.
gi 23296450  249 GDAATI 254
Cdd:PRK10418 223 GDVETL 228
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
39-255 3.65e-12

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 65.89  E-value: 3.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   39 AVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknfVFQN-PDHQ 117
Cdd:PRK10789 315 DVNIRQFTYPQTDH-----PALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDI--------RFHDiPLTK 381
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 -----------VV--MP-----TVEADVAFGlgkYHDMNQEEVKS------------RVIKALEA-VGMRDYMqrpiqtL 166
Cdd:PRK10789 382 lqldswrsrlaVVsqTPflfsdTVANNIALG---RPDATQQEIEHvarlasvhddilRLPQGYDTeVGERGVM------L 452
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  167 SGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTAlwvtHRLEELKYADGAVYMENGRVV 246
Cdd:PRK10789 453 SGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTVIISA----HRLSALTEASEILVMQHGHIA 528

                 ....*....
gi 23296450  247 RHGDAATIS 255
Cdd:PRK10789 529 QRGNHDQLA 537
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1-249 4.10e-12

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 66.03  E-value: 4.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    1 MNGHCLfaaspPRLFPLRSISSSVSPSGSYRikfSDNVA-----VECRNLCFSVSTRQGI------SVPILRDCSFRIPS 69
Cdd:PRK10261 278 MKGLDY-----PRRFPLISLEHPAKQEPPIE---QDTVVdgepiLQVRNLVTRFPLRSGLlnrvtrEVHAVEKVSFDLWP 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   70 GQLWMILGPNGCGKSTLLKILAGVVNPSSGTVF----------------VEKPKNFVFQNPdHQVVMP--TVEADVAFGL 131
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIfngqridtlspgklqaLRRDIQFIFQDP-YASLDPrqTVGDSIMEPL 428
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  132 GKYHDMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKD 210
Cdd:PRK10261 429 RVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLD 508
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 23296450  211 LinAKKGDVTALWVTHRL---EELKYADGAVYMenGRVVRHG 249
Cdd:PRK10261 509 L--QRDFGIAYLFISHDMavvERISHRVAVMYL--GQIVEIG 546
PLN03140 PLN03140
ABC transporter G family member; Provisional
59-257 7.59e-12

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 65.25  E-value: 7.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPS---SGTV---------FV-EKPKNFVFQNPDHQVVMpTVEA 125
Cdd:PLN03140  180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEItyngyrlneFVpRKTSAYISQNDVHVGVM-TVKE 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   126 DVAF-----GLGKYHDMNQE--------------EV----KSRVIKALEAVGMRDY------------------MQRPIq 164
Cdd:PLN03140  259 TLDFsarcqGVGTRYDLLSElarrekdagifpeaEVdlfmKATAMEGVKSSLITDYtlkilgldickdtivgdeMIRGI- 337
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   165 tlSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGR 244
Cdd:PLN03140  338 --SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVLMSLLQPAPETFDLFDDIILLSEGQ 415
                         250
                  ....*....|...
gi 23296450   245 VVRHGDAATISDF 257
Cdd:PLN03140  416 IVYQGPRDHILEF 428
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
164-242 8.65e-12

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 65.05  E-value: 8.65e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450   164 QTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINakKGDVTALWVTHRLEELKYADGAVYMEN 242
Cdd:PTZ00265 1357 KSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKD--KADKTIITIAHRIASIKRSDKIVVFNN 1433
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
58-249 1.00e-11

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: 62.43  E-value: 1.00e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------------KPKNFVFQNPdhQVVMPTVE 124
Cdd:cd03369  22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDgidistipledlrSSLTIIPQDP--TLFSGTIR 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 125 ADVafglgkyhDMNQEEVKSRVIKALEAVGMRDymqrpiqTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGV 204
Cdd:cd03369 100 SNL--------DPFDEYSDEEIYGALRVSEGGL-------NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDALI 164
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 23296450 205 IKAVKDLINakkgDVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:cd03369 165 QKTIREEFT----NSTILTIAHRLRTIIDYDKILVMDAGEVKEYD 205
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
75-250 1.15e-11

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 64.13  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   75 ILGPNGCGKSTLLKILAGVVNPSSG-------TVF---------VEKPK-NFVFQnpDHQVvMP--TVEADVAFGLGKYh 135
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQKGrivlngrVLFdaekgiclpPEKRRiGYVFQ--DARL-FPhyKVRGNLRYGMAKS- 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  136 dMNQEevKSRVIKALeavGMRDYMQR-PIqTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDesdqmgvIKAVKDLIN- 213
Cdd:PRK11144 105 -MVAQ--FDKIVALL---GIEPLLDRyPG-SLSGGEKQRVAIGRALLTAPELLLMDEPLASLD-------LPRKRELLPy 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 23296450  214 ----AKKGDVTALWVTHRLEE-LKYADGAVYMENGRVVRHGD 250
Cdd:PRK11144 171 lerlAREINIPILYVSHSLDEiLRLADRVVVLEQGKVKAFGP 212
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
58-249 1.45e-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: 64.58  E-value: 1.45e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQvvMPTVEADVAFGlgkyHDM 137
Cdd:TIGR00957  652 PTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKGSVAYVPQQAWIQ--NDSLRENILFG----KAL 725
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    138 NQEEVKSrVIKA------LEAV--GMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESdqmgVIKAVK 209
Cdd:TIGR00957  726 NEKYYQQ-VLEAcallpdLEILpsGDRTEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAH----VGKHIF 800
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 23296450    210 DLINAKKG---DVTALWVTHRLEELKYADGAVYMENGRVVRHG 249
Cdd:TIGR00957  801 EHVIGPEGvlkNKTRILVTHGISYLPQVDVIIVMSGGKISEMG 843
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
42-234 2.82e-11

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 61.04  E-value: 2.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   42 CRNLCFSVSTRQgisvpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNP-----DH 116
Cdd:PRK13541   4 LHQLQFNIEQKN------LFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPyctyiGH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  117 QVVMP---TVEADVAFGLGKYhdmNQEEVksrVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK13541  78 NLGLKlemTVFENLKFWSEIY---NSAET---LYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVE 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23296450  194 TFLDESDQmgviKAVKDLI--NAKKGDVTaLWVTHRLEELKYA 234
Cdd:PRK13541 152 TNLSKENR----DLLNNLIvmKANSGGIV-LLSSHLESSIKSA 189
ycf16 CHL00131
sulfate ABC transporter protein; Validated
41-268 4.37e-11

