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Conserved domains on  [gi|1330606456|ref|WP_102503220|]
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ATP-binding cassette domain-containing protein [Vibrio splendidus]

Protein Classification

P-loop NTPase family protein( domain architecture ID 1562424)

P-loop NTPase (nucleoside triphosphate hydrolase) family protein contains two conserved sequence signatures, the Walker A motif (the P-loop proper) and Walker B motif which bind, respectively, the beta and gamma phosphate moieties of the bound nucleotide (typically ATP or GTP), and a Mg(2+) cation

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
 5-230 8.40e-64

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd03257:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 228  Bit Score: 198.88  E-value: 8.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGL-PMLQ 79
Cdd:cd03257     1 LLEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT---SGSIIFDGKDLLKLsRRLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAAQRPAVIFQDALQALNPLVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICI 159
Cdd:cd03257    78 KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLR-IHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLhSALA--CDKLLVIDGGGVVAYG 230
Cdd:cd03257   157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDL-GVVAkiADRVAVMYAGKIVEEG 228
 
Name Accession Description Interval E-value
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 5-230 8.40e-64

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: 198.88  E-value: 8.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGL-PMLQ 79
Cdd:cd03257     1 LLEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT---SGSIIFDGKDLLKLsRRLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAAQRPAVIFQDALQALNPLVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICI 159
Cdd:cd03257    78 KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLR-IHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLhSALA--CDKLLVIDGGGVVAYG 230
Cdd:cd03257   157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDL-GVVAkiADRVAVMYAGKIVEEG 228
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 3-238 4.34e-58

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: 192.43  E-value: 4.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSSRTLF--QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPMLQR 80
Cdd:COG1123     2 TPLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 taAQRPAVIFQDALQALNPlVSIEGQLSLALtgtRTKLKSQDKIK--LTELLVQLGFpnpETILPLYPSQISGGQRQRIC 158
Cdd:COG1123    82 --GRRIGMVFQDPMTQLNP-VTVGDQIAEAL---ENLGLSRAEARarVLELLEAVGL---ERRLDRYPHQLSGGQRQRVA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALE 237
Cdd:COG1123   153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232


                  .
gi 1330606456 238 S 238
Cdd:COG1123   233 A 233
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 20-242 5.35e-45

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


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 150.60  E-value: 5.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  20 LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEGHISLSGDAVCGLPMLQRTAAqrpaVIFQDALQALN 98
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLpPGLTQTSGEILLDGRPLLPLSIRGRHIA----TIMQNPRTAFN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 PLVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:TIGR02770  77 PLFTMGNHAIETLR-SLGKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 179 LDPVTEQEILKLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVvARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 4-251 1.54e-36

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 131.39  E-value: 1.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQL--TIKTS--SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLP--M 77
Cdd:PRK09473   11 ALLDVKDLrvTFSTPdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPekE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  78 LQRTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRI 157
Cdd:PRK09473   91 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 158 CIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDGGGVVAYGAPKHAL 236
Cdd:PRK09473  171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGNARDVF 250

                         250
                  ....*....|....*
gi 1330606456 237 ESSSHAFCCSLRDLI 251
Cdd:PRK09473  251 YQPSHPYSIGLLNAV 265
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 21-177 1.26e-32

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: 116.21  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTaaQRPAVIFQDAlqALNPL 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT---EGTILLDGQDLTDDERKSLR--KEIGYVFQDP--QLFPR 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 101 VSIEGQLSLALTGTRTKlKSQDKIKLTELLVQLGFPN-PETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:pfam00005  74 LTVRENLRLGLLLKGLS-KREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
17-221 4.97e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 81.90  E-value: 4.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDavcglpmLQRTAAQRPA-VIFQDALQ 95
Cdd:NF040873    4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPT---------SGT-------VRRAGGARVAyVPQRSEVP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLvSIEGQLSLALTGTRT---KLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:NF040873   68 DSLPL-TVRDLVAMGRWARRGlwrRLTRDDRAAVDDALERVGL---ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKqRQIGGLLITHDLHSALACDKLLVI 221
Cdd:NF040873  144 DEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
22-223 9.27e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 52.10  E-value: 9.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPeTVEVEGHISLSGDaVCGLPMLqRTAAQRPAVIFQDALqALNPLV 101
Cdd:NF040905   18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSYEGEILFDGE-VCRFKDI-RDSEALGIVIIHQEL-ALIPYL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SI------------EGQLSLALTGTRTKlksqdkikltELLVQLGFP-NPETILplypSQISGGQRQRICIAIGLLSNAD 168
Cdd:NF040905   94 SIaeniflgnerakRGVIDWNETNRRAR----------ELLAKVGLDeSPDTLV----TDIGVGKQQLVEIAKALSKDVK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 169 LIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLH--SALAcDKLLVI-DG 223
Cdd:NF040905  160 LLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNeiRRVA-DSITVLrDG 215
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
102-230 8.26e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 46.27  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSLALTGTRTKLKSQD-KIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:NF000106  100 SFSGRENLYMIGR*LDLSRKDaRARADELLERFSLTEAAG---RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1330606456 181 PVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:NF000106  177 PRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 30-206 1.10e-04

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: 41.20  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   30 RGELLAIMGPSGIGKSMLSRAIAGFLPETVEVeghislsgdavcglpmlqrtaaqrpaVIFqdalqalnplvsiegqlsl 109
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--------------------------VIY------------------- 35

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  110 altgtrtklksqdkIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILK 189
Cdd:smart00382  36 --------------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101

                          170
                   ....*....|....*..
gi 1330606456  190 LIRDNVKQRQIGGLLIT 206
Cdd:smart00382 102 LEELRLLLLLKSEKNLT 118
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
142-242 2.34e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 42.03  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 142 LPLypsqisgGQRQRICIAIGLLSNADLIIADEPTSALDPVTeqeilkliRDNVKQrqiggLLI-------------THD 208
Cdd:NF033858  398 LPL-------GIRQRLSLAVAVIHKPELLILDEPTSGVDPVA--------RDMFWR-----LLIelsredgvtifisTHF 457

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1330606456 209 LHSALACDKLLVIDGGGVVAYGAPKhALESSSHA 242
Cdd:NF033858  458 MNEAERCDRISLMHAGRVLASDTPA-ALVAARGA 490
 
Name Accession Description Interval E-value
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 5-230 8.40e-64

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: 198.88  E-value: 8.40e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGL-PMLQ 79
Cdd:cd03257     1 LLEVKNLSVsfptGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPT---SGSIIFDGKDLLKLsRRLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAAQRPAVIFQDALQALNPLVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICI 159
Cdd:cd03257    78 KIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLR-IHGKLSKKEARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLhSALA--CDKLLVIDGGGVVAYG 230
Cdd:cd03257   157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDL-GVVAkiADRVAVMYAGKIVEEG 228
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 3-238 4.34e-58

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: 192.43  E-value: 4.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSSRTLF--QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPMLQR 80
Cdd:COG1123     2 TPLLEVRDLSVRYPGGDVPavDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGRISGEVLLDGRDLLELSEALR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 taAQRPAVIFQDALQALNPlVSIEGQLSLALtgtRTKLKSQDKIK--LTELLVQLGFpnpETILPLYPSQISGGQRQRIC 158
Cdd:COG1123    82 --GRRIGMVFQDPMTQLNP-VTVGDQIAEAL---ENLGLSRAEARarVLELLEAVGL---ERRLDRYPHQLSGGQRQRVA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALE 237
Cdd:COG1123   153 IAMALALDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEiADRVVVMDDGRIVEDGPPEEILA 232


                  .
gi 1330606456 238 S 238
Cdd:COG1123   233 A 233
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 5-234 6.56e-58

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: 186.80  E-value: 6.56e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTI--KTSSRTLF--QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLP--ML 78
Cdd:COG0444     1 LLEVRNLKVyfPTRRGVVKavDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPPGITSGEILFDGEDLLKLSekEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRIC 158
Cdd:COG0444    81 RKIRGREIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDPERRLDRYPHELSGGMRQRVM 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLhSALA--CDKLLVIDGGGVVAYG------ 230
Cdd:COG0444   161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDL-GVVAeiADRVAVMYAGRIVEEGpveelf 239


                  ....*
gi 1330606456 231 -APKH 234
Cdd:COG0444   240 eNPRH 244
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 5-249 1.68e-54

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: 175.76  E-value: 1.68e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcgLPMLQR 80
Cdd:COG1124     1 MLEVRNLSVsygqGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPW---SGEVTFDGRPV--TRRRRK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRtklKSQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQRICIA 160
Cdd:COG1124    76 AFRRRVQMVFQDPYASLHPRHTVDRILAEPLRIHG---LPDREERIAELLEQVGLP--PSFLDRYPHQLSGGQRQRVAIA 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALESS 239
Cdd:COG1124   151 RALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQNGRIVEELTVADLLAGP 230

                         250
                  ....*....|
gi 1330606456 240 SHAFCCSLRD 249
Cdd:COG1124   231 KHPYTRELLA 240
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 3-242 5.39e-52

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: 176.25  E-value: 5.39e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTI-----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPM 77
Cdd:COG1123   258 EPLLEVRNLSKrypvrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPT---SGSILFDGKDLTKLSR 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  78 LQ-RTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQR 156
Cdd:COG1123   335 RSlRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLP--PDLADRYPHELSGGQRQR 412

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 157 ICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHA 235
Cdd:COG1123   413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYiADRVAVMYDGRIVEDGPTEEV 492


                  ....*..
gi 1330606456 236 LESSSHA 242
Cdd:COG1123   493 FANPQHP 499
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 1-235 6.77e-51

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: 173.72  E-value: 6.77e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPE-TVEVEGHISLSGDAVCGL 75
Cdd:COG4172     2 MSMPLLSVEDLSVafgqGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALSILRLLPDpAAHPSGSILFDGQDLLGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  76 P--MLQRTAAQRPAVIFQDALQALNPLVSIEGQL--SLALTGTRTKLKSQDKIklTELLVQLGFPNPETILPLYPSQISG 151
Cdd:COG4172    82 SerELRRIRGNRIAMIFQEPMTSLNPLHTIGKQIaeVLRLHRGLSGAAARARA--LELLERVGIPDPERRLDAYPHQLSG 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 152 GQRQRICIAIGLLSNADLIIADEPTSALDpVTEQ-EILKLIRDNVKQRQIGGLLITHDLH--SALAcDKLLVIDGGGVVA 228
Cdd:COG4172   160 GQRQRVMIAMALANEPDLLIADEPTTALD-VTVQaQILDLLKDLQRELGMALLLITHDLGvvRRFA-DRVAVMRQGEIVE 237

                         250
                  ....*....|....
gi 1330606456 229 YG-------APKHA 235
Cdd:COG4172   238 QGptaelfaAPQHP 251
nickel_nikD TIGR02770
nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...
 20-242 5.35e-45

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


Pssm-ID: 131817 [Multi-domain]  Cd Length: 230  Bit Score: 150.60  E-value: 5.35e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  20 LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEGHISLSGDAVCGLPMLQRTAAqrpaVIFQDALQALN 98
Cdd:TIGR02770   1 LVQDLNLSLKRGEVLALVGESGSGKSLTCLAILGLLpPGLTQTSGEILLDGRPLLPLSIRGRHIA----TIMQNPRTAFN 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 PLVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:TIGR02770  77 PLFTMGNHAIETLR-SLGKLSKQARALILEALEAVGLPDPEEVLKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTD 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 179 LDPVTEQEILKLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:TIGR02770 156 LDVVNQARVLKLLRELRQLFGTGILLITHDLGVvARIADEVAVMDDGRIVERGTVKEIFYNPKHE 220
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 6-223 2.94e-41

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 140.31  E-value: 2.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPMLQRtaaqR 85
Cdd:COG4136     2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPAFSASGEVLLNGRRLTALPAEQR----R 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDALqaLNPLVSIEGQLSLALTGTRTKLKSQDKIKltELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLLS 165
Cdd:COG4136    78 IGILFQDDL--LFPHLSVGENLAFALPPTIGRAQRRARVE--QALEEAGLAGFAD---RDPATLSGGQRARVALLRALLA 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDG 223
Cdd:COG4136   151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDLGN 208
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 1-243 1.93e-40

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


Pssm-ID: 440744 [Multi-domain]  Cd Length: 241  Bit Score: 139.34  E-value: 1.93e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQR 80
Cdd:COG1127     1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPD---SGEILVDGQDITGLSEKEL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRP-AVIFQDAlqAL--------N---PLvsIEgqlslaltgtRTKLKSQDKIKL-TELLVQLGFPNpetILPLYPS 147
Cdd:COG1127    78 YELRRRiGMLFQGG--ALfdsltvfeNvafPL--RE----------HTDLSEAEIRELvLEKLELVGLPG---AADKMPS 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 148 QISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGV 226
Cdd:COG1127   141 ELSGGMRKRVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAiADRVAVLADGKI 220

                         250
                  ....*....|....*..
gi 1330606456 227 VAYGAPKhALESSSHAF 243
Cdd:COG1127   221 IAEGTPE-ELLASDDPW 236
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
6-226 3.04e-40

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 137.64  E-value: 3.04e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPML---QRTA 82
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPT---SGEIYLDGKPLSAMPPPewrRQVA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 --AQRPAvIFQDalqalnplvSIEGQLSLALtgtRTKLKSQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQRICIA 160
Cdd:COG4619    78 yvPQEPA-LWGG---------TVRDNLPFPF---QLRERKFDRERALELLERLGLP--PDILDKPVERLSGGERQRLALI 142

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDGGGV 226
Cdd:COG4619   143 RALLLQPDVLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEqIERVADRVLTLEAGRL 209
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-250 5.17e-40

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 138.30  E-value: 5.17e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCG------ 74
Cdd:COG1121     2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPT---SGTVRLFGKPPRRarrrig 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  75 -LPmlQRTAAQR--PAVIFQdalqalnpLVSiegqlsLALTGTR---TKLKSQDKIKLTELLVQLGfpnpetILPLYPSQ 148
Cdd:COG1121    79 yVP--QRAEVDWdfPITVRD--------VVL------MGRYGRRglfRRPSRADREAVDEALERVG------LEDLADRP 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 149 I---SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDgG 224
Cdd:COG1121   137 IgelSGGQQQRVLLARALAQDPDLLLLDEPFAGVDAATEEALYELLRE-LRREGKTILVVTHDLGAVREyFDRVLLLN-R 214

                         250       260
                  ....*....|....*....|....*...
gi 1330606456 225 GVVAYGAPKHALESS--SHAFCCSLRDL 250
Cdd:COG1121   215 GLVAHGPPEEVLTPEnlSRAYGGPVALL 242
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 5-236 9.10e-40

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: 137.87  E-value: 9.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaAQ 84
Cdd:COG1120     1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPS---SGEVLLDGRDLASLSRREL--AR 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDALQALNPLVsiegqLSLALTGtRT-------KLKSQDKIKLTELLVQLGfpnpetILPL---YPSQISGGQR 154
Cdd:COG1120    76 RIAYVPQEPPAPFGLTV-----RELVALG-RYphlglfgRPSAEDREAVEEALERTG------LEHLadrPVDELSGGER 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 155 QRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDL-HSALACDKLLVIDGGGVVAYGAPK 233
Cdd:COG1120   144 QRVLIARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLnLAARYADRLVLLKDGRIVAQGPPE 223


                  ...
gi 1330606456 234 HAL 236
Cdd:COG1120   224 EVL 226
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
3-228 2.11e-39

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 136.33  E-value: 2.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTiKT-----SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPM 77
Cdd:COG1136     2 SPLLELRNLT-KSygtgeGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPT---SGEVLIDGQDISSLSE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  78 LQRTA--AQRPAVIFQDA--LQALNPLVSIEgqLSLALTGTRtklKSQDKIKLTELLVQLGFPNpetILPLYPSQISGGQ 153
Cdd:COG1136    78 RELARlrRRHIGFVFQFFnlLPELTALENVA--LPLLLAGVS---RKERRERARELLERVGLGD---RLDHRPSQLSGGQ 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVA 228
Cdd:COG1136   150 QQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIVS 224
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 6-230 8.20e-39

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: 134.18  E-value: 8.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaaqR 85
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPD---SGEILIDGRDVTGVPPERR----N 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDAlqALNPLVSIEGQLSLALTGtRTKLKSQDKIKLTELLVQLGFPNPetiLPLYPSQISGGQRQRICIAIGLLS 165
Cdd:cd03259    74 IGMVFQDY--ALFPHLTVAENIAFGLKL-RGVPKAEIRARVRELLELVGLEGL---LNRYPHELSGGQQQRVALARALAR 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03259   148 EPSLLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALAlADRIAVMNEGRIVQVG 213
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 6-243 3.46e-38

ATP-binding cassette transport system involved in resistance to organic solvents; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213228 [Multi-domain]  Cd Length: 235  Bit Score: 133.40  E-value: 3.46e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGL-PMLQRTAAQ 84
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPD---SGEVLIDGEDISGLsEAELYRLRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDAlqALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLL 164
Cdd:cd03261    78 RMGMLFQSG--ALFDSLTVFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAED---LYPAELSGGMKKRVALARALA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 165 SNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGaPKHALESSSHAF 243
Cdd:cd03261   153 LDPELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAiADRIAVLYDGKIVAEG-TPEELRASDDPL 231
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 22-224 8.21e-37

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: 129.15  E-value: 8.21e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTA--AQRPAVIFQD--ALQAL 97
Cdd:cd03255    21 KGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPT---SGEVRVDGTDISKLSEKELAAfrRRHIGFVFQSfnLLPDL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIEgqLSLALTGTRtklKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:cd03255    98 TALENVE--LPLLLAGVP---KKERRERAEELLERVGL---GDRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTG 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1330606456 178 ALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGG 224
Cdd:cd03255   170 NLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDG 216
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
25-242 1.48e-36

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 129.10  E-value: 1.48e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  25 HFD--VYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqrtAAQRP-AVIFQDalQALNPLV 101
Cdd:COG3840    17 RFDltIAAGERVAILGPSGAGKSTLLNLIAGFLPPD---SGRILWNGQDLTALP-----PAERPvSMLFQE--NNLFPHL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDP 181
Cdd:COG3840    87 TVAQNIGLGLR-PGLKLTAEQRAQVEQALERVGL---AGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 182 VTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:COG3840   163 ALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAADGPTAALLDGEPPP 224
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 4-251 1.54e-36

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 131.39  E-value: 1.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQL--TIKTS--SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLP--M 77
Cdd:PRK09473   11 ALLDVKDLrvTFSTPdgDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAANGRIGGSATFNGREILNLPekE 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  78 LQRTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRI 157
Cdd:PRK09473   91 LNKLRAEQISMIFQDPMTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKMPEARKRMKMYPHEFSGGMRQRV 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 158 CIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDGGGVVAYGAPKHAL 236
Cdd:PRK09473  171 MIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGvVAGICDKVLVMYAGRTMEYGNARDVF 250

                         250
                  ....*....|....*
gi 1330606456 237 ESSSHAFCCSLRDLI 251
Cdd:PRK09473  251 YQPSHPYSIGLLNAV 265
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 7-230 2.40e-36

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: 126.78  E-value: 2.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaAQRP 86
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPS---SGEILLDGKDLASLSPKEL--ARKI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  87 AVIFQdalqalnplvsiegqlSLALTGTrTKLKSQDkikLTELlvqlgfpnpetilplypsqiSGGQRQRICIAIGLLSN 166
Cdd:cd03214    76 AYVPQ----------------ALELLGL-AHLADRP---FNEL--------------------SGGERQRVLLARALAQE 115

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 167 ADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDL-HSALACDKLLVIDGGGVVAYG 230
Cdd:cd03214   116 PPILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLnLAARYADRVILLKDGRIVAQG 180
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 16-224 1.35e-35

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: 124.42  E-value: 1.35e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQRTAAQRPAVIFQDAlq 95
Cdd:cd03228    13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPT---SGEILIDGVDLRDLD--LESLRKNIAYVPQDP-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 alnplvsiegQLslaLTGTrtklksqdkIKltellvqlgfpnpETILplypsqiSGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:cd03228    86 ----------FL---FSGT---------IR-------------ENIL-------SGGQRQRIAIARALLRDPPILILDEA 123

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1330606456 176 TSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGG 224
Cdd:cd03228   124 TSALDPETEALILEALRALAKGKTV--IVIAHRLSTIRDADRIIVLDDG 170
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 14-223 1.37e-35

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 126.05  E-value: 1.37e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGlpmlqrtAAQRPAVIFQDA 93
Cdd:cd03293    13 GGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPT---SGEVLVDGEPVTG-------PGPDRGYVFQQD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 lqALNPLVSIEGQLSLALTGTRTKlKSQDKIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLLSNADLIIAD 173
Cdd:cd03293    83 --ALLPWLTVLDNVALGLELQGVP-KAEARERAEELLELVGLSGFEN---AYPHQLSGGMRQRVALARALAVDPDVLLLD 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 174 EPTSALDPVT----EQEILKLIRdnvkQRQIGGLLITHDLHSALA-CDKLLVIDG 223
Cdd:cd03293   157 EPFSALDALTreqlQEELLDIWR----ETGKTVLLVTHDIDEAVFlADRVVVLSA 207
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 19-230 1.69e-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: 126.16  E-value: 1.69e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  19 TLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQ-RTAAQRPAVIFQ--DALQ 95
Cdd:cd03258    19 TALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPT---SGSVLVDGTDLTLLSGKElRKARRRIGMIFQhfNLLS 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLVSIEgqLSLALTGTRtklKSQDKIKLTELLVQLGFPNPETIlplYPSQISGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:cd03258    96 SRTVFENVA--LPLEIAGVP---KAEIEERVLELLELVGLEDKADA---YPAQLSGGQKQRVGIARALANNPKVLLCDEA 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 176 TSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03258   168 TSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRiCDRVAVMEKGEVVEEG 223
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-224 1.88e-35

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 126.74  E-value: 1.88e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLT----IKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP 76
Cdd:COG1116     3 AAAPALELRGVSkrfpTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPT---SGEVLVDGKPVTGPG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  77 mlqrtaaQRPAVIFQDAlqALNPLVSIEGQLSLALTGtRTKLKSQDKIKLTELL--VQL-GFPNpetilpLYPSQISGGQ 153
Cdd:COG1116    80 -------PDRGVVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLelVGLaGFED------AYPHQLSGGM 143

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:COG1116   144 RQRVAIARALANDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFlADRVVVLSAR 215
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 6-236 1.40e-34

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 124.43  E-value: 1.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSsRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVE-VEGHISLSGDAVCGLPMLQRTAAq 84
Cdd:PRK10418    5 IELRNIALQAA-QPLVHGVSLTLQRGRVLALVGGSGSGKSLTCAAALGILPAGVRqTAGRVLLDGKPVAPCALRGRKIA- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 rpaVIFQDALQALNPLVSIEgqlSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLL 164
Cdd:PRK10418   83 ---TIMQNPRSAFNPLHTMH---THARETCLALGKPADDATLTAALEAVGLENAARVLKLYPFEMSGGMLQRMMIALALL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 165 SNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALAC-DKLLVIDGGGVVAYG-------APKHAL 236
Cdd:PRK10418  157 CEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLaDDVAVMSHGRIVEQGdvetlfnAPKHAV 236
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 14-224 2.74e-34

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: 122.58  E-value: 2.74e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaAQRPAVIFQDA 93
Cdd:cd03225    10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPT---SGEVLVDGKDLTKLSLKEL--RRKVGLVFQNP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 -LQALNPLVSIE---GQLSLALTgtrtklKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADL 169
Cdd:cd03225    85 dDQFFGPTVEEEvafGLENLGLP------EEEIEERVEEALELVGL---EGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 170 IIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:cd03225   156 LLLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLLElADRVIVLEDG 210
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 1-243 4.16e-34

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 128.28  E-value: 4.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPE--TVEVEGHISLSGDAV-- 72
Cdd:PRK15134    1 MTQPLLAIENLSVafrqQQTVRTVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSppVVYPSGDIRFHGESLlh 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  73 CGLPMLQRTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGG 152
Cdd:PRK15134   81 ASEQTLRGVRGNKIAMIFQEPMVSLNPLHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRLTDYPHQLSGG 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA--LAcDKLLVIDGGGVVAYG 230
Cdd:PRK15134  161 ERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVrkLA-DRVAVMQNGRCVEQN 239

                         250
                  ....*....|...
gi 1330606456 231 APKHALESSSHAF 243
Cdd:PRK15134  240 RAATLFSAPTHPY 252
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 7-230 6.91e-34

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: 121.49  E-value: 6.91e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET---VEVEG-HISLSGDAVCGLPmlQRTA 82
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTsgsIRVFGkPLEKERKRIGYVP--QRRS 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 AQR--PavifqdalqalnplVSIEGQLSLALTGTR---TKLKSQDKIKLTELLVQLGfpnpetILPLYPSQI---SGGQR 154
Cdd:cd03235    79 IDRdfP--------------ISVRDVVLMGLYGHKglfRRLSKADKAKVDEALERVG------LSELADRQIgelSGGQQ 138

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 155 QRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSALA-CDKLLVIDgGGVVAYG 230
Cdd:cd03235   139 QRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLR-ELRREGMTILVVTHDLGLVLEyFDRVLLLN-RTVVASG 213
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 6-224 7.15e-34

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: 120.37  E-value: 7.15e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQR 85
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPD---SGSILIDGEDLTDLEDELPPLRRR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDAlqALNPLVSIEGQLSLALtgtrtklksqdkikltellvqlgfpnpetilplypsqiSGGQRQRICIAIGLLS 165
Cdd:cd03229    78 IGMVFQDF--ALFPHLTVLENIALGL--------------------------------------SGGQQQRVALARALAM 117

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:cd03229   118 DPDVLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLRDG 177
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 5-247 2.39e-33

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 122.93  E-value: 2.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTI-----KTSSRTLfQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL--PETVEVEgHISLSGDAVCGLPM 77
Cdd:PRK11022    3 LLNVDKLSVhfgdeSAPFRAV-DRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLIdyPGRVMAE-KLEFNGQDLQRISE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  78 LQRT--AAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQ 155
Cdd:PRK11022   81 KERRnlVGAEVAMIFQDPMTSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGIPDPASRLDVYPHQLSGGMSQ 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDGGGVVAYGAPKH 234
Cdd:PRK11022  161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLAlVAEAAHKIIVMYAGQVVETGKAHD 240

                         250
                  ....*....|...
gi 1330606456 235 ALESSSHAFCCSL 247
Cdd:PRK11022  241 IFRAPRHPYTQAL 253
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 3-237 3.21e-33

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: 126.42  E-value: 3.21e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIK--TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQR 80
Cdd:COG4987   331 GPSLELEDVSFRypGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQ---SGSITLGGVDLRDLD--ED 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVIFQDA----------LQALNPLVSiEGQLSLALtgtrtklksqDKIKLTELLVQLgfpnPE---TILPLYPS 147
Cdd:COG4987   406 DLRRRIAVVPQRPhlfdttlrenLRLARPDAT-DEELWAAL----------ERVGLGDWLAAL----PDgldTWLGEGGR 470

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 148 QISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVV 227
Cdd:COG4987   471 RLSGGERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGRTV--LLITHRLAGLERMDRILVLEDGRIV 548

                         250
                  ....*....|
gi 1330606456 228 AYGAPKHALE 237
Cdd:COG4987   549 EQGTHEELLA 558
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 2-238 5.09e-33

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: 125.64  E-value: 5.09e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQLTIK-TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPM--L 78
Cdd:COG4988   333 GPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPY---SGSILINGVDLSDLDPasW 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTAA---QRPaVIFQDALQ---AL-NPLVSIEgQLSLALtgtrtklksqDKIKLTELLVQLgfPN-PETILPLYPSQIS 150
Cdd:COG4988   410 RRQIAwvpQNP-YLFAGTIRenlRLgRPDASDE-ELEAAL----------EAAGLDEFVAAL--PDgLDTPLGEGGRGLS 475

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:COG4988   476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGRTV--ILITHRLALLAQADRILVLDDGRIVEQG 553


                  ....*...
gi 1330606456 231 APKHALES 238
Cdd:COG4988   554 THEELLAK 561
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 3-235 5.51e-33

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: 125.18  E-value: 5.51e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIK-TSSRTLFQ----------DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPetveVEGHISLSGDA 71
Cdd:COG4172   273 PPLLEARDLKVWfPIKRGLFRrtvghvkavdGVSLTLRRGETLGLVGESGSGKSTLGLALLRLIP----SEGEIRFDGQD 348

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  72 VCGLpmlqRTAAQRPA-----VIFQDALQALNPLVSI-----EGqlsLALTGTRTKLKSQDKiKLTELLVQLGFPnPETi 141
Cdd:COG4172   349 LDGL----SRRALRPLrrrmqVVFQDPFGSLSPRMTVgqiiaEG---LRVHGPGLSAAERRA-RVAEALEEVGLD-PAA- 418

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 142 LPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH--SALaCDKLL 219
Cdd:COG4172   419 RHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAvvRAL-AHRVM 497

                         250       260
                  ....*....|....*....|...
gi 1330606456 220 VIDGGGVVAYG-------APKHA 235
Cdd:COG4172   498 VMKDGKVVEQGpteqvfdAPQHP 520
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 1-209 7.77e-33

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 121.76  E-value: 7.77e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTiKT--SSRTLFQ----------DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLS 68
Cdd:COG4608     3 MAEPLLEVRDLK-KHfpVRGGLFGrtvgvvkavdGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPT---SGEILFD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  69 GDAVCGLPMLQRtAAQRPAV--IFQDALQALNPLVSIEGQLSLALT--GTRTKLKSQDKIKltELLVQLGFpNPETiLPL 144
Cdd:COG4608    79 GQDITGLSGREL-RPLRRRMqmVFQDPYASLNPRMTVGDIIAEPLRihGLASKAERRERVA--ELLELVGL-RPEH-ADR 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 145 YPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDpVTEQ-EILKLIRDNVKQRQIGGLLITHDL 209
Cdd:COG4608   154 YPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD-VSIQaQVLNLLEDLQDELGLTYLFISHDL 218
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 6-237 7.84e-33

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: 119.36  E-value: 7.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIK-TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISlsgdaVCGLPMLQRTAAQ 84
Cdd:COG1122     1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPT---SGEVL-----VDGKDITKKNLRE 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 -RPAV--IFQDA-LQALNPLVSIE---GQLSLALtgtrtklkSQDKIK--LTELLVQLGFpnpETILPLYPSQISGGQRQ 155
Cdd:COG1122    73 lRRKVglVFQNPdDQLFAPTVEEDvafGPENLGL--------PREEIRerVEEALELVGL---EHLADRPPHELSGGQKQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 156 RICIAiGLLS-NADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPK 233
Cdd:COG1122   142 RVAIA-GVLAmEPEVLVLDEPTAGLDPRGRRELLELLKR-LNKEGKTVIIVTHDLDLVAElADRVIVLDDGRIVADGTPR 219


                  ....
gi 1330606456 234 HALE 237
Cdd:COG1122   220 EVFS 223
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 21-177 1.26e-32

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: 116.21  E-value: 1.26e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTaaQRPAVIFQDAlqALNPL 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPT---EGTILLDGQDLTDDERKSLR--KEIGYVFQDP--QLFPR 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 101 VSIEGQLSLALTGTRTKlKSQDKIKLTELLVQLGFPN-PETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:pfam00005  74 LTVRENLRLGLLLKGLS-KREKDARAEEALEKLGLGDlADRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 1-232 1.79e-32

