NCBI Conserved Domain Search

Conserved domains on [gi|14028433|dbj|BAB54985|]

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ATP-binding protein of ABC transporter (plasmid) [Mesorhizobium japonicum MAFF 303099]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11467437)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ATP transporter complex responsible for coupling the energy of ATP hydrolysis to the import of one or more from a variety of substrates including Fe(3+) ions and polyamines such as spermidine and putrescine

CATH: 3.40.50.300

EC: 7.-.-.-

Gene Ontology: GO:0042626|GO:0140359|GO:0005524|GO:0016887

PubMed: 25750732|24638992

SCOP: 4003976

TCDB: 3.A.1

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

10-365

6.10e-155

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 439.53 E-value: 6.10e-155

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGM 89
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNI 249
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 250 VCCSVTARNGRLATVKlgdgtevGVPIPAGVTERLGVGEKSLLLLRPEKAetgyRI--DTSVVAMSGPVLSTTFMGTHYQ 327
Cdd:COG3842 242 LPGTVLGDEGGGVRTG-------GRTLEVPADAGLAAGGPVTVAIRPEDI----RLspEGPENGLPGTVEDVVFLGSHVR 310

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 14028433 328 VVFSTRHG-EITAHLNN----DYAPGQSVDVAWRAGNLIVLPA 365
Cdd:COG3842 311 YRVRLGDGqELVVRVPNraalPLEPGDRVGLSWDPEDVVVLPA 353

Name

Accession

Description

Interval

E-value

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

10-365

6.10e-155

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 439.53 E-value: 6.10e-155

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGM 89
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNI 249
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 250 VCCSVTARNGRLATVKlgdgtevGVPIPAGVTERLGVGEKSLLLLRPEKAetgyRI--DTSVVAMSGPVLSTTFMGTHYQ 327
Cdd:COG3842 242 LPGTVLGDEGGGVRTG-------GRTLEVPADAGLAAGGPVTVAIRPEDI----RLspEGPENGLPGTVEDVVFLGSHVR 310

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 14028433 328 VVFSTRHG-EITAHLNN----DYAPGQSVDVAWRAGNLIVLPA 365
Cdd:COG3842 311 YRVRLGDGqELVVRVPNraalPLEPGDRVGLSWDPEDVVVLPA 353

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

11-364

3.12e-115

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 339.62 E-value: 3.12e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   11 PPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMV 90
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:PRK09452  92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  171 LSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIV 250
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  251 CCSVTARNGR---LATVKlgdgtevGVPIPAGVTERLGVGEKSLLLLRPEKAETGYRID-TSVVAMSGPVLSTTFMGTHY 326
Cdd:PRK09452 252 DATVIERLDEqrvRANVE-------GRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDdEHAEGLIGYVRERNYKGMTL 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 14028433  327 QVVFSTRHG----------EITAHLnnDYAPGQSVDVAWRAGNLIVLP 364
Cdd:PRK09452 325 DSVVELENGkmvmvseffnEDDPDF--DHSLGQKVAVTWVEGWEVVLA 370

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

14-245

2.49e-110

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: 321.88 E-value: 2.49e-110

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03300  81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIG 245
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

45-363

6.31e-105

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: 311.35 E-value: 6.31e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    45 LGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRA 124
Cdd:TIGR01187   2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   125 LEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQ 204
Cdd:TIGR01187  82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   205 SEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVccsvtarngRLATVKLGDGTEV---GVPIPAGVT 281
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVF---------EATVIERKSEQVVlagVEGRRCDIY 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   282 ERLGV--GEKSLLLLRPEKAE-TGYRIDTSVVAMSGPVLSTTFMGTHYQVVFSTRHGEIT--------AHLNNDYAPGQS 350
Cdd:TIGR01187 233 TDVPVekDQPLHVVLRPEKIViEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVlvseffneDDPHMSPSIGDR 312

                         330
                  ....*....|...
gi 14028433   351 VDVAWRAGNLIVL 363
Cdd:TIGR01187 313 VGLTWHPGSEVVL 325

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

29-297

1.26e-75

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 237.28 E-value: 1.26e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEY 108
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  109 PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKE 188
Cdd:NF040840  96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  189 LQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVccSVTARNGRLATVKLGD 268
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENII--EGVAEKGGEGTILDTG 253

                        250       260
                 ....*....|....*....|....*....
gi 14028433  269 GTEVGVPIPAGVTERLGVgeksllllRPE 297
Cdd:NF040840 254 NIKIELPEEKKGKVRIGI--------RPE 274

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

29-172

3.24e-43

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: 147.02 E-value: 3.24e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFPHLTARENV 106
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   107 EYPLKVRRLPREERRRRALEYLERVHLSEWADR----YPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

14-222

1.30e-42

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 147.56 E-value: 1.30e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGA----VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDR------AAR 83
Cdd:NF038007   2 LNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLsysqkiILR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:NF038007  82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  164 LLLLDEPLSALD-KHLRGQMQDfLKELQRDlGITFVHVTHDQsEALALSSLVVIMRDGRL 222
Cdd:NF038007 162 LLLADEPTGNLDsKNARAVLQQ-LKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

23-209

1.09e-32

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 1.09e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVsisgvdvtdRAARARDVGMVFQNYAL---FPh 99
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  100 LTARENVEY----PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:NF040873  72 LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 14028433  176 KHLRGQMQDFLKELQRDlGITFVHVTHDQSEALA 209
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

13-170

1.54e-15

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 1.54e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARdvgmVFQ 92
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA----VCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   93 NYA---------LFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:NF033858  77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156


                 ....*..
gi 14028433  164 LLLLDEP 170
Cdd:NF033858 157 LLILDEP 163

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

7-207

1.47e-14

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 1.47e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    7 DCGSPPAIQISRLKKCYG---AVEvlrGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG--VDVTDRA 81
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGdftAVD---HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIA 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   82 ARARdVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYR 161
Cdd:NF033858 337 TRRR-VGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 14028433  162 PKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGIT-FVHvTHDQSEA 207
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVTiFIS-THFMNEA 461

40850658_otr

NF000106

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

1-238

5.40e-14

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.08 E-value: 5.40e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    1 MSNASKDCGSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGsgkttllriiagfASVSEGTVS--ISGVDV- 77
Cdd:NF000106   1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G-------------AA**RGALPahV*GPDAg 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   78 ----------TDRAARARDVGMVFQ-NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSG 146
Cdd:NF000106  68 rrpwrf*twcANRRALRRTIG*HRPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  147 GQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226

                        250
                 ....*....|..
gi 14028433  227 SPEQIYLEPNSR 238
Cdd:NF000106 227 KVDELKTKVGGR 238

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

44-223

3.13e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 3.13e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     44 FLGPSGSGKTTLLRIIAGFASVSEGTVSIsgVDVTDRAARARDVGMVFQNYalfphltarenveyplkvrrlpreerrrr 123
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVG----------------------------- 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    124 aleylervhlsewadRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQD-----FLKELQRDLGITFV 198
Cdd:smart00382  56 ---------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEKNLTVI 120

                          170       180
                   ....*....|....*....|....*
gi 14028433    199 HVTHDQSEalALSSLVVIMRDGRLE 223
Cdd:smart00382 121 LTTNDEKD--LGPALLRRRFDRRIV 143

GguA

NF040905

sugar ABC transporter ATP-binding protein;

21-221

1.31e-07

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 1.31e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   21 KCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF--ASVSEGTVSISGVDVTDRAARA-RDVGMVF--QNYA 95
Cdd:NF040905   9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDsEALGIVIihQELA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   96 LFPHLTARENV----EyPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPL 171
Cdd:NF040905  89 LIPYLSIAENIflgnE-RAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 14028433  172 SALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:NF040905 168 AALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216

GguA

NF040905

sugar ABC transporter ATP-binding protein;

144-170

1.76e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.76e-03

                         10        20
                 ....*....|....*....|....*..
gi 14028433  144 LSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431

Name

Accession

Description

Interval

E-value

PotA

COG3842

ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...

10-365

6.10e-155

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 439.53 E-value: 6.10e-155

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGM 89
Cdd:COG3842   2 AMPALELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPEKRNVGM 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:COG3842  82 VFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPRVLLLDE 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNI 249
Cdd:COG3842 162 PLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEALALADRIAVMNDGRIEQVGTPEEIYERPATRFVADFIGEANL 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 250 VCCSVTARNGRLATVKlgdgtevGVPIPAGVTERLGVGEKSLLLLRPEKAetgyRI--DTSVVAMSGPVLSTTFMGTHYQ 327
Cdd:COG3842 242 LPGTVLGDEGGGVRTG-------GRTLEVPADAGLAAGGPVTVAIRPEDI----RLspEGPENGLPGTVEDVVFLGSHVR 310

                       330       340       350       360
                ....*....|....*....|....*....|....*....|...
gi 14028433 328 VVFSTRHG-EITAHLNN----DYAPGQSVDVAWRAGNLIVLPA 365
Cdd:COG3842 311 YRVRLGDGqELVVRVPNraalPLEPGDRVGLSWDPEDVVVLPA 353

MalK

COG3839

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

13-362

3.88e-131

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 379.03 E-value: 3.88e-131

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQ 92
Cdd:COG3839   3 SLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKDRNIAMVFQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:COG3839  83 SYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDEPLS 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 173 ALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNS--NIV 250
Cdd:COG3839 163 NLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPANLFVAGFIGSPpmNLL 242

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 251 CCSVTARNGRLAtvklgdgtevGVPIPAGVTERLGVGEKSLLLLRPEKAETGyriDTSVVAMSGPVLSTTFMGTHYQVVF 330
Cdd:COG3839 243 PGTVEGGGVRLG----------GVRLPLPAALAAAAGGEVTLGIRPEHLRLA---DEGDGGLEATVEVVEPLGSETLVHV 309

                       330       340       350
                ....*....|....*....|....*....|....
gi 14028433 331 STRHGEITAHLNND--YAPGQSVDVAWRAGNLIV 362
Cdd:COG3839 310 RLGGQELVARVPGDtrLRPGDTVRLAFDPERLHL 343

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

11-364

3.12e-115

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 339.62 E-value: 3.12e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   11 PPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMV 90
Cdd:PRK09452  12 SPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAENRHVNTV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:PRK09452  92 FQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDES 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  171 LSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIV 250
Cdd:PRK09452 172 LSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARFIGEINIF 251

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  251 CCSVTARNGR---LATVKlgdgtevGVPIPAGVTERLGVGEKSLLLLRPEKAETGYRID-TSVVAMSGPVLSTTFMGTHY 326
Cdd:PRK09452 252 DATVIERLDEqrvRANVE-------GRECNIYVNFAVEPGQKLHVLLRPEDLRVEEINDdEHAEGLIGYVRERNYKGMTL 324

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*...
gi 14028433  327 QVVFSTRHG----------EITAHLnnDYAPGQSVDVAWRAGNLIVLP 364
Cdd:PRK09452 325 DSVVELENGkmvmvseffnEDDPDF--DHSLGQKVAVTWVEGWEVVLA 370

ABC_PotA_N

cd03300

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...