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 61.58  E-value: 4.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   41 ECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGvvNPS----SGTVFVE-------KPKN- 108
Cdd:CHL00131   9 EIKNLHASVNEN-----EILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG--HPAykilEGDILFKgesildlEPEEr 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 ------FVFQNPdhqVVMPTVE-AD---VAFGlGKYHDMNQEEVKS----RVIKA-LEAVGMRD-YMQRPI-QTLSGGQK 171
Cdd:CHL00131  82 ahlgifLAFQYP---IEIPGVSnADflrLAYN-SKRKFQGLPELDPleflEIINEkLKLVGMDPsFLSRNVnEGFSGGEK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  172 QRiaiagalAEACKVLLLDELTTFLDESDQMGVIKAVKDL---INAKKGDVTA-LWVTH--RLEELKYADGAVYMENGRV 245
Cdd:CHL00131 158 KR-------NEILQMALLDSELAILDETDSGLDIDALKIIaegINKLMTSENSiILITHyqRLLDYIKPDYVHVMQNGKI 230
                        250       260
                 ....*....|....*....|...
gi 23296450  246 VRHGDaATISDFIKAKQSSYIDQ 268
Cdd:CHL00131 231 IKTGD-AELAKELEKKGYDWLKQ 252
PLN03073 PLN03073
ABC transporter F family; Provisional
52-212 5.49e-11

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 62.57  E-value: 5.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   52 RQGISVPILRDCSFRIPSGQLWM--------------ILGPNGCGKSTLLKILAGVVNPSSGTVF-VEKPKNFVFQNpdH 116
Cdd:PLN03073 503 RPGPPIISFSDASFGYPGGPLLFknlnfgidldsriaMVGPNGIGKSTILKLISGELQPSSGTVFrSAKVRMAVFSQ--H 580
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  117 QVVMPTVEADVAFGLGK-YHDMNQEEVKSRvikaLEAVGMRDYMQ-RPIQTLSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:PLN03073 581 HVDGLDLSSNPLLYMMRcFPGVPEQKLRAH----LGSFGVTGNLAlQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSN 656
                        170
                 ....*....|....*...
gi 23296450  195 FLDesdqmgvIKAVKDLI 212
Cdd:PLN03073 657 HLD-------LDAVEALI 667
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
49-194 9.99e-11

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 61.68  E-value: 9.99e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   49 VSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknFVF----QNPDH-QVVMPtv 123
Cdd:NF033858   7 VSHRYG-KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRV-------EVLggdmADARHrRAVCP-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  124 eaDVAF---GLGK--YHDM---------------NQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEA 183
Cdd:NF033858  77 --RIAYmpqGLGKnlYPTLsvfenldffgrlfgqDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHD 154
                        170
                 ....*....|.
gi 23296450  184 CKVLLLDELTT 194
Cdd:NF033858 155 PDLLILDEPTT 165
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
75-199 1.06e-10

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 61.49  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKN--FVFQNP---DHQVVMPTVEADVAFGLG----------KY----H 135
Cdd:TIGR03719  36 VLGLNGAGKSTLLRIMAGVDKDFNGEARPQPGIKvgYLPQEPqldPTKTVRENVEEGVAEIKDaldrfneisaKYaepdA 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   136 DMNQ--EEvKSRVIKALEAVGMRDYMQR---------------PIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD- 197
Cdd:TIGR03719 116 DFDKlaAE-QAELQEIIDAADAWDLDSQleiamdalrcppwdaDVTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDa 194

                  ..
gi 23296450   198 ES 199
Cdd:TIGR03719 195 ES 196
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
67-233 1.18e-10

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: 59.12  E-value: 1.18e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  67 IPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGtvfvekpknfvfqNPDHQVVMPTVeadvafglgkyhdmnqeevKSRV 146
Cdd:cd03222  22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGD-------------NDEWDGITPVY-------------------KPQY 69
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 147 IKaleavgmrdymqrpiqtLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLInaKKGDVTALWVTH 226
Cdd:cd03222  70 ID-----------------LSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLS--EEGKKTALVVEH 130

                ....*..
gi 23296450 227 RLEELKY 233
Cdd:cd03222 131 DLAVLDY 137
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
41-197 1.28e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 61.50  E-value: 1.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-EKPKNFVFQ------N 113
Cdd:PRK11147 321 EMENVNYQIDGKQ-----LVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCgTKLEVAYFDqhraelD 395
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  114 PDHqvvmpTVEADVAFGlgkyhdmNQE-EVKSRVIKALeavgmrDYMQ----------RPIQTLSGGQKQRIAIAGALAE 182
Cdd:PRK11147 396 PEK-----TVMDNLAEG-------KQEvMVNGRPRHVL------GYLQdflfhpkramTPVKALSGGERNRLLLARLFLK 457
                        170
                 ....*....|....*
gi 23296450  183 ACKVLLLDELTTFLD 197
Cdd:PRK11147 458 PSNLLILDEPTNDLD 472
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
43-249 1.40e-10

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 59.94  E-value: 1.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   43 RNLCFSVSTRQGisvpiLRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKN------------- 108
Cdd:PRK11701  10 RGLTKLYGPRKG-----CRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVhYRMRDGQlrdlyalseaerr 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 --------FVFQNPdHQVVMPTVEADVAFGlgkyhdmnqeevksrviKALEAVGMRDY----------MQR--------- 161
Cdd:PRK11701  85 rllrtewgFVHQHP-RDGLRMQVSAGGNIG-----------------ERLMAVGARHYgdiratagdwLERveidaarid 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  162 --PiQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINakKGDVTALWVTH-----RLeelkYA 234
Cdd:PRK11701 147 dlP-TTFSGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVR--ELGLAVVIVTHdlavaRL----LA 219
                        250
                 ....*....|....*
gi 23296450  235 DGAVYMENGRVVRHG 249
Cdd:PRK11701 220 HRLLVMKQGRVVESG 234
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
75-199 2.51e-10

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 60.52  E-value: 2.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVEK----------PKnfvfQNPDHQV---VMPTVeADVAFGLGKYH------ 135
Cdd:PRK11819  38 VLGLNGAGKSTLLRIMAGVDKEFEGEARPAPgikvgylpqePQ----LDPEKTVrenVEEGV-AEVKAALDRFNeiyaay 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  136 -----DMN---------QE--------EVKSRVIKALEAVGMRDYMQrPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK11819 113 aepdaDFDalaaeqgelQEiidaadawDLDSQLEIAMDALRCPPWDA-KVTKLSGGERRRVALCRLLLEKPDMLLLDEPT 191

                 ....*..
gi 23296450  194 TFLD-ES 199
Cdd:PRK11819 192 NHLDaES 198
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
59-226 2.72e-10

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 59.02  E-value: 2.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV-----------------EKPKNFVFQNpdhQVVMP 121
Cdd:PRK10584  25 ILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLvgqplhqmdeearaklrAKHVGFVFQS---FMLIP 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  122 TVEADVAFGL-GKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDEsd 200
Cdd:PRK10584 102 TLNALENVELpALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDR-- 179
                        170       180
                 ....*....|....*....|....*...
gi 23296450  201 QMGviKAVKDLINAKKGD--VTALWVTH 226
Cdd:PRK10584 180 QTG--DKIADLLFSLNREhgTTLILVTH 205
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
34-191 2.76e-10