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 121.36  E-value: 1.79e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqr 80
Cdd:COG3842     1 MAMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPD---SGRILLDGRDVTGLP---- 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 tAAQRP-AVIFQDAlqALNPLVSIEGQLSLALTGTRTKlKSQDKIKLTELL--VQLGfpnpetilPL---YPSQISGGQR 154
Cdd:COG3842    74 -PEKRNvGMVFQDY--ALFPHLTVAENVAFGLRMRGVP-KAEIRARVAELLelVGLE--------GLadrYPHQLSGGQQ 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 155 QRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:COG3842   142 QRVALARALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALAlADRIAVMNDGRIEQVGTP 220
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
25-238 9.27e-32

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 116.61  E-value: 9.27e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  25 HFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSG-DAVCGLPmlqrtaAQRP-AVIFQDalQALNPLVS 102
Cdd:PRK10771   19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPA---SGSLTLNGqDHTTTPP------SRRPvSMLFQE--NNLFSHLT 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPV 182
Cdd:PRK10771   88 VAQNIGLGLN-PGLKLNAAQREKLHAIARQMGI---EDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 183 TEQEILKLIRDNVKQRQIGGLLITHDLHSA--LACDKLLVIDGGgvVAYGAPKHALES 238
Cdd:PRK10771  164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAarIAPRSLVVADGR--IAWDGPTDELLS 219
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 4-232 1.90e-31

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 115.92  E-value: 1.90e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTiKT--SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRT 81
Cdd:COG3638     1 PMLELRNLS-KRypGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGEILVDGQDVTALRGRALR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAQRP-AVIFQ--------DALQalNPLVSIEGQLSLALTGTRtKLKSQDKIKLTELLVQLGfpnpetILPLY---PSQI 149
Cdd:COG3638    77 RLRRRiGMIFQqfnlvprlSVLT--NVLAGRLGRTSTWRSLLG-LFPPEDRERALEALERVG------LADKAyqrADQL 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVA 228
Cdd:COG3638   148 SGGQQQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRyADRIIGLRDGRVVF 227


                  ....
gi 1330606456 229 YGAP 232
Cdd:COG3638   228 DGPP 231
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 23-230 2.45e-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: 115.08  E-value: 2.45e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVyRGELLAIMGPSGIGKSMLSRAIAGFlpETVEVeGHISLSG-------DAVCgLPMLQRtaaqRPAVIFQDAlq 95
Cdd:cd03297    16 KIDFDL-NEEVTGIFGASGAGKSTLLRCIAGL--EKPDG-GTIVLNGtvlfdsrKKIN-LPPQQR----KIGLVFQQY-- 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLVSIEGQLSLaltGTRTKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:cd03297    85 ALFPHLNVRENLAF---GLKRKRNREDRISVDELLDLLGL---DHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 176 TSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYG 230
Cdd:cd03297   159 FSALDRALRLQLLPELKQIKKNLNIPVIFVTHDLSEAeYLADRIVVMEDGRLQYIG 214
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 6-232 4.77e-31

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: 114.97  E-value: 4.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTiKT--SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQ-RTA 82
Cdd:cd03256     1 IEVENLS-KTypNGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPT---SGSVLIDGTDINKLKGKAlRQL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 AQRPAVIFQDaLQALNPLVSIEGQLSLALtGTRTKLKS-------QDKIKLTELLVQLGfpnpetILPLY---PSQISGG 152
Cdd:cd03256    77 RRQIGMIFQQ-FNLIERLSVLENVLSGRL-GRRSTWRSlfglfpkEEKQRALAALERVG------LLDKAyqrADQLSGG 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGA 231
Cdd:cd03256   149 QQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIVFDGP 228


                  .
gi 1330606456 232 P 232
Cdd:cd03256   229 P 229
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 6-243 1.44e-30

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: 113.58  E-value: 1.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLfQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETveveGHISLSGDAVCGLPMLQRtaaq 84
Cdd:cd03299     1 LKVENLSKDWKEFKL-KNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIkPDS----GKILLNGKDITNLPPEKR---- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDalQALNPLVSIEGQLSLALtgtrtKLKSQDKIKLTELLVQL-GFPNPETILPLYPSQISGGQRQRICIAIGL 163
Cdd:cd03299    72 DISYVPQN--YALFPHMTVYKNIAYGL-----KKRKVDKKEIERKVLEIaEMLGIDHLLNRKPETLSGGEQQRVAIARAL 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:cd03299   145 VVNPKILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWAlADKVAIMLNGKLIQVGKPEEVFKKPKNE 224


                  .
gi 1330606456 243 F 243
Cdd:cd03299   225 F 225
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 14-241 1.92e-30

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: 114.13  E-value: 1.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQRPA-VIFQD 92
Cdd:TIGR02769  20 AKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPA---QGTVSFRGQDLYQLDRKQRRAFRRDVqLVFQD 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:TIGR02769  97 SPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLR--SEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYgAPKHALESSSH 241
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVMDKGQIVEE-CDVAQLLSFKH 243
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
1-240 2.28e-30

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 113.96  E-value: 2.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTI--KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAG-FLPE--TVEVeGHISLSGDAVCGL 75
Cdd:PRK13635    1 MKEEIIRVEHISFryPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGlLLPEagTITV-GGMVLSEETVWDV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  76 pmlqrtaAQRPAVIFQdalqalNPlvsiEGQLslalTGTRTklksQDKIKLTelLVQLGFPNPETI-------------- 141
Cdd:PRK13635   80 -------RRQVGMVFQ------NP----DNQF----VGATV----QDDVAFG--LENIGVPREEMVervdqalrqvgmed 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 142 -LPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLV 220
Cdd:PRK13635  133 fLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIV 212

                         250       260
                  ....*....|....*....|
gi 1330606456 221 IDGGGVVAYGAPKHALESSS 240
Cdd:PRK13635  213 MNKGEILEEGTPEEIFKSGH 232
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 2-238 2.92e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 113.55  E-value: 2.92e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQLTIK--TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQ 79
Cdd:PRK13632    4 KSVMIKVENVSFSypNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQ---SGEIKIDGITISKENLKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 rtAAQRPAVIFQdalqalNPL-----VSIEGQLSLALTGTRTKLKSQDKIkLTELLVQLGFpnpETILPLYPSQISGGQR 154
Cdd:PRK13632   81 --IRKKIGIIFQ------NPDnqfigATVEDDIAFGLENKKVPPKKMKDI-IDDLAKKVGM---EDYLDKEPQNLSGGQK 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 155 QRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPKH 234
Cdd:PRK13632  149 QRVAIASVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLIAQGKPKE 228


                  ....
gi 1330606456 235 ALES 238
Cdd:PRK13632  229 ILNN 232
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 6-233 3.87e-30

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 114.86  E-value: 3.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSG-DAVCGLPMLQRtaaq 84
Cdd:COG1118     3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGL--ETPD-SGRIVLNGrDLFTNLPPRER---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDAlqALNPLVSIEGQLSLALTGtRTKLKSQDKIKLTELL--VQL-GFPNpetilpLYPSQISGGQRQRICIAI 161
Cdd:COG1118    76 RVGFVFQHY--ALFPHMTVAENIAFGLRV-RPPSKAEIRARVEELLelVQLeGLAD------RYPSQLSGGQRQRVALAR 146

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPK 233
Cdd:COG1118   147 ALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALElADRVVVMNQGRIEQVGTPD 219
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
6-238 4.12e-30

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 112.08  E-value: 4.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDA-VCGLPMLQRTAAQ 84
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPT---------SGEVrVLGEDVARDPAEV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RP--AVIFQDAlqALNPLVSIEGQLSL--ALTGTRtklKSQDKIKLTELLVQLGFPNPETILPlypSQISGGQRQRICIA 160
Cdd:COG1131    72 RRriGYVPQEP--ALYPDLTVRENLRFfaRLYGLP---RKEARERIDELLELFGLTDAADRKV---GTLSGGMKQRLGLA 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrqigG---LLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHAL 236
Cdd:COG1131   144 LALLHDPELLILDEPTSGLDPEARRELWELLRELAAE----GktvLLSTHYLEEAERlCDRVAIIDKGRIVADGTPDELK 219


                  ..
gi 1330606456 237 ES 238
Cdd:COG1131   220 AR 221
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 5-232 8.46e-30

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


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 111.62  E-value: 8.46e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTiKT--SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQ-RT 81
Cdd:TIGR02315   1 MLEVENLS-KVypNGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPS---SGSILLEGTDITKLRGKKlRK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAQRPAVIFQDaLQALNPLVSIEGQLSLALTGTRT------KLKSQDKIKLTELLVQLGfpnpetILPLY---PSQISGG 152
Cdd:TIGR02315  77 LRRRIGMIFQH-YNLIERLTVLENVLHGRLGYKPTwrsllgRFSEEDKERALSALERVG------LADKAyqrADQLSGG 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGA 231
Cdd:TIGR02315 150 QQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIVFDGA 229


                  .
gi 1330606456 232 P 232
Cdd:TIGR02315 230 P 230
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
4-252 8.98e-30

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 112.24  E-value: 8.98e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLF---------QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET---VEVEGHISLSGDA 71
Cdd:COG4167     3 ALLEVRNLSKTFKYRTGLfrrqqfeavKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTsgeILINGHKLEYGDY 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  72 vcglpmlqRTAAQRPAVIFQDALQALNPLVSIEGQLS--LALTGTRTKLKSQDKIKLTELLVQLgfpnpetiLP----LY 145
Cdd:COG4167    83 --------KYRCKHIRMIFQDPNTSLNPRLNIGQILEepLRLNTDLTAEEREERIFATLRLVGL--------LPehanFY 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 146 PSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDL----HSAlacDKLLVI 221
Cdd:COG4167   147 PHMLSSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLgivkHIS---DKVLVM 223

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1330606456 222 DGGGVVAYGAPKHALESSSHAFCcslRDLIE 252
Cdd:COG4167   224 HQGEVVEYGKTAEVFANPQHEVT---KRLIE 251
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 7-224 1.80e-29

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide-binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 108.49  E-value: 1.80e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcgLPMLQRTAAQRP 86
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPT---SGEILIDGKDI--AKLPLEELRRRI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  87 AVIFQdalqalnplvsiegqlslaltgtrtklksqdkikltellvqlgfpnpetilplypsqISGGQRQRICIAIGLLSN 166
Cdd:cd00267    76 GYVPQ---------------------------------------------------------LSGGQRQRVALARALLLN 98

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 167 ADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIgGLLITHDL-HSALACDKLLVIDGG 224
Cdd:cd00267    99 PDLLLLDEPTSGLDPASRERLLELLRELAEEGRT-VIIVTHDPeLAELAADRVIVLKDG 156
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
11-242 3.70e-29

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 110.55  E-value: 3.70e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  11 LTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQRPA-VI 89
Cdd:PRK10419   18 LSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPS---QGNVSWRGEPLAKLNRAQRKAFRRDIqMV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  90 FQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQRICIAIGLLSNADL 169
Cdd:PRK10419   95 FQDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLD--DSVLDKRPPQLSGGQLQRVCLARALAVEPKL 172

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 170 IIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHsaLA---CDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:PRK10419  173 LILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLR--LVerfCQRVMVMDNGQIVETQPVGDKLTFSSPA 246
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 22-230 5.41e-29

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: 108.73  E-value: 5.41e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFD--VYRGELLAIMGPSGIGKSMLSRAIAGFLpetVEVEGHISLSGDAVCGLPmlqrtAAQRP-AVIFQDalQALN 98
Cdd:cd03298    13 QPMHFDltFAQGEITAIVGPSGSGKSTLLNLIAGFE---TPQSGRVLINGVDVTAAP-----PADRPvSMLFQE--NNLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 PLVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFPNPETILPlypSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:cd03298    83 AHLTVEQNVGLGLS-PGLKLTAEDRQAIEVALARVGLAGLEKRLP---GELSGGERQRVALARVLVRDKPVLLLDEPFAA 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 179 LDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLV-IDGGGVVAYG 230
Cdd:cd03298   159 LDPALRAEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVfLDNGRIAAQG 211
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 6-224 7.63e-29

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: 108.39  E-value: 7.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGLPMLQRTAAQR 85
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLL--EEPD-SGTIIIDGLKLTDDKKNINELRQK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDAlqALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETIlplYPSQISGGQRQRICIAIGLLS 165
Cdd:cd03262    78 VGMVFQQF--NLFPHLTVLENITLAPIKVKGMSKAEAEERALELLEKVGLADKADA---YPAQLSGGQQQRVAIARALAM 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSAL-ACDKLLVIDGG 224
Cdd:cd03262   153 NPKVMLFDEPTSALDPELVGEVLDVMKD-LAEEGMTMVVVTHEMGFAReVADRVIFMDDG 211
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 2-234 3.95e-28

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 109.41  E-value: 3.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQL----TIKTSSRTLFQ---------DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLS 68
Cdd:PRK15079    5 KKVLLEVADLkvhfDIKDGKQWFWQppktlkavdGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKAT---DGEVAWL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  69 GDAVCGLPMLQ-RTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQD-KIKLTELLVQLGF-PNpetILPLY 145
Cdd:PRK15079   82 GKDLLGMKDDEwRAVRSDIQMIFQDPLASLNPRMTIGEIIAEPLRTYHPKLSRQEvKDRVKAMMLKVGLlPN---LINRY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 146 PSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnvKQRQIGGLL--ITHDL----HSAlacDKLL 219
Cdd:PRK15079  159 PHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQ--LQREMGLSLifIAHDLavvkHIS---DRVL 233

                         250       260
                  ....*....|....*....|..
gi 1330606456 220 VIDGGGVV-------AYGAPKH 234
Cdd:PRK15079  234 VMYLGHAVelgtydeVYHNPLH 255
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 22-234 4.19e-28

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: 107.90  E-value: 4.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAG-FLPE--TVEVEGHISLSGDAVcglpmlqRTAAQRPAVIFQdalqalN 98
Cdd:TIGR04520  19 KNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGlLLPTsgKVTVDGLDTLDEENL-------WEIRKKVGMVFQ------N 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 PlvsiEGQLsLALT-------GTRTKLKSQDKIK--LTELLVQLG---FPNPEtilplyPSQISGGQRQRICIAiGLLS- 165
Cdd:TIGR04520  86 P----DNQF-VGATveddvafGLENLGVPREEMRkrVDEALKLVGmedFRDRE------PHLLSGGQKQRVAIA-GVLAm 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPKH 234
Cdd:TIGR04520 154 RPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGKIVAEGTPRE 222
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
22-236 6.93e-28

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 108.63  E-value: 6.93e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGfLPE----TVEVEGH--ISLSGDAVcglpmlqRTAAQRPAVIFQDAlq 95
Cdd:COG1135    22 DDVSLTIEKGEIFGIIGYSGAGKSTLIRCINL-LERptsgSVLVDGVdlTALSEREL-------RAARRKIGMIFQHF-- 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 alNPLVS------IEgqLSLALTGTRtklKSQDKIKLTELLVQLGfpnpetilpL------YPSQISGGQRQRICIAIGL 163
Cdd:COG1135    92 --NLLSSrtvaenVA--LPLEIAGVP---KAEIRKRVAELLELVG---------LsdkadaYPSQLSGGQKQRVGIARAL 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYG-------APKHA 235
Cdd:COG1135   156 ANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRiCDRVAVLENGRIVEQGpvldvfaNPQSE 235


                  .
gi 1330606456 236 L 236
Cdd:COG1135   236 L 236
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 6-234 8.08e-28

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: 106.11  E-value: 8.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF--LPETVEVEGHISLSGDAVCGLPMLQRTAA 83
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndLIPGAPDEGEVLLDGKDIYDLDVDVLELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAVIFQDAlqalNPLV-SIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPnPETILPLYPSQISGGQRQRICIAIG 162
Cdd:cd03260    81 RRVGMVFQKP----NPFPgSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALW-DEVKDRLHALGLSGGQQQRLCLARA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 163 LLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALAC-DKLLVIDGGGVVAYGAPKH 234
Cdd:cd03260   156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTI--VIVTHNMQQAARVaDRTAFLLNGRLVEFGPTEQ 226
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
31-241 9.07e-28

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 108.45  E-value: 9.07e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  31 GELLAIMGPSGIGKSMLSRAIAGFLPETVevegHISLSGDAVCGLPMLQRTAAQRP-------AVIFQDALQALNPLVSI 103
Cdd:COG4170    33 GEIRGLVGESGSGKSLIAKAICGITKDNW----HVTADRFRWNGIDLLKLSPRERRkiigreiAMIFQEPSSCLDPSAKI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 104 EGQLSLA-----LTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:COG4170   109 GDQLIEAipswtFKGKWWQRFKWRKKRAIELLHRVGIKDHKDIMNSYPHELTEGECQKVMIAMAIANQPRLLIADEPTNA 188

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 179 LDPVTEQEILKLIrdnVKQRQIGG---LLITHDLHS-ALACDKLLVIDGGGVVAYGAPKHALESSSH 241
Cdd:COG4170   189 MESTTQAQIFRLL---ARLNQLQGtsiLLISHDLESiSQWADTITVLYCGQTVESGPTEQILKSPHH 252
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 1-236 1.08e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 108.13  E-value: 1.08e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLT-IKTSSRTLFQ---------DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGD 70
Cdd:PRK11308    1 SQQPLLQAIDLKkHYPVKRGLFKperlvkaldGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPT---GGELYYQGQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  71 AVCGLPMLQRTAA-QRPAVIFQDALQALNPLVSIEGQLSLALTgTRTKL-KSQDKIKLTELLVQLGFpNPETiLPLYPSQ 148
Cdd:PRK11308   78 DLLKADPEAQKLLrQKIQIVFQNPYGSLNPRKKVGQILEEPLL-INTSLsAAERREKALAMMAKVGL-RPEH-YDRYPHM 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 149 ISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDL----HSAlacDKLLVIDGG 224
Cdd:PRK11308  155 FSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLsvveHIA---DEVMVMYLG 231

                         250
                  ....*....|..
gi 1330606456 225 GVVAYGaPKHAL 236
Cdd:PRK11308  232 RCVEKG-TKEQI 242
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 6-224 1.46e-27

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: 103.63  E-value: 1.46e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISlsgdaVCGLPMLQRTAAQR 85
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPD---SGEIK-----VLGKDIKKEPEEVK 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 P--AVIFQDAlqalnplvsiegQLSLALTGtrtklksQDKIKLtellvqlgfpnpetilplypsqiSGGQRQRICIAIGL 163
Cdd:cd03230    73 RriGYLPEEP------------SLYENLTV-------RENLKL-----------------------SGGMKQRLALAQAL 110

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:cd03230   111 LHDPELLILDEPTSGLDPESRREFWELLRE-LKKEGKTILLSSHILEEAERlCDRVAILNNG 171
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 4-218 3.28e-27

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: 103.71  E-value: 3.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLsgdavCGLPMLQRTAA 83
Cdd:COG4133     1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPS---AGEVLW-----NGEPIRDARED 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAVIFQDALQALNPLVSIEGQLSL--ALTGTRtklksQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAI 161
Cdd:COG4133    73 YRRRLAYLGHADGLKPELTVRENLRFwaALYGLR-----ADREAIDEALEAVGL---AGLADLPVRQLSAGQKRRVALAR 144

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrqiGGLLI--THDLHSALACDKL 218
Cdd:COG4133   145 LLLSPAPLWLLDEPFTALDAAGVALLAELIAAHLAR---GGAVLltTHQPLELAAARVL 200
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 5-247 1.25e-26

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 108.02  E-value: 1.25e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLF----QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDAVCGLPMLQR 80
Cdd:PRK10261   12 VLAVENLNIAFMQEQQKiaavRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQA---------GGLVQCDKMLLRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 -----------TAAQRP-------AVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETIL 142
Cdd:PRK10261   83 rsrqvielseqSAAQMRhvrgadmAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLDQVRIPEAQTIL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 143 PLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVI 221
Cdd:PRK10261  163 SRYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGvVAEIADRVLVM 242

                         250       260
                  ....*....|....*....|....*.
gi 1330606456 222 DGGGVVAYGAPKHALESSSHAFCCSL 247
Cdd:PRK10261  243 YQGEAVETGSVEQIFHAPQHPYTRAL 268
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 4-236 3.67e-26

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 102.54  E-value: 3.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaA 83
Cdd:PRK13548    1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPD---SGEVRLNGRPLADWSPAEL--A 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAVIFQDAlqalnplvsiegQLSLALT---------GTRTKLKSQDKIKLTELLVQLGfpnpetILPL----YPsQIS 150
Cdd:PRK13548   76 RRRAVLPQHS------------SLSFPFTveevvamgrAPHGLSRAEDDALVAAALAQVD------LAHLagrdYP-QLS 136

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGL--LSNAD----LIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDG 223
Cdd:PRK13548  137 GGEQQRVQLARVLaqLWEPDgpprWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNlAARYADRIVLLHQ 216

                         250
                  ....*....|...
gi 1330606456 224 GGVVAYGAPKHAL 236
Cdd:PRK13548  217 GRLVADGTPAEVL 229
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 1-230 7.84e-26

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 101.54  E-value: 7.84e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQR 80
Cdd:PRK11701    2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPD---AGEVHYRMRDGQLRDLYAL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRP-------AVIFQDALQALNPLVSIEGQLS--LALTGTR--TKLKSQDKIKLTEllVQLGfpnPETILPLyPSQI 149
Cdd:PRK11701   79 SEAERRrllrtewGFVHQHPRDGLRMQVSAGGNIGerLMAVGARhyGDIRATAGDWLER--VEID---AARIDDL-PTTF 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVA 228
Cdd:PRK11701  153 SGGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVArLLAHRLLVMKQGRVVE 232


                  ..
gi 1330606456 229 YG 230
Cdd:PRK11701  233 SG 234
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 16-243 8.24e-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: 101.22  E-value: 8.24e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPM--LQRtaaqRPAVIFQDA 93
Cdd:cd03295    12 GGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPT---SGEIFIDGEDIREQDPveLRR----KIGYVIQQI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 lqALNPLVSIEGQLSLALtgtrtKLK--SQDKIK--LTELLVQLGFPnPETILPLYPSQISGGQRQRICIAIGLLSNADL 169
Cdd:cd03295    85 --GLFPHMTVEENIALVP-----KLLkwPKEKIRerADELLALVGLD-PAEFADRYPHELSGGQQQRVGVARALAADPPL 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 170 IIADEPTSALDPVT----EQEILKLirdnvkQRQIGG--LLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:cd03295   157 LLMDEPFGALDPITrdqlQEEFKRL------QQELGKtiVFVTHDIDEAFRlADRIAIMKNGEIVQVGTPDEILRSPAND 230


                  .
gi 1330606456 243 F 243
Cdd:cd03295   231 F 231
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 6-232 1.19e-25

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: 100.31  E-value: 1.19e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTA--- 82
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGKILLDGQDITKLPMHKRARlgi 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 ---AQRPAvIFQDalqalnplVSIEGQLSLALTgTRTKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICI 159
Cdd:cd03218    78 gylPQEAS-IFRK--------LTVEENILAVLE-IRGLSKKEREEKLEELLEEFHI---THLRKSKASSLSGGERRRVEI 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIgGLLIT-HDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:cd03218   145 ARALATNPKFLLLDEPFAGVDPIAVQDIQKIIK-ILKDRGI-GVLITdHNVRETLSiTDRAYIIYEGKVLAEGTP 217
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 3-243 1.46e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 104.40  E-value: 1.46e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTI-----------KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtvevEGHISLSGDa 71
Cdd:PRK15134  273 SPLLDVEQLQVafpirkgilkrTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTTGLALLRLINS----QGEIWFDGQ- 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  72 vcglPMLQRTAAQ------RPAVIFQDALQALNPLVSIEGQLSLALTGTRTKL-KSQDKIKLTELLVQLGFpNPETiLPL 144
Cdd:PRK15134  348 ----PLHNLNRRQllpvrhRIQVVFQDPNSSLNPRLNVLQIIEEGLRVHQPTLsAAQREQQVIAVMEEVGL-DPET-RHR 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 145 YPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDG 223
Cdd:PRK15134  422 YPAEFSGGQRQRIAIARALILKPSLIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRAlCHQVIVLRQ 501

                         250       260
                  ....*....|....*....|
gi 1330606456 224 GGVVAYGAPKHALESSSHAF 243
Cdd:PRK15134  502 GEVVEQGDCERVFAAPQQEY 521
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 17-227 1.48e-25

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: 99.64  E-value: 1.48e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDaVCGLPMLQRTAA---QRPA-VIFQD 92
Cdd:cd03226    12 GTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKES---SGSILLNGK-PIKAKERRKSIGyvmQDVDyQLFTD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 alqalnplvSIEGQLSLALtgtrtKLKSQDKIKLTELLVQLgfpNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:cd03226    88 ---------SVREELLLGL-----KELDAGNEQAETVLKDL---DLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKQRQIgGLLITHDLH-SALACDKLLVIDGGGVV 227
Cdd:cd03226   151 DEPTSGLDYKNMERVGELIRELAAQGKA-VIVITHDYEfLAKVCDRVLLLANGAIV 205
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 16-237 1.59e-25

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: 104.92  E-value: 1.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMlqRTAAQRPAVIFQDalq 95
Cdd:COG2274   486 DSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPT---SGRILIDGIDLRQIDP--ASLRRQIGVVLQD--- 557

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 alnplvsieGQL---SLA--LTGTRTKLkSQDKIK-------LTELLVQL--GFpnpETILPLYPSQISGGQRQRICIAI 161
Cdd:COG2274   558 ---------VFLfsgTIRenITLGDPDA-TDEEIIeaarlagLHDFIEALpmGY---DTVVGEGGSNLSGGQRQRLAIAR 624

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALE 237
Cdd:COG2274   625 ALLRNPRILILDEATSALDAETEAIILENLRRLLKGRTV--IIIAHRLSTIRLADRIIVLDKGRIVEDGTHEELLA 698
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 22-243 2.89e-25

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: 99.62  E-value: 2.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGLPmlqrtAAQRPA-VIFQDalQALNPL 100
Cdd:cd03300    17 DGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGF--ETPT-SGEILLDGKDITNLP-----PHKRPVnTVFQN--YALFPH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 101 VSIEGQLSLALTGTRTKlKSQDKIKLTELL--VQL-GFPNPetilplYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:cd03300    87 LTVFENIAFGLRLKKLP-KAEIKERVAEALdlVQLeGYANR------KPSQLSGGQQQRVAIARALVNEPKVLLLDEPLG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 178 ALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:cd03300   160 ALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTmSDRIAVMNKGKIQQIGTPEEIYEEPANRF 226
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 23-242 3.70e-25

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 99.30  E-value: 3.70e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGLPMLQRTAAQRPAVIFQD--------AL 94
Cdd:COG1126    19 GISLDVEKGEVVVIIGPSGSGKSTLLRCINLL--EEPD-SGTITVDGEDLTDSKKDINKLRRKVGMVFQQfnlfphltVL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 QalNplvsiegqLSLALTgtRTKLKSQDKIKLT--ELLVQLGfpnpetiLP----LYPSQISGGQRQRICIAIGLLSNAD 168
Cdd:COG1126    96 E--N--------VTLAPI--KVKKMSKAEAEERamELLERVG-------LAdkadAYPAQLSGGQQQRVAIARALAMEPK 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 169 LIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:COG1126   157 VMLFDEPTSALDPELVGEVLDVMRD-LAKEGMTMVVVTHEMGFAReVADRVVFMDGGRIVEEGPPEEFFENPQHE 230
3a0106s01 TIGR00968
sulfate ABC transporter, ATP-binding protein; [Transport and binding proteins, Anions]
 8-243 4.60e-25

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


Pssm-ID: 130041 [Multi-domain]  Cd Length: 237  Bit Score: 99.10  E-value: 4.60e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   8 VDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAqrpa 87
Cdd:TIGR00968   3 IANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPD---SGRIRLNGQDATRVHARDRKIG---- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  88 VIFQDalQALNPLVSIEGQLSLALTgTRTKLKSQDKIKLTELL--VQL-GFPNPetilplYPSQISGGQRQRICIAIGLL 164
Cdd:TIGR00968  76 FVFQH--YALFKHLTVRDNIAFGLE-IRKHPKAKIKARVEELLelVQLeGLGDR------YPNQLSGGQRQRVALARALA 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 165 SNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:TIGR00968 147 VEPQVLLLDEPFGALDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMeVADRIVVMSNGKIEQIGSPDEVYDHPANPF 226
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 17-241 4.86e-25

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: 98.84  E-value: 4.86e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCG--LPMLQRTAAQRP--AVIFQD 92
Cdd:cd03253    13 GRPVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVS---SGSILIDGQDIREvtLDSLRRAIGVVPqdTVLFND 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 AL----QALNPLVSIEGQLSLALTGtrtklKSQDKIkltellvqLGFPNP-ETILPLYPSQISGGQRQRICIAIGLLSNA 167
Cdd:cd03253    90 TIgyniRYGRPDATDEEVIEAAKAA-----QIHDKI--------MRFPDGyDTIVGERGLKLSGGEKQRVAIARAILKNP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 168 DLIIADEPTSALDPVTEQEILKLIRDNVKQRQigGLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSSH 241
Cdd:cd03253   157 PILLLDEATSALDTHTEREIQAALRDVSKGRT--TIVIAHRLSTIVNADKIIVLKDGRIVERGTHEELLAKGGL 228
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 18-226 8.07e-25

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 98.01  E-value: 8.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLpetVEVEGHISLSGDAVCGLPmlqrtAAQRP-AVIFQDalQA 96
Cdd:TIGR01277  11 EHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFI---EPASGSIKVNDQSHTGLA-----PYQRPvSMLFQE--NN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIEGQLSLALTGTrTKLKSQDKIKLTELLVQLGFPNpetILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPT 176
Cdd:TIGR01277  81 LFAHLTVRQNIGLGLHPG-LKLNAEQQEKVVDAAQQVGIAD---YLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPF 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 177 SALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGV 226
Cdd:TIGR01277 157 SALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAiASQIAVVSQGKI 207
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
 18-208 1.04e-24

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


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 97.78  E-value: 1.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGLPMLQRTAAQRP-AVIFQdalqA 96
Cdd:TIGR02982  18 KQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGL--RSVQ-EGSLKVLGQELHGASKKQLVQLRRRiGYIFQ----A 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIEG----QLSLALtgtRTKLKSQDKI-KLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLII 171
Cdd:TIGR02982  91 HNLLGFLTArqnvQMALEL---QPNLSYQEAReRARAMLEAVGL---GDHLNYYPHNLSGGQKQRVAIARALVHHPKLVL 164

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1330606456 172 ADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHD 208
Cdd:TIGR02982 165 ADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD 201
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
5-228 1.20e-24

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 98.23  E-value: 1.20e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGlpmlqrTAAQ 84
Cdd:PRK11248    1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQ---HGSITLDGKPVEG------PGAE 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RpAVIFQDalQALNPLVSIEGQ--LSLALTGTRtklKSQDKIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIG 162
Cdd:PRK11248   72 R-GVVFQN--EGLLPWRNVQDNvaFGLQLAGVE---KMQRLEIAHQMLKKVGLEGAEK---RYIWQLSGGQRQRVGIARA 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 163 LLSNADLIIADEPTSALDPVTEQE----ILKLIRDNVKQRqiggLLITHDLHSA--LACDKLLVIDGGGVVA 228
Cdd:PRK11248  143 LAANPQLLLLDEPFGALDAFTREQmqtlLLKLWQETGKQV----LLITHDIEEAvfMATELVLLSPGPGRVV 210
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 7-243 1.28e-24