14-245

2.49e-110

Pssm-ID: 213267 [Multi-domain] Cd Length: 232 Bit Score: 321.88 E-value: 2.49e-110

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:cd03300   1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPHKRPVNTVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03300  81 YALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGA 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIG 245
Cdd:cd03300 161 LDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFIG 232

potA

TIGR01187

spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...

45-363

6.31e-105

Pssm-ID: 162242 [Multi-domain] Cd Length: 325 Bit Score: 311.35 E-value: 6.31e-105

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    45 LGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRA 124
Cdd:TIGR01187   2 LGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVTNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPRAEIKPRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   125 LEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQ 204
Cdd:TIGR01187  82 LEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLGITFVFVTHDQ 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   205 SEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVccsvtarngRLATVKLGDGTEV---GVPIPAGVT 281
Cdd:TIGR01187 162 EEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPANLFVARFIGEINVF---------EATVIERKSEQVVlagVEGRRCDIY 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   282 ERLGV--GEKSLLLLRPEKAE-TGYRIDTSVVAMSGPVLSTTFMGTHYQVVFSTRHGEIT--------AHLNNDYAPGQS 350
Cdd:TIGR01187 233 TDVPVekDQPLHVVLRPEKIViEEEDEANSSNAIIGHVIDITYLGMTLEVHVRLETGQKVlvseffneDDPHMSPSIGDR 312

                         330
                  ....*....|...
gi 14028433   351 VDVAWRAGNLIVL 363
Cdd:TIGR01187 313 VGLTWHPGSEVVL 325

CysA

COG1118

ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...

14-362

1.61e-104

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 311.31 E-value: 1.61e-104

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDVGMVFQ 92
Cdd:COG1118   3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRERRVGFVFQ 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:COG1118  83 HYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPEVLLLDEPFG 162

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 173 ALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVcc 252
Cdd:COG1118 163 ALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPATPFVARFLGCVNVL-- 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 253 SVTARNGRLATVklGDGTEVGVPIPAGVTErLGVGEKSLLLLRPEKAETGYRIDtsvvamsgpVLSTTFMGTHYQVVFST 332
Cdd:COG1118 241 RGRVIGGQLEAD--GLTLPVAEPLPDGPAV-AGVRPHDIEVSREPEGENTFPAT---------VARVSELGPEVRVELKL 308

                       330       340       350
                ....*....|....*....|....*....|....*....
gi 14028433 333 RHGE---ITAHL------NNDYAPGQSVDVAWRAGNLIV 362
Cdd:COG1118 309 EDGEgqpLEAEVtkeawaELGLAPGDPVYLRPRPARVFL 347

ABC_Carb_Solutes_like

cd03259

ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...

14-226

2.82e-102

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: 300.59 E-value: 2.82e-102

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:cd03259   1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPERRNIGMVFQD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03259  81 YALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 14028433 174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:cd03259 161 LDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

21-329

1.11e-95

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 288.93 E-value: 1.11e-95

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   21 KCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHL 100
Cdd:PRK11432  14 KRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQQRDICMVFQSYALFPHM 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  101 TARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRG 180
Cdd:PRK11432  94 SLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFDEPLSNLDANLRR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  181 QMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVccsvtarNGR 260
Cdd:PRK11432 174 SMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASFMGDANIF-------PAT 246

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  261 LAtvklGDGTEVG---VPIPAGVTERLGVGEkSLLLLRPEK---AETGYRidtsvvAMSGPVLSTTFMGTHYQVV 329
Cdd:PRK11432 247 LS----GDYVDIYgyrLPRPAAFAFNLPDGE-CTVGVRPEAitlSEQGEE------SQRCTIKHVAYMGPQYEVT 310

PhnT2

TIGR03265

putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...

12-364

5.85e-94

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

Pssm-ID: 274496 [Multi-domain] Cd Length: 353 Bit Score: 284.62 E-value: 5.85e-94

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVF 91
Cdd:TIGR03265   3 PYLSIDNIRKRFGAFTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGGRDITRLPPQKRDYGIVF 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    92 QNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPL 171
Cdd:TIGR03265  83 QSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALATSPGLLLLDEPL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   172 SALD----KHLRGQMqdflKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNS 247
Cdd:TIGR03265 163 SALDarvrEHLRTEI----RQLQRRLGVTTIMVTHDQEEALSMADRIVVMNHGVIEQVGTPQEIYRHPATPFVADFVGEV 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   248 NIvccsVTARNGRLATVKLGDGTEVGVPipagvtERLGVGEKSLLLLRPEKAetgyRIDTSVVA---MSGPVLSTTFMGT 324
Cdd:TIGR03265 239 NW----LPGTRGGGSRARVGGLTLACAP------GLAQPGASVRLAVRPEDI----RVSPAGNAanlLLARVEDMEFLGA 304

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 14028433   325 HYQVVFSTRH-------GEITAHLNNDYA--PGQSVDVAWRAGNLIVLP 364
Cdd:TIGR03265 305 FYRLRLRLEGlpgqalvADVSASEVERLGirAGQPIWIELPAERLRAFA 353

ABC_CysA_sulfate_importer

cd03296

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...

13-246

2.40e-90

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: 271.13 E-value: 2.40e-90

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQ 92
Cdd:cd03296   2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQERNVGFVFQ 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRR----ALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:cd03296  82 HYALFRHMTVFDNVAFGLRVKPRSERPPEAEirakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGN 246
Cdd:cd03296 162 EPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFVYSFLGE 239

TauB

COG1116

ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...

9-222

1.54e-87

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 264.64 E-value: 1.54e-87

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   9 GSPPAIQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTdraARA 84
Cdd:COG1116   3 AAAPALELRGVSKRFptggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT---GPG 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 RDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:COG1116  80 PDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPEV 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 165 LLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIM--RDGRL 222
Cdd:COG1116 160 LLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEAVFLADRVVVLsaRPGRI 219

ABC_MalK_N

cd03301

The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...

14-226

3.74e-87

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: 262.19 E-value: 3.74e-87

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:cd03301   1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRDIAMVFQN 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03301  81 YALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSN 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|...
gi 14028433 174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:cd03301 161 LDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQIQQIG 213

3a0106s01

TIGR00968

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

14-250

2.12e-86

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

Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 260.89 E-value: 2.12e-86

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:TIGR00968   1 IEIANISKRFGSFQALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQDATRVHARDRKIGFVFQH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:TIGR00968  81 YALFKHLTVRDNIAFGLEIRKHPKAKIKARVEELLELVQLEGLGDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433   174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIV 250
Cdd:TIGR00968 161 LDAKVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPFVMSFLGEVNVL 237

ugpC

PRK11650

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

13-297

3.44e-84

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 259.39 E-value: 3.44e-84

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVF 91
Cdd:PRK11650   3 GLKLQAVRKSYdGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRDIAMVF 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   92 QNYALFPHLTARENVEYPLKVRRLPREERRrraleylERV-------HLSEWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:PRK11650  83 QNYALYPHMSVRENMAYGLKIRGMPKAEIE-------ERVaeaarilELEPLLDRKPRELSGGQRQRVAMGRAIVREPAV 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  165 LLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFI 244
Cdd:PRK11650 156 FLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGVAEQIGTPVEVYEKPASTFVASFI 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  245 GNS--NIVCCSVTARNGRLAtvkLGDgtevGVPIPAGVTERLGVGEKSLLLLRPE 297
Cdd:PRK11650 236 GSPamNLLDGRVSADGAAFE---LAG----GIALPLGGGYRQYAGRKLTLGIRPE 283

ABC_NrtD_SsuB_transporters

cd03293

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...

14-222

1.64e-82

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: 250.47 E-value: 1.64e-82

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYG----AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAaraRDVGM 89
Cdd:cd03293   1 LEVRNVSKTYGggggAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPG---PDRGY 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:cd03293  78 VFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVLLLDE 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433 170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIM--RDGRL 222
Cdd:cd03293 158 PFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLsaRPGRI 212

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

13-248

6.44e-82

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 253.47 E-value: 6.44e-82

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQ 92
Cdd:PRK10851   2 SIEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDRKVGFVFQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   93 NYALFPHLTARENVEYPLKV----RRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:PRK10851  82 HYALFRHMTVFDNIAFGLTVlprrERPNAAAIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQILLLD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  169 EPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSN 248
Cdd:PRK10851 162 EPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATRFVLEFMGEVN 241

ABC_ModC_like

cd03299

ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...

14-249

7.39e-81

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: 246.86 E-value: 7.39e-81

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEvLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:cd03299   1 LKVENLSKDWKEFK-LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPEKRDISYVPQN 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03299  80 YALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNI 249
Cdd:cd03299 160 LDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFLGFNNI 235

LolD

COG1136

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

11-223

1.29e-77

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 238.02 E-value: 1.29e-77

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  11 PPAIQISRLKKCYG----AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT-----DRA 81
Cdd:COG1136   2 SPLLELRNLTKSYGtgegEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISslserELA 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  82 A-RARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVY 160
Cdd:COG1136  82 RlRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVN 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 161 RPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQsEALALSSLVVIMRDGRLE 223
Cdd:COG1136 162 RPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDP-ELAARADRVIRLRDGRIV 223

GlnQ

COG1126

ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...