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 60.37  E-value: 2.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   34 FSDNVAVECRNLCFSVSTrQGISV-PIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQ 112
Cdd:PRK10522 317 FPDWQTLELRNVTFAYQD-NGFSVgPI----NLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQ 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  113 NPDHQVVMPTVEADV-AFG--LGkyhDMNQEEVKSRVIKALEAVGMRDYMQ------RPIQtLSGGQKQRIAIAGALAEA 183
Cdd:PRK10522 392 PEDYRKLFSAVFTDFhLFDqlLG---PEGKPANPALVEKWLERLKMAHKLEledgriSNLK-LSKGQKKRLALLLALAEE 467

                 ....*...
gi 23296450  184 CKVLLLDE 191
Cdd:PRK10522 468 RDILLLDE 475
GguA NF040905
sugar ABC transporter ATP-binding protein;
57-259 4.85e-10

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 59.42  E-value: 4.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVnPSsGT-----VFVEKPKNF--VFQNPDHQVVMPTVE----- 124
Cdd:NF040905  14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVY-PH-GSyegeiLFDGEVCRFkdIRDSEALGIVIIHQElalip 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 ----ADVAFgLG----KYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFL 196
Cdd:NF040905  92 ylsiAENIF-LGneraKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23296450  197 DESDQmgviKAVKDLINA-KKGDVTALWVTHRLEELKY-ADGAVYMENGRVV----RHGDAATISDFIK 259
Cdd:NF040905 171 NEEDS----AALLDLLLElKAQGITSIIISHKLNEIRRvADSITVLRDGRTIetldCRADEVTEDRIIR 235
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
57-231 7.26e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 58.86  E-value: 7.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNfvFQNPD----------HQV--VMP-- 121
Cdd:PRK10762  17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSIlYLGKEVT--FNGPKssqeagigiiHQElnLIPql 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  122 TVEADV--------AFGLGKYHDMNQEevksrVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK10762  95 TIAENIflgrefvnRFGRIDWKKMYAE-----ADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPT 169
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 23296450  194 TFLDESDQMGVIKAVKDLINAKKGDVtalWVTHRLEEL 231
Cdd:PRK10762 170 DALTDTETESLFRVIRELKSQGRGIV---YISHRLKEI 204
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
49-246 7.67e-10

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 57.58  E-value: 7.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   49 VSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQN-----------PDHQ 117
Cdd:PRK11614  11 VSAHYG-KIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTakimreavaivPEGR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 VVMP--TVEADVAFGlGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPiQTLSGGQKQRIAIAGALAEACKVLLLDELTTF 195
Cdd:PRK11614  90 RVFSrmTVEENLAMG-GFFAERDQFQERIKWVYELFPRLHERRIQRA-GTMSGGEQQMLAIGRALMSQPRLLLLDEPSLG 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 23296450  196 LDESdqmgVIKAVKDLINAKKGD-VTALWVTHRLEE-LKYADGAVYMENGRVV 246
Cdd:PRK11614 168 LAPI----IIQQIFDTIEQLREQgMTIFLVEQNANQaLKLADRGYVLENGHVV 216
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
64-254 9.64e-10

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 58.21  E-value: 9.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKS-TLLKILAGVVNPssGTVFVEKpknFVFQNPDHQVVMPT-----VEADVA--------- 128
Cdd:PRK11022  27 SYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYP--GRVMAEK---LEFNGQDLQRISEKerrnlVGAEVAmifqdpmts 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  129 ----FGLG-------KYHDM-NQEEVKSRVIKALEAVGMRDYMQR----PIQtLSGGQKQRIAIAGALAEACKVLLLDEL 192
Cdd:PRK11022 102 lnpcYTVGfqimeaiKVHQGgNKKTRRQRAIDLLNQVGIPDPASRldvyPHQ-LSGGMSQRVMIAMAIACRPKLLIADEP 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23296450  193 TTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHGDAATI 254
Cdd:PRK11022 181 TTALDVTIQAQIIELLLEL--QQKENMALVLITHDLALVaEAAHKIIVMYAGQVVETGKAHDI 241
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
58-197 9.91e-10

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 58.81  E-value: 9.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEK-----------PKNfvfqnpdhqvVMPTVEAD 126
Cdd:PRK11147  17 PLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQdlivarlqqdpPRN----------VEGTVYDF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  127 VAFGLG-------KYHDMN------------------QEEV--------KSRVIKALEAVGMRDYMqrPIQTLSGGQKQR 173
Cdd:PRK11147  87 VAEGIEeqaeylkRYHDIShlvetdpseknlnelaklQEQLdhhnlwqlENRINEVLAQLGLDPDA--ALSSLSGGWLRK 164
                        170       180
                 ....*....|....*....|....
gi 23296450  174 IAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK11147 165 AALGRALVSNPDVLLLDEPTNHLD 188
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
41-191 2.16e-09

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 56.19  E-value: 2.16e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  41 ECRNLCFSVSTRQgisvpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVekpknfvfqnpDHQVV- 119
Cdd:COG1137   5 EAENLVKSYGKRT-----VVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFL-----------DGEDIt 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 120 -MP----------------------TVEADVAFGLgKYHDMNQEEVKSRVIKALEAVG---MRDymqRPIQTLSGGQKQR 173
Cdd:COG1137  69 hLPmhkrarlgigylpqeasifrklTVEDNILAVL-ELRKLSKKEREERLEELLEEFGithLRK---SKAYSLSGGERRR 144
                       170
                ....*....|....*...
gi 23296450 174 IAIAGALAEACKVLLLDE 191
Cdd:COG1137 145 VEIARALATNPKFILLDE 162
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
53-255 2.47e-09

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 57.34  E-value: 2.47e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  53 QGISVP-ILRDCSFRIPSGQlwmIL---GPNGCGKSTLLKILAGVVNPSSGTVFVE-KPKNF------------------ 109
Cdd:COG1129 260 EGLSVGgVVRDVSFSVRAGE---ILgiaGLVGAGRTELARALFGADPADSGEIRLDgKPVRIrsprdairagiayvpedr 336
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 ----------VFQNpdhqVVMPTVEADVAFGLgkyhdMNQEEVKSRVIKALEAVGMR-DYMQRPIQTLSGGQKQRIAIAG 178
Cdd:COG1129 337 kgeglvldlsIREN----ITLASLDRLSRGGL-----LDRRRERALAEEYIKRLRIKtPSPEQPVGNLSGGNQQKVVLAK 407
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 179 ALAEACKVLLLDELTtfldesdqMGV-IKA---VKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRVVRHGDA 251
Cdd:COG1129 408 WLATDPKVLILDEPT--------RGIdVGAkaeIYRLIRelAAEG-KAVIVISSELPElLGLSDRILVMREGRIVGELDR 478