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: 98.48  E-value: 1.28e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP--MLQRTAAQ 84
Cdd:cd03294    26 SKEEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPT---SGKVLIDGQDIAAMSrkELRELRRK 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDAlqALNP----LVSIEGQLSLALTGTRTKLKsqdkiKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIA 160
Cdd:cd03294   103 KISMVFQSF--ALLPhrtvLENVAFGLEVQGVPRAEREE-----RAAEALELVGLEGWEH---KYPDELSGGMQQRVGLA 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALAC-DKLLVIDGGGVVAYGAPKHALESS 239
Cdd:cd03294   173 RALAVDPDILLMDEAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLgDRIAIMKDGRLVQVGTPEEILTNP 252


                  ....
gi 1330606456 240 SHAF 243
Cdd:cd03294   253 ANDY 256
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 23-232 1.37e-24

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: 100.19  E-value: 1.37e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpeTVEVEGHISLSG----DAVCG--LPMLQRtaaqRPAVIFQDAlqA 96
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGL---TRPDEGEIVLNGrtlfDSRKGifLPPEKR----RIGYVFQEA--R 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLvqlgfpNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPT 176
Cdd:TIGR02142  86 LFPHLSVRGNLRYGMKRARPSERRISFERVIELL------GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPL 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 177 SALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAP 232
Cdd:TIGR02142 160 AALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEvLRLADRVVVLEDGRVAAAGPI 216
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
 3-243 1.95e-24

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


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 97.98  E-value: 1.95e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPMLQ--- 79
Cdd:TIGR02323   1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELELYQLSEaer 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 -RTAAQRPAVIFQDALQALNPLVSIEGQLS--LALTGTR----TKLKSQDKIKLTELlvqlgfpnPETILPLYPSQISGG 152
Cdd:TIGR02323  81 rRLMRTEWGFVHQNPRDGLRMRVSAGANIGerLMAIGARhygnIRATAQDWLEEVEI--------DPTRIDDLPRAFSGG 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYGA 231
Cdd:TIGR02323 153 MQQRLQIARNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVArLLAQRLLVMQQGRVVESGL 232

                         250
                  ....*....|..
gi 1330606456 232 PKHALESSSHAF 243
Cdd:TIGR02323 233 TDQVLDDPQHPY 244
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 23-236 2.42e-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: 99.40  E-value: 2.42e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAvcglpmLQRTAA-------QRP-AVIFQDAl 94
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPD---SGRIRLGGEV------LQDSARgiflpphRRRiGYVFQEA- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 qALNPLVSIEGQLSLALTGTRtklKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:COG4148    87 -RLFPHLSVRGNLLYGRKRAP---RAERRISFDEVVELLGI---GHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 175 PTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH--SALAcDKLLVIDGGGVVAYGAPKHAL 236
Cdd:COG4148   160 PLAALDLARKAEILPYLERLRDELDIPILYVSHSLDevARLA-DHVVLLEQGRVVASGPLAEVL 222
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
18-210 2.55e-24

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 96.66  E-value: 2.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET---VEVEGH--ISLSGDAVcglPMLQRtaaqRPAVIFQD 92
Cdd:COG2884    15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTsgqVLVNGQdlSRLKRREI---PYLRR----RIGVVFQD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 aLQALNPLvSIEGQLSLAL--TGTRtklKSQDKIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:COG2884    88 -FRLLPDR-TVYENVALPLrvTGKS---RKEIRRRVREVLDLVGLSDKAK---ALPHELSGGEQQRVAIARALVNRPELL 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLH 210
Cdd:COG2884   160 LADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLE 198
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
4-213 4.89e-24

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 96.85  E-value: 4.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTI----KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGlPmlq 79
Cdd:COG4525     2 SMLTVRHVSVrypgGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPS---SGEITLDGVPVTG-P--- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 rtAAQRpAVIFQDalQALNPLVSIEGQLSLALtgtrtKLKSQDKIKLT----ELLVQLGFPNPETilpLYPSQISGGQRQ 155
Cdd:COG4525    75 --GADR-GVVFQK--DALLPWLNVLDNVAFGL-----RLRGVPKAERRaraeELLALVGLADFAR---RRIWQLSGGMRQ 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAL 213
Cdd:COG4525   142 RVGIARALAADPRFLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEAL 199
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 1-228 5.98e-24

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: 95.96  E-value: 5.98e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSR----TLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP 76
Cdd:COG4181     4 SSAPIIELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPT---SGTVRLAGQDLFALD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  77 MLQRTA--AQRPAVIFQD-----ALQAL-NPLVSIEgqlslaLTGTRtklksQDKIKLTELLVQLGfpnpetilpL---- 144
Cdd:COG4181    81 EDARARlrARHVGFVFQSfqllpTLTALeNVMLPLE------LAGRR-----DARARARALLERVG---------Lghrl 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 145 --YPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVID 222
Cdd:COG4181   141 dhYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLR 220


                  ....*.
gi 1330606456 223 GGGVVA 228
Cdd:COG4181   221 AGRLVE 226
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 5-242 8.71e-24

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: 95.69  E-value: 8.71e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqRTAAQ 84
Cdd:COG4555     1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPD---SGSILIDGEDVRKEP---REARR 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDalqalNPLVSIegqLS----LALTGTRTKLKSQDKIKLTELLVQ-LGFPNpetILPLYPSQISGGQRQRICI 159
Cdd:COG4555    75 QIGVLPDE-----RGLYDR---LTvrenIRYFAELYGLFDEELKKRIEELIElLGLEE---FLDRRVGELSTGMKKKVAL 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALES 238
Cdd:COG4555   144 ARALVHDPKVLLLDEPTNGLDVMARRLLREILR-ALKKEGKTVLFSSHIMQEVEAlCDRVVILHKGKVVAQGSLDELREE 222


                  ....
gi 1330606456 239 SSHA 242
Cdd:COG4555   223 IGEE 226
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
17-230 8.85e-24

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 99.47  E-value: 8.85e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQRTAAQRPAVIFQDALqa 96
Cdd:COG1132   352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPT---SGRILIDGVDIRDLT--LESLRRQIGVVPQDTF-- 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 lnpLV--SIEGQLSLALTGTrtklkSQDKIK-------LTELLVQL--GFpnpETILPLYPSQISGGQRQRICIAIGLLS 165
Cdd:COG1132   425 ---LFsgTIRENIRYGRPDA-----TDEEVEeaakaaqAHEFIEALpdGY---DTVVGERGVNLSGGQRQRIAIARALLK 493

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:COG1132   494 DPPILILDEATSALDTETEALIQEALERLMKGRTT--IVIAHRLSTIRNADRILVLDDGRIVEQG 556
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 18-227 1.17e-23

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 95.92  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaAQRPAVIFQDALQAL 97
Cdd:COG1101    19 KRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPD---SGSILIDGKDVTKLPEYKR--AKYIGRVFQDPMMGT 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIEGQLSLALT-GTRTKLK----SQDKIKLTELLVQLGFpNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:COG1101    94 APSMTIEENLALAYRrGKRRGLRrgltKKRRELFRELLATLGL-GLENRLDTKVGLLSGGQRQALSLLMATLTKPKLLLL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALAC-DKLLVIDGGGVV 227
Cdd:COG1101   173 DEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYgNRLIMMHEGRII 228
cbiO PRK13640
energy-coupling factor transporter ATPase;
1-232 2.00e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 95.64  E-value: 2.00e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQL--TIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPML 78
Cdd:PRK13640    1 MKDNIVEFKHVsfTYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QrtAAQRPAVIFQDALqalNPLV--SIEGQLSLALTGTRTKLKSQDKIkLTELLVQLG---FPNPEtilplyPSQISGGQ 153
Cdd:PRK13640   81 D--IREKVGIVFQNPD---NQFVgaTVGDDVAFGLENRAVPRPEMIKI-VRDVLADVGmldYIDSE------PANLSGGQ 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAP 232
Cdd:PRK13640  149 KQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSP 227
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 22-236 6.12e-23

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 95.25  E-value: 6.12e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQRP-AVIFQDalqaLNPL 100
Cdd:PRK11153   22 NNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPT---SGRVLVDGQDLTALSEKELRKARRQiGMIFQH----FNLL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 101 VS--IEGQLSLALTGTRTKlKSQDKIKLTELLVQLGfpnpetilpL------YPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:PRK11153   95 SSrtVFDNVALPLELAGTP-KAEIKARVTELLELVG---------LsdkadrYPAQLSGGQKQRVAIARALASNPKVLLC 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDnvKQRQIGG--LLITH--DLHSALaCDKLLVIDGGGVVAYGA-------PKHAL 236
Cdd:PRK11153  165 DEATSALDPATTRSILELLKD--INRELGLtiVLITHemDVVKRI-CDRVAVIDAGRLVEQGTvsevfshPKHPL 236
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 23-232 6.19e-23

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: 92.94  E-value: 6.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQ-RTA----AQRPaVIFQDALQA- 96
Cdd:cd03244    22 NISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELS---SGSILIDGVDISKIGLHDlRSRisiiPQDP-VLFSGTIRSn 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPL-VSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGfpnpetilplyPSQISGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:cd03244    98 LDPFgEYSDEELWQALERVGLKEFVESLPGGLDTVVEEG-----------GENLSVGQRQLLCLARALLRKSKILVLDEA 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 176 TSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAP 232
Cdd:cd03244   167 TASVDPETDALIQKTIREAFKDCTV--LTIAHRLDTIIDSDRILVLDKGRVVEFDSP 221
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
 23-233 1.08e-22

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 93.99  E-value: 1.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDA-VCGLPMLQ--RTAAQRPAVIFQDA-----L 94
Cdd:TIGR01188  11 GVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPT---------SGTArVAGYDVVRepRKVRRSIGIVPQYAsvdedL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 QALNPLVSIEGqlslaLTGTRTKLKSQDKIKLTELlVQLGFPNPEtilplYPSQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:TIGR01188  82 TGRENLEMMGR-----LYGLPKDEAEERAEELLEL-FELGEAADR-----PVGTYSGGMRRRLDIAASLIHQPDVLFLDE 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 175 PTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYGAPK 233
Cdd:TIGR01188 151 PTTGLDPRTRRAIWDYIRA-LKEEGVTILLTTHYMEEAdKLCDRIAIIDHGRIIAEGTPE 209
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 22-233 1.60e-22

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: 91.73  E-value: 1.60e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAA------QRPAVIfqdalq 95
Cdd:cd03224    17 FGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPR---SGSIRFDGRDITGLPPHERARAgigyvpEGRRIF------ 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 alnPLVSIEGQLSLALTgTRTKLKSQDKI--------KLTELLVQLGfpnpetilplypSQISGGQRQRICIAIGLLSNA 167
Cdd:cd03224    88 ---PELTVEENLLLGAY-ARRRAKRKARLervyelfpRLKERRKQLA------------GTLSGGEQQMLAIARALMSRP 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 168 DLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPK 233
Cdd:cd03224   152 KLLLLDEPSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNARFALEiADRAYVLERGRVVLEGTAA 217
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 3-221 1.62e-22

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: 95.82  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSSRT-LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP--MLQ 79
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPT---EGSIAVNGVPLADADadSWR 395

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAA---QRPaVIFQDalqalnplvSIEGQLSLALTGTrTKLKSQDKIKLTEL--LVQLGFPNPETILPLYPSQISGGQR 154
Cdd:TIGR02857 396 DQIAwvpQHP-FLFAG---------TIAENIRLARPDA-SDAEIREALERAGLdeFVAALPQGLDTPIGEGGAGLSGGQA 464

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 155 QRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVI 221
Cdd:TIGR02857 465 QRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQGRTV--LLVTHRLALAALADRIVVL 529
3a0107s01c2 TIGR00972
phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...
 22-242 1.85e-22

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein of a family of ABC transporters for inorganic phosphate. In the model species Escherichia coli, a constitutive transporter for inorganic phosphate, with low affinity, is also present. The high affinity transporter that includes this polypeptide is induced when extracellular phosphate concentrations are low. The proteins most similar to the members of this family but not included appear to be amino acid transporters. [Transport and binding proteins, Anions]


Pssm-ID: 273372 [Multi-domain]  Cd Length: 247  Bit Score: 92.36  E-value: 1.85e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAI--AGFLPETVEVEGHISLSGDAVCGLPMLQRTAAQRPAVIFQDalqaLNP 99
Cdd:TIGR00972  18 KNINLDIPKNQVTALIGPSGCGKSTLLRSLnrMNDLVPGVRIEGKVLFDGQDIYDKKIDVVELRRRVGMVFQK----PNP 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 L-VSIEGQLSLALT--GTRTKlKSQDKIkLTELLVQLGFPNP-ETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:TIGR00972  94 FpMSIYDNIAYGPRlhGIKDK-KELDEI-VEESLKKAALWDEvKDRLHDSALGLSGGQQQRLCIARALAVEPEVLLLDEP 171

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 176 TSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALAC-DKLLVIDGGGVVAYGAPKHALESSSHA 242
Cdd:TIGR00972 172 TSALDPIATGKIEELIQELKKKYTI--VIVTHNMQQAARIsDRTAFFYDGELVEYGPTEQIFTNPKEK 237
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 29-237 2.00e-22

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 95.88  E-value: 2.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  29 YRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVcGLPMLQRtaaqRPAVIFQDALqaLNPLVSIEGQL- 107
Cdd:TIGR00955  49 KPGELLAVMGSSGAGKTTLMNALAFRSPKGVKGSGSVLLNGMPI-DAKEMRA----ISAYVQQDDL--FIPTLTVREHLm 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 108 -SLALTGTRTKLKSQDKIKLTELLVQLGFPN-PETIL--PLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVT 183
Cdd:TIGR00955 122 fQAHLRMPRRVTKKEKRERVDEVLQALGLRKcANTRIgvPGRVKGLSGGERKRLAFASELLTDPPLLFCDEPTSGLDSFM 201

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 184 EQEILKLIRDNVKQRQIGGLLItHDLHSALAC--DKLLVIDGGGVVAYGAPKHALE 237
Cdd:TIGR00955 202 AYSVVQVLKGLAQKGKTIICTI-HQPSSELFElfDKIILMAEGRVAYLGSPDQAVP 256
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-233 3.17e-22

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 93.86  E-value: 3.17e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGLPmlqr 80
Cdd:PRK09452   10 SLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGF--ETPD-SGRIMLDGQDITHVP---- 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 tAAQRPA-VIFQDalQALNPLVSIEGQLSLALtgtRTKLKSQDKIK--LTELL--VQLgfpnpETILPLYPSQISGGQRQ 155
Cdd:PRK09452   83 -AENRHVnTVFQS--YALFPHMTVFENVAFGL---RMQKTPAAEITprVMEALrmVQL-----EEFAQRKPHQLSGGQQQ 151

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALDPVTEQEI---LKLIrdnvkQRQIGGLLI--THDLHSALA-CDKLLVIDGGGVVAY 229
Cdd:PRK09452  152 RVAIARAVVNKPKVLLLDESLSALDYKLRKQMqneLKAL-----QRKLGITFVfvTHDQEEALTmSDRIVVMRDGRIEQD 226


                  ....
gi 1330606456 230 GAPK 233
Cdd:PRK09452  227 GTPR 230
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
4-247 7.71e-22

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 92.17  E-value: 7.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTI--KTSSRTL--FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDavcgLPMLQ 79
Cdd:PRK15093    2 PLLDIRNLTIefKTSDGWVkaVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKDNWRVTADRMRFDD----IDLLR 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAAQRPAV-------IFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKI-----KLTELLVQLGFPNPETILPLYPS 147
Cdd:PRK15093   78 LSPRERRKLvghnvsmIFQEPQSCLDPSERVGRQLMQNIPGWTYKGRWWQRFgwrkrRAIELLHRVGIKDHKDAMRSFPY 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 148 QISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH--SALAcDKLLVIDGGG 225
Cdd:PRK15093  158 ELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQmlSQWA-DKINVLYCGQ 236

                         250       260
                  ....*....|....*....|..
gi 1330606456 226 VVAYGAPKHALESSSHAFCCSL 247
Cdd:PRK15093  237 TVETAPSKELVTTPHHPYTQAL 258
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
4-237 9.23e-22

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 92.59  E-value: 9.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqrtAA 83
Cdd:PRK11607   18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPT---AGQIMLDGVDLSHVP-----PY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPA-VIFQDalQALNPLVSIEGQLSLALtgtrtklkSQDKIKLTELLVQ----LGFPNPETILPLYPSQISGGQRQRIC 158
Cdd:PRK11607   90 QRPInMMFQS--YALFPHMTVEQNIAFGL--------KQDKLPKAEIASRvnemLGLVHMQEFAKRKPHQLSGGQRQRVA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALE 237
Cdd:PRK11607  160 LARSLAKRPKLLLLDEPMGALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTmAGRIAIMNRGKFVQIGEPEEIYE 239
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 14-234 1.08e-21

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: 89.49  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDA-VCGLPML-QRTAAQRP-AVIF 90
Cdd:cd03263    11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPT---------SGTAyINGYSIRtDRKAARQSlGYCP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  91 Q-DAL-QALNPLVSIEgqLSLALTGTRtklKSQDKIKLTELLVQLGFPNPETILPlypSQISGGQRQRICIAIGLLSNAD 168
Cdd:cd03263    82 QfDALfDELTVREHLR--FYARLKGLP---KSEIKEEVELLLRVLGLTDKANKRA---RTLSGGMKRKLSLAIALIGGPS 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 169 LIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKH 234
Cdd:cd03263   154 VLLLDEPTSGLDPASRRAIWDLILEVRKGRSI--ILTTHSMDEAEAlCDRIAIMSDGKLRCIGSPQE 218
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 10-230 1.15e-21

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 88.52  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  10 QLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpetveveghislsgdavcglpmlqrtaaqrpavi 89
Cdd:cd03247     7 SFSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTG------------------------------------ 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  90 fqdALQALNPLVSIEGQLSLALTGTRTKLKS--QDKIKL--TELLVQLGfpnpetilplypSQISGGQRQRICIAIGLLS 165
Cdd:cd03247    51 ---DLKPQQGEITLDGVPVSDLEKALSSLISvlNQRPYLfdTTLRNNLG------------RRFSGGERQRLALARILLQ 115

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:cd03247   116 DAPIVLLDEPTVGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHMDKILFLENGKIIMQG 178
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 4-238 1.34e-21

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 89.70  E-value: 1.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaA 83
Cdd:COG1137     2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPD---SGRIFLDGEDITHLPMHKR--A 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QR-----PavifQDAlqalnplvSIEGQLS-----LALTGTRTKLKSQDKIKLTELLVQLGfpnpetILPLYPS---QIS 150
Cdd:COG1137    77 RLgigylP----QEA--------SIFRKLTvedniLAVLELRKLSKKEREERLEELLEEFG------ITHLRKSkaySLS 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIgGLLIT-HDLHSALA-CDKLLVIDGGGVVA 228
Cdd:COG1137   139 GGERRRVEIARALATNPKFILLDEPFAGVDPIAVADIQKIIRH-LKERGI-GVLITdHNVRETLGiCDRAYIISEGKVLA 216

                         250
                  ....*....|
gi 1330606456 229 YGAPKHALES 238
Cdd:COG1137   217 EGTPEEILNN 226
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 22-232 1.39e-21

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 91.67  E-value: 1.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqrtAAQRP-AVIFQDAlqALNPL 100
Cdd:COG3839    20 KDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPT---SGEILIGGRDVTDLP-----PKDRNiAMVFQSY--ALYPH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 101 VSIEGQLSLALTGTRTKLKSQDKiKLTEL--LVQLgfpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:COG3839    90 MTVYENIAFPLKLRKVPKAEIDR-RVREAaeLLGL-----EDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLSN 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 179 LDP----VTEQEILKLirdnvkQRQIGGLLI--THDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:COG3839   164 LDAklrvEMRAEIKRL------HRRLGTTTIyvTHDQVEAMTlADRIAVMNDGRIQQVGTP 218
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 22-232 1.43e-21

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: 89.80  E-value: 1.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAA------QRPAvIFQDaLQ 95
Cdd:cd03219    17 DDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPT---SGSVLFDGEDITGLPPHEIARLgigrtfQIPR-LFPE-LT 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 AL-NPLVSIEGQLSLALTGTRTKlKSQDKI--KLTELLVQLGfpnpetilpLYP------SQISGGQRQRICIAIGLLSN 166
Cdd:cd03219    92 VLeNVMVAAQARTGSGLLLARAR-REEREAreRAEELLERVG---------LADladrpaGELSYGQQRRLEIARALATD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 167 ADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:cd03219   162 PKLLLLDEPAAGLNPEETEELAELIRE-LRERGITVLLVEHDMDVVMSlADRVTVLDQGRVIAEGTP 227
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 6-230 1.44e-21

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


Pssm-ID: 213180 [Multi-domain]  Cd Length: 194  Bit Score: 88.76  E-value: 1.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIK------TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLpETVEVEGHISLSGdavcgLPMLQ 79
Cdd:cd03213     4 LSFRNLTVTvksspsKSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRR-TGLGVSGEVLING-----RPLDK 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAAQRPAVIFQDalQALNPLVSIEGQLSLALtgtrtKLKSqdkikltellvqlgfpnpetilplypsqISGGQRQRICI 159
Cdd:cd03213    78 RSFRKIIGYVPQD--DILHPTLTVRETLMFAA-----KLRG----------------------------LSGGERKRVSI 122

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSAL--ACDKLLVIDGGGVVAYG 230
Cdd:cd03213   123 ALELVSNPSLLFLDEPTSGLDSSSALQVMSLLR-RLADTGRTIICSIHQPSSEIfeLFDKLLLLSQGRVIYFG 194
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 6-226 1.55e-21

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: 88.04  E-value: 1.55e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTS--SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGdavcglpmlqrtaa 83
Cdd:cd03246     1 LEVENVSFRYPgaEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPT---SGRVRLDG-------------- 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 qrpAVIFQDALQALNPLVSIEGQLSLALTGTRTklksqdkikltellvqlgfpnpETILplypsqiSGGQRQRICIAIGL 163
Cdd:cd03246    64 ---ADISQWDPNELGDHVGYLPQDDELFSGSIA----------------------ENIL-------SGGQRQRLGLARAL 111

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSALACDKLLVIDGGGV 226
Cdd:cd03246   112 YGNPRILVLDEPNSHLDVEGERALNQAIA-ALKAAGATRIVIAHRPETLASADRILVLEDGRV 173
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 23-243 2.94e-21

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: 88.94  E-value: 2.94e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAqrpaVIFQDalQALNPLVS 102
Cdd:cd03296    20 DVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPD---SGTILFGGEDATDVPVQERNVG----FVFQH--YALFRHMT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IEGQLSLAL-TGTRTKLKSQDKI--KLTELL--VQL-GFPNPetilplYPSQISGGQRQRICIAIGLLSNADLIIADEPT 176
Cdd:cd03296    91 VFDNVAFGLrVKPRSERPPEAEIraKVHELLklVQLdWLADR------YPAQLSGGQRQRVALARALAVEPKVLLLDEPF 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 177 SALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:cd03296   165 GALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALeVADRVVVMNKGRIEQVGTPDEVYDHPASPF 232
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 23-208 3.01e-21

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where FtsE is the ATPase and the membrane subunit FtsX resembles a permease subunit. But rather than transporting any substrate, the complex acts in cell division by undergoing conformational changes that alter the activity of cell wall hydrolases located outside the plasma membrane. The complex is widely conserved in bacteria, but also extremely divergent in sequence between different lineages


Pssm-ID: 213259 [Multi-domain]  Cd Length: 214  Bit Score: 88.23  E-value: 3.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLSGDAVCGL-----PMLQRTAAqrpaVIFQDALQAL 97
Cdd:cd03292    19 GINISISAGEFVFLVGPSGAGKSTLLKLIYK---EELPTSGTIRVNGQDVSDLrgraiPYLRRKIG----VVFQDFRLLP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIEGQLSLALTGTRTKLKSQdkiKLTELLVQLGFPNPETIlplYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:cd03292    92 DRNVYENVAFALEVTGVPPREIRK---RVPAALELVGLSHKHRA---LPAELSGGEQQRVAIARAIVNSPTILIADEPTG 165

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1330606456 178 ALDPVTEQEILKLIRDnVKQRQIGGLLITHD 208
Cdd:cd03292   166 NLDPDTTWEIMNLLKK-INKAGTTVVVATHA 195
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 7-237 3.05e-21

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: 92.17  E-value: 3.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTssrtlFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETV-EVEGHIslsGDAVCGL----PMLQRT 81
Cdd:TIGR03269 291 SVDRGVVKA-----VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSgEVNVRV---GDEWVDMtkpgPDGRGR 362

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAQRPAVIFQDalQALNPLVSIEGQLSLALTgtrtkLKSQD---KIKLTELLVQLGFPN--PETILPLYPSQISGGQRQR 156
Cdd:TIGR03269 363 AKRYIGILHQE--YDLYPHRTVLDNLTEAIG-----LELPDelaRMKAVITLKMVGFDEekAEEILDKYPDELSEGERHR 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 157 ICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPKHA 235
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLdVCDRAALMRDGKIVKIGDPEEI 515


                  ..
gi 1330606456 236 LE 237
Cdd:TIGR03269 516 VE 517
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 23-228 3.18e-21

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: 87.10  E-value: 3.18e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLpmlqrtaaqRPAvifqDALQAlnplvs 102
Cdd:cd03216    18 GVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPD---SGEILVDGKEVSFA---------SPR----DARRA------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 iegqlslaltgtrtklksqdKIkltellvqlgfpnpETIlplypSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPV 182
Cdd:cd03216    76 --------------------GI--------------AMV-----YQLSVGERQMVEIARALARNARLLILDEPTAALTPA 116

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1330606456 183 TEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVA 228
Cdd:cd03216   117 EVERLFKVIRR-LRAQGVAVIFISHRLDEVFEiADRVTVLRDGRVVG 162
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 6-231 4.93e-21

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: 91.73  E-value: 4.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKT--SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGdavcglpmlqrtaa 83
Cdd:COG4618   331 LSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPT---AGSVRLDG-------------- 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 qrpAVIFQDALQALNPLVsieGQLSlaltgtrtklksQDkikltellVQL----------GFPNP--------------- 138
Cdd:COG4618   394 ---ADLSQWDREELGRHI---GYLP------------QD--------VELfdgtiaeniaRFGDAdpekvvaaaklagvh 447

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 139 ETILPL---YPSQI-------SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHD 208
Cdd:COG4618   448 EMILRLpdgYDTRIgeggarlSGGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIR-ALKARGATVVVITHR 526

                         250       260
                  ....*....|....*....|....
gi 1330606456 209 LhSALA-CDKLLVIDGGGVVAYGA 231
Cdd:COG4618   527 P-SLLAaVDKLLVLRDGRVQAFGP 549
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 14-240 4.95e-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: 88.31  E-value: 4.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET---VEVEGHislsgD-AVCGLPMLQRTAAqrpaVI 89
Cdd:cd03252    11 KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPEngrVLVDGH-----DlALADPAWLRRQVG----VV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  90 FQDALqALNPlvSIEGQLSLALTGTRTKlKSQDKIKLT---ELLVQL--GFpnpETILPLYPSQISGGQRQRICIAIGLL 164
Cdd:cd03252    82 LQENV-LFNR--SIRDNIALADPGMSME-RVIEAAKLAgahDFISELpeGY---DTIVGEQGAGLSGGQRQRIAIARALI 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 165 SNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSS 240
Cdd:cd03252   155 HNPRILIFDEATSALDYESEHAIMRNMHDICAGRTV--IIIAHRLSTVKNADRIIVMEKGRIVEQGSHDELLAENG 228
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
5-234 5.20e-21

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 88.92  E-value: 5.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPMLQRTAAQ 84
Cdd:PRK09984    4 IIRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITGDKSAGSHIELLGRTVQREGRLARDIRK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPA---VIFQDaLQALNPLVSIEGQLSLALTGT---RTKLK---SQDKIKLTELLVQLG---FPNPETilplypSQISGG 152
Cdd:PRK09984   84 SRAntgYIFQQ-FNLVNRLSVLENVLIGALGSTpfwRTCFSwftREQKQRALQALTRVGmvhFAHQRV------STLSGG 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGA 231
Cdd:PRK09984  157 QQQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRyCERIVALRQGHVFYDGS 236


                  ...
gi 1330606456 232 PKH 234
Cdd:PRK09984  237 SQQ 239
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 3-238 6.21e-21

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 90.67  E-value: 6.21e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVeveGHISLSGDAVCGLPmlQRTA 82
Cdd:PRK09536    1 MPMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTA---GTVLVAGDDVEALS--ARAA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 AQRPAVIFQDALQALNplVSIEGQLSLALTGTRTKLK---SQDKIKLTELLVQLG---FPN-PETILplypsqiSGGQRQ 155
Cdd:PRK09536   76 SRRVASVPQDTSLSFE--FDVRQVVEMGRTPHRSRFDtwtETDRAAVERAMERTGvaqFADrPVTSL-------SGGERQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLItHDLH-SALACDKLLVIDGGGVVAYGAPKH 234
Cdd:PRK09536  147 RVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAI-HDLDlAARYCDELVLLADGRVRAAGPPAD 225


                  ....
gi 1330606456 235 ALES 238
Cdd:PRK09536  226 VLTA 229
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
19-239 6.97e-21

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 87.84  E-value: 6.97e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  19 TLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGLPMLQRTAAQRPAVIFQDAlqALN 98
Cdd:PRK09493   15 QVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKL--EEIT-SGDLIVDGLKVNDPKVDERLIRQEAGMVFQQF--YLF 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 PLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:PRK09493   90 PHLTALENVMFGPLRVRGASKEEAEKQARELLAKVGL---AERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 179 LDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPKHALESS 239
Cdd:PRK09493  167 LDPELRHEVLKVMQD-LAEEGMTMVIVTHEIGFAEkVASRLIFIDKGRIAEDGDPQVLIKNP 227
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
23-233 1.02e-20

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 89.37  E-value: 1.02e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtaaqRPAVIFQDalQALNPLVS 102
Cdd:PRK10851   20 DISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQT---SGHIRFHGTDVSRLHARDR----KVGFVFQH--YALFRHMT 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IEGQLSLALTG-TRTKLKSQDKI--KLTELL--VQLGFpnpetILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:PRK10851   91 VFDNIAFGLTVlPRRERPNAAAIkaKVTQLLemVQLAH-----LADRYPAQLSGGQKQRVALARALAVEPQILLLDEPFG 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 178 ALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK10851  166 ALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMeVADRVVVMSQGNIEQAGTPD 222
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 8-233 1.10e-20

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 87.88  E-value: 1.10e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   8 VDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIaGFL--PET-------VEVEGHISLSGDAvcglpML 78
Cdd:PRK11264    6 VKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCI-NLLeqPEAgtirvgdITIDTARSLSQQK-----GL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTAAQRPAVIFQD--------ALQALnplvsIEGQLSLaltgtRTKLKSQDKIKLTELLVQLGFPNPETIlplYPSQIS 150
Cdd:PRK11264   80 IRQLRQHVGFVFQNfnlfphrtVLENI-----IEGPVIV-----KGEPKEEATARARELLAKVGLAGKETS---YPRRLS 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIgGLLITHDLHSAL-ACDKLLVIDGGGVVAY 229
Cdd:PRK11264  147 GGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT-MVIVTHEMSFARdVADRAIFMDQGRIVEQ 225