14-237

3.56e-77

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 237.58 E-value: 3.56e-77

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-----RAARaRDVG 88
Cdd:COG1126   2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDskkdiNKLR-RKVG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  89 MVFQNYALFPHLTARENVEY-PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:COG1126  81 MVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEPKVMLF 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 168 DEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNS 237
Cdd:COG1126 161 DEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQH 229

tungstate_WtpC

NF040840

tungstate ABC transporter ATP-binding protein WtpC;

29-297

1.26e-75

tungstate ABC transporter ATP-binding protein WtpC;

Pssm-ID: 468779 [Multi-domain] Cd Length: 347 Bit Score: 237.28 E-value: 1.26e-75

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEY 108
Cdd:NF040840  16 LRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDGKDITNLPPEKRGIAYVYQNYMLFPHKTVFENIAF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  109 PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKE 188
Cdd:NF040840  96 GLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEPKLLLLDEPLSALDVQTRDELIREMKR 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  189 LQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVccSVTARNGRLATVKLGD 268
Cdd:NF040840 176 WHREFGFTAIHVTHNFEEALSLADRVGIMLNGRLSQVGDVREVFRRPKNEFVARFVGFENII--EGVAEKGGEGTILDTG 253

                        250       260
                 ....*....|....*....|....*....
gi 14028433  269 GTEVGVPIPAGVTERLGVgeksllllRPE 297
Cdd:NF040840 254 NIKIELPEEKKGKVRIGI--------RPE 274

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

21-328

1.18e-74

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 235.69 E-value: 1.18e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   21 KCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHL 100
Cdd:PRK11000  11 KAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERGVGMVFQSYALYPHL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  101 TARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRG 180
Cdd:PRK11000  91 SVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAALRV 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  181 QMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNS--NIVCCSVTARN 258
Cdd:PRK11000 171 QMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFVAGFIGSPkmNFLPVKVTATA 250

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  259 GRLATVKLGDGTEVGVPIP-AGVTerlgVGEKSLLLLRPEKAETGyriDTSVVAMSGPVLSTTFMGTHYQV 328
Cdd:PRK11000 251 IEQVQVELPNRQQVWLPVEgRGVQ----VGANMSLGIRPEHLLPS---DIADVTLEGEVQVVEQLGNETQI 314

OpuBA

COG1125

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

14-245

3.09e-74

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

Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 232.29 E-value: 3.09e-74

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMV 90
Cdd:COG1125   2 IEFENVTKRYpDGTVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVElrRRIGYV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHL--SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:COG1125  82 IQQIGLFPHMTVAENIATVPRLLGWDKERIRARVDELLELVGLdpEEYRDRYPHELSGGQQQRVGVARALAADPPILLMD 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIG 245
Cdd:COG1125 162 EPFGALDPITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFVG 238

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

12-363

6.96e-74

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 233.96 E-value: 6.96e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVF 91
Cdd:PRK11607  18 PLLEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRPINMMF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   92 QNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPL 171
Cdd:PRK11607  98 QSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPM 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  172 SALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVC 251
Cdd:PRK11607 178 GALDKKLRDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRYSAEFIGSVNVFE 257

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  252 CSVTARN---------GRLATVKLGDGTEV--GVPIpagvterlgvgeksLLLLRPEKAETGYRI--DTSVVAMsGPVLS 318
Cdd:PRK11607 258 GVLKERQedglvidspGLVHPLKVDADASVvdNVPV--------------HVALRPEKIMLCEEPpaDGCNFAV-GEVIH 322

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14028433  319 TTFMG--THYQVVFSTRHgEITAHLNNDY-----AP--GQSVDVAWRAGNLIVL 363
Cdd:PRK11607 323 IAYLGdlSIYHVRLKSGQ-MISAQLQNAHryrkgLPtwGDEVRLCWEADSCVVL 375

ABC_MJ0796_LolCDE_FtsE

cd03255

ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...

14-222

4.19e-73

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: 226.22 E-value: 4.19e-73

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGA----VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT-----DRAA-R 83
Cdd:cd03255   1 IELKNLSKTYGGggekVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISklsekELAAfR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:cd03255  81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRL 222
Cdd:cd03255 161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218

ABC_Pro_Gly_Betaine

cd03294

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...

15-244

8.27e-73

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: 227.53 E-value: 8.27e-73

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  15 QISRLKKCYGAVevlRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARDVG 88
Cdd:cd03294  29 EILKKTGQTVGV---NDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAmsrkelRELRRKKIS 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  89 MVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:cd03294 106 MVFQSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMD 185

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFI 244
Cdd:cd03294 186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFF 261

ProV

COG4175

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

46-248

9.16e-73

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

Pssm-ID: 443334 [Multi-domain] Cd Length: 389 Bit Score: 231.15 E-value: 9.16e-73

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  46 GPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREE 119
Cdd:COG4175  60 GLSGSGKSTLVRCLNRLIEPTAGEVLIDGEDITKlskkelRELRRKKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAE 139

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 120 RRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVH 199
Cdd:COG4175 140 RRERAREALELVGLAGWEDSYPDELSGGMQQRVGLARALATDPDILLMDEAFSALDPLIRREMQDELLELQAKLKKTIVF 219

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14028433 200 VTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSN 248
Cdd:COG4175 220 ITHDLDEALRLGDRIAIMKDGRIVQIGTPEEILTNPANDYVADFVEDVD 268

PhnT

TIGR03258

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding ...

9-250

5.07e-71

2-aminoethylphosphonate ABC transport system, ATP-binding component PhnT; This ATP-binding component of an ABC transport system is found in Salmonella and Burkholderia lineages in the vicinity of enzymes for the breakdown of 2-aminoethylphosphonate.

Pssm-ID: 132302 [Multi-domain] Cd Length: 362 Bit Score: 226.03 E-value: 5.07e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     9 GSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF--ASVSEGTVSISGVDVTDRAARARD 86
Cdd:TIGR03258   1 GACGGIRIDHLRVAYGANTVLDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFvkAAGLTGRIAIADRDLTHAPPHKRG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    87 VGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLL 166
Cdd:TIGR03258  81 LALLFQNYALFPHLKVEDNVAFGLRAQKMPKADIAERVADALKLVGLGDAAAHLPAQLSGGMQQRIAIARAIAIEPDVLL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   167 LDEPLSALDKHLRGQMQDFLKELQRDL-GITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIG 245
Cdd:TIGR03258 161 LDEPLSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLG 240


                  ....*
gi 14028433   246 NSNIV 250
Cdd:TIGR03258 241 AANIL 245

ABC_OpuCA_Osmoprotection

cd03295

ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...

14-245

8.50e-71

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

Pssm-ID: 213262 [Multi-domain] Cd Length: 242 Bit Score: 221.41 E-value: 8.50e-71

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVE-VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMV 90
Cdd:cd03295   1 IEFENVTKRYGGGKkAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIReqDPVELRRKIGYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHL--SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:cd03295  81 IQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAADPPLLLMD 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIG 245
Cdd:cd03295 161 EPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVG 237

ABC_Class3

cd03229

ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...

14-221

5.75e-70

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: 216.67 E-value: 5.75e-70

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD----RAARARDVGM 89
Cdd:cd03229   1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDledeLPPLRRRIGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYALFPHLTARENVEYPlkvrrlpreerrrraleylervhlsewadrypreLSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:cd03229  81 VFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDVLLLDE 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14028433 170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:cd03229 127 PTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178

ABC_HisP_GlnQ

cd03262

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...

14-222

1.45e-67

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: 212.00 E-value: 1.45e-67

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA----RDVGM 89
Cdd:cd03262   1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNInelrQKVGM 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYALFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:cd03262  81 VFQQFNLFPHLTVLENItLAPIKVKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFD 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03262 161 EPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213

MlaF

COG1127

ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...

10-231

1.29e-66

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: 210.61 E-value: 1.29e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAAR 83
Cdd:COG1127   2 SEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekelYELR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  84 ARdVGMVFQNYALFPHLTARENVEYPLK-------------VRRlpreerrrraleYLERVHLSEWADRYPRELSGGQQQ 150
Cdd:COG1127  82 RR-IGMLFQGGALFDSLTVFENVAFPLRehtdlseaeirelVLE------------KLELVGLPGAADKMPSELSGGMRK 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 151 RVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:COG1127 149 RVALARALALDPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEE 228


                .
gi 14028433 231 I 231
Cdd:COG1127 229 L 229

CcmA

COG1131

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

14-234

1.51e-66

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 209.92 E-value: 1.51e-66

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARD-VGMVFQ 92
Cdd:COG1131   1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRrIGYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:COG1131  81 EPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDEPTS 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433 173 ALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI---YLE 234
Cdd:COG1131 161 GLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDELkarLLE 224

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

10-235

1.71e-64

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: 213.23 E-value: 1.71e-64

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCY-----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT-----D 79
Cdd:COG1123 257 AEPLLEVRNLSKRYpvrgkGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTklsrrS 336

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  80 RAARARDVGMVFQN--YALFPHLTARENVEYPLKVRRLPREERRRRA-LEYLERVHLS-EWADRYPRELSGGQQQRVALA 155
Cdd:COG1123 337 LRELRRRVQMVFQDpySSLNPRMTVGDIIAEPLRLHGLLSRAERRERvAELLERVGLPpDLADRYPHELSGGQRQRVAIA 416

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 156 RSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:COG1123 417 RALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANP 496

proV

TIGR01186

glycine betaine/L-proline transport ATP binding subunit; This model describes the glycine ...

21-306

3.70e-64

glycine betaine/L-proline transport ATP binding subunit; This model describes 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 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. Functionally, this transport system is involved in osmoregulation. Under conditions of stress, the organism recruits these transport system to accumulate glycine betaine and other solutes which offer osmo-protection. It has been demonstrated that glycine betaine uptake is accompanied by symport with sodium ions. The locus has been named variously as proU or opuA. A gene library from L.lactis functionally complements an E.coli proU mutant. The comlementing locus is similar to a opuA locus in B.sutlis. This clarifies the differences in nomenclature. [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 130254 [Multi-domain] Cd Length: 363 Bit Score: 208.17 E-value: 3.70e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    21 KCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARDVGMVFQNY 94
Cdd:TIGR01186   1 KKTGGKKGVNDADLAIAKGEIFVIMGLSGSGKSTTVRMLNRLIEPTAGQIFIDGENIMKqspvelREVRRKKIGMVFQQF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    95 ALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:TIGR01186  81 ALFPHMTILQNTSLGPELLGWPEQERKEKALELLKLVGLEEYEHRYPDELSGGMQQRVGLARALAAEPDILLMDEAFSAL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   175 DKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVCCSV 254
Cdd:TIGR01186 161 DPLIRDSMQDELKKLQATLQKTIVFITHDLDEAIRIGDRIVIMKAGEIVQVGTPDEILRNPANEYVEEFIGKVDLSQVFD 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 14028433   255 TARNGRLATVKLgdgtevgVPIPAGVTERlgvgeKSLLLLRPEKAETGYRID 306
Cdd:TIGR01186 241 AERIAQRMNTGP-------ITKTADKGPR-----SALQLMRDERVDSLYVVD 280

ABC_ModC_molybdenum_transporter

cd03297

ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...