                ....
gi 23296450 252 ATIS 255
Cdd:COG1129 479 EEAT 482
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
59-249 2.57e-09

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 56.64  E-value: 2.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSG------------TVF-------VEKPKNFVFQNPDHqvv 119
Cdd:PRK14271  36 VLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgdvllggrSIFnyrdvleFRRRVGMLFQRPNP--- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  120 MP-TVEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQT----LSGGQKQRIAIAGALAEACKVLLLDELTT 194
Cdd:PRK14271 113 FPmSIMDNVLAGVRAHKLVPRKEFRGVAQARLTEVGLWDAVKDRLSDspfrLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450  195 FLDESdqmgVIKAVKDLINAKKGDVTALWVTHRL-EELKYADGAVYMENGRVVRHG 249
Cdd:PRK14271 193 ALDPT----TTEKIEEFIRSLADRLTVIIVTHNLaQAARISDRAALFFDGRLVEEG 244
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
35-254 3.86e-09

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 56.79  E-value: 3.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   35 SDNVAVECRNLCFSVSTRQgisVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpknFVFQNP 114
Cdd:PRK10261  10 RDVLAVENLNIAFMQEQQK---IAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK---MLLRRR 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  115 DHQVV---------MPTVE-ADVA-------------FGLGK--------YHDMNQEEVKSRVIKALEAVGMRD---YMQ 160
Cdd:PRK10261  84 SRQVIelseqsaaqMRHVRgADMAmifqepmtslnpvFTVGEqiaesirlHQGASREEAMVEAKRMLDQVRIPEaqtILS 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  161 RPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDVTALWVTHRLEEL-KYADGAVY 239
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVL--QKEMSMGVIFITHDMGVVaEIADRVLV 241
                        250
                 ....*....|....*
gi 23296450  240 MENGRVVRHGDAATI 254
Cdd:PRK10261 242 MYQGEAVETGSVEQI 256
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
43-214 4.82e-09

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 54.56  E-value: 4.82e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  43 RNLCFSVSTRQGiSVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILA-----GVVnpsSGTVFV---EKPKNF----- 109
Cdd:cd03232   7 KNLNYTVPVKGG-KRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAgrktaGVI---TGEILIngrPLDKNFqrstg 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 110 -VFQNPDHqvvmptveadvafglgkyhdmnqeEVKSRVIKALE--AVgmrdymqrpIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:cd03232  83 yVEQQDVH------------------------SPNLTVREALRfsAL---------LRGLSVEQRKRLTIGVELAAKPSI 129
                       170       180
                ....*....|....*....|....*...
gi 23296450 187 LLLDELTTFLDESDQMGVIKAVKDLINA 214
Cdd:cd03232 130 LFLDEPTSGLDSQAAYNIVRFLKKLADS 157
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
64-193 5.34e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 56.67  E-value: 5.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVfvekpknFVFQNPdhqvvmptVEAD-------V-----AFGL 131
Cdd:NF033858 286 SFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEA-------WLFGQP--------VDAGdiatrrrVgymsqAFSL 350
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  132 gkY-----------H----DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:NF033858 351 --YgeltvrqnlelHarlfHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPT 425
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
67-240 9.28e-09

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: 53.52  E-value: 9.28e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  67 IPSGQLWMILGPNGCGKSTLLKILAgvvnpssgtvfvekpknfvfqnpdhqvvmptveadVAFGLGKYHDMNQEEVKSRV 146
Cdd:cd03227  18 FGEGSLTIITGPNGSGKSTILDAIG-----------------------------------LALGGAQSATRRRSGVKAGC 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 147 IKALEAVgmrDYMQRPIQtLSGGQKQRIAIAGALAEA----CKVLLLDELTTFLDESDQMGVIKAVKDLInakKGDVTAL 222
Cdd:cd03227  63 IVAAVSA---ELIFTRLQ-LSGGEKELSALALILALAslkpRPLYILDEIDRGLDPRDGQALAEAILEHL---VKGAQVI 135
                       170
                ....*....|....*...
gi 23296450 223 WVTHRLEELKYADGAVYM 240
Cdd:cd03227 136 VITHLPELAELADKLIHI 153
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
64-191 9.30e-09

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 54.61  E-value: 9.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   64 SFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPknfVFQNPDHQVV----------------MPTVE-- 124
Cdd:PRK11300  25 NLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTIlLRGQH---IEGLPGHQIArmgvvrtfqhvrlfreMTVIEnl 101
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  125 ---------ADVAFGLGKYHDMNQEEVKS--RVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDE 191
Cdd:PRK11300 102 lvaqhqqlkTGLFSGLLKTPAFRRAESEAldRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDE 179
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
48-197 1.12e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.56  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   48 SVSTRQGISVpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGT-----------VFVEKPK------NFV 110
Cdd:PRK10636   6 SLQIRRGVRV-LLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSytfpgnwqlawVNQETPAlpqpalEYV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  111 ------FQNPDHQVVMPTVEAD---VAFGLGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGAL 180
Cdd:PRK10636  85 idgdreYRQLEAQLHDANERNDghaIATIHGKLDAIDAWTIRSRAASLLHGLGFsNEQLERPVSDFSGGWRMRLNLAQAL 164
                        170
                 ....*....|....*..
gi 23296450  181 AEACKVLLLDELTTFLD 197
Cdd:PRK10636 165 ICRSDLLLLDEPTNHLD 181
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
75-235 1.43e-08

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 53.38  E-value: 1.43e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  75 ILGPNGCGKSTLLKILagvvnpsSGTVFVEKPKNFVFQNPDHQVVMPT---VEADVAFGLGKYHDMnqeeVKSRVIKALE 151
Cdd:cd03240  27 IVGQNGAGKTTIIEAL-------KYALTGELPPNSKGGAHDPKLIREGevrAQVKLAFENANGKKY----TITRSLAILE 95
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 152 AV------GMRDYMQRPIQTLSGGQK--QRIAIAGALAEA----CKVLLLDELTTFLDESDqmgVIKAVKDLINAKKGDV 219
Cdd:cd03240  96 NVifchqgESNWPLLDMRGRCSGGEKvlASLIIRLALAETfgsnCGILALDEPTTNLDEEN---IEESLAEIIEERKSQK 172
                       170
                ....*....|....*...
gi 23296450 220 T--ALWVTHRLEELKYAD 235
Cdd:cd03240 173 NfqLIVITHDEELVDAAD 190
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
54-230 5.59e-08