                  ....
gi 1330606456 230 GAPK 233
Cdd:PRK11264  226 GPAK 229
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 23-233 1.11e-20

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


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 88.28  E-value: 1.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PE--TVEVEGHISLSGDAVCGLPMLQRTAaqrpaVIFQdalqalNP 99
Cdd:TIGR04521  23 DVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLkPTsgTVTIDGRDITAKKKKKLKDLRKKVG-----LVFQ------FP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 lvsiEGQLsLALT-------GTRTKLKSQDKIKLT--ELLVQLGFPnpETILPLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:TIGR04521  92 ----EHQL-FEETvykdiafGPKNLGLSEEEAEERvkEALELVGLD--EEYLERSPFELSGGQMRRVAIAGVLAMEPEVL 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPK 233
Cdd:TIGR04521 165 ILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEyADRVIVMHKGKIVLDGTPR 228
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 2-225 1.65e-20

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 90.25  E-value: 1.65e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQLTIKTSS-RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISL-SGDAVCGLPmlq 79
Cdd:COG4178   359 EDGALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYG---SGRIARpAGARVLFLP--- 432

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 rtaaQRPAVifqdalqalnPLVSIEGQLSLALTGTRTklksqDKIKLTELLVQLGFPNpetilpLYP--------SQI-S 150
Cdd:COG4178   433 ----QRPYL----------PLGTLREALLYPATAEAF-----SDAELREALEAVGLGH------LAErldeeadwDQVlS 487

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHdlHSALA--CDKLLVIDGGG 225
Cdd:COG4178   488 LGEQQRLAFARLLLHKPDWLFLDEATSALDEENEAALYQLLREELPGTTV--ISVGH--RSTLAafHDRVLELTGDG 560
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 8-232 2.59e-20

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: 85.88  E-value: 2.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   8 VDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDA-VCGLPMLQRTAAQRP 86
Cdd:cd03265     3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPT---------SGRAtVAGHDVVREPREVRR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  87 --AVIFQDalqalnplVSIEGQLS----LALTGTRTKLKSQD-KIKLTELLVQLGFPN-PETILPLYpsqiSGGQRQRIC 158
Cdd:cd03265    74 riGIVFQD--------LSVDDELTgwenLYIHARLYGVPGAErRERIDELLDFVGLLEaADRLVKTY----SGGMRRRLE 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYGAP 232
Cdd:cd03265   142 IARSLVHRPEVLFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAeQLCDRVAIIDHGRIIAEGTP 216
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 22-209 3.41e-20

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 89.14  E-value: 3.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAiagfLPETVEV-EGHISLSGDAVCGLPMLQRTAAQRP-AVIFQDALQALNP 99
Cdd:PRK10261  341 EKVSFDLWPGETLSLVGESGSGKSTTGRA----LLRLVESqGGEIIFNGQRIDTLSPGKLQALRRDiQFIFQDPYASLDP 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 LVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFpNPETILPlYPSQISGGQRQRICIAIGLLSNADLIIADEPTSAL 179
Cdd:PRK10261  417 RQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGL-LPEHAWR-YPHEFSGGQRQRICIARALALNPKVIIADEAVSAL 494

                         170       180       190
                  ....*....|....*....|....*....|
gi 1330606456 180 DPVTEQEILKLIRDNVKQRQIGGLLITHDL 209
Cdd:PRK10261  495 DVSIRGQIINLLLDLQRDFGIAYLFISHDM 524
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 6-230 3.46e-20

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: 85.38  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAqr 85
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPT---SGRIYIGGRDVTDLPPKDRDIA-- 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 paVIFQDalQALNPLVSIEGQLSLALtgtrtKLKSQDKIKLTEL------LVQLgfpnpETILPLYPSQISGGQRQRICI 159
Cdd:cd03301    76 --MVFQN--YALYPHMTVYDNIAFGL-----KLRKVPKDEIDERvrevaeLLQI-----EHLLDRKPKQLSGGQRQRVAL 141

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPV----TEQEILKLirdnvkQRQIGG--LLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03301   142 GRAIVREPKVFLMDEPLSNLDAKlrvqMRAELKRL------QQRLGTttIYVTHDQVEAMTmADRIAVMNDGQIQQIG 213
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 23-232 5.97e-20

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: 84.77  E-value: 5.97e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqrtaaqrpavifqdaLQALNPLVS 102
Cdd:cd03369    26 NVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAE---EGKIEIDGIDISTIP-----------------LEDLRSSLT 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IEGQLSLALTGT-RTKL----KSQDKIKLTELLVQLGFPNpetilplypsqISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:cd03369    86 IIPQDPTLFSGTiRSNLdpfdEYSDEEIYGALRVSEGGLN-----------LSQGQRQLLCLARALLKRPRVLVLDEATA 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 178 ALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAP 232
Cdd:cd03369   155 SIDYATDALIQKTIREEFTNSTI--LTIAHRLRTIIDYDKILVMDAGEVKEYDHP 207
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 6-230 7.27e-20

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: 84.58  E-value: 7.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLpmlqRTAAQR 85
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPD---SGEITFDGKSYQKN----IEALRR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDalQALNPLVSIEGQLSLALTGTRTKLKSQDKIkltELLVQLGFPNPETIlplypSQISGGQRQRICIAIGLLS 165
Cdd:cd03268    74 IGALIEA--PGFYPNLTARENLRLLARLLGIRKKRIDEV---LDVVGLKDSAKKKV-----KGFSLGMKQRLGIALALLG 143

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYG 230
Cdd:cd03268   144 NPDLLILDEPTNGLDPDGIKELRELILS-LRDQGITVLISSHLLSEiQKVADRIGIINKGKLIEEG 208
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
6-232 7.67e-20

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 85.45  E-value: 7.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETveveGHISLSGDAVCGLPmlQRTAAQ 84
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLtPQS----GTVFLGDKPISMLS--SRQLAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQdalQALNP-------LVSIEGQLSLALTGtrtKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRI 157
Cdd:PRK11231   77 RLALLPQ---HHLTPegitvreLVAYGRSPWLSLWG---RLSAEDNARVNQAMEQTRI---NHLADRRLTDLSGGQRQRA 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 158 CIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRdnvKQRQIGGLLIT--HDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:PRK11231  148 FLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMR---ELNTQGKTVVTvlHDLNQASRyCDHLVVLANGHVMAQGTP 222
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
 19-228 8.59e-20

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 84.71  E-value: 8.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  19 TLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQRPAVIFQDALQALN 98
Cdd:TIGR02211  19 RVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPT---SGEVLFNGQSLSKLSSNERAKLRNKKLGFIYQFHHLL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 PLVSI-EGQLSLALTGTRTKLKSQDKIKltELLVQLGFPNPetiLPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:TIGR02211  96 PDFTAlENVAMPLLIGKKSVKEAKERAY--EMLEKVGLEHR---INHRPSELSGGERQRVAIARALVNQPSLVLADEPTG 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 178 ALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVA 228
Cdd:TIGR02211 171 NLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQLFN 221
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 22-230 9.23e-20

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: 84.97  E-value: 9.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSmlsrAIAGFLPETVEV-EGHISLSGDAVCG--LPMLQRTAA--QRPAVIFQDalqa 96
Cdd:cd03251    19 RDISLDIPAGETVALVGPSGSGKS----TLVNLIPRFYDVdSGRILIDGHDVRDytLASLRRQIGlvSQDVFLFND---- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 lnplvSIEGQLSLALTG-TRTKLKSQDKI-KLTELLVQL--GFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:cd03251    91 -----TVAENIAYGRPGaTREEVEEAARAaNAHEFIMELpeGY---DTVIGERGVKLSGGQRQRIAIARALLKDPPILIL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKQRQigGLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:cd03251   163 DEATSALDTESERLVQAALERLMKNRT--TFVIAHRLSTIENADRIVVLEDGKIVERG 218
cbiO PRK13642
energy-coupling factor transporter ATPase;
5-239 1.11e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 85.53  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIK---TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtveVEGHISLSGDAVCGLPMLQrt 81
Cdd:PRK13642    4 ILEVENLVFKyekESDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEE---FEGKVKIDGELLTAENVWN-- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAQRPAVIFQDALqalNPLVSIEGQLSLALTGTRTKLKSQDKIK-LTELLVQLGFPNPETilpLYPSQISGGQRQRICIA 160
Cdd:PRK13642   79 LRRKIGMVFQNPD---NQFVGATVEDDVAFGMENQGIPREEMIKrVDEALLAVNMLDFKT---REPARLSGGQKQRVAVA 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESS 239
Cdd:PRK13642  153 GIIALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKAGEIIKEAAPSELFATS 231
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 36-243 1.13e-19

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


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 86.39  E-value: 1.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  36 IMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVcglpmLQRTAAQRP-AVIFQDalQALNPLVSIEGQLSLALtgt 114
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGF--EQPD-SGSIMLDGEDV-----TNVPPHLRHiNMVFQS--YALFPHMTVEENVAFGL--- 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 115 rtKLKSQDKIKLTE-LLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDpvteQEILKLIRD 193
Cdd:TIGR01187  68 --KMRKVPRAEIKPrVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALD----KKLRDQMQL 141

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 194 NVK--QRQIG--GLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:TIGR01187 142 ELKtiQEQLGitFVFVTHDQEEAMTmSDRIAIMRKGKIAQIGTPEEIYEEPANLF 196
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 6-231 4.50e-19

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: 82.96  E-value: 4.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQR 85
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVK---SGSIRLDGEDITKLPPHERARAGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAV-----IFqdalqalnPLVSIEGQLSLALTGTRTKLKsqdKIkltellvqlgfpnPETILPLYP----------SQIS 150
Cdd:TIGR03410  78 AYVpqgreIF--------PRLTVEENLLTGLAALPRRSR---KI-------------PDEIYELFPvlkemlgrrgGDLS 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALAC-DKLLVIDGGGVVAY 229
Cdd:TIGR03410 134 GGQQQQLAIARALVTRPKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELaDRYYVMERGRVVAS 213


                  ..
gi 1330606456 230 GA 231
Cdd:TIGR03410 214 GA 215
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
17-221 4.97e-19

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 81.90  E-value: 4.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDavcglpmLQRTAAQRPA-VIFQDALQ 95
Cdd:NF040873    4 GRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPT---------SGT-------VRRAGGARVAyVPQRSEVP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLvSIEGQLSLALTGTRT---KLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:NF040873   68 DSLPL-TVRDLVAMGRWARRGlwrRLTRDDRAAVDDALERVGL---ADLAGRQLGELSGGQRQRALLAQGLAQEADLLLL 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKqRQIGGLLITHDLHSALACDKLLVI 221
Cdd:NF040873  144 DEPTTGLDAESRERIIALLAEEHA-RGATVVVVTHDLELVRRADPCVLL 191
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 2-224 6.49e-19

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 81.32  E-value: 6.49e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQLTIKTSsrtlFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRT 81
Cdd:cd03215     1 GEPVLEVRGLSVKGA----VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPA---SGEITLDGKPVTRRSPRDAI 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAqRPAVIFQD-ALQALNPLVSIEGQLSLaltgtrtklksqdkikltellvqlgfpnpetilplyPSQISGGQRQRICIA 160
Cdd:cd03215    74 RA-GIAYVPEDrKREGLVLDLSVAENIAL------------------------------------SSLLSGGNQQKVVLA 116

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:cd03215   117 RWLARDPRVLILDEPTRGVDVGAKAEIYRLIRE-LADAGKAVLLISSELDELLGlCDRILVMYEG 180
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
14-233 7.72e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 83.21  E-value: 7.72e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLpetVEVEGHISLSGDAVCGLPMLQrTAAQRPAVIFQDA 93
Cdd:PRK13633   19 ESTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALL---IPSEGKVYVDGLDTSDEENLW-DIRNKAGMVFQNP 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 LqalNPLVS--IE-----GQLSLALTGTRTKLKSQDKIKLTELLVQLGFPnpetilplyPSQISGGQRQRICIAIGLLSN 166
Cdd:PRK13633   95 D---NQIVAtiVEedvafGPENLGIPPEEIRERVDESLKKVGMYEYRRHA---------PHLLSGGQKQRVAIAGILAMR 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 167 ADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13633  163 PECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVVMEGTPK 229
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
17-233 1.19e-18

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 83.62  E-value: 1.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCglpmlQRTAAQRP-AVIFQDalQ 95
Cdd:PRK11432   18 SNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPT---EGQIFIDGEDVT-----HRSIQQRDiCMVFQS--Y 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLVSIEGQLS--LALTGtRTKLKSQDKIKLTELLVQL-GFPNPetilplYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:PRK11432   88 ALFPHMSLGENVGygLKMLG-VPKEERKQRVKEALELVDLaGFEDR------YVDQISGGQQQRVALARALILKPKVLLF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALAC-DKLLVIDGGGVVAYGAPK 233
Cdd:PRK11432  161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVsDTVIVMNKGKIMQIGSPQ 222
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
1-238 1.68e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 82.55  E-value: 1.68e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpeTVEVEGHISLSGDAVcglPMLQR 80
Cdd:PRK13537    3 MSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGL---THPDAGSISLCGEPV---PSRAR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVIFQdaLQALNPLVSIegQLSLALTGTRTKLKSQDKIKLTELLvqLGFPNPETILPLYPSQISGGQRQRICIA 160
Cdd:PRK13537   77 HARQRVGVVPQ--FDNLDPDFTV--RENLLVFGRYFGLSAAAARALVPPL--LEFAKLENKADAKVGELSGGMKRRLTLA 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYGAPKHALES 238
Cdd:PRK13537  151 RALVNDPDVLVLDEPTTGLDPQARHLMWERLR-SLLARGKTILLTTHFMEEAeRLCDRLCVIEEGRKIAEGAPHALIES 228
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
1-212 1.98e-18

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 81.40  E-value: 1.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTS----SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDAVC-GL 75
Cdd:PRK11629    1 MNKILLQCDNLCKRYQegsvQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPT---------SGDVIFnGQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  76 PMLQRTAAQRPAV-------IFQdaLQALNP-LVSIEGQLSLALTGTRTKLKSQDKIKltELLVQLGFpnpETILPLYPS 147
Cdd:PRK11629   72 PMSKLSSAAKAELrnqklgfIYQ--FHHLLPdFTALENVAMPLLIGKKKPAEINSRAL--EMLAAVGL---EHRANHRPS 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 148 QISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA 212
Cdd:PRK11629  145 ELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLA 209
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 6-237 2.43e-18

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


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 80.26  E-value: 2.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlPETVEVEGHISLSGDAVCGLPMLQRTAA-- 83
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGH-PKYEVTEGEILFKGEDITDLPPEERARLgi 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 ----QRPavifqdalqalnplVSIEGqlslaltgtrtklksqdkIKLTELL--VQLGFpnpetilplypsqiSGGQRQRI 157
Cdd:cd03217    80 flafQYP--------------PEIPG------------------VKNADFLryVNEGF--------------SGGEKKRN 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 158 CIAIGLLSNADLIIADEPTSALD----PVTEQEILKLIRDNVkqrqiGGLLITH--DLHSALACDKLLVIDGGGVVAYGA 231
Cdd:cd03217   114 EILQLLLLEPDLAILDEPDSGLDidalRLVAEVINKLREEGK-----SVLIITHyqRLLDYIKPDRVHVLYDGRIVKSGD 188


                  ....*.
gi 1330606456 232 PKHALE 237
Cdd:cd03217   189 KELALE 194
cbiO PRK13646
energy-coupling factor transporter ATPase;
23-233 4.59e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 81.36  E-value: 4.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVeveGHISLSGDAVCGLPMLQ--RTAAQRPAVIFQDALQALNPl 100
Cdd:PRK13646   25 DVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTT---GTVTVDDITITHKTKDKyiRPVRKRIGMVFQFPESQLFE- 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 101 VSIEGQLSLALTGTRTKLKsQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:PRK13646  101 DTVEREIIFGPKNFKMNLD-EVKNYAHRLLMDLGFS--RDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 181 PVTEQEILKLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13646  178 PQSKRQVMRLLKSLQTDENKTIILVSHDMNEvARYADEVIVMKEGSIVSQTSPK 231
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 23-231 4.81e-18

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: 82.83  E-value: 4.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGL-PMLQRT----AAQRPAVIFQDALQAL 97
Cdd:TIGR02204 358 GLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQ---SGRILLDGVDLRQLdPAELRArmalVPQDPVLFAASVMENI 434

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 ---NPLVSIEGQLSLAltgtrtklksqDKIKLTELLVQL--GFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:TIGR02204 435 rygRPDATDEEVEAAA-----------RAAHAHEFISALpeGY---DTYLGERGVTLSGGQRQRIAIARAILKDAPILLL 500

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 173 DEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGA 231
Cdd:TIGR02204 501 DEATSALDAESEQLVQQALETLMKGRTT--LIIAHRLATVLKADRIVVMDQGRIVAQGT 557
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 6-230 4.91e-18

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: 82.78  E-value: 4.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKT--SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGdavcglpmlqrtaa 83
Cdd:TIGR01842 317 LSVENVTIVPpgGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPT---SGSVRLDG-------------- 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 qrpAVIFQDALQALNPLVSIEGQLSLALTGT--------RTKLKSQDKI---KLT---ELLvqLGFPNP-ETILPLYPSQ 148
Cdd:TIGR01842 380 ---ADLKQWDRETFGKHIGYLPQDVELFPGTvaeniarfGENADPEKIIeaaKLAgvhELI--LRLPDGyDTVIGPGGAT 454

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 149 ISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLhSALAC-DKLLVIDGGGVV 227
Cdd:TIGR01842 455 LSGGQRQRIALARALYGDPKLVVLDEPNSNLDEEGEQALANAIKA-LKARGITVVVITHRP-SLLGCvDKILVLQDGRIA 532


                  ...
gi 1330606456 228 AYG 230
Cdd:TIGR01842 533 RFG 535
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
5-233 7.02e-18

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 80.58  E-value: 7.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglPMLQR---- 80
Cdd:PRK11831    7 LVDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPD---HGEILFDGENI---PAMSRsrly 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVIFQDAlqALNPLVSIEGQLSLALtgtRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIA 160
Cdd:PRK11831   81 TVRKRMSMLFQSG--ALFTDMNVFDNVAYPL---REHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPK 233
Cdd:PRK11831  156 RAIALEPDLIMFDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSiADHAYIVADKKIVAHGSAQ 229
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 22-238 9.48e-18

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: 79.19  E-value: 9.48e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQRTAAQRPAVIFQDalqalnPLV 101
Cdd:cd03254    20 KDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQ---KGQILIDGIDIRDIS--RKSLRSMIGVVLQD------TFL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 ---SIEGQLSLA-LTGTRTKLKSQDK-IKLTELLVQLgfPNP-ETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:cd03254    89 fsgTIMENIRLGrPNATDEEVIEAAKeAGAHDFIMKL--PNGyDTVLGENGGNLSQGERQLLAIARAMLRDPKILILDEA 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 176 TSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALES 238
Cdd:cd03254   167 TSNIDTETEKLIQEALEKLMKGRTS--IIIAHRLSTIKNADKILVLDDGKIIEEGTHDELLAK 227
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 27-247 1.22e-17

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: 79.37  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  27 DVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglpmlqrtaAQRPAVIFQDAlqalnplvsiegq 106
Cdd:cd03237    21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPD---EGDIEIELDTV----------SYKPQYIKADY------------- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 107 lslalTGT-RTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQI---SGGQRQRICIAIGLLSNADLIIADEPTSALDpv 182
Cdd:cd03237    75 -----EGTvRDLLSSITKDFYTHPYFKTEIAKPLQIEQILDREVpelSGGELQRVAIAACLSKDADIYLLDEPSAYLD-- 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 183 TEQEIL--KLIRDNVKQRQIGGLLITHDLHSA-LACDKLLVIDG-GGVVAYGAPKHALESSSHAFCCSL 247
Cdd:cd03237   148 VEQRLMasKVIRRFAENNEKTAFVVEHDIIMIdYLADRLIVFEGePSVNGVANPPQSLRSGMNRFLKNL 216
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 21-209 1.26e-17

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: 81.64  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP--MLQRTA---AQRPAVIFQDALQ 95
Cdd:TIGR02868 351 LDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPL---QGEVTLDGVPVSSLDqdEVRRRVsvcAQDAHLFDTTVRE 427

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 AL---NPLVSIEgQLSLALtgtrtklksqDKIKLTELLVQLgfpnPE---TILPLYPSQISGGQRQRICIAIGLLSNADL 169
Cdd:TIGR02868 428 NLrlaRPDATDE-ELWAAL----------ERVGLADWLRAL----PDgldTVLGEGGARLSGGERQRLALARALLADAPI 492

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1330606456 170 IIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDL 209
Cdd:TIGR02868 493 LLLDEPTEHLDAETADELLEDLLAALSGRTV--VLITHHL 530
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 14-227 1.91e-17

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: 78.47  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLSGDAVCGLPMLQRTAaqrpaviFQDA 93
Cdd:cd03234    16 WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGGGTTSGQILFNGQPRKPDQFQKCVA-------YVRQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 LQALNPLVSIEGQL--SLALTGTRTKLKSQ-DKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:cd03234    89 DDILLPGLTVRETLtyTAILRLPRKSSDAIrKKRVEDVLLRDLAL---TRIGGNLVKGISGGERRRVSIAVQLLWDPKVL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDNVKQRQIggLLIT-H----DLHSALacDKLLVIDGGGVV 227
Cdd:cd03234   166 ILDEPTSGLDSFTALNLVSTLSQLARRNRI--VILTiHqprsDLFRLF--DRILLLSSGEIV 223
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 14-230 1.92e-17

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: 78.53  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDavcgLPMLQRTA-AQRPAVIFQD 92
Cdd:cd03267    30 KYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPT---SGEVRVAGL----VPWKRRKKfLRRIGVVFGQ 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALQALNPLVSIEG--------QLSLALTGTRTKlksqdkiKLTELLvqlgfpNPETILPLYPSQISGGQRQRICIAIGLL 164
Cdd:cd03267   103 KTQLWWDLPVIDSfyllaaiyDLPPARFKKRLD-------ELSELL------DLEELLDTPVRQLSLGQRMRAEIAAALL 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 165 SNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03267   170 HEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEAlARRVLVIDKGRLLYDG 236
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 11-241 2.26e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 78.73  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  11 LTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF--LPETVEVEGHISLSGDAVCGLPMLQRTAAQRPAV 88
Cdd:PRK14267   10 LRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLleLNEEARVEGEVRLFGRNIYSPDVDPIEVRREVGM 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  89 IFQDAlqalNPLVSIEGQLSLALTGTRTKL-KSQDKI-KLTELLVQLG--FPNPETILPLYPSQISGGQRQRICIAIGLL 164
Cdd:PRK14267   90 VFQYP----NPFPHLTIYDNVAIGVKLNGLvKSKKELdERVEWALKKAalWDEVKDRLNDYPSNLSGGQRQRLVIARALA 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 165 SNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHD-LHSALACDKLLVIDGGGVVAYGAPKHALESSSH 241
Cdd:PRK14267  166 MKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTI--VLVTHSpAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEH 241
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
22-234 2.43e-17

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 80.92  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRaIAGFLPE----TVEVEGH--ISLSGDAvcgLPMLQRtaaQRPAVIFQ--DA 93
Cdd:PRK10535   25 KGISLDIYAGEMVAIVGASGSGKSTLMN-ILGCLDKptsgTYRVAGQdvATLDADA---LAQLRR---EHFGFIFQryHL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 LQALNPLVSIEGQLSLALTGTRTKLKsqdkiKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIAD 173
Cdd:PRK10535   98 LSHLTAAQNVEVPAVYAGLERKQRLL-----RAQELLQRLGL---EDRVEYQPSQLSGGQQQRVSIARALMNGGQVILAD 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 174 EPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPKH 234
Cdd:PRK10535  170 EPTGALDSHSGEEVMAILH-QLRDRGHTVIIVTHDPQVAAQAERVIEIRDGEIVRNPPAQE 229
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 1-212 3.15e-17

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 78.28  E-value: 3.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAI--AGFLPETVEVEGHISLSGDAVCGLPML 78
Cdd:PRK14239    1 MTEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPEVTITGSIVYNGHNIYSPRTD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTAAQRPAVIFQDAlqalNPL-VSIEGQL--SLALTGTRtklksqDKIKLTEL----LVQLGFPNpETILPLYPSQI-- 149
Cdd:PRK14239   81 TVDLRKEIGMVFQQP----NPFpMSIYENVvyGLRLKGIK------DKQVLDEAveksLKGASIWD-EVKDRLHDSALgl 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTE---QEILKLIRDnvkqrQIGGLLITHDLHSA 212
Cdd:PRK14239  150 SGGQQQRVCIARVLATSPKIILLDEPTSALDPISAgkiEETLLGLKD-----DYTMLLVTRSMQQA 210
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
22-232 3.22e-17

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 79.69  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEveghislSGDAVCGLpmlQRTAAQRPA-----VIFQDalQA 96
Cdd:PRK11000   20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGL--EDIT-------SGDLFIGE---KRMNDVPPAergvgMVFQS--YA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIEGQLSLALtgtrtKLKSQDKIKL-------TELLvQLGFpnpetILPLYPSQISGGQRQRICIAIGLLSNADL 169
Cdd:PRK11000   86 LYPHLSVAENMSFGL-----KLAGAKKEEInqrvnqvAEVL-QLAH-----LLDRKPKALSGGQRQRVAIGRTLVAEPSV 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 170 IIADEPTSALDPV----TEQEILKLirdnvkQRQIGGLLI--THDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:PRK11000  155 FLLDEPLSNLDAAlrvqMRIEISRL------HKRLGRTMIyvTHDQVEAMTlADKIVVLDAGRVAQVGKP 218
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
22-228 3.66e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 80.06  E-value: 3.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglPMLQRTAAQRP--AVIFQDalQALNP 99
Cdd:COG1129    21 DGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPD---SGEILLDGEPV---RFRSPRDAQAAgiAIIHQE--LNLVP 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 LVSIEGQLSLALTGTRTKLKSQDKI--KLTELLVQLGFP-NPETILplypSQISGGQRQRICIAIGLLSNADLIIADEPT 176
Cdd:COG1129    93 NLSVAENIFLGREPRRGGLIDWRAMrrRARELLARLGLDiDPDTPV----GDLSVAQQQLVEIARALSRDARVLILDEPT 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 177 SALDPvTEQEIL-KLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVA 228
Cdd:COG1129   169 ASLTE-REVERLfRIIRR-LKAQGVAIIYISHRLDEVFEiADRVTVLRDGRLVG 220
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 2-219 4.61e-17

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 77.45  E-value: 4.61e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP---ML 78
Cdd:PRK10247    4 NSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPT---SGTLLFEGEDISTLKpeiYR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTA--AQRPAvIFQDalqalnplvSIEGQLSLALtgtRTKLKSQDKIKLTELLVQLGFPnpETILPLYPSQISGGQRQR 156
Cdd:PRK10247   81 QQVSycAQTPT-LFGD---------TVYDNLIFPW---QIRNQQPDPAIFLDDLERFALP--DTILTKNIAELSGGEKQR 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 157 ICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLL 219
Cdd:PRK10247  146 ISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 3-233 4.96e-17

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: 77.33  E-value: 4.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTikTS---SRTLFqDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlq 79
Cdd:COG0410     1 MPMLEVENLH--AGyggIHVLH-GVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPR---SGSIRFDGEDITGLP--- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 rtAAQRPAV----------IFqdalqalnPLVSIEGQLSLALTGTRTKLKSQDKI--------KLTELLVQLGfpnpeti 141
Cdd:COG0410    72 --PHRIARLgigyvpegrrIF--------PSLTVEENLLLGAYARRDRAEVRADLervyelfpRLKERRRQRA------- 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 142 lplypSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLV 220
Cdd:COG0410   135 -----GTLSGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRR-LNREGVTILLVEQNARFALEiADRAYV 208

                         250
                  ....*....|...
gi 1330606456 221 IDGGGVVAYGAPK 233
Cdd:COG0410   209 LERGRIVLEGTAA 221
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 6-230 5.22e-17

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


Pssm-ID: 213236 [Multi-domain]  Cd Length: 210  Bit Score: 76.94  E-value: 5.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglpmlqrTAAQR 85
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPD---SGEVLFDGKPL--------DIAAR 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDALQALNPLVSIEGQLsLALTGTRTKLKSQDKIKLTELLVQLGFPNPETIlPLypSQISGGQRQRICIAIGLLS 165
Cdd:cd03269    70 NRIGYLPEERGLYPKMKVIDQL-VYLAQLKGLKKEEARRRIDEWLERLELSEYANK-RV--EELSKGNQQKVQFIAAVIH 145

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDnvkQRQIGGLLI--THDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03269   146 DPELLILDEPFSGLDPVNVELLKDVIRE---LARAGKTVIlsTHQMELVEElCDRVLLLNKGRAVLYG 210
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
35-243 6.01e-17

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 78.76  E-value: 6.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  35 AIMGPSGIGKSMLSRAIAGFlpeTVEVEGHISLSG----DAVCG--LPMLQRtaaqRPAVIFQDAlqALNPLVSIEGQLs 108
Cdd:PRK11144   28 AIFGRSGAGKTSLINAISGL---TRPQKGRIVLNGrvlfDAEKGicLPPEKR----RIGYVFQDA--RLFPHYKVRGNL- 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 109 laLTGTRTKLKSQ-DKIklTELLvqlGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEI 187
Cdd:PRK11144   98 --RYGMAKSMVAQfDKI--VALL---GI---EPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKREL 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 188 LKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGapkhALES--SSHAF 243
Cdd:PRK11144  168 LPYLERLAREINIPILYVSHSLDEILRlADRVVVLEQGKVKAFG----PLEEvwASSAM 222
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 1-240 7.87e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 77.48  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLF--QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCglPML 78
Cdd:PRK13648    3 DKNSIIVFKNVSFQYQSDASFtlKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVK---SGEIFYNNQAIT--DDN 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTAAQRPAVIFQDALqalNPLVSIEGQLSLALtGTRTKLKSQDKI--KLTELLVQLG---FPNPEtilplyPSQISGGQ 153
Cdd:PRK13648   78 FEKLRKHIGIVFQNPD---NQFVGSIVKYDVAF-GLENHAVPYDEMhrRVSEALKQVDmleRADYE------PNALSGGQ 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13648  148 KQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKGTVYKEGTPT 227


                  ....*..
gi 1330606456 234 HALESSS 240
Cdd:PRK13648  228 EIFDHAE 234
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
5-241 8.16e-17

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 77.52  E-value: 8.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRT-LF--------QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET---VEVEGHISLSGDav 72
Cdd:PRK15112    4 LLEVRNLSKTFRYRTgWFrrqtveavKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTsgeLLIDDHPLHFGD-- 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  73 cglpmlQRTAAQRPAVIFQDALQALNPLVSIEGQLSLALTgTRTKLKSQDKIK-LTELLVQLGfpnpetILP----LYPS 147
Cdd:PRK15112   82 ------YSYRSQRIRMIFQDPSTSLNPRQRISQILDFPLR-LNTDLEPEQREKqIIETLRQVG------LLPdhasYYPH 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 148 QISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDL----HSAlacDKLLVIDG 223
Cdd:PRK15112  149 MLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLgmmkHIS---DQVLVMHQ 225