32-226

1.27e-62

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: 199.44 E-value: 1.27e-62

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  32 LDLVIPEGsYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDR------AARARDVGMVFQNYALFPHLTAREN 105
Cdd:cd03297  17 IDFDLNEE-VTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSrkkinlPPQQRKIGLVFQQYALFPHLNVREN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 106 VEYPLKVRRLPREERRRRALeyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDF 185
Cdd:cd03297  96 LAFGLKRKRNREDRISVDEL--LDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPE 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 14028433 186 LKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:cd03297 174 LKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

14-244

2.93e-61

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 196.85 E-value: 2.93e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDV----GM 89
Cdd:PRK09493   2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIrqeaGM 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQNYALFPHLTARENVEY-PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:PRK09493  82 VFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKLMLFD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  169 EPLSALDKHLRGQ----MQDFLKElqrdlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFI 244
Cdd:PRK09493 162 EPTSALDPELRHEvlkvMQDLAEE-----GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQEFL 236

ThiQ

COG3840

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

14-245

3.83e-61

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 196.13 E-value: 3.83e-61

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGaVEVLRgLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:COG3840   2 LRLDDLTYRYG-DFPLR-FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAERPVSMLFQE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:COG3840  80 NNLFPHLTVAQNIGLGLRPGLKLTAEQRAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSA 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 174 LDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIG 245
Cdd:COG3840 160 LDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAYLG 231

DppF

COG1124

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

13-231

1.13e-60

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: 195.41 E-value: 1.13e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  13 AIQISRLKKCYGA----VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RD 86
Cdd:COG1124   1 MLEVRNLSVSYGQggrrVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAfrRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 VGMVFQNY--ALFPHLTARENVEYPLKVRRLPREERRRRALeyLERVHL-SEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:COG1124  81 VQMVFQDPyaSLHPRHTVDRILAEPLRIHGLPDREERIAEL--LEQVGLpPSFLDRYPHQLSGGQRQRVAIARALILEPE 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG1124 159 LLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADL 226

ModC

COG4148

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...

33-270

2.17e-60

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: 198.40 E-value: 2.17e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  33 DLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR------ARDVGMVFQNYALFPHLTARENV 106
Cdd:COG4148  19 DFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGiflpphRRRIGYVFQEARLFPHLSVRGNL 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 107 EYPLKVRRLPREERRrraleyLERV-------HLsewADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:COG4148  99 LYGRKRAPRAERRIS------FDEVvellgigHL---LDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIVCCSVTARNG 259
Cdd:COG4148 170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGEEAGSVLEATVAAHDP 249

                       250
                ....*....|...
gi 14028433 260 R--LATVKLGDGT 270
Cdd:COG4148 250 DygLTRLALGGGR 262

NatA

COG4555

ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...

14-231

2.51e-60

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: 194.31 E-value: 2.51e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARAR-DVGMVFQ 92
Cdd:COG4555   2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARrQIGVLPD 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:COG4555  82 ERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTN 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433 173 ALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG4555 162 GLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219

ABC_Org_Solvent_Resistant

cd03261

ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...

14-231

3.88e-60

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: 193.49 E-value: 3.88e-60

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARdV 87
Cdd:cd03261   1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGlseaelYRLRRR-M 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  88 GMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEY-LERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLL 166
Cdd:cd03261  80 GMLFQSGALFDSLTVFENVAFPLREHTRLSEEEIREIVLEkLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELLL 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433 167 LDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:cd03261 160 YDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEEL 224

ABC_NikE_OppD_transporters

cd03257

ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...

14-222

2.01e-59

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: 191.57 E-value: 2.01e-59

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-----RAARA 84
Cdd:cd03257   2 LEVKNLSVSFptggGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKlsrrlRKIRR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 RDVGMVFQNY--ALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHL---SEWADRYPRELSGGQQQRVALARSLV 159
Cdd:cd03257  82 KEIQMVFQDPmsSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLLLVGVglpEEVLNRYPHELSGGQRQRVAIARALA 161

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 160 YRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03257 162 LNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKI 224

YbbA

COG4181

Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...

8-224

1.13e-58

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: 189.95 E-value: 1.13e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   8 CGSPPAIQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD---- 79
Cdd:COG4181   3 SSSAPIIELRGLTKTVgtgaGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAlded 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  80 -RAA-RARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRAleYLERVHLSEWADRYPRELSGGQQQRVALARS 157
Cdd:COG4181  83 aRARlRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRDARARARA--LLERVGLGHRLDHYPAQLSGGEQQRVALARA 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 158 LVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQ 224
Cdd:COG4181 161 FATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALA-ARCDRVLRLRAGRLVE 226

TauB

COG4525

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

24-242

3.93e-58

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 189.30 E-value: 3.93e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAArarDVGMVFQNYALFPHLTAR 103
Cdd:COG4525  18 QPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGA---DRGVVFQKDALLPWLNVL 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 104 ENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQ 183
Cdd:COG4525  95 DNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQMQ 174

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 184 DFLKELQRDLGITFVHVTHDQSEALALSSLVVIM--RDGRLEqvgspEQIYLEPNSRFVAG 242
Cdd:COG4525 175 ELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMspGPGRIV-----ERLELDFSRRFLAG 230

AbcC

COG1135

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

14-286

4.22e-58

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 191.83 E-value: 4.22e-58

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAAR 83
Cdd:COG1135   2 IELENLSKTFptkgGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTAlserelRAAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  84 aRDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:COG1135  82 -RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGF 243
Cdd:COG1135 161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 14028433 244 IG--------NSNIVCCSVTARNGRLATVKLgDGTEVGVPIPAGVTERLGV 286
Cdd:COG1135 241 LPtvlndelpEELLARLREAAGGGRLVRLTF-VGESADEPLLSELARRFGV 290

ABC_MetN_methionine_transporter

cd03258

ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...

14-235

1.06e-57

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: 187.40 E-value: 1.06e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYG----AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAAR 83
Cdd:cd03258   2 IELKNVSKVFGdtggKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLlsgkelRKAR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  84 aRDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:cd03258  82 -RRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:cd03258 161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANP 232

EcfA2

COG1122

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...

14-232

1.29e-57

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: 186.77 E-value: 1.29e-57

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMV 90
Cdd:COG1122   1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRElrRKVGLV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQN--YALFpHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:COG1122  81 FQNpdDQLF-APTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:COG1122 160 EPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVF 222

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

13-226

1.58e-57

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 187.14 E-value: 1.58e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG------VDVTDRAARA-- 84
Cdd:PRK11124   2 SIQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsKTPSDKAIRElr 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   85 RDVGMVFQNYALFPHLTAREN-VEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:PRK11124  82 RNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMMEPQ 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433  164 LLLLDEPLSALDKHLRGQMQDFLKELQrDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:PRK11124 162 VLLFDEPTAALDPEITAQIVSIIRELA-ETGITQVIVTHEVEVARKTASRVVYMENGHIVEQG 223

ABC_cobalt_CbiO_domain1

cd03225

First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...

24-221

7.57e-56

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: 181.90 E-value: 7.57e-56

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD--RAARARDVGMVFQN--YALFpH 99
Cdd:cd03225  12 GARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKlsLKELRRKVGLVFQNpdDQFF-G 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 100 LTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:cd03225  91 PTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGR 170

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 14028433 180 GQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:cd03225 171 RELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211

HisP

COG4598

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

10-247

2.08e-55

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

Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 182.31 E-value: 2.08e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV------------ 77
Cdd:COG4598   5 APPALEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIrlkpdrdgelvp 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  78 TDRAA----RARdVGMVFQNYALFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRV 152
Cdd:COG4598  85 ADRRQlqriRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 153 ALARSLVYRPKLLLLDEPLSALDKHLRGQ----MQDFLKElqrdlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSP 228
Cdd:COG4598 164 AIARALAMEPEVMLFDEPTSALDPELVGEvlkvMRDLAEE-----GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPP 238

                       250
                ....*....|....*....
gi 14028433 229 EQIYLEPNSRFVAGFIGNS 247
Cdd:COG4598 239 AEVFGNPKSERLRQFLSSS 257

ABC_PstB_phosphate_transporter

cd03260

ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...

14-231

4.97e-55

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: 180.07 E-value: 4.97e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASV-----SEGTVSISGVDV----TDRAARA 84
Cdd:cd03260   1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNDLipgapDEGEVLLDGKDIydldVDVLELR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 RDVGMVFQNYALFPhLTARENVEYPLKVRRLPREERRRRALEY-LERVHLS-EWADR-YPRELSGGQQQRVALARSLVYR 161
Cdd:cd03260  81 RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKLKEELDERVEEaLRKAALWdEVKDRlHALGLSGGQQQRLCLARALANE 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 162 PKLLLLDEPLSALDKHLRGQMQDFLKELQRDlgITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:cd03260 160 PEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227

FepC

COG1120

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...

13-231

5.48e-55

ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion transport and metabolism, Coenzyme transport and metabolism];

Pssm-ID: 440737 [Multi-domain] Cd Length: 254 Bit Score: 181.01 E-value: 5.48e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD--RAARARDVGMV 90
Cdd:COG1120   1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASlsRRELARRIAYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENVE---YP-LKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLL 166
Cdd:COG1120  81 PQEPPAPFGLTVRELVAlgrYPhLGLFGRPSAEDREAVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLLL 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 167 LDEPLSALDkhLRGQMQ--DFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG1120 161 LDEPTSHLD--LAHQLEvlELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEV 225

ArtP

COG4161

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

13-222

7.40e-55

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 180.21 E-value: 7.40e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG------VDVTDRAARA-- 84
Cdd:COG4161   2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLlr 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 RDVGMVFQNYALFPHLTAREN-VEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:COG4161  82 QKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMMEPQ 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQrDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG4161 162 VLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRI 219

PhnC

COG3638

ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...