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: 53.86  E-value: 5.59e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     54 GISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVV--MPTVEADVAFGL 131
Cdd:TIGR01257 1949 GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMgyCPQFDAIDDLLT 2028
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    132 GKYH--------DMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMG 203
Cdd:TIGR01257 2029 GREHlylyarlrGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRM 2108
                          170       180
                   ....*....|....*....|....*..
gi 23296450    204 VIKAVKDLINAKKGDVTalwVTHRLEE 230
Cdd:TIGR01257 2109 LWNTIVSIIREGRAVVL---TSHSMEE 2132
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
39-226 5.83e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 53.36  E-value: 5.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   39 AVECRNLCFSVSTRqgisvPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHqv 118
Cdd:PRK15064 319 ALEVENLTKGFDNG-----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKWSENANIGYYAQDH-- 391
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  119 vmptvEADVAFGLGKYHDMNQEEVKSRVIKALEAVGMR-----DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK15064 392 -----AYDFENDLTLFDWMSQWRQEGDDEQAVRGTLGRllfsqDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPT 466
                        170       180       190
                 ....*....|....*....|....*....|....
gi 23296450  194 TFLDesdqMGVIKAvkdLINA-KKGDVTALWVTH 226
Cdd:PRK15064 467 NHMD----MESIES---LNMAlEKYEGTLIFVSH 493
PLN03232 PLN03232
ABC transporter C family member; Provisional
58-248 6.04e-08

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 53.44  E-value: 6.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTV-------EADVAFG 130
Cdd:PLN03232 1250 PVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRVLSIIpqspvlfSGTVRFN 1329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   131 LGKYHDMNQEEVksrvIKALEAVGMRDYMQR-PI----------QTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD-E 198
Cdd:PLN03232 1330 IDPFSEHNDADL----WEALERAHIKDVIDRnPFgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASVDvR 1405
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 23296450   199 SDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRH 248
Cdd:PLN03232 1406 TDSL-----IQRTIREEFKSCTMLVIAHRLNTIIDCDKILVLSSGQVLEY 1450
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
77-216 7.39e-08

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 52.97  E-value: 7.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   77 GPNGCGKSTLLKILAGVVNPSSGTVFVE--------KPKNFVFQNpdhQVVMPTV------------------------E 124
Cdd:PRK15064  34 GANGCGKSTFMKILGGDLEPSAGNVSLDpnerlgklRQDQFAFEE---FTVLDTVimghtelwevkqerdriyalpemsE 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  125 AD---VAFGLGKYHDMNQEEVKSRVIKALEAVGM-RDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDesd 200
Cdd:PRK15064 111 EDgmkVADLEVKFAEMDGYTAEARAGELLLGVGIpEEQHYGLMSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD--- 187
                        170
                 ....*....|....*.
gi 23296450  201 qMGVIKAVKDLINAKK 216
Cdd:PRK15064 188 -INTIRWLEDVLNERN 202
PLN03232 PLN03232
ABC transporter C family member; Provisional
39-255 1.94e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 51.90  E-value: 1.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    39 AVECRNLCFSVSTRqgISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGT-VFVEKPKNFVFQNPdhQ 117
Cdd:PLN03232  614 AISIKNGYFSWDSK--TSKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETSsVVIRGSVAYVPQVS--W 689
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   118 VVMPTVEADVAFGlGKYHdmnqeevKSRVIKALEAVGM---------RDYM---QRPIQtLSGGQKQRIAIAGALAEACK 185
Cdd:PLN03232  690 IFNATVRENILFG-SDFE-------SERYWRAIDVTALqhdldllpgRDLTeigERGVN-ISGGQKQRVSMARAVYSNSD 760
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450   186 VLLLDELTTFLDESDQMGVIKA-VKDLINAKkgdvTALWVTHRLEELKYADGAVYMENGRVVRHGDAATIS 255
Cdd:PLN03232  761 IYIFDDPLSALDAHVAHQVFDScMKDELKGK----TRVLVTNQLHFLPLMDRIILVSEGMIKEEGTFAELS 827
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
52-262 2.14e-07

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 51.65  E-value: 2.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     52 RQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-------------FVEKPKNFVFQNPDHQV 118
Cdd:TIGR00956   69 RDTKTFDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASNTDGFHIGVegvitydgitpeeIKKHYRGDVVYNAETDV 148
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    119 VMP--TVEADVAFGL------GKYHDMNQEE-VKSRVIKALEAVGMR--------DYMQRPIqtlSGGQKQRIAIAGALA 181
Cdd:TIGR00956  149 HFPhlTVGETLDFAArcktpqNRPDGVSREEyAKHIADVYMATYGLShtrntkvgNDFVRGV---SGGERKRVSIAEASL 225
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    182 EACKVLLLDELTTFLDESDQMGVIKAVKdlINAKKGDVTALWVTHRLEELKYA--DGAVYMENGRVVRHGDAAtisdfiK 259
Cdd:TIGR00956  226 GGAKIQCWDNATRGLDSATALEFIRALK--TSANILDTTPLVAIYQCSQDAYElfDKVIVLYEGYQIYFGPAD------K 297

                   ...
gi 23296450    260 AKQ 262
Cdd:TIGR00956  298 AKQ 300
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
57-231 2.44e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 51.27  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   57 VPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTV-FVEKPKNF-------------VFQNPDhQVVMPT 122
Cdd:PRK10982  11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSIlFQGKEIDFksskealengismVHQELN-LVLQRS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  123 VEADVafGLGKY--------HDMNQEEVKsRVIKALEA-VGMRDymqrPIQTLSGGQKQRIAIAGALAEACKVLLLDELT 193
Cdd:PRK10982  90 VMDNM--WLGRYptkgmfvdQDKMYRDTK-AIFDELDIdIDPRA----KVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 23296450  194 TFLDESDQMGVIKAVKDLinaKKGDVTALWVTHRLEEL 231
Cdd:PRK10982 163 SSLTEKEVNHLFTIIRKL---KERGCGIVYISHKMEEI 197
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
59-245 2.49e-07

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: 50.62  E-value: 2.49e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  59 ILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---------SSGTVFVEK---------PKNFVFQNPDHQVVM 120
Cdd:cd03289  19 VLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLNTegdiqidgvSWNSVPLQKwrkafgvipQKVFIFSGTFRKNLD 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 121 PTveadvafglGKYHDmnqEEvksrVIKALEAVGMRDYM-QRPIQ----------TLSGGQKQRIAIAGALAEACKVLLL 189
Cdd:cd03289  99 PY---------GKWSD---EE----IWKVAEEVGLKSVIeQFPGQldfvlvdggcVLSHGHKQLMCLARSVLSKAKILLL 162
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450 190 DELTTFLDESdqmgVIKAVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRV 245
Cdd:cd03289 163 DEPSAHLDPI----TYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKV 214
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
58-92 3.56e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 50.78  E-value: 3.56e-07
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAG 92
Cdd:PRK10938 274 PILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITG 308
PLN03130 PLN03130
ABC transporter C family member; Provisional
58-264 4.12e-07