                         250
                  ....*....|....*...
gi 1330606456 224 GGVVAYGAPKHALESSSH 241
Cdd:PRK15112  226 GEVVERGSTADVLASPLH 243
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 22-213 1.10e-16

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: 76.35  E-value: 1.10e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglpmlQRTAAQRpAVIFQDalQALNPLV 101
Cdd:TIGR01184   2 KGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPT---SGGVILEGKQI------TEPGPDR-MVVFQN--YSLLPWL 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSLALTGTRTKLKSQDKIKLTE---LLVQLGFPNPEtilplYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:TIGR01184  70 TVRENIALAVDRVLPDLSKSERRAIVEehiALVGLTEAADK-----RPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGA 144

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1330606456 179 LDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAL 213
Cdd:TIGR01184 145 LDALTRGNLQEELMQIWEEHRVTVLMVTHDVDEAL 179
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 4-210 1.28e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 77.00  E-value: 1.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF--LPETVEVEGHISLSGDAVCGLPM-LQR 80
Cdd:PRK14258    6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMneLESEVRVEGRVEFFNQNIYERRVnLNR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVIFQDALQALNPLVSIegQLSLALTGTRTKLKSQD----KIKLTELLVQLGFPNPETILPLypsqiSGGQRQR 156
Cdd:PRK14258   86 LRRQVSMVHPKPNLFPMSVYDNV--AYGVKIVGWRPKLEIDDivesALKDADLWDEIKHKIHKSALDL-----SGGQQQR 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 157 ICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH 210
Cdd:PRK14258  159 LCIARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLH 212
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 24-233 1.36e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 77.04  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  24 IHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQRPAVIFQDA-LQALNPLVS 102
Cdd:PRK13639   21 INFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPT---SGEVLIKGEPIKYDKKSLLEVRKTVGIVFQNPdDQLFAPTVE 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IE---GQLSLALTGTRTKLKSQDKIKLTELLvqlGFPNPEtilplyPSQISGGQRQRICIAIGLLSNADLIIADEPTSAL 179
Cdd:PRK13639   98 EDvafGPLNLGLSKEEVEKRVKEALKAVGME---GFENKP------PHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGL 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 180 DPVTEQEILKLIRDnVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13639  169 DPMGASQIMKLLYD-LNKEGITIIISTHDVDLVpVYADKVYVMSDGKIIKEGTPK 222
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 5-236 1.43e-16

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 76.47  E-value: 1.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRtAAQ 84
Cdd:PRK10895    3 TLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRD---AGNIIIDDEDISLLPLHAR-ARR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDAlqalnplvSIEGQLS-----LALTGTRTKLKS-QDKIKLTELLVQLGFPNPETILPlypSQISGGQRQRIC 158
Cdd:PRK10895   79 GIGYLPQEA--------SIFRRLSvydnlMAVLQIRDDLSAeQREDRANELMEEFHIEHLRDSMG---QSLSGGERRRVE 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIrDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHAL 236
Cdd:PRK10895  148 IARALAANPKFILLDEPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNVRETLAvCERAYIVSQGHLIAHGTPTEIL 225
cbiO PRK13650
energy-coupling factor transporter ATPase;
23-233 1.76e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 76.69  E-value: 1.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETVE--VEGHIsLSGDAVCGLPMLQRTAAQRPAVIFQDAlqalnp 99
Cdd:PRK13650   25 DVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLeAESGQiiIDGDL-LTEENVWDIRHKIGMVFQNPDNQFVGA------ 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 lvSIEGQLSLALTGTRTKLKsQDKIKLTELLVQLG---FPNPEtilplyPSQISGGQRQRICIAIGLLSNADLIIADEPT 176
Cdd:PRK13650   98 --TVEDDVAFGLENKGIPHE-EMKERVNEALELVGmqdFKERE------PARLSGGQKQRVAIAGAVAMRPKIIILDEAT 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 177 SALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13650  169 SMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQVESTSTPR 225
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 35-236 2.04e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 76.10  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  35 AIMGPSGIGKSMLSRAIAGFL---PETvEVEGHISLSGDAVCGLPMLQrtAAQRPAVIFQDAlqalNPL--VSIEGQLSL 109
Cdd:PRK14247   33 ALMGPSGSGKSTLLRVFNRLIelyPEA-RVSGEVYLDGQDIFKMDVIE--LRRRVQMVFQIP----NPIpnLSIFENVAL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 110 ALTGTR---TKLKSQDKIKLTELLVQLgFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQE 186
Cdd:PRK14247  106 GLKLNRlvkSKKELQERVRWALEKAQL-WDEVKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPTANLDPENTAK 184

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 187 ILKLIRDNVKQRQIggLLITH-DLHSALACDKLLVIDGGGVVAYGA-------PKHAL 236
Cdd:PRK14247  185 IESLFLELKKDMTI--VLVTHfPQQAARISDYVAFLYKGQIVEWGPtrevftnPRHEL 240
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 8-229 2.07e-16

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 78.18  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   8 VDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCG-LPmlQRTAAQRP 86
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPD---SGEVSIPKGLRIGyLP--QEPPLDDD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  87 AVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKI-----------------KLTELLVQLGFPNPETILPLypSQI 149
Cdd:COG0488    76 LTVLDTVLDGDAELRALEAELEELEAKLAEPDEDLERLaelqeefealggweaeaRAEEILSGLGFPEEDLDRPV--SEL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTeqeILKLiRDNVKQRQIGGLLITHD---LHSalACDKLLVIDGGGV 226
Cdd:COG0488   154 SGGWRRRVALARALLSEPDLLLLDEPTNHLDLES---IEWL-EEFLKNYPGTVLVVSHDryfLDR--VATRILELDRGKL 227


                  ...
gi 1330606456 227 VAY 229
Cdd:COG0488   228 TLY 230
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 18-230 3.07e-16

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


Pssm-ID: 130261 [Multi-domain]  Cd Length: 708  Bit Score: 77.86  E-value: 3.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAvcgLPMLQRTA--------AQRPaVI 89
Cdd:TIGR01193 487 SNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQAR---SGEILLNGFS---LKDIDRHTlrqfinylPQEP-YI 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  90 FQDALqalnplvsiegqLSLALTGTRTKLKSQDKIKLTELL--------VQLGFpnpETILPLYPSQISGGQRQRICIAI 161
Cdd:TIGR01193 560 FSGSI------------LENLLLGAKENVSQDEIWAACEIAeikddienMPLGY---QTELSEEGSSISGGQKQRIALAR 624

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:TIGR01193 625 ALLTDSKVLILDESTSNLDTITEKKIVNNLL-NLQDKTI--IFVAHRLSVAKQSDKIIVLDHGKIIEQG 690
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-230 3.12e-16

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 77.56  E-value: 3.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   2 NAPLLSVDQL--TIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKS----MLSRAiagFLPEtvevEGHISLSGDAVCGL 75
Cdd:PRK11160  335 DQVSLTLNNVsfTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKStllqLLTRA---WDPQ----QGEILLNGQPIADY 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  76 PMLQRTAA-----QRPAvIFQDALQalnplvsieGQLSLAltgtrtKLKSQDKiKLTELLVQLGFpnpETILPLYPS--- 147
Cdd:PRK11160  408 SEAALRQAisvvsQRVH-LFSATLR---------DNLLLA------APNASDE-ALIEVLQQVGL---EKLLEDDKGlna 467

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 148 -------QISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLV 220
Cdd:PRK11160  468 wlgeggrQLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNKTV--LMITHRLTGLEQFDRICV 545

                         250
                  ....*....|
gi 1330606456 221 IDGGGVVAYG 230
Cdd:PRK11160  546 MDNGQIIEQG 555
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 20-224 3.41e-16

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 74.43  E-value: 3.41e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  20 LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLSGDA--VCGLPMLQrTAAQRPAVIF------- 90
Cdd:cd03250    20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLG---ELEKLSGSVSVPGSIayVSQEPWIQ-NGTIRENILFgkpfdee 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  91 --QDALQA--LNPLVSIegqlslaltgtrtkLKSQDkikLTEL------LvqlgfpnpetilplypsqiSGGQRQRICIA 160
Cdd:cd03250    96 ryEKVIKAcaLEPDLEI--------------LPDGD---LTEIgekginL-------------------SGGQKQRISLA 139

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEIL-KLIRD---NVKQRqiggLLITHDLHSALACDKLLVIDGG 224
Cdd:cd03250   140 RAVYSDADIYLLDDPLSAVDAHVGRHIFeNCILGlllNNKTR----ILVTHQLQLLPHADQIVVLDNG 203
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 4-226 4.16e-16

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 75.48  E-value: 4.16e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLsVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHIsLSGDAvcglPMLQRTAA 83
Cdd:PRK11247   12 PLL-LNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPS---AGEL-LAGTA----PLAEARED 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRpaVIFQDAlqALNPLVSIEGQLSLALTGtrtklksQDKIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGL 163
Cdd:PRK11247   83 TR--LMFQDA--RLLPWKKVIDNVGLGLKG-------QWRDAALQALAAVGLADRAN---EWPAALSGGQKQRVALARAL 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGV 226
Cdd:PRK11247  149 IHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAmADRVLLIEEGKI 212
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
9-233 4.30e-16

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 75.41  E-value: 4.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   9 DQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLpetVEVEGHISLSGDAVcglpmlQRTA----AQ 84
Cdd:PRK10253   11 EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLM---TPAHGHVWLDGEHI------QHYAskevAR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDALQ----ALNPLVSiEGQLSLALTGTRTKLKSQDKIK-------LTELLVQlgfpNPETIlplypsqiSGGQ 153
Cdd:PRK10253   82 RIGLLAQNATTpgdiTVQELVA-RGRYPHQPLFTRWRKEDEEAVTkamqatgITHLADQ----SVDTL--------SGGQ 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:PRK10253  149 RQRAWIAMVLAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRyASHLIALREGKIVAQGAP 228


                  .
gi 1330606456 233 K 233
Cdd:PRK10253  229 K 229
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 6-225 4.45e-16

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 72.87  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLsgdavcglpmlqrtaaqr 85
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAG---ELEPDEGIVTW------------------ 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 pavifqdalqalnplvsiegqlslaltgtrtklksqdkikltellvqlgfpnPETILPLYPSQISGGQRQRICIAIGLLS 165
Cdd:cd03221    60 ----------------------------------------------------GSTVKIGYFEQLSGGEKMRLALAKLLLE 87

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 166 NADLIIADEPTSALDPVTeqeILKLIrDNVKQRQIGGLLITHDlHSAL--ACDKLLVIDGGG 225
Cdd:cd03221    88 NPNLLLLDEPTNHLDLES---IEALE-EALKEYPGTVILVSHD-RYFLdqVATKIIELEDGK 144
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 17-230 7.97e-16

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: 76.29  E-value: 7.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLsraiAGFLPETVEVE-GHISLSGDAVCGLPM--LQRTAAQ--RPAVIFQ 91
Cdd:TIGR02203 344 DRPALDSISLVIEPGETVALVGRSGSGKSTL----VNLIPRFYEPDsGQILLDGHDLADYTLasLRRQVALvsQDVVLFN 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  92 DALqALNPLVSIEGQLSLAltgtRTKLKSQDKiKLTELLVQL--GFpnpETILPLYPSQISGGQRQRICIAIGLLSNADL 169
Cdd:TIGR02203 420 DTI-ANNIAYGRTEQADRA----EIERALAAA-YAQDFVDKLplGL---DTPIGENGVLLSGGQRQRLAIARALLKDAPI 490

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 170 IIADEPTSALDpvTEQEilKLIRDNVKQRQIG--GLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:TIGR02203 491 LILDEATSALD--NESE--RLVQAALERLMQGrtTLVIAHRLSTIEKADRIVVMDDGRIVERG 549
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
17-230 8.81e-16

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 76.15  E-value: 8.81e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  17 SRTLFQDIHFDVYRGELLAIMGPSGIGKS----MLSRAiagFLPETveveGHISLSGDAVCGLPM--LQRTAAqrpaVIF 90
Cdd:PRK13657  347 SRQGVEDVSFEAKPGQTVAIVGPTGAGKStlinLLQRV---FDPQS----GRILIDGTDIRTVTRasLRRNIA----VVF 415

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  91 QDALqALNPlvSIEGQLSLALTGT-----RTKLK---SQDKIKLTELlvqlGFpnpETILPLYPSQISGGQRQRICIAIG 162
Cdd:PRK13657  416 QDAG-LFNR--SIEDNIRVGRPDAtdeemRAAAEraqAHDFIERKPD----GY---DTVVGERGRQLSGGERQRLAIARA 485

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 163 LLSNADLIIADEPTSALDPVTEQEiLKLIRDNVKQRQIgGLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:PRK13657  486 LLKDPPILILDEATSALDVETEAK-VKAALDELMKGRT-TFIIAHRLSTVRNADRILVFDNGRVVESG 551
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 23-237 9.18e-16

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 75.12  E-value: 9.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAI-AGFLPETVEVE--------GHISLSGDAVCGLPMLQRTAAQ--------- 84
Cdd:PRK13651   25 NVSVEINQGEFIAIIGQTGSGKTTFIEHLnALLLPDTGTIEwifkdeknKKKTKEKEKVLEKLVIQKTRFKkikkikeir 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 -RPAVIFQDALQALNPlVSIE-----GQLSLALTGTRTKLKSQDKIKLTELlvqlgfpnPETILPLYPSQISGGQRQRIC 158
Cdd:PRK13651  105 rRVGVVFQFAEYQLFE-QTIEkdiifGPVSMGVSKEEAKKRAAKYIELVGL--------DESYLQRSPFELSGGQKRRVA 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKlIRDNVKQRQIGGLLITHDLHSALACDK-LLVIDGGGVVAYGAPKHALE 237
Cdd:PRK13651  176 LAGILAMEPDFLVFDEPTAGLDPQGVKEILE-IFDNLNKQGKTIILVTHDLDNVLEWTKrTIFFKDGKIIKDGDTYDILS 254
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 4-207 1.02e-15

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 73.37  E-value: 1.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPetvEVEGHISLSGDAvcglpmlQRTAA 83
Cdd:PRK13539    1 MMLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLP---PAAGTIKLDGGD-------IDDPD 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAVIFQDALQALNPLVSIEGQLSLAltgtrTKLKSQDKIKLTELLVQLGFPNpetILPLYPSQISGGQRQRICIAIGL 163
Cdd:PRK13539   71 VAEACHYLGHRNAMKPALTVAENLEFW-----AAFLGGEELDIAAALEAVGLAP---LAHLPFGYLSAGQKRRVALARLL 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrqiGGLLI--TH 207
Cdd:PRK13539  143 VSNRPIWILDEPTAALDAAAVALFAELIRAHLAQ---GGIVIaaTH 185
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 5-240 1.09e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 74.89  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRT-----LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPE---TVEVEG-----HISLSGDA 71
Cdd:PRK13631   21 ILRVKNLYCVFDEKQenelvALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSkygTIQVGDiyigdKKNNHELI 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  72 VCGLPM-------LQRTAA---QRPAV-IFQDalqalnplvSIEGQLSLALTGTRTKlKSQDKIKLTELLVQLGFPnpET 140
Cdd:PRK13631  101 TNPYSKkiknfkeLRRRVSmvfQFPEYqLFKD---------TIEKDIMFGPVALGVK-KSEAKKLAKFYLNKMGLD--DS 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 141 ILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIgGLLITHDLHSAL-ACDKLL 219
Cdd:PRK13631  169 YLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKT-VFVITHTMEHVLeVADEVI 247

                         250       260
                  ....*....|....*....|....*..
gi 1330606456 220 VIDGGGVVAYGAP------KHALESSS 240
Cdd:PRK13631  248 VMDKGKILKTGTPyeiftdQHIINSTS 274
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 22-230 1.14e-15

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


Pssm-ID: 213212 [Multi-domain]  Cd Length: 220  Bit Score: 73.39  E-value: 1.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPM--LQR---TAAQRPAVIF---QDA 93
Cdd:cd03245    21 DNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPT---SGSVLLDGTDIRQLDPadLRRnigYVPQDVTLFYgtlRDN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 LQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLtELLVQLGfpnpetilplyPSQISGGQRQRICIAIGLLSNADLIIAD 173
Cdd:cd03245    98 ITLGAPLADDERILRAAELAGVTDFVNKHPNGL-DLQIGER-----------GRGLSGGQRQAVALARALLNDPPILLLD 165

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 174 EPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLhSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03245   166 EPTSAMDMNSEERLKERLRQLLGDKTL--IIITHRP-SLLDlVDRIIVMDSGRIVADG 220
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
6-243 1.43e-15

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 75.45  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLP--MLQRTAA 83
Cdd:PRK10070   29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPT---RGQVLIDGVDIAKISdaELREVRR 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAVIFQDAlqALNPLVSI--EGQLSLALTGTRTKLKSQdkiKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAI 161
Cdd:PRK10070  106 KKIAMVFQSF--ALMPHMTVldNTAFGMELAGINAEERRE---KALDALRQVGL---ENYAHSYPDELSGGMRQRVGLAR 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEIL-KLIRDNVK-QRQIggLLITHDLHSALAC-DKLLVIDGGGVVAYGAPKHALES 238
Cdd:PRK10070  178 ALAINPDILLMDEAFSALDPLIRTEMQdELVKLQAKhQRTI--VFISHDLDEAMRIgDRIAIMQNGEVVQVGTPDEILNN 255


                  ....*
gi 1330606456 239 SSHAF 243
Cdd:PRK10070  256 PANDY 260
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 1-209 1.48e-15

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: 73.24  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNaPLLSVDQLTiKT------SSRTL--FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAG-FLPEtvevEGHISL-SGD 70
Cdd:COG4778     1 MT-TLLEVENLS-KTftlhlqGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGnYLPD----SGSILVrHDG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  71 AVcgLPMLQRTAAQ----RPAVI-----FqdaLQALnPLVS-----IEgqlSLALTGTRTKlKSQDKIKltELLVQLGFP 136
Cdd:COG4778    75 GW--VDLAQASPREilalRRRTIgyvsqF---LRVI-PRVSaldvvAE---PLLERGVDRE-EARARAR--ELLARLNLP 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 137 npETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDL 209
Cdd:COG4778   143 --ERLWDLPPATFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEE-AKARGTAIIGIFHDE 212
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 6-207 1.53e-15

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: 72.78  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglpmlqrtAAQR 85
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPD---SGEVRWNGTPL---------AEQR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PavIFQDALQALNPLVSIEGQLSLA--LTGTRTKLKSQDKiKLTELLVQLGFPNPETILPlypSQISGGQRQRICIAIGL 163
Cdd:TIGR01189  69 D--EPHENILYLGHLPGLKPELSALenLHFWAAIHGGAQR-TIEDALAAVGLTGFEDLPA---AQLSAGQQRRLALARLW 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVkQRQIGGLLITH 207
Cdd:TIGR01189 143 LSRRPLWILDEPTTALDKAGVALLAGLLRAHL-ARGGIVLLTTH 185
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
1-236 1.79e-15

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 74.48  E-value: 1.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTS--SRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglPML 78
Cdd:PRK13536   35 GSMSTVAIDLAGVSKSygDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPD---AGKITVLGVPV---PAR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  79 QRTAAQRPAVIFQdaLQALNPLVSIegQLSLALTGTRTKLKSQDKIKLTELLvqLGFPNPETILPLYPSQISGGQRQRIC 158
Cdd:PRK13536  109 ARLARARIGVVPQ--FDNLDLEFTV--RENLLVFGRYFGMSTREIEAVIPSL--LEFARLESKADARVSDLSGGMKRRLT 182

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSA-LACDKLLVIDGGGVVAYGAPkHAL 236
Cdd:PRK13536  183 LARALINDPQLLILDEPTTGLDPHARHLIWERLR-SLLARGKTILLTTHFMEEAeRLCDRLCVLEAGRKIAEGRP-HAL 259
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 27-223 1.81e-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: 75.21  E-value: 1.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  27 DVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEGHISLSgdavcglpmlqrtaaQRPavifqdalQALNPlvSIEG 105
Cdd:COG1245   362 EIREGEVLGIVGPNGIGKTTFAKILAGVLkPDEGEVDEDLKIS---------------YKP--------QYISP--DYDG 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 106 QLSLALTGTRTKlKSQDKIKLTELLvqlgfpNPETILPLYPSQI---SGGQRQRICIAIGLLSNADLIIADEPTSALDpv 182
Cdd:COG1245   417 TVEEFLRSANTD-DFGSSYYKTEII------KPLGLEKLLDKNVkdlSGGELQRVAIAACLSRDADLYLLDEPSAHLD-- 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1330606456 183 TEQEIL--KLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDG 223
Cdd:COG1245   488 VEQRLAvaKAIRRFAENRGKTAMVVDHDIYLiDYISDRLMVFEG 531
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
22-230 1.90e-15

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 73.12  E-value: 1.90e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAgfLPETVEvEGHISLSGDAVCGLPMLQRTAAQ--RPAV--IFQDalQAL 97
Cdd:COG4161    19 FDINLECPSGETLVLLGPSGAGKSSLLRVLN--LLETPD-SGQLNIAGHQFDFSQKPSEKAIRllRQKVgmVFQQ--YNL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLypsQISGGQRQRICIAIGLLSNADLIIADEPTS 177
Cdd:COG4161    94 WPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPL---HLSGGQQQRVAIARALMMEPQVLLFDEPTA 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 178 ALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYG 230
Cdd:COG4161   171 ALDPEITAQVVEIIRE-LSQTGITQVIVTHEVEFARkVASQVVYMEKGRIIEQG 223
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 26-232 2.79e-15

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


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 72.58  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  26 FDVYRGELLAIMGPSGIGKSMLSRAIAGFLPE---TVEVEGHISLSGDAVCG-LPMLQRTAAQRPAVIFQDALQALNPLV 101
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPakgTVKVAGASPGKGWRHIGyVPQRHEFAWDFPISVAHTVMSGRTGHI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSLA-LTGTRTKLksqDKIKLTELLVQlgfpnpetilPLypSQISGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:TIGR03771  81 GWLRRPCVAdFAAVRDAL---RRVGLTELADR----------PV--GELSGGQRQRVLVARALATRPSVLLLDEPFTGLD 145

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 181 PVTeQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDgGGVVAYGAP 232
Cdd:TIGR03771 146 MPT-QELLTELFIELAGAGTAILMTTHDLAQAMAtCDRVVLLN-GRVIADGTP 196
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 24-230 2.82e-15

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 74.88  E-value: 2.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  24 IHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPetveVEGHISLSGDAVCGLPMLQ--RTAA------QRPAVIFQDALQ 95
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLP----YQGSLKINGIELRELDPESwrKHLSwvgqnpQLPHGTLRDNVL 444

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLVSiEGQLSLALtgtrtklksqDKIKLTELLVQLgfPNP-ETILPLYPSQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:PRK11174  445 LGNPDAS-DEQLQQAL----------ENAWVSEFLPLL--PQGlDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDE 511

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 175 PTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:PRK11174  512 PTASLDAHSEQLVMQALNAASRRQTT--LMVTHQLEDLAQWDQIWVMQDGQIVQQG 565
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
 23-208 3.19e-15

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: 71.69  E-value: 3.19e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVC----GLpmlqRTAAQRPAVIFQDA-LQAL 97
Cdd:TIGR01166  10 GLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQ---SGAVLIDGEPLDysrkGL----LERRQRVGLVFQDPdDQLF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIE---GQLSLALTGTRTKLKSQDKIkltELLVQLGFPNPETilplypSQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:TIGR01166  83 AADVDQDvafGPLNLGLSEAEVERRVREAL---TAVGASGLRERPT------HCLSGGEKKRVAIAGAVAMRPDVLLLDE 153

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1330606456 175 PTSALDPVTEQEILKLIRdNVKQRQIGGLLITHD 208
Cdd:TIGR01166 154 PTAGLDPAGREQMLAILR-RLRAEGMTVVISTHD 186
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 11-248 3.91e-15

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: 74.60  E-value: 3.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   11 LTIKTSSRTLFQD-------IHFDVYRGELLAIMGPSGIGKSMLsraIAGFLPETVEVEGHISLSGdAVCGLPmlQRTAA 83
Cdd:TIGR00957  637 ITVHNATFTWARDlpptlngITFSIPEGALVAVVGQVGCGKSSL---LSALLAEMDKVEGHVHMKG-SVAYVP--QQAWI 710

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   84 Q----RPAVIFQDALQALNPLVSIEgqlSLALTGTRTKLKSQDKIKLTELLVQLgfpnpetilplypsqiSGGQRQRICI 159
Cdd:TIGR00957  711 QndslRENILFGKALNEKYYQQVLE---ACALLPDLEILPSGDRTEIGEKGVNL----------------SGGQKQRVSL 771

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  160 AIGLLSNADLIIADEPTSALDpvteQEILKLIRDNV---------KQRqiggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:TIGR00957  772 ARAVYSNADIYLFDDPLSAVD----AHVGKHIFEHVigpegvlknKTR----ILVTHGISYLPQVDVIIVMSGGKISEMG 843

                          250
                   ....*....|....*...
gi 1330606456  231 aPKHALESSSHAFCCSLR 248
Cdd:TIGR00957  844 -SYQELLQRDGAFAEFLR 860
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 6-193 4.49e-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: 70.65  E-value: 4.49e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKT-SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDavCGLPMLqrtaAQ 84
Cdd:cd03223     1 IELENLSLATpDGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWG---SGRIGMPEG--EDLLFL----PQ 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVifqdalqalnPLVSIEGQLslaltgtrtklksqdkikltellvqlgfpnpetilpLYPSQ--ISGGQRQRICIAIG 162
Cdd:cd03223    72 RPYL----------PLGTLREQL------------------------------------IYPWDdvLSGGEQQRLAFARL 105

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1330606456 163 LLSNADLIIADEPTSALDPVTEQEILKLIRD 193
Cdd:cd03223   106 LLHKPKFVFLDEATSALDEESEDRLYQLLKE 136
NHLM_micro_ABC1 TIGR03796
NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...
 147-230 5.23e-15

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


Pssm-ID: 274788 [Multi-domain]  Cd Length: 710  Bit Score: 74.21  E-value: 5.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 147 SQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILklirDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGV 226
Cdd:TIGR03796 614 ANLSGGQRQRLEIARALVRNPSILILDEATSALDPETEKIID----DNLRRRGCTCIIVAHRLSTIRDCDEIIVLERGKV 689


                  ....
gi 1330606456 227 VAYG 230
Cdd:TIGR03796 690 VQRG 693
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 19-223 7.84e-15

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 71.35  E-value: 7.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  19 TLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTA--AQRPAVIFQDAL-- 94
Cdd:PRK10584   24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGS---SGEVSLVGQPLHQMDEEARAKlrAKHVGFVFQSFMli 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 QALNPLVSIegQLSLALTGTRTKlksQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:PRK10584  101 PTLNALENV--ELPALLRGESSR---QSRNGAKALLEQLGL---GKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADE 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1330606456 175 PTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLL-VIDG 223
Cdd:PRK10584  173 PTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLrLVNG 222
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 18-227 8.66e-15

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 71.14  E-value: 8.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvEVEGHISLSGDAVcglpmlqrtaAQRPAVIfqDALqal 97
Cdd:COG2401    43 RYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGT-PVAGCVDVPDNQF----------GREASLI--DAI--- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 nplvsiegqlslaltgtrtkLKSQDKIKLTELLVQLGFPNPetilPLY---PSQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:COG2401   107 --------------------GRKGDFKDAVELLNAVGLSDA----VLWlrrFKELSTGQKFRFRLALLLAERPKLLVIDE 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 175 PTSALDPVTEQEILKLIRDNVKQRQIGGLLITH--DLHSALACDKLLVIDGGGVV 227
Cdd:COG2401   163 FCSHLDRQTAKRVARNLQKLARRAGITLVVATHhyDVIDDLQPDLLIFVGYGGVP 217
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 6-230 9.15e-15

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 72.06  E-value: 9.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDavcglPMLQRTAAQ- 84
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPD---SGEVLWDGE-----PLDPEDRRRi 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 ------RpavifqdalqALNPLVSIEGQLS-LA-LTGTRtklKSQDKIKLTELLVQLGfpnpetiLPLYP----SQISGG 152
Cdd:COG4152    74 gylpeeR----------GLYPKMKVGEQLVyLArLKGLS---KAEAKRRADEWLERLG-------LGDRAnkkvEELSKG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnvkQRQIGGLLI--THDLHSA--LaCDKLLVIDGGGVVA 228
Cdd:COG4152   134 NQQKVQLIAALLHDPELLILDEPFSGLDPVNVELLKDVIRE---LAAKGTTVIfsSHQMELVeeL-CDRIVIINKGRKVL 209


                  ..
gi 1330606456 229 YG 230
Cdd:COG4152   210 SG 211
hmuV PRK13547
heme ABC transporter ATP-binding protein;
5-244 9.85e-15

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 71.78  E-value: 9.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET-----VEVEGHISLSGDAVCGLPMLQ 79
Cdd:PRK13547    1 MLTADHLHVARRHRAILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgARVTGDVTLNGEPLAAIDAPR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 rtAAQRPAVIFQDALQAL----NPLVSIeGQLSLALTGTRTKLKSQDKIKLTellvqLGFPNPETILPLYPSQISGGQRQ 155
Cdd:PRK13547   81 --LARLRAVLPQAAQPAFafsaREIVLL-GRYPHARRAGALTHRDGEIAWQA-----LALAGATALVGRDVTTLSGGELA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 156 RICIAIGL---------LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDGGG 225
Cdd:PRK13547  153 RVQFARVLaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAMLADGA 232

                         250
                  ....*....|....*....
gi 1330606456 226 VVAYGAPKHALESSSHAFC 244
Cdd:PRK13547  233 IVAHGAPADVLTPAHIARC 251
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 22-233 1.37e-14

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 72.75  E-value: 1.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PE--TVEVEG---HISLSGDAV-CGLPMlqrtaaqrpavIFQ--- 91
Cdd:COG3845    22 DDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYqPDsgEILIDGkpvRIRSPRDAIaLGIGM-----------VHQhfm 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  92 --DALQAL-NplvsiegqLSLALTGTRTKLKSQDKI--KLTELLVQLGFP-NPETILplypSQISGGQRQRICIAIGLLS 165
Cdd:COG3845    91 lvPNLTVAeN--------IVLGLEPTKGGRLDRKAAraRIRELSERYGLDvDPDAKV----EDLSVGEQQRVEILKALYR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 166 NADLIIADEPTSALDPvteQEILKLIR--DNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPK 233
Cdd:COG3845   159 GARILILDEPTAVLTP---QEADELFEilRRLAAEGKSIIFITHKLREVMAiADRVTVLRRGKVVGTVDTA 226
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 6-207 1.59e-14

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 69.83  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglpmlqrtAAQR 85
Cdd:cd03231     1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPL---AGRVLLNGGPL---------DFQR 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PavIFQDALQALNPLVSIEGQLSlALTGTRTKLKSQDKIKLTELLVQLGFPNPETILplyPSQISGGQRQRICIAIGLLS 165
Cdd:cd03231    69 D--SIARGLLYLGHAPGIKTTLS-VLENLRFWHADHSDEQVEEALARVGLNGFEDRP---VAQLSAGQQRRVALARLLLS 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIRDNVKQrqiGG--LLITH 207
Cdd:cd03231   143 GRPLWILDEPTTALDKAGVARFAEAMAGHCAR---GGmvVLTTH 183
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 4-230 1.71e-14