12-231

1.30e-54

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 179.87 E-value: 1.30e-54

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  12 PAIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARa 84
Cdd:COG3638   1 PMLELRNLSKRYpGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTAlrgralRRLR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 RDVGMVFQNYALFPHLTARENV----------------EYPlkvrrlprEERRRRALEYLERVHLSEWADRYPRELSGGQ 148
Cdd:COG3638  80 RRIGMIFQQFNLVPRLSVLTNVlagrlgrtstwrsllgLFP--------PEDRERALEALERVGLADKAYQRADQLSGGQ 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 149 QQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSP 228
Cdd:COG3638 152 QQRVAIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPP 231


                ...
gi 14028433 229 EQI 231
Cdd:COG3638 232 AEL 234

ABC_DR_subfamily_A

cd03230

ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...

14-222

1.66e-54

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: 176.82 E-value: 1.66e-54

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARAR-DVGMVFQ 92
Cdd:cd03230   1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKrRIGYLPE 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYplkvrrlpreerrrraleylervhlsewadryprelSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:cd03230  81 EPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDPELLILDEPTS 124

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 14028433 173 ALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03230 125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173

FtsE

COG2884

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

14-222

8.92e-54

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 176.78 E-value: 8.92e-54

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCY-GAVEVLRGLDLVIPEGSYTtFL-GPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA-----RD 86
Cdd:COG2884   2 IRFENVSKRYpGGREALSDVSLEIEKGEFV-FLtGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipylrRR 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 VGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLL 166
Cdd:COG2884  81 IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLL 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 167 LDEPLSALDKHLRGQMQDFLKELQRdLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG2884 161 ADEPTGNLDPETSWEIMELLEEINR-RGTTVLIATHDLELVDRMPKRVLELEDGRL 215

ABC_ThiQ_thiamine_transporter

cd03298

ATP-binding cassette domain of the thiamine transport system; Part of the ...

32-222

2.20e-50

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: 167.67 E-value: 2.20e-50

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  32 LDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEYPLK 111
Cdd:cd03298  17 FDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRPVSMLFQENNLFAHLTVEQNVGLGLS 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 112 VRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQR 191
Cdd:cd03298  97 PGLKLTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHA 176

                       170       180       190
                ....*....|....*....|....*....|.
gi 14028433 192 DLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03298 177 ETKMTVLMVTHQPEDAKRLAQRVVFLDNGRI 207

ABC_DrrA

cd03265

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...

14-231

1.91e-49

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: 165.62 E-value: 1.91e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARAR-DVGMVFQ 92
Cdd:cd03265   1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRrRIGIVFQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:cd03265  81 DLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTI 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433 173 ALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:cd03265 161 GLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219

GsiA

COG1123

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...

12-235

2.89e-49

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: 173.17 E-value: 2.89e-49

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  12 PAIQISRLKKCY--GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAG---FASVSEGTVSISGVDVTD--RAARA 84
Cdd:COG1123   3 PLLEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGllpHGGRISGEVLLDGRDLLElsEALRG 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 RDVGMVFQN--YALFPhLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRP 162
Cdd:COG1123  83 RRIGMVFQDpmTQLNP-VTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 163 KLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:COG1123 162 DLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP 234

modC_ABC

TIGR02142

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...

32-297

3.80e-49

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: 168.75 E-value: 3.80e-49

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    32 LDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA------RDVGMVFQNYALFPHLTAREN 105
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppekRRIGYVFQEARLFPHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   106 VEYPLKvrRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDF 185
Cdd:TIGR02142  96 LRYGMK--RARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPY 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   186 LKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN----SRFVAGFIGNSNIVccSVTARNGrL 261
Cdd:TIGR02142 174 LERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDlpwlAREDQGSLIEGVVA--EHDQHYG-L 250

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 14028433   262 ATVKLGDGTEV--GVPIPAGVTERLGVGEK--SLLLLRPE 297
Cdd:TIGR02142 251 TALRLGGGHLWvpENLGPTGARLRLRVPARdvSLALQKPE 290

ntrCD

TIGR01184

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...

29-226

1.64e-48

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: 163.41 E-value: 1.64e-48

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAArarDVGMVFQNYALFPHLTARENVEY 108
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGP---DRMVVFQNYSLLPWLTVRENIAL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   109 PLK--VRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFL 186
Cdd:TIGR01184  78 AVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQEEL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 14028433   187 KELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:TIGR01184 158 MQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIG 197

LivG

COG0411

ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...

10-231

2.71e-48

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

Pssm-ID: 440180 [Multi-domain] Cd Length: 257 Bit Score: 163.67 E-value: 2.71e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARAR-DVG 88
Cdd:COG0411   1 SDPLLEVRGLTKRFGGLVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIaRLG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  89 MV--FQNYALFPHLTARENV---------EYPLKVRRLPREERRRRALEY------LERVHLSEWADRYPRELSGGQQQR 151
Cdd:COG0411  81 IArtFQNPRLFPELTVLENVlvaaharlgRGLLAALLRLPRARREEREAReraeelLERVGLADRADEPAGNLSYGQQRR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 152 VALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG0411 161 LEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEV 240

FetA

COG4619

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

14-222

4.12e-48

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 161.52 E-value: 4.12e-48

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVF 91
Cdd:COG4619   1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEwrRQVAYVP 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  92 QNYALFPHlTARENVEYPLKVRRLPREERRRRAleYLERVHLSEWA-DRYPRELSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:COG4619  81 QEPALWGG-TVRDNLPFPFQLRERKFDRERALE--LLERLGLPPDIlDKPVERLSGGERQRLALIRALLLQPDVLLLDEP 157

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14028433 171 LSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG4619 158 TSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209

ZnuC

COG1121

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

10-236

4.37e-47

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 160.25 E-value: 4.37e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARardVGM 89
Cdd:COG1121   3 MMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRARRR---IGY 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQNYAL---FPhLTARENVE---YP-LKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRP 162
Cdd:COG1121  80 VPQRAEVdwdFP-ITVRDVVLmgrYGrRGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDP 158

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433 163 KLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQvGSPEQIYLEPN 236
Cdd:COG1121 159 DLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRGLVAH-GPPEEVLTPEN 230

ABC_PhnC_transporter

cd03256

ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...

14-231

6.22e-47

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: 159.66 E-value: 6.22e-47

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGA-VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARaRD 86
Cdd:cd03256   1 IEVENLSKTYPNgKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKlkgkalRQLR-RQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 VGMVFQNYALFPHLTARENV-------EYPLKVRRLPREERRRRALEY-LERVHLSEWADRYPRELSGGQQQRVALARSL 158
Cdd:cd03256  80 IGMIFQQFNLIERLSVLENVlsgrlgrRSTWRSLFGLFPKEEKQRALAaLERVGLLDKAYQRADQLSGGQQQRVAIARAL 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 159 VYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:cd03256 160 MQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232

FtsE

TIGR02673

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...

14-221

2.40e-46

cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC transporter ATP-binding protein family. This protein, and its permease partner FtsX, localize to the division site. In a number of species, the ftsEX gene pair is located next to FtsY, the signal recognition particle-docking protein. [Cellular processes, Cell division]

Pssm-ID: 131721 [Multi-domain] Cd Length: 214 Bit Score: 157.41 E-value: 2.40e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA-----RDV 87
Cdd:TIGR02673   2 IEFHNVSKAYpGGVAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQlpllrRRI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    88 GMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:TIGR02673  82 GVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSPPLLLA 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 14028433   168 DEPLSALDKHLRGQMQDFLKELQRdLGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:TIGR02673 162 DEPTGNLDPDLSERILDLLKRLNK-RGTTVIVATHDLSLVDRVAHRVIILDDGR 214

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

9-222

2.43e-46

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 158.69 E-value: 2.43e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    9 GSPPAIQisRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVsISGvdvTDRAARAR-DV 87
Cdd:PRK11247  10 GTPLLLN--AVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAG---TAPLAEAReDT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 GMVFQNYALFPHLTARENVEYPLKvrrlprEERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:PRK11247  84 RLMFQDARLLPWKKVIDNVGLGLK------GQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  168 DEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK11247 158 DEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGKI 212

heterocyst_DevA

TIGR02982

ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...

13-222

3.18e-46

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: 157.10 E-value: 3.18e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    13 AIQISRLKKCYGAVE----VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSI-----SGVDVTDRAAR 83
Cdd:TIGR02982   1 VISIRNLNHYYGHGSlrkqVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVlgqelHGASKKQLVQL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREE-RRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRP 162
Cdd:TIGR02982  81 RRRIGYIFQAHNLLGFLTARQNVQMALELQPNLSYQeARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   163 KLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDqSEALALSSLVVIMRDGRL 222
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

13-242

4.33e-46

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 157.94 E-value: 4.33e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAArarDVGMVFQ 92
Cdd:PRK11248   1 MLQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGA---ERGVVFQ 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:PRK11248  78 NEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFG 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  173 ALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVgspEQIYLEPNSRFVAG 242
Cdd:PRK11248 158 ALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPGPGRVV---ERLPLNFARRFVAG 224

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

14-286

4.98e-46

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 160.35 E-value: 4.98e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAAR 83
Cdd:PRK11153   2 IELKNISKVFpqggRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekelRKAR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   84 aRDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:PRK11153  82 -RQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNS----RF 239
Cdd:PRK11153 161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHpltrEF 240

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 14028433  240 VAGFIGNSNIVC----CSVTARNGRLATVKLG-DGTEVGVPIPAGVTERLGV 286
Cdd:PRK11153 241 IQSTLHLDLPEDylarLQAEPTTGSGPLLRLEfTGESVDAPLLSETARRFGV 292

YnjD

COG4136

ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...

23-216

5.31e-46

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 156.10 E-value: 5.31e-46

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFAS---VSEGTVSISGVDVTDRAARARDVGMVFQNYALFPH 99
Cdd:COG4136  11 LGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSpafSASGEVLLNGRRLTALPAEQRRIGILFQDDLLFPH 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 100 LTARENVEYPLKVRRLPREERRRRALEyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:COG4136  91 LSVGENLAFALPPTIGRAQRRARVEQA-LEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALR 169

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14028433 180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVI 216
Cdd:COG4136 170 AQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206

ectoine_ehuA

TIGR03005

ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...