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 50.89  E-value: 4.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTV-------EADVAFG 130
Cdd:PLN03130 1253 PVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKVLGIIpqapvlfSGTVRFN 1332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   131 LGKYHDMNQEEVksrvIKALEAVGMRDYMQRPIQTL-----------SGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PLN03130 1333 LDPFNEHNDADL----WESLERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAVDVR 1408
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   200 DQMGVIKAVKDLINAkkgdVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI-----SDFIKAKQSS 264
Cdd:PLN03130 1409 TDALIQKTIREEFKS----CTMLIIAHRLNTIIDCDRILVLDAGRVVEFDTPENLlsnegSAFSKMVQST 1474
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
41-103 4.62e-07

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 50.57  E-value: 4.62e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  41 ECRNLCFSVSTRQGISV----PIlrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFV 103
Cdd:COG4615 329 ELRGVTYRYPGEDGDEGftlgPI----DLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILL 391
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
41-254 5.24e-07

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 50.11  E-value: 5.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   41 ECRNLCFSVSTRQGIsVPILRDCSFRIPSGQLWMILGPNGCGKS----TLLKILA--GVVNPSS---GTVFVEKPKN--- 108
Cdd:PRK09473  14 DVKDLRVTFSTPDGD-VTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAanGRIGGSAtfnGREILNLPEKeln 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  109 --------FVFQNPdhqvvMPTVEADVAFG------LGKYHDMNQEEVKSRVIKALEAVGM---RDYMQRPIQTLSGGQK 171
Cdd:PRK09473  93 klraeqisMIFQDP-----MTSLNPYMRVGeqlmevLMLHKGMSKAEAFEESVRMLDAVKMpeaRKRMKMYPHEFSGGMR 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  172 QRIAIAGALAEACKVLLLDELTTFLDESDQ---MGVIKAVKDLINakkgdvTA-LWVTHRLEELK-YADGAVYMENGRVV 246
Cdd:PRK09473 168 QRVMIAMALLCRPKLLIADEPTTALDVTVQaqiMTLLNELKREFN------TAiIMITHDLGVVAgICDKVLVMYAGRTM 241

                 ....*...
gi 23296450  247 RHGDAATI 254
Cdd:PRK09473 242 EYGNARDV 249
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
81-263 6.16e-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: 6.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    81 CGKSTLlkilagvvNPSSGTVFVEKpKNFvfqnpdHQVV-MPTVEADvAFGLGKYHDMNQEEVKSRVIKA-------LEA 152
Cdd:TIGR00630 411 CGGTRL--------KPEALAVTVGG-KSI------ADVSeLSIREAH-EFFNQLTLTPEEKKIAEEVLKEirerlgfLID 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   153 VGMrDYM--QRPIQTLSGGQKQRIAIAGAL-AEACKVL-LLDELTTFLDESDQ---MGVIKAVKDLINakkgdvTALWVT 225
Cdd:TIGR00630 475 VGL-DYLslSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRDNrrlINTLKRLRDLGN------TLIVVE 547
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 23296450   226 HRLEELKYADGAVYM------ENGRVVRHGdaaTISDFIKAKQS 263
Cdd:TIGR00630 548 HDEDTIRAADYVIDIgpgageHGGEVVASG---TPEEILANPDS 588
ABC_SMC3_euk cd03272
ATP-binding cassette domain of eukaryotic SMC3 proteins; The structural maintenance of ...
75-235 6.21e-07

ATP-binding cassette domain of eukaryotic SMC3 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: 213239 [Multi-domain]  Cd Length: 243  Bit Score: 49.18  E-value: 6.21e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  75 ILGPNGCGKSTLL--------------------KILAGVVNPSSGTVFVEkpknFVFQNPDHQVVMPTVEADVAFGLGKY 134
Cdd:cd03272  28 VVGRNGSGKSNFFaairfvlsdeythlreeqrqALLHEGSGPSVMSAYVE----IIFDNSDNRFPIDKEEVRLRRTIGLK 103
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 135 HD----MNQEEVKSRVIKALEAVG--------------------MRDYMQRPIQTLSGGQKQRIAIAGALA-EACK---V 186
Cdd:cd03272 104 KDeyflDKKNVTKNDVMNLLESAGfsrsnpyyivpqgkinsltnMKQDEQQEMQQLSGGQKSLVALALIFAiQKCDpapF 183
                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 23296450 187 LLLDELTTFLDESDQmgviKAVKDLINAKKGDVTALWVTHRLEELKYAD 235
Cdd:cd03272 184 YLFDEIDAALDAQYR----TAVANMIKELSDGAQFITTTFRPELLEVAD 228
PLN03211 PLN03211
ABC transporter G-25; Provisional
30-222 1.19e-06

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 49.49  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   30 YRIKFSD--NVAVECRNLC-----FSVSTRQGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSS--GT 100
Cdd:PLN03211  47 YRVKFENmkNKGSNIKRILghkpkISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGT 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  101 VFVEKPK---------NFVFQNpdhQVVMP--TVEADVAF-GLGKYHDMNQEEVKSRVIKA------LEAVGMRDYMQRP 162
Cdd:PLN03211 127 ILANNRKptkqilkrtGFVTQD---DILYPhlTVRETLVFcSLLRLPKSLTKQEKILVAESviselgLTKCENTIIGNSF 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  163 IQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLINAKKGDVTAL 222
Cdd:PLN03211 204 IRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSM 263
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
40-254 1.47e-06

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: 49.17  E-value: 1.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     40 VECRNLCfsVSTRQGISVpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPK-------NFVFQ 112
Cdd:TIGR00957 1285 VEFRNYC--LRYREDLDL-VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNiakiglhDLRFK 1361
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    113 ---NPDHQVVMptvEADVAFGLGKYHDMNQEEVKSrvikALEAVGMRDYMQ-RPI----------QTLSGGQKQRIAIAG 178
Cdd:TIGR00957 1362 itiIPQDPVLF---SGSLRMNLDPFSQYSDEEVWW----ALELAHLKTFVSaLPDkldhecaeggENLSVGQRQLVCLAR 1434
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450    179 ALAEACKVLLLDELTTFLD-ESDQMgvikaVKDLINAKKGDVTALWVTHRLEELKYADGAVYMENGRVVRHGDAATI 254
Cdd:TIGR00957 1435 ALLRKTKILVLDEATAAVDlETDNL-----IQSTIRTQFEDCTVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNL 1506
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
75-197 1.99e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 48.63  E-value: 1.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   75 ILGPNGCGKSTLLKILAGVVNPSSGTVFVEKP-KNFVFQNpdHQvvMPTVEADVAfGLGKYHDMNQEEVKSRVIKALEAV 153
Cdd:PRK10636 343 LLGRNGAGKSTLIKLLAGELAPVSGEIGLAKGiKLGYFAQ--HQ--LEFLRADES-PLQHLARLAPQELEQKLRDYLGGF 417
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 23296450  154 GMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLD 197
Cdd:PRK10636 418 GFQgDKVTEETRRFSGGEKARLVLALIVWQRPNLLLLDEPTNHLD 462
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
144-235 2.00e-06