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 70.84  E-value: 1.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRA-------IAGflpetVEVEGHISLSG----DAV 72
Cdd:COG1117    10 PKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRClnrmndlIPG-----ARVEGEILLDGediyDPD 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  73 CGLPMLQRtaaqRPAVIFQDAlqalNPL-VSIE-----GqlsLALTGTRTK----------LKS-------QDKIKltel 129
Cdd:COG1117    85 VDVVELRR----RVGMVFQKP----NPFpKSIYdnvayG---LRLHGIKSKseldeiveesLRKaalwdevKDRLK---- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 130 lvQLGFpnpetilplypsQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDL 209
Cdd:COG1117   150 --KSAL------------GLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDYTI--VIVTHNM 213

                         250       260
                  ....*....|....*....|..
gi 1330606456 210 HSALAC-DKLLVIDGGGVVAYG 230
Cdd:COG1117   214 QQAARVsDYTAFFYLGELVEFG 235
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 16-226 2.14e-14

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: 70.19  E-value: 2.14e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAV-----CGLPMLQRTAAQRPaVIF 90
Cdd:cd03248    25 PDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQ---GGQVLLDGKPIsqyehKYLHSKVSLVGQEP-VLF 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  91 QDALQAlNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELlvqlgfpNPETILPLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:cd03248   101 ARSLQD-NIAYGLQSCSFECVKEAAQKAHAHSFISELAS-------GYDTEVGEKGSQLSGGQKQRVAIARALIRNPQVL 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGV 226
Cdd:cd03248   173 ILDEATSALDAESEQQVQQALYDWPERRTV--LVIAHRLSTVERADQILVLDGGRI 226
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 21-230 2.37e-14

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: 70.26  E-value: 2.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKS----MLSRAiagFLPEtvevEGHISLSGDAVCGLpmlqrtaaqrpavifqdALQA 96
Cdd:cd03249    19 LKGLSLTIPPGKTVALVGSSGCGKStvvsLLERF---YDPT----SGEILLDGVDIRDL-----------------NLRW 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIEGQLSLALTGT-----------RTKLKSQDKIKLTELL-VQLGFPNP-ETILPLYPSQISGGQRQRICIAIGL 163
Cdd:cd03249    75 LRSQIGLVSQEPVLFDGTiaenirygkpdATDEEVEEAAKKANIHdFIMSLPDGyDTLVGERGSQLSGGQKQRIAIARAL 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:cd03249   155 LRNPKILLLDEATSALDAESEKLVQEALDRAMKGRTT--IVIAHRLSTIRNADLIAVLQNGQVVEQG 219
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 4-248 2.66e-14

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: 70.11  E-value: 2.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLP----ETVEVEG-------------HIs 66
Cdd:COG1119     2 PLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPptygNDVRLFGerrggedvwelrkRI- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  67 lsgdavcGL--PMLQRTaaqrpaviFQDALQALNPLVSiegqlslALTGT---RTKLKSQDKIKLTELLVQLGfpnpetI 141
Cdd:COG1119    81 -------GLvsPALQLR--------FPRDETVLDVVLS-------GFFDSiglYREPTDEQRERARELLELLG------L 132

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 142 LPL---YPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALAC-DK 217
Cdd:COG1119   133 AHLadrPFGTLSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGiTH 212

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1330606456 218 LLVIDGGGVVAYGAPKHAL--ESSSHAFCCSLR 248
Cdd:COG1119   213 VLLLKDGRVVAAGPKEEVLtsENLSEAFGLPVE 245
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 6-241 3.29e-14

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 71.87  E-value: 3.29e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456    6 LSVDQLTIKTSS--RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLpetvEVEGHISLSG---DAVcglpmlqr 80
Cdd:TIGR01271 1218 MDVQGLTAKYTEagRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLL----STEGEIQIDGvswNSV-------- 1285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   81 taaqrpavifqdALQALNPLVSIEGQLSLALTGT-RTKL------------KSQDKIKLTELLVQlgFPNP-ETILPLYP 146
Cdd:TIGR01271 1286 ------------TLQTWRKAFGVIPQKVFIFSGTfRKNLdpyeqwsdeeiwKVAEEVGLKSVIEQ--FPDKlDFVLVDGG 1351

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  147 SQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGV 226
Cdd:TIGR01271 1352 YVLSNGHKQLMCLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFSNCTV--ILSEHRVEALLECQQFLVIEGSSV 1429

                          250
                   ....*....|....*
gi 1330606456  227 VAYGAPKHALESSSH 241
Cdd:TIGR01271 1430 KQYDSIQKLLNETSL 1444
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
7-238 6.12e-14

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 69.43  E-value: 6.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGL--PMLQRTAAQ 84
Cdd:PRK10575   13 ALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPS---EGEILLDAQPLESWssKAFARKVAY 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDALQALNPLVSIeGQLSLAltGTRTKLKSQDKIKLTELLVQLGF-PNPETILplypSQISGGQRQRICIAIGL 163
Cdd:PRK10575   90 LPQQLPAAEGMTVRELVAI-GRYPWH--GALGRFGAADREKVEEAISLVGLkPLAHRLV----DSLSGGERQRAWIAMLV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH-SALACDKLLVIDGGGVVAYGAPKHALES 238
Cdd:PRK10575  163 AQDSRCLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINmAARYCDYLVALRGGEMIAQGTPAELMRG 238
PLN03211 PLN03211
ABC transporter G-25; Provisional
 12-180 6.15e-14

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 71.06  E-value: 6.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  12 TIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpetvEVEGHiSLSGDAVCGLPMLQRTAAQRPAVIFQ 91
Cdd:PLN03211   75 TRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAG------RIQGN-NFTGTILANNRKPTKQILKRTGFVTQ 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  92 DALqaLNPLVSIEGQLSL-ALTGTRTKLKSQDKIKLTE-LLVQLGFPNPE-TIL-PLYPSQISGGQRQRICIAIGLLSNA 167
Cdd:PLN03211  148 DDI--LYPHLTVRETLVFcSLLRLPKSLTKQEKILVAEsVISELGLTKCEnTIIgNSFIRGISGGERKRVSIAHEMLINP 225

                         170
                  ....*....|...
gi 1330606456 168 DLIIADEPTSALD 180
Cdd:PLN03211  226 SLLILDEPTSGLD 238
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 14-230 6.18e-14

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


Pssm-ID: 213200 [Multi-domain]  Cd Length: 202  Bit Score: 68.44  E-value: 6.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  14 KTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEVEGHISLsgdavCGLPMLQRTAAQRPAVIFQda 93
Cdd:cd03233    16 GRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVSVEGDIHY-----NGIPYKEFAEKYPGEIIYV-- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 lqalnplvsiegqlslaltgtrtklkSQDKIKLTELLVQlgfpnpETI---LPL----YPSQISGGQRQRICIAIGLLSN 166
Cdd:cd03233    89 --------------------------SEEDVHFPTLTVR------ETLdfaLRCkgneFVRGISGGERKRVSIAEALVSR 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 167 ADLIIADEPTSALDPVTEQEILKLIRdnvkqrqigglLITHDLH-----SALAC--------DKLLVIDGGGVVAYG 230
Cdd:cd03233   137 ASVLCWDNSTRGLDSSTALEILKCIR-----------TMADVLKtttfvSLYQAsdeiydlfDKVLVLYEGRQIYYG 202
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 16-237 8.32e-14

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 70.52  E-value: 8.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGdavcglpmlqrtaaqRPAVIFQDalQ 95
Cdd:TIGR00958 492 PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPT---GGQVLLDG---------------VPLVQYDH--H 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 ALNPLVSIEGQLSLALTGTRTK-----LKSQDKIKLTELLVQ-------LGFPNP-ETILPLYPSQISGGQRQRICIAIG 162
Cdd:TIGR00958 552 YLHRQVALVGQEPVLFSGSVREniaygLTDTPDEEIMAAAKAanahdfiMEFPNGyDTEVGEKGSQLSGGQKQRIAIARA 631

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 163 LLSNADLIIADEPTSALDPVTEQeilkLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALE 237
Cdd:TIGR00958 632 LVRKPRVLILDEATSALDAECEQ----LLQESRSRASRTVLLIAHRLSTVERADQILVLKKGSVVEMGTHKQLME 702
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 3-235 8.64e-14

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 69.35  E-value: 8.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpeTVEVEGHiSLSGDAVCG-------- 74
Cdd:PRK14271   19 APAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRM---NDKVSGY-RYSGDVLLGgrsifnyr 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  75 --LPMLQRTAA--QRPAVIFQDALQalNPLVSIEGQLSLAltgtRTKLKSQDKIKLTELLVqlgFPNPETILPLYPSQIS 150
Cdd:PRK14271   95 dvLEFRRRVGMlfQRPNPFPMSIMD--NVLAGVRAHKLVP----RKEFRGVAQARLTEVGL---WDAVKDRLSDSPFRLS 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDL--------HSALACDKLLVID 222
Cdd:PRK14271  166 GGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRLTV--IIVTHNLaqaarisdRAALFFDGRLVEE 243

                         250
                  ....*....|...
gi 1330606456 223 GGGVVAYGAPKHA 235
Cdd:PRK14271  244 GPTEQLFSSPKHA 256
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-230 9.44e-14

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 70.20  E-value: 9.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQR 80
Cdd:PRK09700    1 MATPYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPT---KGTITINNINYNKLD--HK 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVIFQDALQALNPLvSIEGQLSLALTGTRTKLK------SQDKIKLTELLVQLGFP-NPETILplypSQISGGQ 153
Cdd:PRK09700   76 LAAQLGIGIIYQELSVIDEL-TVLENLYIGRHLTKKVCGvniidwREMRVRAAMMLLRVGLKvDLDEKV----ANLSISH 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALdpvTEQEI--LKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:PRK09700  151 KQMLEIAKTLMLDAKVIIMDEPTSSL---TNKEVdyLFLIMNQLRKEGTAIVYISHKLAEIRRiCDRYTVMKDGSSVCSG 227
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 6-232 9.68e-14

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: 70.22  E-value: 9.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLS---RAIAGFLPETVEVEGHISLSGD------------ 70
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMhvlRGMDQYEPTSGRIIYHVALCEKcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  71 --AVCGLPM-------------LQRTAAQRPAVIFQDALQALNPLVSIEGQL-SLALTGTRTKLKSQDKIKLTELlVQLG 134
Cdd:TIGR03269  81 pcPVCGGTLepeevdfwnlsdkLRRRIRKRIAIMLQRTFALYGDDTVLDNVLeALEEIGYEGKEAVGRAVDLIEM-VQLS 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 135 fpnpETILPLyPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITH--DLHSA 212
Cdd:TIGR03269 160 ----HRITHI-ARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHwpEVIED 234

                         250       260
                  ....*....|....*....|
gi 1330606456 213 LAcDKLLVIDGGGVVAYGAP 232
Cdd:TIGR03269 235 LS-DKAIWLENGEIKEEGTP 253
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
22-237 1.29e-13

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 70.05  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSmlsrAIAGFLPETVEV-EGHISLSGDAV--CGLPMLQRTAA--QRPAVIFQDalqa 96
Cdd:PRK11176  360 RNINFKIPAGKTVALVGRSGSGKS----TIANLLTRFYDIdEGEILLDGHDLrdYTLASLRNQVAlvSQNVHLFND---- 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 lnplvSIEGQLSLALTGTRTKlksQDKIKLTELLVQLGFPNP-----ETILPLYPSQISGGQRQRICIAIGLLSNADLII 171
Cdd:PRK11176  432 -----TIANNIAYARTEQYSR---EQIEEAARMAYAMDFINKmdnglDTVIGENGVLLSGGQRQRIAIARALLRDSPILI 503

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 172 ADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALE 237
Cdd:PRK11176  504 LDEATSALDTESERAIQAALDELQKNRTS--LVIAHRLSTIEKADEILVVEDGEIVERGTHAELLA 567
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
28-223 1.49e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 69.84  E-value: 1.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  28 VYRGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEGHISLSgdavcglpmlqrtaaQRPAVIFQDalqalnplvsIEGQ 106
Cdd:PRK13409  362 IYEGEVIGIVGPNGIGKTTFAKLLAGVLkPDEGEVDPELKIS---------------YKPQYIKPD----------YDGT 416

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 107 LSLALTGTRTKLKSqdKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDpvTEQE 186
Cdd:PRK13409  417 VEDLLRSITDDLGS--SYYKSEIIKPLQL---ERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLD--VEQR 489

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1330606456 187 IL--KLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDG 223
Cdd:PRK13409  490 LAvaKAIRRIAEEREATALVVDHDIYMiDYISDRLMVFEG 529
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 21-233 1.56e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 68.34  E-value: 1.56e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtveVEGHISLSGDAV----CGLPMLQRTAAqrpaVIFQDALQA 96
Cdd:PRK13636   22 LKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKP---SSGRILFDGKPIdysrKGLMKLRESVG----MVFQDPDNQ 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIE----GQLSLALTGTRTKLKSQDKIKLTellvqlgfpnpeTILPLY--PSQ-ISGGQRQRICIAIGLLSNADL 169
Cdd:PRK13636   95 LFSASVYQdvsfGAVNLKLPEDEVRKRVDNALKRT------------GIEHLKdkPTHcLSFGQKKRVAIAGVLVMEPKV 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 170 IIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13636  163 LVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIvPLYCDNVFVMKEGRVILQGNPK 227
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 16-243 2.09e-13

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 67.73  E-value: 2.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFqDIHFDVYRGELLAIMGPSGIGKSMLSRAIAgfLPEtVEVEGHISLSGDAvcgLPMLQRTAAQRPAVIFQDA-- 93
Cdd:PRK11124   14 AHQALF-DITLDCPQGETLVLLGPSGAGKSSLLRVLN--LLE-MPRSGTLNIAGNH---FDFSKTPSDKAIRELRRNVgm 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  94 -LQALN--PLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:PRK11124   87 vFQQYNlwPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRL---KPYADRFPLHLSGGQQQRVAIARALMMEPQVL 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSAL-ACDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:PRK11124  164 LFDEPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVEVARkTASRVVYMENGHIVEQGDASCFTQPQTEAF 236
cbiO PRK13637
energy-coupling factor transporter ATPase;
23-233 2.40e-13

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 68.15  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRTAAQRPAVIFQ-DALQALNPLV 101
Cdd:PRK13637   25 NVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPT---SGKIIIDGVDITDKKVKLSDIRKKVGLVFQyPEYQLFEETI 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 --SIE-GQLSLALTGTRTKlksqDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:PRK13637  102 ekDIAfGPINLGLSEEEIE----NRVKRAMNIVGLDY---EDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAG 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 179 LDPVTEQEILKLIRDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13637  175 LDPKGRDEILNKIKELHKEYNMTIILVSHSMEDvAKLADRIIVMNKGKCELQGTPR 230
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
 22-240 2.50e-13

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: 69.00  E-value: 2.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF-LPE--TVEVEGHISLSGDAVcglpMLQRTAAqrpaVIFQDAL---- 94
Cdd:TIGR01846 474 SNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLyTPQhgQVLVDGVDLAIADPA----WLRRQMG----VVLQENVlfsr 545

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 ------QALNPLVSIEGQLSLA-LTGTRTKLKSQDKikltellvqlGFpnpETILPLYPSQISGGQRQRICIAIGLLSNA 167
Cdd:TIGR01846 546 sirdniALCNPGAPFEHVIHAAkLAGAHDFISELPQ----------GY---NTEVGEKGANLSGGQRQRIAIARALVGNP 612

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 168 DLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSS 240
Cdd:TIGR01846 613 RILIFDEATSALDYESEALIMRNMREICRGRTV--IIIAHRLSTVRACDRIIVLEKGQIAESGRHEELLALQG 683
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 18-234 2.77e-13

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 67.74  E-value: 2.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFqDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLsGDAVCglpmlqrTAAQRpavifQDALQAL 97
Cdd:PRK13634   21 RALY-DVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPT---SGTVTI-GERVI-------TAGKK-----NKKLKPL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSI-----EGQL--------------SLALTGTRTKLKSQDKIKLTELlvqlgfpnPETILPLYPSQISGGQRQRIC 158
Cdd:PRK13634   84 RKKVGIvfqfpEHQLfeetvekdicfgpmNFGVSEEDAKQKAREMIELVGL--------PEELLARSPFELSGGQMRRVA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKH 234
Cdd:PRK13634  156 IAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVMHKGTVFLQGTPRE 232
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 22-235 2.89e-13

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


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 68.74  E-value: 2.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlqrtaaqrPAVIFQDalqalnplV 101
Cdd:TIGR03375 482 DNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPT---EGSVLLDGVDIRQID---------PADLRRN--------I 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSLALTGTrtkLKsqDKIKL-------TELLVQLGFPNPETILPLYPS----QI-------SGGQRQRICIAIGL 163
Cdd:TIGR03375 542 GYVPQDPRLFYGT---LR--DNIALgapyaddEEILRAAELAGVTEFVRRHPDgldmQIgergrslSGGQRQAVALARAL 616

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 164 LSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLhSALA-CDKLLVIDGGGVVAYGaPKHA 235
Cdd:TIGR03375 617 LRDPPILLLDEPTSAMDNRSEERFKDRLKRWLAGKTL--VLVTHRT-SLLDlVDRIIVMDNGRIVADG-PKDQ 685
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 5-238 2.95e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 67.38  E-value: 2.95e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLP---ETVEVEGHISLSGDAVCGLPMLQrt 81
Cdd:PRK14246   10 VFNISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEiydSKIKVDGKVLYFGKDIFQIDAIK-- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAQRPAVIFQDAlqalNPL--VSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLG-FPNPETILPLYPSQISGGQRQRIC 158
Cdd:PRK14246   88 LRKEVGMVFQQP----NPFphLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGlWKEVYDRLNSPASQLSGGQQQRLT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 159 IAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHD-LHSALACDKLLVIDGGGVVAYGAPKHALE 237
Cdd:PRK14246  164 IARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAI--VIVSHNpQQVARVADYVAFLYNGELVEWGSSNEIFT 241


                  .
gi 1330606456 238 S 238
Cdd:PRK14246  242 S 242
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 6-237 2.96e-13

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 67.01  E-value: 2.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVeVEGHISLSGDAVCGLPMLQRTAA-- 83
Cdd:COG0396     1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKYEV-TSGSILLDGEDILELSPDERARAgi 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 ----QRPAVIfqdalqalnPLVSIEGQLSLALTGTRTKLKS--QDKIKLTELLVQLGFPnpetilplyPSQI-------- 149
Cdd:COG0396    80 flafQYPVEI---------PGVSVSNFLRTALNARRGEELSarEFLKLLKEKMKELGLD---------EDFLdryvnegf 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDpvteqeI--LKLIRDNVKQ---RQIGGLLITH-----DLhsaLACDKLL 219
Cdd:COG0396   142 SGGEKKRNEILQMLLLEPKLAILDETDSGLD------IdaLRIVAEGVNKlrsPDRGILIITHyqrilDY---IKPDFVH 212

                         250
                  ....*....|....*...
gi 1330606456 220 VIDGGGVVAYGAPKHALE 237
Cdd:COG0396   213 VLVDGRIVKSGGKELALE 230
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 4-229 4.40e-13

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 68.17  E-value: 4.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLsGDAVcglpmlqRTA- 82
Cdd:COG0488   314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPD---SGTVKL-GETV-------KIGy 382

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 -AQRpavifQDALQA-LNPLVSIEgqlSLALTGTRTKLKSqdkiklteLLVQLGFPNPETILPLypSQISGGQRQRICIA 160
Cdd:COG0488   383 fDQH-----QEELDPdKTVLDELR---DGAPGGTEQEVRG--------YLGRFLFSGDDAFKPV--GVLSGGEKARLALA 444

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRD---NVkqrqiggLLITHDLH--SALaCDKLLVIDGGGVVAY 229
Cdd:COG0488   445 KLLLSPPNVLLLDEPTNHLDIETLEALEEALDDfpgTV-------LLVSHDRYflDRV-ATRILEFEDGGVREY 510
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 1-232 4.64e-13

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 66.94  E-value: 4.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMlQR 80
Cdd:PRK11300    1 MSQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPT---GGTILLRGQHIEGLPG-HQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAaqRPAVI--FQDA-----LQAL-NPLVSIEGQLSLALTGTRTKLKS---------------QDKIKLTEllvqlgFPN 137
Cdd:PRK11300   77 IA--RMGVVrtFQHVrlfreMTVIeNLLVAQHQQLKTGLFSGLLKTPAfrraesealdraatwLERVGLLE------HAN 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 138 PETilplypSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CD 216
Cdd:PRK11300  149 RQA------GNLAYGQQRRLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGiSD 222

                         250
                  ....*....|....*.
gi 1330606456 217 KLLVIDGGGVVAYGAP 232
Cdd:PRK11300  223 RIYVVNQGTPLANGTP 238
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
145-193 4.72e-13

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 66.75  E-value: 4.72e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1330606456 145 YPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRD 193
Cdd:COG4598   151 YPAHLSGGQQQRAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRD 199
PLN03232 PLN03232
ABC transporter C family member; Provisional
 26-243 6.15e-13

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 68.08  E-value: 6.15e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   26 FDVYRGELLAIMGPSGIGKSMLSRAiagfLPETVEVE-GHISLSGDAVC--GLPMLQRTAA---QRPaVIFQDALQ-ALN 98
Cdd:PLN03232  1257 FFVSPSEKVGVVGRTGAGKSSMLNA----LFRIVELEkGRIMIDDCDVAkfGLTDLRRVLSiipQSP-VLFSGTVRfNID 1331

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   99 PLvSIEGQLSLALTGTRTKLK---SQDKIKLTELLVQLGfpnpetilplypSQISGGQRQRICIAIGLLSNADLIIADEP 175
Cdd:PLN03232  1332 PF-SEHNDADLWEALERAHIKdviDRNPFGLDAEVSEGG------------ENFSVGQRQLLSLARALLRRSKILVLDEA 1398

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456  176 TSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:PLN03232  1399 TASVDVRTDSLIQRTIREEFKSCTM--LVIAHRLNTIIDCDKILVLSSGQVLEYDSPQELLSRDTSAF 1464
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
22-232 7.26e-13

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 67.18  E-value: 7.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETVEvEGHISLSGDAVCGL-PmlqrtaAQRP-AVIFQDalQALNP 99
Cdd:PRK11650   21 KGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGL--ERIT-SGEIWIGGRVVNELeP------ADRDiAMVFQN--YALYP 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 LVSIEGQLSLALtgtrtklksqdKIKltellvqlGFPNPE---------TILPL------YPSQISGGQRQRICIAIGLL 164
Cdd:PRK11650   90 HMSVRENMAYGL-----------KIR--------GMPKAEieervaeaaRILELeplldrKPRELSGGQRQRVAMGRAIV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 165 SNADLIIADEPTSALDP---VteQ---EILKLirdnvkQRQIG--GLLITHDLHSA--LAcDKLLVIDGGGVVAYGAP 232
Cdd:PRK11650  151 REPAVFLFDEPLSNLDAklrV--QmrlEIQRL------HRRLKttSLYVTHDQVEAmtLA-DRVVVMNGGVAEQIGTP 219
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 5-212 7.67e-13

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 66.34  E-value: 7.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF--LPETVEVEGHISLSGDAVCGLPMLQRTA 82
Cdd:PRK14243   10 VLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGFRVEGKVTFHGKNLYAPDVDPVEV 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 AQRPAVIFQDAlqalNPL-VSIEGQLSLaltGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPS--QISGGQRQRICI 159
Cdd:PRK14243   90 RRRIGMVFQKP----NPFpKSIYDNIAY---GARINGYKGDMDELVERSLRQAALWDEVKDKLKQSglSLSGGQQQRLCI 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSA 212
Cdd:PRK14243  163 ARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTI--IIVTHNMQQA 213
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
 6-243 8.83e-13

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: 65.74  E-value: 8.83e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflPETVEV-EGHISLSGDAVCGLPMLQRTAA- 83
Cdd:TIGR01978   1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG--HPSYEVtSGTILFKGQDLLELEPDERARAg 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 -----QRPAVIfqdalqalnPLVSIEGQLSLALTgTRTKLKSQDKIK-------LTELLVQLGFPnpetilPLYPSQ--- 148
Cdd:TIGR01978  79 lflafQYPEEI---------PGVSNLEFLRSALN-ARRSARGEEPLDlldfeklLKEKLALLDMD------EEFLNRsvn 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 149 --ISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIrDNVKQRQIGGLLITH--DLHSALACDKLLVIDGG 224
Cdd:TIGR01978 143 egFSGGEKKRNEILQMALLEPKLAILDEIDSGLDIDALKIVAEGI-NRLREPDRSFLIITHyqRLLNYIKPDYVHVLLDG 221

                         250
                  ....*....|....*....
gi 1330606456 225 GVVAYGAPKHALESSSHAF 243
Cdd:TIGR01978 222 RIVKSGDVELAKELEAKGY 240
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
5-207 1.23e-12

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 64.83  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGdavcglpmlQRTAAQ 84
Cdd:PRK13538    1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPD---AGEVLWQG---------EPIRRQ 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAviFQDALQALNPLVSIEGQLS--------LALTGtrtklkSQDKIKLTELLVQLGFPNPETILplyPSQISGGQRQR 156
Cdd:PRK13538   69 RDE--YHQDLLYLGHQPGIKTELTalenlrfyQRLHG------PGDDEALWEALAQVGLAGFEDVP---VRQLSAGQQRR 137

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 157 ICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrqiGGLLI--TH 207
Cdd:PRK13538  138 VALARLWLTRAPLWILDEPFTAIDKQGVARLEALLAQHAEQ---GGMVIltTH 187
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
3-228 1.33e-12

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 66.58  E-value: 1.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLtiktSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGdavcglpmlQRTA 82
Cdd:COG1129   254 EVVLEVEGL----SVGGVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPAD---SGEIRLDG---------KPVR 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 AQRPAvifqDALQA-------------LNPLVSIEGQLSLALTGTRTK---LKSQDKIKLTELLV-QLG--FPNPETILp 143
Cdd:COG1129   318 IRSPR----DAIRAgiayvpedrkgegLVLDLSIRENITLASLDRLSRgglLDRRRERALAEEYIkRLRikTPSPEQPV- 392

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 144 lypSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrQIGGLLITHDLHSALA-CDKLLVID 222
Cdd:COG1129   393 ---GNLSGGNQQKVVLAKWLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGlSDRILVMR 468


                  ....*.
gi 1330606456 223 GGGVVA 228
Cdd:COG1129   469 EGRIVG 474
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
 6-192 1.94e-12

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


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 64.73  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDavcglPMLQRTAAQR 85
Cdd:TIGR03740   1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPT---SGEIIFDGH-----PWTRKDLHKI 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQDALqaLNPLVSIEGQLslaltgTRTKLKSQDKIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLLS 165
Cdd:TIGR03740  73 GSLIESPPL--YENLTARENLK------VHTTLLGLPDSRIDEVLNIVDLTNTGK---KKAKQFSLGMKQRLGIAIALLN 141

                         170       180
                  ....*....|....*....|....*..
gi 1330606456 166 NADLIIADEPTSALDPVTEQEILKLIR 192
Cdd:TIGR03740 142 HPKLLILDEPTNGLDPIGIQELRELIR 168
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 6-241 3.08e-12

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


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 64.88  E-value: 3.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIK--TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAiagFLpETVEVEGHISLSGDAVCGLPMLQRTAA 83
Cdd:cd03289     3 MTVKDLTAKytEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSA---FL-RLLNTEGDIQIDGVSWNSVPLQKWRKA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 ----QRPAVIFQDAL-QALNPLvsieGQLSlaltgTRTKLKSQDKIKLTELLVQlgFPNPETILPLYPSQI-SGGQRQRI 157
Cdd:cd03289    79 fgviPQKVFIFSGTFrKNLDPY----GKWS-----DEEIWKVAEEVGLKSVIEQ--FPGQLDFVLVDGGCVlSHGHKQLM 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 158 CIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALE 237
Cdd:cd03289   148 CLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFADCTV--ILSEHRIEAMLECQRFLVIEENKVRQYDSIQKLLN 225


                  ....
gi 1330606456 238 SSSH 241
Cdd:cd03289   226 EKSH 229
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 1-207 3.18e-12

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 64.28  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVeVEGHISLSGDAVCGLPMLQR 80
Cdd:CHL00131    3 KNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAYKI-LEGDILFKGESILDLEPEER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 T------AAQRPAVIfqdalqalnPLVSIEGQLSLALtgtRTKLKSQDKIKLtELLVQLGFPNPE-TILPLYPSQI---- 149
Cdd:CHL00131   82 AhlgiflAFQYPIEI---------PGVSNADFLRLAY---NSKRKFQGLPEL-DPLEFLEIINEKlKLVGMDPSFLsrnv 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 150 ----SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIrDNVKQRQIGGLLITH 207
Cdd:CHL00131  149 negfSGGEKKRNEILQMALLDSELAILDETDSGLDIDALKIIAEGI-NKLMTSENSIILITH 209
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 20-231 3.35e-12

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 66.09  E-value: 3.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   20 LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLSGDavcgLPMLQRTAAQRPAVIFQDALQALN- 98
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMG---ELEPSEGKIKHSGR----ISFSPQTSWIMPGTIKDNIIFGLSy 513

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   99 -----PLVSIEGQLSLALTgtrtKLKSQDKIKLTELLVQLgfpnpetilplypsqiSGGQRQRICIAIGLLSNADLIIAD 173
Cdd:TIGR01271  514 deyryTSVIKACQLEEDIA----LFPEKDKTVLGEGGITL----------------SGGQRARISLARAVYKDADLYLLD 573

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456  174 EPTSALDPVTEQEIL-----KLIRDNVKqrqiggLLITHDLHSALACDKLLVIDGGGVVAYGA 231
Cdd:TIGR01271  574 SPFTHLDVVTEKEIFesclcKLMSNKTR------ILVTSKLEHLKKADKILLLHEGVCYFYGT 630
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 5-228 3.79e-12

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 65.62  E-value: 3.79e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvEVEGHISLSGDAVCGlPMLQRTAAQ 84
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHG-TWDGEIYWSGSPLKA-SNIRDTERA 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDAlqALNPLVSIEGQL----SLALTGTRTKLKSQdKIKLTELLVQLGFPNPETILPLypSQISGGQRQRICIA 160
Cdd:TIGR02633  79 GIVIIHQEL--TLVPELSVAENIflgnEITLPGGRMAYNAM-YLRAKNLLRELQLDADNVTRPV--GDYGGGQQQLVEIA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 161 IGLLSNADLIIADEPTSALdpvTEQEI---LKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVA 228
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSL---TEKETeilLDIIRD-LKAHGVACVYISHKLNEVKAvCDTICVIRDGQHVA 221
cbiO PRK13644
energy-coupling factor transporter ATPase;
21-240 5.49e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 63.85  E-value: 5.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PEtvevEGHISLSGDAVCGLPMLQRTAaQRPAVIFQdalqalNP 99
Cdd:PRK13644   18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLrPQ----KGKVLVSGIDTGDFSKLQGIR-KLVGIVFQ------NP 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 100 LVSIEGQL---SLALTGTRTKLKSQDKIKLTELLVQlgfpnpETILPLY----PSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:PRK13644   87 ETQFVGRTveeDLAFGPENLCLPPIEIRKRVDRALA------EIGLEKYrhrsPKTLSGGQGQCVALAGILTMEPECLIF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 173 DEPTSALDPVTEQEILKLIRD-NVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSS 240
Cdd:PRK13644  161 DEVTSMLDPDSGIAVLERIKKlHEKGKTI--VYITHNLEELHDADRIIVMDRGKIVLEGEPENVLSDVS 227
cbiO PRK13643
energy-coupling factor transporter ATPase;
16-237 8.15e-12