14-244

6.26e-46

ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of a conserved four gene ABC transporter operon found next to ectoine unilization operons and ectoine biosynthesis operons. Ectoine is a compatible solute that protects enzymes from high osmolarity. It is released by some species in response to hypoosmotic shock, and it is taken up by a number of bacteria as a compatible solute or for consumption. This family shows strong sequence similiarity to a number of amino acid ABC transporter ATP-binding proteins.

Pssm-ID: 132050 [Multi-domain] Cd Length: 252 Bit Score: 157.30 E-value: 6.26e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--------- 84
Cdd:TIGR03005   1 VRFSDVTKRFGILTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMPGRNgplvpadek 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    85 ------RDVGMVFQNYALFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARS 157
Cdd:TIGR03005  81 hlrqmrNKIGMVFQSFNLFPHKTVLDNVtEAPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   158 LVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNS 237
Cdd:TIGR03005 161 LAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFRQPKE 240


                  ....*..
gi 14028433   238 RFVAGFI 244
Cdd:TIGR03005 241 ERTREFL 247

PRK10619

histidine ABC transporter ATP-binding protein HisP;

14-247

1.03e-45

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 157.05 E-value: 1.03e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-----TD--------- 79
Cdd:PRK10619   6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTInlvrdKDgqlkvadkn 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   80 --RAARARdVGMVFQNYALFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSEWA-DRYPRELSGGQQQRVALA 155
Cdd:PRK10619  86 qlRLLRTR-LTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAqGKYPVHLSGGQQQRVSIA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  156 RSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK10619 165 RALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNP 243

                        250
                 ....*....|..
gi 14028433  236 NSRFVAGFIGNS 247
Cdd:PRK10619 244 QSPRLQQFLKGS 255

ABC_subfamily_A

cd03263

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...

14-228

1.36e-45

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: 155.36 E-value: 1.36e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVE--VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDVGMV 90
Cdd:cd03263   1 LQIRNLTKTYKKGTkpAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIrTDRKAARQSLGYC 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:cd03263  81 PQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 171 LSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIMRDGRLEQVGSP 228
Cdd:cd03263 161 TSGLDPASRRAIWDLILEVRKGR--SIILTTHSMDEAEALCDRIAIMSDGKLRCIGSP 216

LolD_lipo_ex

TIGR02211

lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...

14-222

1.54e-45

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: 155.59 E-value: 1.54e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYG----AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-----TDRAA-R 83
Cdd:TIGR02211   2 LKCENLGKRYQegklDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLsklssNERAKlR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:TIGR02211  82 NKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQPS 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433   164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVViMRDGRL 222
Cdd:TIGR02211 162 LVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLE-MKDGQL 219

ABC_ATPase

cd00267

ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...

15-221

3.22e-45

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

Pssm-ID: 213179 [Multi-domain] Cd Length: 157 Bit Score: 152.40 E-value: 3.22e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  15 QISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQ 92
Cdd:cd00267   1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEElrRRIGYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 nyalfphltarenveyplkvrrlpreerrrraleylervhlsewadrypreLSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:cd00267  81 ---------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTS 109

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14028433 173 ALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:cd00267 110 GLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157

PRK11264

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

13-246

4.28e-45

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 155.29 E-value: 4.28e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISgvDVTDRAARA-------- 84
Cdd:PRK11264   3 AIEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVG--DITIDTARSlsqqkgli 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   85 ----RDVGMVFQNYALFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLV 159
Cdd:PRK11264  81 rqlrQHVGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARALA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  160 YRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNS-- 237
Cdd:PRK11264 161 MRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQpr 239

                        250
                 ....*....|.
gi 14028433  238 --RFVAGFIGN 246
Cdd:PRK11264 240 trQFLEKFLLQ 250

ABC_Mj1267_LivG_branched

cd03219

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...

14-231

6.88e-45

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).

Pssm-ID: 213186 [Multi-domain] Cd Length: 236 Bit Score: 154.13 E-value: 6.88e-45

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARAR---DVGMV 90
Cdd:cd03219   1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIarlGIGRT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALEY----------LERVHLSEWADRYPRELSGGQQQRVALARSLVY 160
Cdd:cd03219  81 FQIPRLFPELTVLENVMVAAQARTGSGLLLARARREEreareraeelLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 161 RPKLLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:cd03219 161 DPKLLLLDEPAAGLNPEETEELAELIREL-RERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEV 230

ABC_Iron-Siderophores_B12_Hemin

cd03214

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...

15-222

1.67e-44

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: 151.43 E-value: 1.67e-44

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  15 QISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQ 92
Cdd:cd03214   1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAslSPKELARKIAYVPQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NyalfphltarenveyplkvrrlpreerrrraleyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:cd03214  81 A----------------------------------LELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTS 126

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14028433 173 ALDkhLRGQMQ--DFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03214 127 HLD--IAHQIEllELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRI 176

thiQ

TIGR01277

thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...

33-226

1.90e-44

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: 152.32 E-value: 1.90e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    33 DLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEYPLKV 112
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTGLAPYQRPVSMLFQENNLFAHLTVRQNIGLGLHP 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   113 RRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRD 192
Cdd:TIGR01277  98 GLKLNAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLREEMLALVKQLCSE 177

                         170       180       190
                  ....*....|....*....|....*....|....
gi 14028433   193 LGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:TIGR01277 178 RQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211

ABC_phnC

TIGR02315

phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...

14-232

1.69e-43

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: 150.91 E-value: 1.69e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYG-AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARd 86
Cdd:TIGR02315   2 LEVENLSKVYPnGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKlrgkklRKLRRR- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    87 VGMVFQNYALFPHLTARENVEYP-------LKVRRLPREERRRRALEY-LERVHLSEWADRYPRELSGGQQQRVALARSL 158
Cdd:TIGR02315  81 IGMIFQHYNLIERLTVLENVLHGrlgykptWRSLLGRFSEEDKERALSaLERVGLADKAYQRADQLSGGQQQRVAIARAL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433   159 VYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:TIGR02315 161 AQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELD 234

ABC_tran

pfam00005

ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...

29-172

3.24e-43

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 147.02 E-value: 3.24e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFPHLTARENV 106
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTddERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   107 EYPLKVRRLPREERRRRALEYLERVHLSEWADR----YPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAEEALEKLGLGDLADRpvgeRPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150

CcmA

COG4133

ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...

12-215

4.66e-43

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

Pssm-ID: 443308 [Multi-domain] Cd Length: 206 Bit Score: 148.40 E-value: 4.66e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-RAARARDVGMV 90
Cdd:COG4133   1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDaREDYRRRLAYL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENVEYPLKVRRLPREERRRRALeyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:COG4133  81 GHADGLKPELTVRENLRFWAALYGLRADREAIDEA--LEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEP 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 14028433 171 LSALDKHLRGQMQDFLKELQRDLGITFVhVTHDQSEALALSSLVV 215
Cdd:COG4133 159 FTALDAAGVALLAELIAAHLARGGAVLL-TTHQPLELAAARVLDL 202

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

33-231

4.76e-43

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 149.35 E-value: 4.76e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   33 DLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNYALFPHLTARENVEYPLKV 112
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPSRRPVSMLFQENNLFSHLTVAQNIGLGLNP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  113 RRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRD 192
Cdd:PRK10771  99 GLKLNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQE 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 14028433  193 LGITFVHVTHDQSEA--LALSSLVVImrDGRLEQVGSPEQI 231
Cdd:PRK10771 179 RQLTLLMVSHSLEDAarIAPRSLVVA--DGRIAWDGPTDEL 217

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

19-235

6.09e-43

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: 156.38 E-value: 6.09e-43

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  19 LKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTL----LRIIAgfasvSEGTVSISGVDVTDRAARA-----RDVGM 89
Cdd:COG4172 292 FRRTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLIP-----SEGEIRFDGQDLDGLSRRAlrplrRRMQV 366

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  90 VFQN-YA-LFPHLTARENVEYPLKVRRLPREERRRRA--LEYLERVHLS-EWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:COG4172 367 VFQDpFGsLSPRMTVGQIIAEGLRVHGPGLSAAERRArvAEALEEVGLDpAARHRYPHEFSGGQRQRIAIARALILEPKL 446

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 165 LLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL-EQvGSPEQIYLEP 235
Cdd:COG4172 447 LVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVvEQ-GPTEQVFDAP 517

3a0107s01c2

TIGR00972

phosphate ABC transporter, ATP-binding protein; This model represents the ATP-binding protein ...

13-244

8.50e-43

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: 148.98 E-value: 8.50e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLR-------IIAGFASvsEGTVSISGVDVTDR----- 80
Cdd:TIGR00972   1 AIEIENLNLFYGEKEALKNINLDIPKNQVTALIGPSGCGKSTLLRslnrmndLVPGVRI--EGKVLFDGQDIYDKkidvv 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    81 AARARdVGMVFQNYALFPhLTARENVEYPLKVRRLPREERRRraleylERVHLS--------EWADR---YPRELSGGQQ 149
Cdd:TIGR00972  79 ELRRR-VGMVFQKPNPFP-MSIYDNIAYGPRLHGIKDKKELD------EIVEESlkkaalwdEVKDRlhdSALGLSGGQQ 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   150 QRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPE 229
Cdd:TIGR00972 151 QRLCIARALAVEPEVLLLDEPTSALDPIATGKIEELIQELKKKY--TIVIVTHNMQQAARISDRTAFFYDGELVEYGPTE 228

                         250
                  ....*....|....*
gi 14028433   230 QIYLEPNSRFVAGFI 244
Cdd:TIGR00972 229 QIFTNPKEKRTEDYI 243

ABC_TM1139_LivF_branched

cd03224

ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...