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: 47.99  E-value: 2.00e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 144 SRVIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTTFLDESDqmgvikaVKDLINA---- 214
Cdd:cd03271 147 ARKLQTLCDVGL-GYIKlgQPATTLSGGEAQRIKLAKELSKRSTgktLYILDEPTTGLHFHD-------VKKLLEVlqrl 218
                        90       100
                ....*....|....*....|..
gi 23296450 215 -KKGDvTALWVTHRLEELKYAD 235
Cdd:cd03271 219 vDKGN-TVVVIEHNLDVIKCAD 239
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
129-249 2.41e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 48.19  E-value: 2.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  129 FGLGKYHDMNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAV 208
Cdd:NF000106 108 YMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEV 187
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 23296450  209 KDLInakKGDVTALWVTHRLEEL-KYADGAVYMENGRVVRHG 249
Cdd:NF000106 188 RSMV---RDGATVLLTTQYMEEAeQLAHELTVIDRGRVIADG 226
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
53-245 4.15e-06

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 47.69  E-value: 4.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   53 QGISVPILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNP-----------------D 115
Cdd:PRK10762 261 DNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDG-HEVVTRSPqdglangivyisedrkrD 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  116 HQVVMPTVEADVA------FGLGKYHDMNQEEVksrvikalEAVGmrDY----------MQRPIQTLSGGQKQRIAIAGA 179
Cdd:PRK10762 340 GLVLGMSVKENMSltalryFSRAGGSLKHADEQ--------QAVS--DFirlfniktpsMEQAIGLLSGGNQQKVAIARG 409
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23296450  180 LAEACKVLLLDELTTFLDesdqMGVIKAVKDLINA-KKGDVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:PRK10762 410 LMTRPKVLILDEPTRGVD----VGAKKEIYQLINQfKAEGLSIILVSSEMPEvLGMSDRILVMHEGRI 473
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
60-254 5.40e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 46.73  E-value: 5.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   60 LRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPDHQVVMPTVEaDVAFG---LGkyhd 136
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAISAGLSGQLTGIE-NIEFKmlcMG---- 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  137 MNQEEVKSRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELttfLDESDQMGVIKAVKDLINAKK 216
Cdd:PRK13546 115 FKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEA---LSVGDQTFAQKCLDKIYEFKE 191
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 23296450  217 GDVTALWVTHRLEELK-YADGAVYMENGRVVRHGDAATI 254
Cdd:PRK13546 192 QNKTIFFVSHNLGQVRqFCTKIAWIEGGKLKDYGELDDV 230
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
61-245 9.52e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 46.58  E-value: 9.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   61 RDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVE-------KPKN-----FVFQNPDHQVVMPTVEADVA 128
Cdd:PRK15439 280 RNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNgkeinalSTAQrlargLVYLPEDRQSSGLYLDAPLA 359
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  129 FGLGK--YHDMN--QEEVKSRVIkaLE----AVGMR-DYMQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDES 199
Cdd:PRK15439 360 WNVCAltHNRRGfwIKPARENAV--LEryrrALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVS 437
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  200 DQMGVIKAVKDLinAKKGdVTALWVTHRLEEL-KYADGAVYMENGRV 245
Cdd:PRK15439 438 ARNDIYQLIRSI--AAQN-VAVLFISSDLEEIeQMADRVLVMHQGEI 481
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
43-214 1.80e-05

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 45.87  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450     43 RNLCFSVSTRQGISVpILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNP---SSGTVFVEKPK---------NFV 110
Cdd:TIGR00956  763 RNLTYEVKIKKEKRV-ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPldssfqrsiGYV 841
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    111 FQNPDHqVVMPTVEADVAFG--LGKYHDMNQEEVKSRVIKALEAVGMRDYMQR----PIQTLSGGQKQRIAIAGALAEAC 184
Cdd:TIGR00956  842 QQQDLH-LPTSTVRESLRFSayLRQPKSVSKSEKMEYVEEVIKLLEMESYADAvvgvPGEGLNVEQRKRLTIGVELVAKP 920
                          170       180       190
                   ....*....|....*....|....*....|.
gi 23296450    185 KVLL-LDELTTFLDESDQMGVIKAVKDLINA 214
Cdd:TIGR00956  921 KLLLfLDEPTSGLDSQTAWSICKLMRKLADH 951
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
53-251 3.04e-05

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 44.90  E-value: 3.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   53 QGISVPILR-DCSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGTVFVEKpKNFVFQNPDHQ-------------- 117
Cdd:PRK11288 261 DGLKGPGLRePISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDG-KPIDIRSPRDAiragimlcpedrka 339
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  118 ---VVMPTVEADVAFGLGKYH-------DMNQE-EVKSRVIKALeAVGMRDYMQrPIQTLSGGQKQRIAIAGALAEACKV 186
Cdd:PRK11288 340 egiIPVHSVADNINISARRHHlragcliNNRWEaENADRFIRSL-NIKTPSREQ-LIMNLSGGNQQKAILGRWLSEDMKV 417
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450  187 LLLDELTTFLDesdqMGVIKAVKDLIN--AKKGdVTALWVTHRLEE-LKYADGAVYMENGRV---VRHGDA 251
Cdd:PRK11288 418 ILLDEPTRGID----VGAKHEIYNVIYelAAQG-VAVLFVSSDLPEvLGVADRIVVMREGRIageLAREQA 483
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
60-249 3.33e-05

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 43.79  E-value: 3.33e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  60 LRDCSFRIPSGQLWMILGPNGCGKSTLlkilagvvnpSSGTVFVEKPKNFV------FQNPDHQvvMPTVEADVAFGLGK 133
Cdd:cd03270  11 LKNVDVDIPRNKLVVITGVSGSGKSSL----------AFDTIYAEGQRRYVeslsayARQFLGQ--MDKPDVDSIEGLSP 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 134 YHDMNQE--------------EVKS--RVIKALEAVGMR---------DY--MQRPIQTLSGGQKQRIAIAGAL-AEACK 185
Cdd:cd03270  79 AIAIDQKttsrnprstvgtvtEIYDylRLLFARVGIRERlgflvdvglGYltLSRSAPTLSGGEAQRIRLATQIgSGLTG 158
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450 186 VL-LLDELTTFLDESDQMGVIKAVKDLINAkkGDvTALWVTHRLEELKYADGAVYM------ENGRVVRHG 249
Cdd:cd03270 159 VLyVLDEPSIGLHPRDNDRLIETLKRLRDL--GN-TVLVVEHDEDTIRAADHVIDIgpgagvHGGEIVAQG 226
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
58-250 6.34e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 43.24  E-value: 6.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   58 PILRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGV--VNPSSGTVfVEKPKNFV---------------FQNPdhqVVM 120
Cdd:PRK09580  15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTV-EFKGKDLLelspedragegifmaFQYP---VEI 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  121 PTVEADvaFGLgkyhdmnQEEV----KSRVIKALEAVGMRDYMQRPIQTL---------------SGGQKQRIAIAGALA 181
Cdd:PRK09580  91 PGVSNQ--FFL-------QTALnavrSYRGQEPLDRFDFQDLMEEKIALLkmpedlltrsvnvgfSGGEKKRNDILQMAV 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23296450  182 EACKVLLLDELTTFLDesdqMGVIKAVKDLINA-KKGDVTALWVTHRLEELKY--ADGAVYMENGRVVRHGD 250
Cdd:PRK09580 162 LEPELCILDESDSGLD----IDALKIVADGVNSlRDGKRSFIIVTHYQRILDYikPDYVHVLYQGRIVKSGD 229
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
136-235 7.81e-05