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 63.60  E-value: 8.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  16 SSRTLFqDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLsGDAVCGLPMLQRT---AAQRPAVIFQD 92
Cdd:PRK13643   18 ASRALF-DIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPT---EGKVTV-GDIVVSSTSKQKEikpVRKKVGVVFQF 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALQALNPLVSIE----GQLSLALTGTRTKLKSQDKIKLTELlvqlgfpnPETILPLYPSQISGGQRQRICIAIGLLSNAD 168
Cdd:PRK13643   93 PESQLFEETVLKdvafGPQNFGIPKEKAEKIAAEKLEMVGL--------ADEFWEKSPFELSGGQMRRVAIAGILAMEPE 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 169 LIIADEPTSALDPVTEQEILKLIrDNVKQRQIGGLLITHDLHS-ALACDKLLVIDGGGVVAYGAPKHALE 237
Cdd:PRK13643  165 VLVLDEPTAGLDPKARIEMMQLF-ESIHQSGQTVVLVTHLMDDvADYADYVYLLEKGHIISCGTPSDVFQ 233
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 15-233 8.97e-12

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 63.28  E-value: 8.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  15 TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMlqRTAAQRPAVIFQDAL 94
Cdd:PRK13652   14 SGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPT---SGSVLIRGEPITKENI--REVRKFVGLVFQNPD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 -QALNPLVSIE---GQLSLALTGTRTKLKSQDKIKLTELlvqlgfpnpETILPLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:PRK13652   89 dQIFSPTVEQDiafGPINLGLDEETVAHRVSSALHMLGL---------EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITH--DLHSALAcDKLLVIDGGGVVAYGAPK 233
Cdd:PRK13652  160 VLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHqlDLVPEMA-DYIYVMDKGRIVAYGTVE 223
PLN03130 PLN03130
ABC transporter C family member; Provisional
 150-243 1.07e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 64.37  E-value: 1.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAY 229
Cdd:PLN03130  1376 SVGQRQLLSLARALLRRSKILVLDEATAAVDVRTDALIQKTIREEFKSCTM--LIIAHRLNTIIDCDRILVLDAGRVVEF 1453

                           90
                   ....*....|....
gi 1330606456  230 GAPKHALESSSHAF 243
Cdd:PLN03130  1454 DTPENLLSNEGSAF 1467
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 26-233 2.16e-11

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 61.87  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  26 FDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtvevEGHISLSGDAVCGLPmlQRTAAQRPAVIFQDALQALNPLVSIEG 105
Cdd:PRK03695   17 AEVRAGEILHLVGPNGAGKSTLLARMAGLLPG----SGSIQFAGQPLEAWS--AAELARHRAYLSQQQTPPFAMPVFQYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 106 QLSLAlTGTRTklkSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLL-------SNADLIIADEPTSA 178
Cdd:PRK03695   91 TLHQP-DKTRT---EAVASALNEVAEALGL---DDKLGRSVNQLSGGEWQRVRLAAVVLqvwpdinPAGQLLLLDEPMNS 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 179 LDpVTEQEILKLIRDNVKQRQIGGLLITHDL-HSALACDKLLVIDGGGVVAYGAPK 233
Cdd:PRK03695  164 LD-VAQQAALDRLLSELCQQGIAVVMSSHDLnHTLRHADRVWLLKQGKLLASGRRD 218
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
1-230 2.54e-11

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 62.21  E-value: 2.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIK-TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISlsgdaVCGLPMLQ 79
Cdd:PRK15056    2 MQQAGIVVNDVTVTwRNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLA---SGKIS-----ILGQPTRQ 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 RTAAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKL---KSQDKIKLTELLVQLGfpnpetILPLYPSQI---SGGQ 153
Cdd:PRK15056   74 ALQKNLVAYVPQSEEVDWSFPVLVEDVVMMGRYGHMGWLrraKKRDRQIVTAALARVD------MVEFRHRQIgelSGGQ 147

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDgGGVVAYG 230
Cdd:PRK15056  148 KKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRE-LRDEGKTMLVSTHNLGSVTEfCDYTVMVK-GTVLASG 223
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 20-230 2.77e-11

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: 62.18  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  20 LFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLSGDavcgLPMLQRTAAQRPAVIFQDALQALN- 98
Cdd:cd03291    52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILG---ELEPSEGKIKHSGR----ISFSSQFSWIMPGTIKENIIFGVSy 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  99 -----PLVSIEGQLSLALTgtrtKLKSQDKIKLTELLVQLgfpnpetilplypsqiSGGQRQRICIAIGLLSNADLIIAD 173
Cdd:cd03291   125 deyryKSVVKACQLEEDIT----KFPEKDNTVLGEGGITL----------------SGGQRARISLARAVYKDADLYLLD 184

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 174 EPTSALDPVTEQEIL-----KLIRDNVKqrqiggLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:cd03291   185 SPFGYLDVFTEKEIFescvcKLMANKTR------ILVTSKMEHLKKADKILILHEGSSYFYG 240
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 33-230 2.85e-11

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: 61.05  E-value: 2.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  33 LLAIMGPSGIGKSMLSRAIAGFLPETvevEGHIslsgdAVCGLPMLQRTAAQRPAVIF--QDALqaLNPLVSIEGQL--S 108
Cdd:cd03264    27 MYGLLGPNGAGKTTLMRILATLTPPS---SGTI-----RIDGQDVLKQPQKLRRRIGYlpQEFG--VYPNFTVREFLdyI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 109 LALTGTRtklKSQDKIKLTELL--VQLGFPNPETIlplypSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQE 186
Cdd:cd03264    97 AWLKGIP---SKEVKARVDEVLelVNLGDRAKKKI-----GSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPEERIR 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1330606456 187 ILKLIRDNVKQRQIggLLITHDLHS-ALACDKLLVIDGGGVVAYG 230
Cdd:cd03264   169 FRNLLSELGEDRIV--ILSTHIVEDvESLCNQVAVLNKGKLVFEG 211
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 1-223 2.93e-11

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 62.64  E-value: 2.93e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvEVEGHISLSGDavcglPMLQR 80
Cdd:PRK13549    1 MMEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHG-TYEGEIIFEGE-----ELQAS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 ----TAAQRPAVIFQDAlqALNPLVSIEGQLSLALTGTRTKLKSQDKIKL--TELLVQLGFP-NPETILplypSQISGGQ 153
Cdd:PRK13549   75 nirdTERAGIAIIHQEL--ALVKELSVLENIFLGNEITPGGIMDYDAMYLraQKLLAQLKLDiNPATPV----GNLGLGQ 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALdpvTEQEI---LKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVI-DG 223
Cdd:PRK13549  149 QQLVEIAKALNKQARLLILDEPTASL---TESETavlLDIIRD-LKAHGIACIYISHKLNEVKAiSDTICVIrDG 219
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 4-231 2.94e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 62.76  E-value: 2.94e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQrtaA 83
Cdd:PRK15439   10 PLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPD---SGTLEIGGNPCARLTPAK---A 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAV--IFQDALqaLNPLVSIEGQLSLALTGTRtklksQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAI 161
Cdd:PRK15439   84 HQLGIylVPQEPL--LFPNLSVKENILFGLPKRQ-----ASMQKMKQLLAALGC---QLDLDSSAGSLEVADRQIVEILR 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGA 231
Cdd:PRK15439  154 GLMRDSRILILDEPTASLTPAETERLFSRIRE-LLAQGVGIVFISHKLPEIRQlADRISVMRDGTIALSGK 223
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 15-224 3.32e-11

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: 61.19  E-value: 3.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  15 TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLSGDAVCGLPMLQRTAAQRPAVIFqdAL 94
Cdd:cd03290    11 GSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILG---EMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAY--AA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 QA---LNplVSIEGQLSLALTGTRTKLKS-QDKIKLTELLVQLGFPNpETILPLYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:cd03290    86 QKpwlLN--ATVEENITFGSPFNKQRYKAvTDACSLQPDIDLLPFGD-QTEIGERGINLSGGQRQRICVARALYQNTNIV 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 171 IADEPTSAL-----DPVTEQEILKLIRDNvkQRQIggLLITHDLHSALACDKLLVIDGG 224
Cdd:cd03290   163 FLDDPFSALdihlsDHLMQEGILKFLQDD--KRTL--VLVTHKLQYLPHADWIIAMKDG 217
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
7-239 3.33e-11

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 62.81  E-value: 3.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAvcgLPMLQRTAAQ-R 85
Cdd:PRK10789  317 NIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVS---EGDIRFHDIP---LTKLQLDSWRsR 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQdalqalNPLV---SIEGQLSLALTGTrtklkSQDKIKLTELLVQLGfpnpETILPL---YPSQI-------SGG 152
Cdd:PRK10789  391 LAVVSQ------TPFLfsdTVANNIALGRPDA-----TQQEIEHVARLASVH----DDILRLpqgYDTEVgergvmlSGG 455

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLhSALA-CDKLLVIDGGGVVAYGA 231
Cdd:PRK10789  456 QKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGEGRTV--IISAHRL-SALTeASEILVMQHGHIAQRGN 532


                  ....*...
gi 1330606456 232 PKHALESS 239
Cdd:PRK10789  533 HDQLAQQS 540
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 23-230 3.38e-11

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 60.84  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEghislsgdaVCGLPMLQRTAAQRPAVIFQDALQALNPLV 101
Cdd:cd03266    23 GVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLePDAGFAT---------VDGFDVVKEPAEARRRLGFVSDSTGLYDRL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSL--ALTGtrtkLKSQD-KIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:cd03266    94 TARENLEYfaGLYG----LKGDElTARLEELADRLGM---EELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTG 166

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 179 LDPVTEQEILKLIRdnvKQRQIGGLLI--THDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03266   167 LDVMATRALREFIR---QLRALGKCILfsTHIMQEVERlCDRVVVLHRGRVVYEG 218
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
6-212 3.38e-11

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 61.52  E-value: 3.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIaGFLPETVEveGHISLSGDAVcglPMLQRTAAQ- 84
Cdd:PRK10619    6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCI-NFLEKPSE--GSIVVNGQTI---NLVRDKDGQl 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 -------------RPAVIFQ-----DALQALNPLVSIEGQ-LSLALTGTRTK-LKSQDKIKLTELLVQLgfpnpetilpl 144
Cdd:PRK10619   80 kvadknqlrllrtRLTMVFQhfnlwSHMTVLENVMEAPIQvLGLSKQEARERaVKYLAKVGIDERAQGK----------- 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 145 YPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIgGLLITHDLHSA 212
Cdd:PRK10619  149 YPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKT-MVVVTHEMGFA 215
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
18-209 3.76e-11

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 61.04  E-value: 3.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVeveGHISLSGDAVCGL-----PMLQRtaaqRPAVIFQD 92
Cdd:PRK10908   15 RQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSA---GKIWFSGHDITRLknrevPFLRR----QIGMIFQD 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALQALNPLVSIEGQLSLALTGTrtklkSQDKI--KLTELLVQLGFPNPETIlplYPSQISGGQRQRICIAIGLLSNADLI 170
Cdd:PRK10908   88 HHLLMDRTVYDNVAIPLIIAGA-----SGDDIrrRVSAALDKVGLLDKAKN---FPIQLSGGEQQRVGIARAVVNKPAVL 159

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDL 209
Cdd:PRK10908  160 LADEPTGNLDDALSEGILRLFEE-FNRVGVTVLMATHDI 197
PLN03130 PLN03130
ABC transporter C family member; Provisional
 15-226 4.64e-11

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.45  E-value: 4.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   15 TSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETVEveGHISLSGdAVCGLPMLQR--TAAQRPAVIFQD 92
Cdd:PLN03130   627 KAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSD--ASVVIRG-TVAYVPQVSWifNATVRDNILFGS 703

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   93 ALQALNPLVSIEgqlslaLTGTRTKLKSQDKIKLTELlVQLGFpnpetilplypsQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:PLN03130   704 PFDPERYERAID------VTALQHDLDLLPGGDLTEI-GERGV------------NISGGQKQRVSMARAVYSNSDVYIF 764

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456  173 DEPTSALDP-VTEQEILKLIRDNVKQRQigGLLITHDLHSALACDKLLVIDGGGV 226
Cdd:PLN03130   765 DDPLSALDAhVGRQVFDKCIKDELRGKT--RVLVTNQLHFLSQVDRIILVHEGMI 817
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 150-230 5.41e-11

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: 62.14  E-value: 5.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAY 229
Cdd:COG5265   496 SGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVARGRTT--LVIAHRLSTIVDADEILVLEAGRIVER 573


                  .
gi 1330606456 230 G 230
Cdd:COG5265   574 G 574
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 21-230 7.20e-11

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: 60.24  E-value: 7.20e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDaVCGLPMLQrtaaqrpavifqdalqalnpl 100
Cdd:cd03220    38 LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPD---SGTVTVRGR-VSSLLGLG--------------------- 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 101 VSIEGQLS-----------LALTGTRTKLKSQDKIKLTELlvqlgfpnPETI-LPLypSQISGGQRQRICIAIGLLSNAD 168
Cdd:cd03220    93 GGFNPELTgreniylngrlLGLSRKEIDEKIDEIIEFSEL--------GDFIdLPV--KTYSSGMKARLAFAIATALEPD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 169 LIIADEPTSALDPVTEQEILKLIRDNVKQRQIgGLLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:cd03220   163 ILLIDEVLAVGDAAFQEKCQRRLRELLKQGKT-VILVSHDPSSIKRlCDRALVLEKGKIRFDG 224
cbiO PRK13641
energy-coupling factor transporter ATPase;
23-239 7.27e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 61.00  E-value: 7.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVC------GLPMLQRTAA---QRP-AVIFQD 92
Cdd:PRK13641   25 NISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPS---SGTITIAGYHITpetgnkNLKKLRKKVSlvfQFPeAQLFEN 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALqalnpLVSIE-GQLSLALTGTRTKLKSQDKIKltellvQLGFPnpETILPLYPSQISGGQRQRICIAIGLLSNADLII 171
Cdd:PRK13641  102 TV-----LKDVEfGPKNFGFSEDEAKEKALKWLK------KVGLS--EDLISKSPFELSGGQMRRVAIAGVMAYEPEILC 168

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 172 ADEPTSALDPVTEQEILKLIRDnvkqRQIGG---LLITHDLHS-ALACDKLLVIDGGGVVAYGAPKHALESS 239
Cdd:PRK13641  169 LDEPAAGLDPEGRKEMMQLFKD----YQKAGhtvILVTHNMDDvAEYADDVLVLEHGKLIKHASPKEIFSDK 236
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
22-193 9.26e-11

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 61.47  E-value: 9.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF-LPETveveGHISLSGDAVcglpMLQRTAA---QRPAVIFQDaLQAL 97
Cdd:PRK11288   21 DDISFDCRAGQVHALMGENGAGKSTLLKILSGNyQPDA----GSILIDGQEM----RFASTTAalaAGVAIIYQE-LHLV 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIE----GQLSLALtG--TRTKLKSQDKIKLTELLVQLgfpNPETILplypSQISGGQRQRICIAIGLLSNADLII 171
Cdd:PRK11288   92 PEMTVAEnlylGQLPHKG-GivNRRLLNYEAREQLEHLGVDI---DPDTPL----KYLSIGQRQMVEIAKALARNARVIA 163

                         170       180
                  ....*....|....*....|...
gi 1330606456 172 ADEPTSALDpVTEQEIL-KLIRD 193
Cdd:PRK11288  164 FDEPTSSLS-AREIEQLfRVIRE 185
cbiO PRK13645
energy-coupling factor transporter ATPase;
125-232 9.35e-11

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 60.79  E-value: 9.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 125 KLTELL--VQLgfpnPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKL---IRDNVKQRQ 199
Cdd:PRK13645  129 KVPELLklVQL----PEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLferLNKEYKKRI 204

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1330606456 200 IgglLITHDLHSAL-ACDKLLVIDGGGVVAYGAP 232
Cdd:PRK13645  205 I---MVTHNMDQVLrIADEVIVMHEGKVISIGSP 235
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 24-232 1.08e-10

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 60.13  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  24 IHFDVYRGELLAIMGPSGIGKSMLSRAIAG-FLPEtvevEGHISLSGDAVCglPMLQRTAAQRPAVIFQDALQALNPLVS 102
Cdd:PRK13647   24 LSLSIPEGSKTALLGPNGAGKSTLLLHLNGiYLPQ----RGRVKVMGREVN--AENEKWVRSKVGLVFQDPDDQVFSSTV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IE----GQLSLALTGTRTKLKSQDKIKLTELlvqlgfpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:PRK13647   98 WDdvafGPVNMGLDKDEVERRVEEALKAVRM---------WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAY 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 179 LDPvTEQEILKLIRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAP 232
Cdd:PRK13647  169 LDP-RGQETLMEILDRLHNQGKTVIVATHDVDLAAEwADQVIVLKEGRVLAEGDK 222
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 22-230 1.17e-10

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 60.49  E-value: 1.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKS----MLSraiaGFLPETvevEGHISlsgdaVCGL-PMLQRTA-AQRPAVIFqdalq 95
Cdd:COG4586    39 DDISFTIEPGEIVGFIGPNGAGKSttikMLT----GILVPT---SGEVR-----VLGYvPFKRRKEfARRIGVVF----- 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  96 alnplvsieGQ---L--------SLALTGT---------RTKLKsqdkiKLTELLvQLGfpnpetilPLYPSQI---SGG 152
Cdd:COG4586   102 ---------GQrsqLwwdlpaidSFRLLKAiyripdaeyKKRLD-----ELVELL-DLG--------ELLDTPVrqlSLG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLH--SALaCDKLLVIDGGGVVAYG 230
Cdd:COG4586   159 QRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDdiEAL-CDRVIVIDHGRIIYDG 237
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 20-238 1.77e-10

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 60.73  E-value: 1.77e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   20 LFQDIHFDVYRGELLAIMGPSGIGKSMLSraiAGFLPETVEVEGHISLSGDAVC--GLPML--QRTAAQRPAVIFQDALQ 95
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLT---LGLFRINESAEGEIIIDGLNIAkiGLHDLrfKITIIPQDPVLFSGSLR 1377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   96 A-LNPLVSIEGQ---LSLALTGTRTKLKSQDKiKLTELLVQLGfpnpetilplypSQISGGQRQRICIAIGLLSNADLII 171
Cdd:TIGR00957 1378 MnLDPFSQYSDEevwWALELAHLKTFVSALPD-KLDHECAEGG------------ENLSVGQRQLVCLARALLRKTKILV 1444

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456  172 ADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALES 238
Cdd:TIGR00957 1445 LDEATAAVDLETDNLIQSTIRTQFEDCTV--LTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLLQQ 1509
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 3-235 1.99e-10

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 60.43  E-value: 1.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTSS-RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQRT 81
Cdd:COG3845   255 EVVLEVENLSVRDDRgVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPA---SGSIRLDGEDITGLSPRERR 331

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  82 AAqRPAVIFQDAL-QALNPLVSIEgqLSLALTGTRTKLKS------QDKI-KLTELLVQlGF----PNPETILplypSQI 149
Cdd:COG3845   332 RL-GVAYIPEDRLgRGLVPDMSVA--ENLILGRYRRPPFSrggfldRKAIrAFAEELIE-EFdvrtPGPDTPA----RSL 403

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnvkQRQIGG--LLITHDLHSALA-CDKLLVIDGGGV 226
Cdd:COG3845   404 SGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLE---LRDAGAavLLISEDLDEILAlSDRIAVMYEGRI 480


                  ....*....
gi 1330606456 227 VAYGAPKHA 235
Cdd:COG3845   481 VGEVPAAEA 489
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 31-248 2.77e-10

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 58.77  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  31 GELLAIMGPSGIGKSMLSRAiagFLPETVEVEGHISLSGDAVCGLPMlqRTAAQRPAVIFQDalqalnPLV---SIEGQL 107
Cdd:cd03288    47 GQKVGICGRTGSGKSSLSLA---FFRMVDIFDGKIVIDGIDISKLPL--HTLRSRLSIILQD------PILfsgSIRFNL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 108 SLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEI 187
Cdd:cd03288   116 DPECKCTDDRLWEALEIAQLKNMVKSLPGGLDAVVTEGGENFSVGQRQLFCLARAFVRKSSILIMDEATASIDMATENIL 195

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 188 LKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSSHAFCCSLR 248
Cdd:cd03288   196 QKVVMTAFADRTV--VTIAHRVSTILDADLVLVLSRGILVECDTPENLLAQEDGVFASLVR 254
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 23-224 3.37e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 59.63  E-value: 3.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVcglpmlqrtAAQRPavifQDALQA------ 96
Cdd:PRK10762  270 DVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRT---SGYVTLDGHEV---------VTRSP----QDGLANgivyis 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 ----LNPLV---SIEGQLSLA----LTGTRTKLKSQDKIKLTELLVQLgF----PNPETILPLypsqISGGQRQRICIAI 161
Cdd:PRK10762  334 edrkRDGLVlgmSVKENMSLTalryFSRAGGSLKHADEQQAVSDFIRL-FniktPSMEQAIGL----LSGGNQQKVAIAR 408

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIrDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:PRK10762  409 GLMTRPKVLILDEPTRGVDVGAKKEIYQLI-NQFKAEGLSIILVSSEMPEVLGmSDRILVMHEG 471
PLN03232 PLN03232
ABC transporter C family member; Provisional
 14-224 5.75e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 59.22  E-value: 5.75e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   14 KTSSRTLfQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPE----TVEVEGhislsgdAVCGLPMLQR--TAAQRPA 87
Cdd:PLN03232   627 KTSKPTL-SDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHaetsSVVIRG-------SVAYVPQVSWifNATVREN 698

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   88 VIFQDALQALNPLVSIEgqlSLALTGTRTKLKSQDKIKLTELLVQlgfpnpetilplypsqISGGQRQRICIAIGLLSNA 167
Cdd:PLN03232   699 ILFGSDFESERYWRAID---VTALQHDLDLLPGRDLTEIGERGVN----------------ISGGQKQRVSMARAVYSNS 759

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456  168 DLIIADEPTSALDP-VTEQEILKLIRDNVKQRQigGLLITHDLHSALACDKLLVIDGG 224
Cdd:PLN03232   760 DIYIFDDPLSALDAhVAHQVFDSCMKDELKGKT--RVLVTNQLHFLPLMDRIILVSEG 815
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
4-213 9.01e-10

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.78  E-value: 9.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PET--VEVEGHISLSGDAVCGLPMLQR 80
Cdd:PRK13543   10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLhVESgqIQIDGKTATRGDRSRFMAYLGH 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 TAAQRPAVifqDALQALNPLVSIEGQLSLALTGTRtklksqdkikltelLVQLGFPNPETILPlypSQISGGQRQRICIA 160
Cdd:PRK13543   90 LPGLKADL---STLENLHFLCGLHGRRAKQMPGSA--------------LAIVGLAGYEDTLV---RQLSAGQKKRLALA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrQIGGLLITHDLHSAL 213
Cdd:PRK13543  150 RLWLSPAPLWLLDEPYANLDLEGITLVNRMISAHLRG-GGAALVTTHGAYAAP 201
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 7-232 9.73e-10

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 57.40  E-value: 9.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   7 SVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQRTAAQRP 86
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPD---SGEVLVDGLDVATTP--SRELAKRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  87 AVIFQDalqalNplvsiegQLSLALT-------G----TRTKLKSQDKIKLTELLVQLGfpnpetILPL---YPSQISGG 152
Cdd:COG4604    78 AILRQE-----N-------HINSRLTvrelvafGrfpySKGRLTAEDREIIDEAIAYLD------LEDLadrYLDELSGG 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSAlAC--DKLLVIDGGGVVAYG 230
Cdd:COG4604   140 QRQRAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFA-SCyaDHIVAMKDGRVVAQG 218


                  ..
gi 1330606456 231 AP 232
Cdd:COG4604   219 TP 220
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
 21-230 1.70e-09

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


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 57.66  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGF-LPETveveGHISLSGDAVCGLpmlqRTAAQRP--AVIFQDA-LQA 96
Cdd:TIGR03797 469 LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFeTPES----GSVFYDGQDLAGL----DVQAVRRqlGVVLQNGrLMS 540

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPLVSIEG--QLSL--ALTGTRTKLKSQDkikLTELLVQLgfpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:TIGR03797 541 GSIFENIAGgaPLTLdeAWEAARMAGLAED---IRAMPMGM-----HTVISEGGGTLSGGQRQRLLIARALVRKPRILLF 612

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 173 DEPTSALDPVTeQEIlklIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:TIGR03797 613 DEATSALDNRT-QAI---VSESLERLKVTRIVIAHRLSTIRNADRIYVLDAGRVVQQG 666
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
5-232 2.92e-09

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 56.17  E-value: 2.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PEtvevEGHISLSGDAVC----GLPMLQ 79
Cdd:PRK13638    1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLrPQ----KGAVLWQGKPLDyskrGLLALR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  80 rtaaQRPAVIFQDALQALNpLVSIEGQLSLALtgtRTKLKSQDKI--KLTELLVQL---GFPNPetilplyPSQ-ISGGQ 153
Cdd:PRK13638   77 ----QQVATVFQDPEQQIF-YTDIDSDIAFSL---RNLGVPEAEItrRVDEALTLVdaqHFRHQ-------PIQcLSHGQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 154 RQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQ-RQIggLLITHDLHSAL-ACDKLLVIDGGGVVAYGA 231
Cdd:PRK13638  142 KKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQgNHV--IISSHDIDLIYeISDAVYVLRQGQILTHGA 219


                  .
gi 1330606456 232 P 232
Cdd:PRK13638  220 P 220
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 21-237 2.93e-09

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 55.86  E-value: 2.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  21 FQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPET---VEVEGHISlsgdavcglPMLqrtaaqrpavifqdALQA- 96
Cdd:COG1134    42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTsgrVEVNGRVS---------ALL--------------ELGAg 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 LNPlvsiegqlslALTGtrtklksQDKIKLTELLvqLGFPNPEtILPLYP-----SQI-----------SGGQRQRICIA 160
Cdd:COG1134    99 FHP----------ELTG-------RENIYLNGRL--LGLSRKE-IDEKFDeivefAELgdfidqpvktySSGMRARLAFA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrqiGG--LLITHDLHSALA-CDKLLVIDGGGVVAYGAPKHALE 237
Cdd:COG1134   159 VATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES---GRtvIFVSHSMGAVRRlCDRAIWLEKGRLVMDGDPEEVIA 235
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 4-214 3.07e-09

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 55.89  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHIslsgdavcglpmlQRTAA 83
Cdd:PRK09544    3 SLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPD---EGVI-------------KRNGK 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QR----PAVIFQDAlqalnplvsiegqlSLALTGTRTkLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICI 159
Cdd:PRK09544   67 LRigyvPQKLYLDT--------------TLPLTVNRF-LRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLL 131

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 160 AIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALA 214
Cdd:PRK09544  132 ARALLNRPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMA 186
PTZ00243 PTZ00243
ABC transporter; Provisional
 24-243 4.26e-09

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 56.71  E-value: 4.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   24 IHFDVYRGELLAIMGPSGIGKSMLsraIAGFLpETVEV-EGHISLSGDAVC--GLPMLQRTAAQRPA--VIFQDAL-QAL 97
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTL---LLTFM-RMVEVcGGEIRVNGREIGayGLRELRRQFSMIPQdpVLFDGTVrQNV 1404

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   98 NPLV---SIEGQLSLALTGTRTKLKSQDKikLTELLVQLGFPNpetilplypsqISGGQRQRICIAIGLLS-NADLIIAD 173
Cdd:PTZ00243  1405 DPFLeasSAEVWAALELVGLRERVASESE--GIDSRVLEGGSN-----------YSVGQRQLMCMARALLKkGSGFILMD 1471

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  174 EPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALESSSHAF 243
Cdd:PTZ00243  1472 EATANIDPALDRQIQATVMSAFSAYTV--ITIAHRLHTVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 23-228 7.21e-09

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 55.60  E-value: 7.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtvEVEGHISLSGDAVCGLPMLQRTAAQRPAVIFQDALQALNPLVS 102
Cdd:TIGR02633 278 DVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPG--KFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILG 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IEGQLSLALTGTRTKLKSQDKIK----LTELLVQLGFPNPETILPLypSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:TIGR02633 356 VGKNITLSVLKSFCFKMRIDAAAelqiIGSAIQRLKVKTASPFLPI--GRLSGGNQQKAVLAKMLLTNPRVLILDEPTRG 433

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330606456 179 LDPVTEQEILKLIrDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVA 228
Cdd:TIGR02633 434 VDVGAKYEIYKLI-NQLAQEGVAIIVVSSELAEVLGlSDRVLVIGEGKLKG 483
PLN03140 PLN03140
ABC transporter G family member; Provisional
 31-241 8.74e-09

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 55.62  E-value: 8.74e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   31 GELLAIMGPSGIGKSMLSRAIAGfLPETVEVEGHISLSGdavcgLPMLQRTAAQRPAVIFQDALQAlnPLVSI-EGQLSL 109
Cdd:PLN03140   906 GVLTALMGVSGAGKTTLMDVLAG-RKTGGYIEGDIRISG-----FPKKQETFARISGYCEQNDIHS--PQVTVrESLIYS 977

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  110 ALTGTRTKLKSQDKIKLTELLVQL-----------GFPNPetilplypSQISGGQRQRICIAIGLLSNADLIIADEPTSA 178
Cdd:PLN03140   978 AFLRLPKEVSKEEKMMFVDEVMELveldnlkdaivGLPGV--------TGLSTEQRKRLTIAVELVANPSIIFMDEPTSG 1049

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456  179 LDPVTEQEILKLIRDNVKQrqigGLLITHDLHSAL-----ACDKLLVIDGGGVVAYGAPkhaLESSSH 241
Cdd:PLN03140  1050 LDARAAAIVMRTVRNTVDT----GRTVVCTIHQPSidifeAFDELLLMKRGGQVIYSGP---LGRNSH 1110
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 3-224 1.02e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 55.06  E-value: 1.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   3 APLLSVDQLTIKTssrtlFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtveVEGHISLSGDAVCGLPMLQRTA 82
Cdd:PRK15439  266 APVLTVEDLTGEG-----FRNISLEVRAGEILGLAGVVGAGRTELAETLYGLRPA---RGGRIMLNGKEINALSTAQRLA 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 A--------QRPAVIFQDALQALNPLVSIEGQLSLALTGTRtklksqDKIKLTELLVQLG--FPNPETILplypSQISGG 152
Cdd:PRK15439  338 RglvylpedRQSSGLYLDAPLAWNVCALTHNRRGFWIKPAR------ENAVLERYRRALNikFNHAEQAA----RTLSGG 407

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 153 QRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrQIGGLLITHDLHS--ALAcDKLLVIDGG 224
Cdd:PRK15439  408 NQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEieQMA-DRVLVMHQG 479
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 10-229 1.85e-08

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 54.73  E-value: 1.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   10 QLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpetvEVEGHISLSGDAVCGLPMLQRTAAQRPAVI 89
Cdd:TIGR00956  768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE------RVTTGVITGGDRLVNGRPLDSSFQRSIGYV 841