14-231

1.10e-42

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: 147.97 E-value: 1.10e-42

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA--RARD-VGMV 90
Cdd:cd03224   1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPheRARAgIGYV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQNYALFPHLTARENveypLKVRRLPREERRRRALeyLERVH-----LSEWADRYPRELSGGQQQRVALARSLVYRPKLL 165
Cdd:cd03224  81 PEGRRIFPELTVEEN----LLLGAYARRRAKRKAR--LERVYelfprLKERRKQLAGTLSGGEQQMLAIARALMSRPKLL 154

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 166 LLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:cd03224 155 LLDEPSEGLAPKIVEEIFEAIREL-RDEGVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAEL 219

ABC_ATP_DarD

NF038007

darobactin export ABC transporter ATP-binding protein;

14-222

1.30e-42

darobactin export ABC transporter ATP-binding protein;

Pssm-ID: 411600 [Multi-domain] Cd Length: 218 Bit Score: 147.56 E-value: 1.30e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGA----VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDR------AAR 83
Cdd:NF038007   2 LNMQNAEKCYITktikTKVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVTNLsysqkiILR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:NF038007  82 RELIGYIFQSFNLIPHLSIFDNVALPLKYRGVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPA 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  164 LLLLDEPLSALD-KHLRGQMQDfLKELQRDlGITFVHVTHDQsEALALSSLVVIMRDGRL 222
Cdd:NF038007 162 LLLADEPTGNLDsKNARAVLQQ-LKYINQK-GTTIIMVTHSD-EASTYGNRIINMKDGKL 218

PRK10070

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

34-306

5.98e-42

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 150.95 E-value: 5.98e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   34 LVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARDVGMVFQNYALFPHLTARENVE 107
Cdd:PRK10070  49 LAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKisdaelREVRRKKIAMVFQSFALMPHMTVLDNTA 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  108 YPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLK 187
Cdd:PRK10070 129 FGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQDELV 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  188 ELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVAGFIGNSNIvccsvtarngrlatVKLG 267
Cdd:PRK10070 209 KLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDI--------------SQVF 274

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 14028433  268 DGTEVGVPIPAGVTERL-GVGEKSLL-LLRPEKAETGYRID 306
Cdd:PRK10070 275 SAKDIARRTPNGLIRKTpGFGPRSALkLLQDEDREYGYVIE 315

ECF_ATPase_2

TIGR04521

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

29-232

1.30e-41

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: 146.83 E-value: 1.30e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARaRDVGMVFQN--YALFpHL 100
Cdd:TIGR04521  21 LDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAkkkkklKDLR-KKVGLVFQFpeHQLF-EE 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   101 TARENVEYPLKVRRLPREERRRRALEYLERVHLSE-WADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:TIGR04521  99 TVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEeYLERSPFELSGGQMRRVAIAGVLAMEPEVLILDEPTAGLDPKGR 178

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 14028433   180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:TIGR04521 179 KEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVF 231

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

14-224

1.76e-41

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 144.92 E-value: 1.76e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVE----VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT-----DRAA-R 83
Cdd:PRK10584   7 VEVHHLKKSVGQGEhelsILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHqmdeeARAKlR 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:PRK10584  87 AKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPD 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQ 224
Cdd:PRK10584 167 VLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLA-ARCDRRLRLVNGQLQE 226

ABC_Metallic_Cations

cd03235

ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...

23-203

2.12e-41

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

Pssm-ID: 213202 [Multi-domain] Cd Length: 213 Bit Score: 144.21 E-value: 2.12e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARardVGMVFQNYAL---FPh 99
Cdd:cd03235   9 YGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKERKR---IGYVPQRRSIdrdFP- 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 100 LTARENVE---YPLKVRRLPREERRRRALEY-LERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:cd03235  85 ISVRDVVLmglYGHKGLFRRLSKADKAKVDEaLERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVD 164

                       170       180
                ....*....|....*....|....*...
gi 14028433 176 KHLRGQMQDFLKELQRDlGITFVHVTHD 203
Cdd:cd03235 165 PKTQEDIYELLRELRRE-GMTILVVTHD 191

nickel_nikE

TIGR02769

nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...

28-222

2.67e-41

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: 145.72 E-value: 2.67e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARA---RDVGMVFQNY--ALFPHL 100
Cdd:TIGR02769  26 VLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYqlDRKQRRafrRDVQLVFQDSpsAVNPRM 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   101 TARENVEYPLK-VRRLPREERRRRALEYLERVHL-SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:TIGR02769 106 TVRQIIGEPLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARALAVKPKLIVLDEAVSNLDMVL 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 14028433   179 RGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:TIGR02769 186 QAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229

DppD

COG0444

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...

14-235

2.82e-41

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: 147.12 E-value: 2.82e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF---ASVSEGTVSISGVDVTD------R 80
Cdd:COG0444   2 LEVRNLKVYFptrrGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLlppPGITSGEILFDGEDLLKlsekelR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  81 AARARDVGMVFQN-Y-ALFPHLTARENVEYPLKV-RRLPREERRRRALEYLERVHLS---EWADRYPRELSGGQQQRVAL 154
Cdd:COG0444  82 KIRGREIQMIFQDpMtSLNPVMTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPdpeRRLDRYPHELSGGMRQRVMI 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 155 ARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLE 234
Cdd:COG0444 162 ARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFEN 241


                .
gi 14028433 235 P 235
Cdd:COG0444 242 P 242

ABC_FtsE

cd03292

Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...

14-222

3.33e-41

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: 144.09 E-value: 3.33e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGA-VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA-----RDV 87
Cdd:cd03292   1 IEFINVTKTYPNgTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipylrRKI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  88 GMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:cd03292  81 GVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIA 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433 168 DEPLSALDKHLRGQMQDFLKELQrDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03292 161 DEPTGNLDPDTTWEIMNLLKKIN-KAGTTVVVATHAKELVDTTRHRVIALERGKL 214

AppF

COG4608

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

9-235

6.06e-41

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 146.42 E-value: 6.06e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   9 GSPPAIQISRLKKCY-----------GAVEVLRGLDLVIPEGSytTF--LGPSGSGKTTLLRIIAGFASVSEGTVSISGV 75
Cdd:COG4608   3 MAEPLLEVRDLKKHFpvrgglfgrtvGVVKAVDGVSFDIRRGE--TLglVGESGCGKSTLGRLLLRLEEPTSGEILFDGQ 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  76 DVTDRAARA-----RDVGMVFQN-YA-LFPHLTARENVEYPLKVRRLPREERRRRALEY-LERVHLS-EWADRYPRELSG 146
Cdd:COG4608  81 DITGLSGRElrplrRRMQMVFQDpYAsLNPRMTVGDIIAEPLRIHGLASKAERRERVAElLELVGLRpEHADRYPHEFSG 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 147 GQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDqseaLA----LSSLVVIMRDGRL 222
Cdd:COG4608 161 GQRQRIGIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHD----LSvvrhISDRVAVMYLGKI 236

                       250
                ....*....|...
gi 14028433 223 EQVGSPEQIYLEP 235
Cdd:COG4608 237 VEIAPRDELYARP 249

ECF_ATPase_1

TIGR04520

energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...

14-232

8.73e-41

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: 144.50 E-value: 8.73e-41

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCY--GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA----RaRDV 87
Cdd:TIGR04520   1 IEVENVSFSYpeSEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEENlweiR-KKV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    88 GMVFQN---------------YAL----FPHLTARENVEYplkvrrlpreerrrraleYLERVHLSEWADRYPRELSGGQ 148
Cdd:TIGR04520  80 GMVFQNpdnqfvgatveddvaFGLenlgVPREEMRKRVDE------------------ALKLVGMEDFRDREPHLLSGGQ 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   149 QQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQVGSP 228
Cdd:TIGR04520 142 KQRVAIAGVLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEA-VLADRVIVMNKGKIVAEGTP 220


                  ....
gi 14028433   229 EQIY 232
Cdd:TIGR04520 221 REIF 224

ABC_BcrA_bacitracin_resist

cd03268

ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...

14-222

1.78e-40

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: 141.59 E-value: 1.78e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN 93
Cdd:cd03268   1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALRRIGALIEA 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENveypLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03268  81 PGFYPNLTAREN----LRLLARLLGIRKKRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNG 156

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14028433 174 LDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03268 157 LDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKL 204

ABCC_MRP_Like

cd03228

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...

24-221

2.42e-40

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: 140.21 E-value: 2.42e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFpHLT 101
Cdd:cd03228  13 RPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRdlDLESLRKNIAYVPQDPFLF-SGT 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 102 ARENVeyplkvrrlpreerrrraleylervhlsewadrypreLSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ 181
Cdd:cd03228  92 IRENI-------------------------------------LSGGQRQRIAIARALLRDPPILILDEATSALDPETEAL 134

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14028433 182 MQDFLKELQRdlGITFVHVTHDQSeALALSSLVVIMRDGR 221
Cdd:cd03228 135 ILEALRALAK--GKTVIVIAHRLS-TIRDADRIIVLDDGR 171

L_ocin_972_ABC

TIGR03608

putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...

16-204

5.41e-40

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

Pssm-ID: 188353 [Multi-domain] Cd Length: 206 Bit Score: 140.44 E-value: 5.41e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    16 ISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVD---VTDRAARA--RD-VGM 89
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQEtppLNSKKASKfrREkLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    90 VFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLILADE 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 14028433   170 PLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQ 204
Cdd:TIGR03608 161 PTGSLDPKNRDEVLDLLLEL-NDEGKTIIIVTHDP 194

ABC_NatA_sodium_exporter

cd03266

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...

14-226

6.33e-40

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: 140.58 E-value: 6.33e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGA----VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDVG 88
Cdd:cd03266   2 ITADALTKRFRDvkktVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVvKEPAEARRRLG 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  89 MVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:cd03266  82 FVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLD 161

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 169 EPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:cd03266 162 EPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218

PstB

COG1117

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

1-235

6.33e-40

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 141.71 E-value: 6.33e-40

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   1 MSNASKDcgSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLR-------IIAGfASVsEGTVSIS 73
Cdd:COG1117   1 MTAPAST--LEPKIEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPG-ARV-EGEILLD 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  74 GVDVTDR-----AARARdVGMVFQNYALFPHlTARENVEYPLKVRRLPREERRRraleylERVhlsEWA----------- 137
Cdd:COG1117  77 GEDIYDPdvdvvELRRR-VGMVFQKPNPFPK-SIYDNVAYGLRLHGIKSKSELD------EIV---EESlrkaalwdevk 145

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 138 DR---YPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLV 214
Cdd:COG1117 146 DRlkkSALGLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYT 223

                       250       260
                ....*....|....*....|.
gi 14028433 215 VIMRDGRLEQVGSPEQIYLEP 235
Cdd:COG1117 224 AFFYLGELVEFGPTEQIFTNP 244

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

24-222

2.01e-39

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 140.98 E-value: 2.01e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARA---RDVGMVFQNY--AL 96
Cdd:PRK10419  23 QHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAklNRAQRKafrRDIQMVFQDSisAV 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   97 FPHLTARENVEYPLK-VRRLPREERRRRALEYLERVHLS-EWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PRK10419 103 NPRKTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 14028433  175 DKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK10419 183 DLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQI 230

SunT

COG2274

ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...