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 43.85  E-value: 7.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   136 DMNQEEVK---------SRVIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTTFLDESDQ 201
Cdd:TIGR00630 790 DMTVEEAYeffeavpsiSRKLQTLCDVGL-GYIRlgQPATTLSGGEAQRIKLAKELSKRSTgrtLYILDEPTTGLHFDDI 868
                          90       100       110
                  ....*....|....*....|....*....|....
gi 23296450   202 MGVIKAVKDLInaKKGDvTALWVTHRLEELKYAD 235
Cdd:TIGR00630 869 KKLLEVLQRLV--DKGN-TVVVIEHNLDVIKTAD 899
COG3950 COG3950
Predicted ATP-binding protein involved in virulence [General function prediction only];
60-115 2.43e-04

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


Pssm-ID: 443150 [Multi-domain]  Cd Length: 276  Bit Score: 41.52  E-value: 2.43e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 23296450  60 LRDCSFRIPSGQLWMIL-GPNGCGKSTLLKILAGVVNPSSGTVFVEKPKNFVFQNPD 115
Cdd:COG3950  14 FEDLEIDFDNPPRLTVLvGENGSGKTTLLEAIALALSGLLSRLDDVKFRKLLIRNGE 70
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
143-265 5.97e-04

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 40.56  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  143 KSRVIKALEAVGMRDY---MQRPIQTLSGGQKQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGDV 219
Cdd:PRK15093 133 KRRAIELLHRVGIKDHkdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRL--NQNNNT 210
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 23296450  220 TALWVTHRLEEL-KYADGAVYMENGRVVrhgDAATISDFIKAKQSSY 265
Cdd:PRK15093 211 TILLISHDLQMLsQWADKINVLYCGQTV---ETAPSKELVTTPHHPY 254
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
43-191 8.87e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 40.38  E-value: 8.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   43 RNLCFSVSTRQGISVPilrdcSFRIPSGQLWMILGPNGCGKSTLLKILAGVVNPSSGT----------VFVEKPKNFV-- 110
Cdd:PRK10938   7 SQGTFRLSDTKTLQLP-----SLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFEQLQKLVsd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  111 -FQNPDHQVVMPTvEADvaFGLgKYHDMNQEEVK--SRVIKALEAVGMRDYMQRPIQTLSGGQKQRIAIAGALAEACKVL 187
Cdd:PRK10938  82 eWQRNNTDMLSPG-EDD--TGR-TTAEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLL 157

                 ....
gi 23296450  188 LLDE 191
Cdd:PRK10938 158 ILDE 161
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
145-194 1.28e-03

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 40.01  E-value: 1.28e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 23296450 145 RVIKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTT 194
Cdd:COG0178 805 RKLQTLQDVGL-GYIKlgQPATTLSGGEAQRVKLASELSKRSTgktLYILDEPTT 858
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
71-129 1.36e-03

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).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: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 39.94  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23296450    71 QLWMILGPNGCGKSTLLKILAGVVNPSsgtvFVE--KPKNFVFQNPDHQVVMPTVEADVAF 129
Cdd:TIGR00602 111 RILLITGPSGCGKSTTIKILSKELGIQ----VQEwsNPTLPDFQKNDHKVTLSLESCFSNF 167
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
147-235 1.48e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.81  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   147 IKALEAVGMrDYMQ--RPIQTLSGGQKQRIAIAGALAEACK---VLLLDELTTFLDESDQMGVIKAVKDLINAKKgdvTA 221
Cdd:PRK00635  790 IHALCSLGL-DYLPlgRPLSSLSGGEIQRLKLAYELLAPSKkptLYVLDEPTTGLHTHDIKALIYVLQSLTHQGH---TV 865
                          90
                  ....*....|....
gi 23296450   222 LWVTHRLEELKYAD 235
Cdd:PRK00635  866 VIIEHNMHVVKVAD 879
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
37-245 1.90e-03

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: 39.42  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450    37 NVAVECRNL-CFSVSTRQGISVpilRDCSFRIPSGQLWMILGPNGCGKSTLLKILAGVV-NPSSGTVFVEKpKNFVFQNP 114
Cdd:TIGR02633 255 DVILEARNLtCWDVINPHRKRV---DDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYpGKFEGNVFING-KPVDIRNP 330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450   115 ----DHQVVMptVEAD-------VAFGLGK---YHDMNQEEVKSRVIKALEAVGMRDYMQR----------PIQTLSGGQ 170
Cdd:TIGR02633 331 aqaiRAGIAM--VPEDrkrhgivPILGVGKnitLSVLKSFCFKMRIDAAAELQIIGSAIQRlkvktaspflPIGRLSGGN 408
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23296450   171 KQRIAIAGALAEACKVLLLDELTTFLDESDQMGVIKAVKDLinAKKGdVTALWVTHRLEE-LKYADGAVYMENGRV 245
Cdd:TIGR02633 409 QQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQL--AQEG-VAIIVVSSELAEvLGLSDRVLVIGEGKL 481
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
75-215 5.10e-03

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: 37.67  E-value: 5.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450  75 ILGPNGCGKSTLLKILAGVVNPSSGTVFveKPKNFvFQNPDHQVVMPTVEADVAFGLGK-YHDMNQEEVKSRVIKALEA- 152
Cdd:COG3593  28 LVGENNSGKSSILEALRLLLGPSSSRKF--DEEDF-YLGDDPDLPEIEIELTFGSLLSRlLRLLLKEEDKEELEEALEEl 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23296450 153 ---------------------------------------------VGMRDYMQRPIQTLSGGQKQRIAIA--GALAEACK 185
Cdd:COG3593 105 neelkealkalnellseylkelldgldlelelsldeledllkslsLRIEDGKELPLDRLGSGFQRLILLAllSALAELKR 184
                       170       180       190
                ....*....|....*....|....*....|....*
gi 23296450 186 -----VLLLDELTTFLDESDQMGVIKAVKDLINAK 215
Cdd:COG3593 185 apanpILLIEEPEAHLHPQAQRRLLKLLKELSEKP 219
 
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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