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   90 FQDALQALNPLVSIEGQLSLALTGTRTKLKSQ-----DK-IKLTELLVQlgfpnPETILPLYPSQISGGQRQRICIAIGL 163
Cdd:TIGR00956  842 QQQDLHLPTSTVRESLRFSAYLRQPKSVSKSEkmeyvEEvIKLLEMESY-----ADAVVGVPGEGLNVEQRKRLTIGVEL 916

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  164 LSNADLII-ADEPTSALDPVTEQEILKLIRDNVKQRQigGLLITHDLHSAL---ACDKLLVIDGGGVVAY 229
Cdd:TIGR00956  917 VAKPKLLLfLDEPTSGLDSQTAWSICKLMRKLADHGQ--AILCTIHQPSAIlfeEFDRLLLLQKGGQTVY 984
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 16-232 2.44e-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: 54.63  E-value: 2.44e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   16 SSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSG-DAVCGLPMLQRTAAQRPA--VIFQD 92
Cdd:TIGR01257  941 SGRPAVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPT---SGTVLVGGkDIETNLDAVRQSLGMCPQhnILFHH 1017

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   93 alqalnpLVSIEGQLSLALTGTRTKLKSQdkIKLTELLVQLGF---PNPETilplypSQISGGQRQRICIAIGLLSNADL 169
Cdd:TIGR01257 1018 -------LTVAEHILFYAQLKGRSWEEAQ--LEMEAMLEDTGLhhkRNEEA------QDLSGGMQRKLSVAIAFVGDAKV 1082

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456  170 IIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITHDLHSA-LACDKLLVIDGGGVVAYGAP 232
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI--IMSTHHMDEAdLLGDRIAIISQGRLYCSGTP 1144
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 13-229 2.91e-08

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: 52.25  E-value: 2.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  13 IKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGfLPETVEVEGHISLSGdavcglpmLQRTAAQRPAVIFQD 92
Cdd:cd03232    15 VKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAG-RKTAGVITGEILING--------RPLDKNFQRSTGYVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALQALNPLVSIEGQL--SLALTGtrtklksqdkikltellvqlgfpnpetilplypsqISGGQRQRICIAIGLLSNADLI 170
Cdd:cd03232    86 QQDVHSPNLTVREALrfSALLRG-----------------------------------LSVEQRKRLTIGVELAAKPSIL 130

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 171 IADEPTSALDPVTEQEILKLIRDNVKQRQiggllithdlhsALAC-------------DKLLVIDGGGVVAY 229
Cdd:cd03232   131 FLDEPTSGLDSQAAYNIVRFLKKLADSGQ------------AILCtihqpsasifekfDRLLLLKRGGKTVY 190
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
18-238 4.14e-08

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 53.57  E-value: 4.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPmlQRTAAQRPAVIFQDalqal 97
Cdd:PRK10790  354 NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLT---EGEIRLDGRPLSSLS--HSVLRQGVAMVQQD----- 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 nPLVSIEgqlSLALTGTRTKLKSQDKIKLTELLVQL-----GFPNP-ETILPLYPSQISGGQRQRICIAIGLLSNADLII 171
Cdd:PRK10790  424 -PVVLAD---TFLANVTLGRDISEEQVWQALETVQLaelarSLPDGlYTPLGEQGNNLSVGQKQLLALARVLVQTPQILI 499

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 172 ADEPTSALDPVTEQEI---LKLIRDNVKQrqiggLLITHDLHSALACDKLLVIDGGGVVAYGAPKHALES 238
Cdd:PRK10790  500 LDEATANIDSGTEQAIqqaLAAVREHTTL-----VVIAHRLSTIVEADTILVLHRGQAVEQGTHQQLLAA 564
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 5-207 5.21e-08

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 51.87  E-value: 5.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFL-PETveveGHISLSGDAVcglpmLQRTAA 83
Cdd:PRK13540    1 MLDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLnPEK----GEILFERQSI-----KKDLCT 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  84 QRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNpetilplypSQISGGQRQRICIAIGL 163
Cdd:PRK13540   72 YQKQLCFVGHRSGINPYLTLRENCLYDIHFSPGAVGITELCRLFSLEHLIDYPC---------GLLSSGQKRQVALLRLW 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1330606456 164 LSNADLIIADEPTSALDpvtEQEILKLIRDNVKQRQIGG--LLITH 207
Cdd:PRK13540  143 MSKAKLWLLDEPLVALD---ELSLLTIITKIQEHRAKGGavLLTSH 185
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
4-224 8.39e-08

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 52.48  E-value: 8.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTSSRTlfQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtveVEGHISLSG---------DAV-C 73
Cdd:PRK09700  264 TVFEVRNVTSRDRKKV--RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKR---AGGEIRLNGkdisprsplDAVkK 338

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  74 GLPMLqrTAAQRPAVIFQDALQALNplVSIEGQLSLA-LTGTRTKLKSQDKIKLTEL---LVQLGFPNPETILplypSQI 149
Cdd:PRK09700  339 GMAYI--TESRRDNGFFPNFSIAQN--MAISRSLKDGgYKGAMGLFHEVDEQRTAENqreLLALKCHSVNQNI----TEL 410

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 150 SGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:PRK09700  411 SGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR-QLADDGKVILMVSSELPEIITvCDRIAVFCEG 485
GguA NF040905
sugar ABC transporter ATP-binding protein;
22-223 9.27e-08

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 52.10  E-value: 9.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPeTVEVEGHISLSGDaVCGLPMLqRTAAQRPAVIFQDALqALNPLV 101
Cdd:NF040905   18 DDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYP-HGSYEGEILFDGE-VCRFKDI-RDSEALGIVIIHQEL-ALIPYL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SI------------EGQLSLALTGTRTKlksqdkikltELLVQLGFP-NPETILplypSQISGGQRQRICIAIGLLSNAD 168
Cdd:NF040905   94 SIaeniflgnerakRGVIDWNETNRRAR----------ELLAKVGLDeSPDTLV----TDIGVGKQQLVEIAKALSKDVK 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 169 LIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLH--SALAcDKLLVI-DG 223
Cdd:NF040905  160 LLILDEPTAALNEEDSAALLDLLLE-LKAQGITSIIISHKLNeiRRVA-DSITVLrDG 215
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 114-222 1.25e-07

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 52.34  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  114 TRTKLKSQDKIKLTELLVQlGFPNP-ETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIR 192
Cdd:PTZ00265  1324 TREDVKRACKFAAIDEFIE-SLPNKyDTNVGPYGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIV 1402

                           90       100       110
                   ....*....|....*....|....*....|
gi 1330606456  193 DNVKQRQIGGLLITHDLHSALACDKLLVID 222
Cdd:PTZ00265  1403 DIKDKADKTIITIAHRIASIKRSDKIVVFN 1432
cbiO PRK13649
energy-coupling factor transporter ATPase;
146-233 2.31e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 50.51  E-value: 2.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 146 PSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRdNVKQRQIGGLLITHDLHS-ALACDKLLVIDGG 224
Cdd:PRK13649  143 PFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFK-KLHQSGMTIVLVTHLMDDvANYADFVYVLEKG 221


                  ....*....
gi 1330606456 225 GVVAYGAPK 233
Cdd:PRK13649  222 KLVLSGKPK 230
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
30-209 4.74e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.19  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  30 RGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEGhiSLSGDAVcgLPMLQRTAaqrpaviFQDALQAL-----NPLVSI 103
Cdd:PRK13409   98 EGKVTGILGPNGIGKTTAVKILSGELiPNLGDYEE--EPSWDEV--LKRFRGTE-------LQNYFKKLyngeiKVVHKP 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 104 E--GQLSLALTGT-RTKLKSQDKI-KLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSAL 179
Cdd:PRK13409  167 QyvDLIPKVFKGKvRELLKKVDERgKLDEVVERLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL 243

                         170       180       190
                  ....*....|....*....|....*....|
gi 1330606456 180 DPVTEQEILKLIRDNVKQRQIggLLITHDL 209
Cdd:PRK13409  244 DIRQRLNVARLIRELAEGKYV--LVVEHDL 271
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 18-180 5.34e-07

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: 49.93  E-value: 5.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpeTVEVEGHISLSGDAVCGL----PMLQRTAAQRPAVI--FQ 91
Cdd:TIGR03719  18 KEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV---DKDFNGEARPQPGIKVGYlpqePQLDPTKTVRENVEegVA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  92 DALQALNPLVSIEGQLSL------ALTGTRTKLksQDKI----------KLTELLVQLGFPNPETILplypSQISGGQRQ 155
Cdd:TIGR03719  95 EIKDALDRFNEISAKYAEpdadfdKLAAEQAEL--QEIIdaadawdldsQLEIAMDALRCPPWDADV----TKLSGGERR 168

                         170       180
                  ....*....|....*....|....*
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALD 180
Cdd:TIGR03719 169 RVALCRLLLSKPDMLLLDEPTNHLD 193
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 22-230 7.09e-07

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


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 48.79  E-value: 7.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  22 QDIHFDVYRGELLAIMGPSGIGKSMLSraiagFlpETVEVEGHI----SLSGDAVCGLPMLQRtaaqrPAVifqDALQAL 97
Cdd:cd03270    12 KNVDVDIPRNKLVVITGVSGSGKSSLA-----F--DTIYAEGQRryveSLSAYARQFLGQMDK-----PDV---DSIEGL 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 NPLVSIE----GQLSLALTGTRTK-------LKSQDKIKLT-ELLVQLGFPNpetiLPLYPS--QISGGQRQRICIAIGL 163
Cdd:cd03270    77 SPAIAIDqkttSRNPRSTVGTVTEiydylrlLFARVGIRERlGFLVDVGLGY----LTLSRSapTLSGGEAQRIRLATQI 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1330606456 164 LSNAD--LIIADEPTSALDPvteQEILKLIRDNVKQRQIGG--LLITHDLHSALACDKllVID--------GGGVVAYG 230
Cdd:cd03270   153 GSGLTgvLYVLDEPSIGLHP---RDNDRLIETLKRLRDLGNtvLVVEHDEDTIRAADH--VIDigpgagvhGGEIVAQG 226
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 139-221 1.16e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 49.26  E-value: 1.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  139 ETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIrDNVK--QRQIgGLLITHDLHSALACD 216
Cdd:PTZ00265   570 ETLVGSNASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTI-NNLKgnENRI-TIIIAHRLSTIRYAN 647


                   ....*
gi 1330606456  217 KLLVI 221
Cdd:PTZ00265   648 TIFVL 652
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 6-180 1.24e-06

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: 48.78  E-value: 1.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflPETVEvEGHISLsGDAVcglpmlqrtaaqR 85
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITG--QEQPD-SGTIEI-GETV------------K 386

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  86 PAVIFQ--DALQAlNPLV--SIEGQLSLALTGTRT----------KLKSQDKIKLTellvqlgfpnpetilplypSQISG 151
Cdd:TIGR03719 387 LAYVDQsrDALDP-NKTVweEISGGLDIIKLGKREipsrayvgrfNFKGSDQQKKV-------------------GQLSG 446

                         170       180
                  ....*....|....*....|....*....
gi 1330606456 152 GQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:TIGR03719 447 GERNRVHLAKTLKSGGNVLLLDEPTNDLD 475
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 26-209 1.60e-06

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 47.75  E-value: 1.60e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  26 FDVYR------GELLAIMGPSGIGKSMLSRAIAGFL----------PETVEVEGHisLSGDAvcglpmLQRTAAQrpavI 89
Cdd:cd03236    15 FKLHRlpvpreGQVLGLVGPNGIGKSTALKILAGKLkpnlgkfddpPDWDEILDE--FRGSE------LQNYFTK----L 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  90 FQDALQALNPLVSIEgQLSLALTGTRTKL--KSQDKIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNA 167
Cdd:cd03236    83 LEGDVKVIVKPQYVD-LIPKAVKGKVGELlkKKDERGKLDELVDQLEL---RHVLDRNIDQLSGGELQRVAIAAALARDA 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1330606456 168 DLIIADEPTSALDPVTEQEILKLIRDNVKQ-RQIggLLITHDL 209
Cdd:cd03236   159 DFYFFDEPSSYLDIKQRLNAARLIRELAEDdNYV--LVVEHDL 199
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 30-209 2.21e-06

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: 48.24  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  30 RGELLAIMGPSGIGKSMLSRAIAGFL-PETVEVEGhiSLSGDAVcglpmLQRTAAQrpavIFQDALQAL---NPLVSIEG 105
Cdd:COG1245    98 KGKVTGILGPNGIGKSTALKILSGELkPNLGDYDE--EPSWDEV-----LKRFRGT----ELQDYFKKLangEIKVAHKP 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 106 Q----LSLALTGT-RTKLKSQD-KIKLTELLVQLGFpnpETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSAL 179
Cdd:COG1245   167 QyvdlIPKVFKGTvRELLEKVDeRGKLDELAEKLGL---ENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL 243

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1330606456 180 DpVTEQ-EILKLIRDNVKQ-RQIggLLITHDL 209
Cdd:COG1245   244 D-IYQRlNVARLIRELAEEgKYV--LVVEHDL 272
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
9-230 2.81e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 47.12  E-value: 2.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   9 DQLTIKTSSRTLF--QDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAvcglpmlqrtaaqrp 86
Cdd:PRK13546   26 DALIPKHKNKTFFalDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPT---VGKVDRNGEV--------------- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  87 avifqdalqalnPLVSIEGQLSLALTGTrtklksqDKIKLTELLvqLGFpNPETILPLYPSQI----------------S 150
Cdd:PRK13546   88 ------------SVIAISAGLSGQLTGI-------ENIEFKMLC--MGF-KRKEIKAMTPKIIefselgefiyqpvkkyS 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAY 229
Cdd:PRK13546  146 SGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE-FKEQNKTIFFVSHNLGQVRQfCTKIAWIEGGKLKDY 224


                  .
gi 1330606456 230 G 230
Cdd:PRK13546  225 G 225
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 5-180 3.26e-06

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 47.09  E-value: 3.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflPETVEV-EGHISLSGDAVCGLPMLQRTA- 82
Cdd:PRK09580    1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAG--REDYEVtGGTVEFKGKDLLELSPEDRAGe 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 ---------AQRPAVIFQDALQ-ALNPLVSIEGQLSLaltgTRTKLKS--QDKIKL----TELL---VQLGFpnpetilp 143
Cdd:PRK09580   79 gifmafqypVEIPGVSNQFFLQtALNAVRSYRGQEPL----DRFDFQDlmEEKIALlkmpEDLLtrsVNVGF-------- 146

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1330606456 144 lypsqiSGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:PRK09580  147 ------SGGEKKRNDILQMAVLEPELCILDESDSGLD 177
PLN03073 PLN03073
ABC transporter F family; Provisional
 19-229 3.64e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.55  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  19 TLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDAVcglpmlqRTAAQRPAVIFQDALQAL- 97
Cdd:PLN03073  523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPS---------SGTVF-------RSAKVRMAVFSQHHVDGLd 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  98 ---NPLVsiegQLSLALTGTRTKlksqdkiKLTELLVQLGFPNPETILPLYpsQISGGQRQRICIAIGLLSNADLIIADE 174
Cdd:PLN03073  587 lssNPLL----YMMRCFPGVPEQ-------KLRAHLGSFGVTGNLALQPMY--TLSGGQKSRVAFAKITFKKPHILLLDE 653

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 175 PTSALD-PVTEQEILKLIrdnvkQRQIGGLLITHDLH-SALACDKLLVIDGGGVVAY 229
Cdd:PLN03073  654 PSNHLDlDAVEALIQGLV-----LFQGGVLMVSHDEHlISGSVDELWVVSEGKVTPF 705
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 141-223 3.72e-06

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 46.03  E-value: 3.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 141 ILPLYPSQ---ISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSA-LACD 216
Cdd:cd03222    61 ITPVYKPQyidLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLdYLSD 140


                  ....*..
gi 1330606456 217 KLLVIDG 223
Cdd:cd03222   141 RIHVFEG 147
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 23-224 4.39e-06

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 47.23  E-value: 4.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtvEVEGHISLSGdavcglpmlQRTAAQRPavifQDALQA------ 96
Cdd:PRK13549  280 DVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPG--RWEGEIFIDG---------KPVKIRNP----QQAIAQgiamvp 344

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  97 -------LNPLVSIEGQLSLALTGTRTKLKSQDKIK--------LTELLVQLgfPNPEtiLPLypSQISGGQRQRICIAI 161
Cdd:PRK13549  345 edrkrdgIVPVMGVGKNITLAALDRFTGGSRIDDAAelktilesIQRLKVKT--ASPE--LAI--ARLSGGNQQKAVLAK 418

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1330606456 162 GLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQrQIGGLLITHDLHSALA-CDKLLVIDGG 224
Cdd:PRK13549  419 CLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGlSDRVLVMHEG 481
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 5-226 5.10e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 47.03  E-value: 5.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   5 LLSVDQLTIKTSSRtlFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETvevEGHISLSGDAVCGLPMLQR---- 80
Cdd:PRK10982  250 ILEVRNLTSLRQPS--IRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKS---AGTITLHGKKINNHNANEAinhg 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 ----TAAQRPAVIFQDALQALNPLVS-IEGQLSLALTGTRTKLKSQDKIKLTELLVQLgfPNPETILplypSQISGGQRQ 155
Cdd:PRK10982  325 falvTEERRSTGIYAYLDIGFNSLISnIRNYKNKVGLLDNSRMKSDTQWVIDSMRVKT--PGHRTQI----GSLSGGNQQ 398

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKQRQiGGLLITHDLHSALA-CDKLLVIDGGGV 226
Cdd:PRK10982  399 KVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDK-GIIIISSEMPELLGiTDRILVMSNGLV 469
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-227 5.19e-06

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 46.41  E-value: 5.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   1 MNAPLLSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGflpETVEVEGHISLSGDAVCGLPMLQr 80
Cdd:PRK11614    1 MEKVMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCG---DPRATSGRIVFDGKDITDWQTAK- 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  81 taAQRPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELlvqlgFPNPETILPLYPSQISGGQRQRICIA 160
Cdd:PRK11614   77 --IMREAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERIKWVYEL-----FPRLHERRIQRAGTMSGGEQQMLAIG 149

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 161 IGLLSNADLIIADEPTSALDPVTEQEILKLIrDNVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVV 227
Cdd:PRK11614  150 RALMSQPRLLLLDEPSLGLAPIIIQQIFDTI-EQLREQGMTIFLVEQNANQALKlADRGYVLENGHVV 216
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
102-230 8.26e-06

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 46.27  E-value: 8.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 102 SIEGQLSLALTGTRTKLKSQD-KIKLTELLVQLGFPNPETilpLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:NF000106  100 SFSGRENLYMIGR*LDLSRKDaRARADELLERFSLTEAAG---RAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLD 176

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1330606456 181 PVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGGGVVAYG 230
Cdd:NF000106  177 PRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 148-219 1.38e-05

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: 44.27  E-value: 1.38e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1330606456 148 QISGGQRQRICIAIgLLSNAD-----LIIADEPTSALDPVTEQEILKLIRDN-VKQRQigGLLITHDLHSALACDKLL 219
Cdd:cd03227    77 QLSGGEKELSALAL-ILALASlkprpLYILDEIDRGLDPRDGQALAEAILEHlVKGAQ--VIVITHLPELAELADKLI 151
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 24-224 1.58e-05

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 45.73  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  24 IHFDVYRGELLAIMGPSGIGKSMLSRAIAG-FLPetveVEGHISLSGDAVcglpmlqrTAAQRPA------VIFQDAL-- 94
Cdd:PRK10522  342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGlYQP----QSGEILLDGKPV--------TAEQPEDyrklfsAVFTDFHlf 409

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  95 -QALNPlvsiEGQLSLALTGTR--TKLKSQDKIKLTEllvqlgfpnpETILPLypsQISGGQRQRICIAIGLLSNADLII 171
Cdd:PRK10522  410 dQLLGP----EGKPANPALVEKwlERLKMAHKLELED----------GRISNL---KLSKGQKKRLALLLALAEERDILL 472

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1330606456 172 ADEPTSALDPVTEQEILKLIRDNVKQRQIGGLLITHDLHSALACDKLLVIDGG 224
Cdd:PRK10522  473 LDEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 28-234 1.88e-05

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: 45.77  E-value: 1.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   28 VYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDA-VCGLPMLQRTAAQRPAVIFQDALQALNPLVSieGQ 106
Cdd:TIGR01257 1962 VRPGECFGLLGVNGAGKTTTFKMLTGDTTVT---------SGDAtVAGKSILTNISDVHQNMGYCPQFDAIDDLLT--GR 2030

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  107 LSLALTGTRTKLKSQDKIKLTELLVQ-LGfpnpetiLPLYPSQI----SGGQRQRICIAIGLLSNADLIIADEPTSALDP 181
Cdd:TIGR01257 2031 EHLYLYARLRGVPAEEIEKVANWSIQsLG-------LSLYADRLagtySGGNKRKLSTAIALIGCPPLVLLDEPTTGMDP 2103

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1330606456  182 VTEQEILKLIRDNVKQRQiGGLLITHDLHSALA-CDKLLVIDGGGVVAYGAPKH 234
Cdd:TIGR01257 2104 QARRMLWNTIVSIIREGR-AVVLTSHSMEECEAlCTRLAIMVKGAFQCLGTIQH 2156
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 23-230 3.31e-05

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 44.50  E-value: 3.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  23 DIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpeTVEVEGHISLSGDAVcglpmlqrtaaqrpavifqdalqalnpLVS 102
Cdd:PRK13545   42 NISFEVPEGEIVGIIGLNGSGKSTLSNLIAGV---TMPNKGTVDIKGSAA---------------------------LIA 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 103 IEGQLSLALTGTrtklksqDKIKLTELLVQLgfpNPETILPLYPSQI----------------SGGQRQRICIAIGLLSN 166
Cdd:PRK13545   92 ISSGLNGQLTGI-------ENIELKGLMMGL---TKEKIKEIIPEIIefadigkfiyqpvktySSGMKSRLGFAISVHIN 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1330606456 167 ADLIIADEPTSALDPVTEQEILKLIRDnVKQRQIGGLLITHDLHSALA-CDKLLVIDGGGVVAYG 230
Cdd:PRK13545  162 PDILVIDEALSVGDQTFTKKCLDKMNE-FKEQGKTIFFISHSLSQVKSfCTKALWLHYGQVKEYG 225
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 141-208 3.48e-05

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 43.36  E-value: 3.48e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1330606456 141 ILPLYPSQISGGQRQRICIAIGLL------SNADLIIADEPTSALDPVT-EQEILKLIRDNVKQ--RQIGglLITHD 208
Cdd:cd03240   108 PLLDMRGRCSGGEKVLASLIIRLAlaetfgSNCGILALDEPTTNLDEENiEESLAEIIEERKSQknFQLI--VITHD 182
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 4-193 4.29e-05

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 44.24  E-value: 4.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   4 PLLSVDQLTIKTS-SRTLFQDiHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPEtveveghisLSGDAVCGLpmlqrta 82
Cdd:PRK10938    2 SSLQISQGTFRLSdTKTLQLP-SLTLNAGDSWAFVGANGSGKSALARALAGELPL---------LSGERQSQF------- 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  83 aQRPAVIfqdALQALNPLVSIEGQ------LSLAL--TGTRTKLKSQDKIKLT----ELLVQLGFpnpETILPLYPSQIS 150
Cdd:PRK10938   65 -SHITRL---SFEQLQKLVSDEWQrnntdmLSPGEddTGRTTAEIIQDEVKDParceQLAQQFGI---TALLDRRFKYLS 137

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1330606456 151 GGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRD 193
Cdd:PRK10938  138 TGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLAS 180
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 149-237 6.76e-05

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 43.94  E-value: 6.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  149 ISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILKLIRDNVKqrqiggLLITHDLHSALAC--------DKLLV 220
Cdd:TIGR00956  210 VSGGERKRVSIAEASLGGAKIQCWDNATRGLDSATALEFIRALKTSAN------ILDTTPLVAIYQCsqdayelfDKVIV 283

                           90
                   ....*....|....*..
gi 1330606456  221 IDGGGVVAYGAPKHALE 237
Cdd:TIGR00956  284 LYEGYQIYFGPADKAKQ 300
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 18-208 1.09e-04

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 43.02  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLPETveveghislSGDAVCGLPML-----QRTAAQRPAVIFQD 92
Cdd:PRK11147  332 KQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQAD---------SGRIHCGTKLEvayfdQHRAELDPEKTVMD 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  93 ALQALNPLVSIEGQLSLALTgtrtklksqdkiKLTELLvqlgFPNPETILPLypSQISGGQRQRICIAIGLLSNADLIIA 172
Cdd:PRK11147  403 NLAEGKQEVMVNGRPRHVLG------------YLQDFL----FHPKRAMTPV--KALSGGERNRLLLARLFLKPSNLLIL 464

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1330606456 173 DEPTSALDpvteQEILKLIRDNVKQRQIGGLLITHD 208
Cdd:PRK11147  465 DEPTNDLD----VETLELLEELLDSYQGTVLLVSHD 496
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 30-206 1.10e-04

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: 41.20  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456   30 RGELLAIMGPSGIGKSMLSRAIAGFLPETVEVeghislsgdavcglpmlqrtaaqrpaVIFqdalqalnplvsiegqlsl 109
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGG--------------------------VIY------------------- 35

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  110 altgtrtklksqdkIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTEQEILK 189
Cdd:smart00382  36 --------------IDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLL 101

                          170
                   ....*....|....*..
gi 1330606456  190 LIRDNVKQRQIGGLLIT 206
Cdd:smart00382 102 LEELRLLLLLKSEKNLT 118
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 6-56 1.88e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 42.19  E-value: 1.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1330606456   6 LSVDQLTIKTSSRTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFLP 56
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELE 370
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
142-242 2.34e-04

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 42.03  E-value: 2.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 142 LPLypsqisgGQRQRICIAIGLLSNADLIIADEPTSALDPVTeqeilkliRDNVKQrqiggLLI-------------THD 208
Cdd:NF033858  398 LPL-------GIRQRLSLAVAVIHKPELLILDEPTSGVDPVA--------RDMFWR-----LLIelsredgvtifisTHF 457

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1330606456 209 LHSALACDKLLVIDGGGVVAYGAPKhALESSSHA 242
Cdd:NF033858  458 MNEAERCDRISLMHAGRVLASDTPA-ALVAARGA 490
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 149-240 2.88e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 41.92  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 149 ISGGQRQRICIA--IGLLSNADLIIADEPTSALDPvteQEILKLIRDNVKQRQIGGLLIT--HDLHSALACDKllVID-- 222
Cdd:TIGR00630 489 LSGGEAQRIRLAtqIGSGLTGVLYVLDEPSIGLHQ---RDNRRLINTLKRLRDLGNTLIVveHDEDTIRAADY--VIDig 563

                          90       100
                  ....*....|....*....|....
gi 1330606456 223 ------GGGVVAYGAPKHALESSS 240
Cdd:TIGR00630 564 pgagehGGEVVASGTPEEILANPD 587
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 129-180 2.93e-04

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 41.69  E-value: 2.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1330606456 129 LLVQLGFPNPETILPLypSQISGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:PRK10636  132 LLHGLGFSNEQLERPV--SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLD 181
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 147-228 2.95e-04

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 41.64  E-value: 2.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 147 SQISGGQRQRICIAIGLLSNADLIIADEPTSALdpvTEQEILKL--IRDNVKQRQIGGLLITHDLHSALA-CDKLLVIDG 223
Cdd:PRK10982  133 ATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSL---TEKEVNHLftIIRKLKERGCGIVYISHKMEEIFQlCDEITILRD 209


                  ....*
gi 1330606456 224 GGVVA 228
Cdd:PRK10982  210 GQWIA 214
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 128-210 3.08e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.42  E-value: 3.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 128 ELLVQLGFPNPETILPLypSQISGGQRQRICIAIGLLSNADLIIADEPTSALDPVTeqeilklIR---DNVKQRQIGGLL 204
Cdd:PRK15064  137 ELLLGVGIPEEQHYGLM--SEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT-------IRwleDVLNERNSTMII 207


                  ....*.
gi 1330606456 205 ITHDLH 210
Cdd:PRK15064  208 ISHDRH 213
PTZ00243 PTZ00243
ABC transporter; Provisional
 149-248 8.02e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.53  E-value: 8.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  149 ISGGQRQRICIAIGLLSNADLIIADEPTSALDP-----VTEQEILKLIRDnvKQRqiggLLITHDLHSALACDKLLVIDG 223
Cdd:PTZ00243   783 LSGGQKARVSLARAVYANRDVYLLDDPLSALDAhvgerVVEECFLGALAG--KTR----VLATHQVHVVPRADYVVALGD 856

                           90       100
                   ....*....|....*....|....*
gi 1330606456  224 GGVVAYGAPKHALESSshaFCCSLR 248
Cdd:PTZ00243   857 GRVEFSGSSADFMRTS---LYATLA 878
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 18-180 1.16e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 39.72  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAGFlpETvEVEGHISLSGDAVCGL----PMLQRTAAQRPAVI--FQ 91
Cdd:PRK11819   20 KQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGV--DK-EFEGEARPAPGIKVGYlpqePQLDPEKTVRENVEegVA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  92 DALQALNPLVSIEGQLSL------ALTGTRTKLksQDKI---KLTELLVQ-------LGFPNPETILplypSQISGGQRQ 155
Cdd:PRK11819   97 EVKAALDRFNEIYAAYAEpdadfdALAAEQGEL--QEIIdaaDAWDLDSQleiamdaLRCPPWDAKV----TKLSGGERR 170

                         170       180
                  ....*....|....*....|....*
gi 1330606456 156 RICIAIGLLSNADLIIADEPTSALD 180
Cdd:PRK11819  171 RVALCRLLLEKPDMLLLDEPTNHLD 195
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 85-210 1.26e-03

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


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 39.30  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456  85 RPAVIFQDALQALNPLVSIEGQLSLALTGTRTKLKSQDKIKLTELLVQLGFPNPETILPLYPSQISGGQRQRICIAIGLL 164
Cdd:pfam13304 173 ADLALFPDLKELLQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGELPAFELSDGTKRLLALLAALL 252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1330606456 165 SNAD---LIIADEPTSALDPVTEQEILKLIRDNVKQR-QIggLLITHDLH 210
Cdd:pfam13304 253 SALPkggLLLIDEPESGLHPKLLRRLLELLKELSRNGaQL--ILTTHSPL 300
COG4637 COG4637
Predicted ATPase [General function prediction only];
143-222 1.86e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443675 [Multi-domain]  Cd Length: 371  Bit Score: 39.14  E-value: 1.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1330606456 143 PLYPSQISGGQRQRICIAIGLLSNA--DLIIADEPTSALDPVTEQEILKLIRDNVKQRQIggLLITH--DLHSALACDKL 218
Cdd:COG4637   253 PFPARELSDGTLRFLALLAALLSPRppPLLCIEEPENGLHPDLLPALAELLREASERTQV--IVTTHspALLDALEPEEV 330


                  ....
gi 1330606456 219 LVID 222
Cdd:COG4637   331 LVLE 334
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 125-180 3.66e-03

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 38.39  E-value: 3.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1330606456 125 KLTELLVQLGFpNPETILplypSQISGGQRQRICIAIGLLSNADLIIADEPTSALD 180
Cdd:PRK11147  138 RINEVLAQLGL-DPDAAL----SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLD 188
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 18-53 7.24e-03

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 37.41  E-value: 7.24e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1330606456  18 RTLFQDIHFDVYRGELLAIMGPSGIGKSMLSRAIAG 53
Cdd:PRK11819  337 RLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITG 372
 
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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