12-231

1.21e-38

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: 146.13 E-value: 1.21e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  12 PAIQISRLKKCYG--AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDV 87
Cdd:COG2274 472 GDIELENVSFRYPgdSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRqiDPASLRRQI 551

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  88 GMVFQNYALFpHLTARENV-----EYPL-KVRRLpreerrrraleyLERVHLSEWADRYP-----------RELSGGQQQ 150
Cdd:COG2274 552 GVVLQDVFLF-SGTIRENItlgdpDATDeEIIEA------------ARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQ 618

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 151 RVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRdlGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:COG2274 619 RLAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLS-TIRLADRIIVLDKGRIVEDGTHEE 695


                .
gi 14028433 231 I 231
Cdd:COG2274 696 L 696

CeuD

COG4604

ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...

14-231

1.42e-38

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 138.29 E-value: 1.42e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV--TDRAARARDVGMVF 91
Cdd:COG4604   2 IEIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVatTPSRELAKRLAILR 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  92 QNYALFPHLTARENVE---YP-----------LKVRRlpreerrrraleYLERVHLSEWADRYPRELSGGQQQRVALARS 157
Cdd:COG4604  82 QENHINSRLTVRELVAfgrFPyskgrltaedrEIIDE------------AIAYLDLEDLADRYLDELSGGQRQRAFIAMV 149

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433 158 LVYRPKLLLLDEPLSALD-KHLRgQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG4604 150 LAQDTDYVLLDEPLNNLDmKHSV-QMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEEI 223

ABC_drug_resistance_like

cd03264

ABC-type multidrug transport system, ATPase component; The biological function of this family ...

14-226

4.77e-38

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: 135.40 E-value: 4.77e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTtFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARD-VGMVFQ 92
Cdd:cd03264   1 LQLENLTKRYGKKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRrIGYLPQ 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:cd03264  80 EFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTA 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 14028433 173 ALDKHLRGQMQDFLKELQRDlgITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:cd03264 160 GLDPEERIRFRNLLSELGED--RIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211

LivF

COG0410

ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...

11-231

5.38e-38

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: 136.27 E-value: 5.38e-38

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  11 PPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA--RARD-V 87
Cdd:COG0410   1 MPMLEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPhrIARLgI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  88 GMVFQNYALFPHLTARENveypLKVRRLPREERRRRALEyLERVHlsewaDRYPR----------ELSGGQQQRVALARS 157
Cdd:COG0410  81 GYVPEGRRIFPSLTVEEN----LLLGAYARRDRAEVRAD-LERVY-----ELFPRlkerrrqragTLSGGEQQMLAIGRA 150

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 158 LVYRPKLLLLDEP---LSALdkhLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG0410 151 LMSRPKLLLLDEPslgLAPL---IVEEIFEIIRRL-NREGVTILLVEQNARFALEIADRAYVLERGRIVLEGTAAEL 223

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

13-245

2.85e-37

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 134.97 E-value: 2.85e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS-----EGTVSISGVDV----TDRAAR 83
Cdd:PRK14267   4 AIETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLLELNeearvEGEVRLFGRNIyspdVDPIEV 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   84 ARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRaleylERVhlsEWA-----------DR---YPRELSGGQQ 149
Cdd:PRK14267  84 RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKSKKELD-----ERV---EWAlkkaalwdevkDRlndYPSNLSGGQR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  150 QRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPE 229
Cdd:PRK14267 156 QRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTR 233

                        250       260
                 ....*....|....*....|
gi 14028433  230 QIYLEP----NSRFVAGFIG 245
Cdd:PRK14267 234 KVFENPehelTEKYVTGALG 253

CydD

COG4988

ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...

9-230

6.50e-36

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: 137.20 E-value: 6.50e-36

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   9 GSPPAIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARAR 85
Cdd:COG4988 332 AGPPSIELEDVSFSYpGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSdlDPASWRR 411

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  86 DVGMVFQNYALFpHLTARENV---------EYPLKVrrlpreerrrraleyLERVHLSEWADRYP-----------RELS 145
Cdd:COG4988 412 QIAWVPQNPYLF-AGTIRENLrlgrpdasdEELEAA---------------LEAAGLDEFVAALPdgldtplgeggRGLS 475

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 146 GGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSeALALSSLVVIMRDGRLEQV 225
Cdd:COG4988 476 GGQAQRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLA-LLAQADRILVLDDGRIVEQ 552


                ....*
gi 14028433 226 GSPEQ 230
Cdd:COG4988 553 GTHEE 557

ABC_cobalt_CbiO_domain2

cd03226

Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...

27-220

1.13e-35

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: 128.91 E-value: 1.13e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTdRAARARDVGMVFQN--YALFphltaRE 104
Cdd:cd03226  14 EILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK-AKERRKSIGYVMQDvdYQLF-----TD 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 105 NVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQD 184
Cdd:cd03226  88 SVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGE 167

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 14028433 185 FLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDG 220
Cdd:cd03226 168 LIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANG 202

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

12-224

2.96e-35

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 128.78 E-value: 2.96e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCY--GAV--EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTV-----SISGVDVTDRAA 82
Cdd:PRK11629   4 ILLQCDNLCKRYqeGSVqtDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVifngqPMSKLSSAAKAE 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   83 -RARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYR 161
Cdd:PRK11629  84 lRNQKLGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNN 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433  162 PKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVViMRDGRLEQ 224
Cdd:PRK11629 164 PRLVLADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLE-MRDGRLTA 225

ABC_Carb_Monos_I

cd03216

First domain of the ATP-binding cassette component of monosaccharide transport system; This ...

14-222

3.44e-35

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: 126.39 E-value: 3.44e-35

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV---TDRAARARDVGMV 90
Cdd:cd03216   1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVsfaSPRDARRAGIAMV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  91 FQnyalfphltarenveyplkvrrlpreerrrraleylervhlsewadrypreLSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:cd03216  81 YQ---------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14028433 171 LSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03216 110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRV 160

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

12-230

4.22e-35

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 129.12 E-value: 4.22e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD--RAARARDVGM 89
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADwsPAELARRRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQNYAL-FPhLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLV------YRP 162
Cdd:PRK13548  81 LPQHSSLsFP-FTVEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLARVLAqlwepdGPP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433  163 KLLLLDEPLSALDkhLRGQMQ--DFLKELQRDLGITFVHVTHDqseaLALSSL----VVIMRDGRLEQVGSPEQ 230
Cdd:PRK13548 160 RWLLLDEPTSALD--LAHQHHvlRLARQLAHERGLAVIVVLHD----LNLAARyadrIVLLHQGRLVADGTPAE 227

ABC_putative_ATPase

cd03269

ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...

14-221

1.60e-34

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: 126.24 E-value: 1.60e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTdrAARARDVGMVFQN 93
Cdd:cd03269   1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD--IAARNRIGYLPEE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03269  79 RGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFSG 158

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 14028433 174 LDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:cd03269 159 LDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGR 205

CydC

COG4987

ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...

10-239

1.84e-34

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: 133.35 E-value: 1.84e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCY--GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARAR 85
Cdd:COG4987 330 GGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRdlDEDDLRR 409

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  86 DVGMVFQNYALFpHLTARENV---------EYPLKVrrlpreerrrraleyLERVHLSEWADRYP-----------RELS 145
Cdd:COG4987 410 RIAVVPQRPHLF-DTTLRENLrlarpdatdEELWAA---------------LERVGLGDWLAALPdgldtwlgeggRRLS 473

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 146 GGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ-MQDFLKELQRDlgiTFVHVTHDQSeALALSSLVVIMRDGRLEQ 224
Cdd:COG4987 474 GGERRRLALARALLRDAPILLLDEPTEGLDAATEQAlLADLLEALAGR---TVLLITHRLA-GLERMDRILVLEDGRIVE 549

                       250
                ....*....|....*
gi 14028433 225 VGSPEQIyLEPNSRF 239
Cdd:COG4987 550 QGTHEEL-LAQNGRY 563

COG4559

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

14-230

2.19e-34

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

Pssm-ID: 443620 [Multi-domain] Cd Length: 258 Bit Score: 127.15 E-value: 2.19e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD--RAARARDVGMVF 91
Cdd:COG4559   2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwsPWELARRRAVLP 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  92 QNYAL-FPhLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLV-------YRPK 163
Cdd:COG4559  82 QHSSLaFP-FTVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRVQLARVLAqlwepvdGGPR 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433 164 LLLLDEPLSALDkhLRGQmQDFLkELQRDL---GITFVHVTHDqseaLALSSL----VVIMRDGRLEQVGSPEQ 230
Cdd:COG4559 161 WLFLDEPTSALD--LAHQ-HAVL-RLARQLarrGGGVVAVLHD----LNLAAQyadrILLLHQGRLVAQGTPEE 226

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

14-242

4.07e-34

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 126.57 E-value: 4.07e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS-----EGTVSISGVDV--TDRAARARD 86
Cdd:PRK14247   4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLIELYpearvSGEVYLDGQDIfkMDVIELRRR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   87 VGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEY--LERVHL-SEWADRY---PRELSGGQQQRVALARSLVY 160
Cdd:PRK14247  84 VQMVFQIPNPIPNLSIFENVALGLKLNRLVKSKKELQERVRwaLEKAQLwDEVKDRLdapAGKLSGGQQQRLCIARALAF 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  161 RPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP----N 236
Cdd:PRK14247 164 QPEVLLADEPTANLDPENTAKIESLFLELKKDM--TIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPrhelT 241


                 ....*.
gi 14028433  237 SRFVAG 242
Cdd:PRK14247 242 EKYVTG 247

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

46-235

4.70e-34

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 128.16 E-value: 4.70e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   46 GPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARA---RDVGMVFQN-YA-LFPHLTARENVEYPLKV-RRLPR 117
Cdd:PRK11308  48 GESGCGKSTLARLLTMIETPTGGELYYQGQDLLkaDPEAQKllrQKIQIVFQNpYGsLNPRKKVGQILEEPLLInTSLSA 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  118 EERRRRALEYLERVHL-SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGIT 196
Cdd:PRK11308 128 AERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLS 207

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 14028433  197 FVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK11308 208 YVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNP 246

MdlB

COG1132

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

24-230

4.77e-34

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 132.21 E-value: 4.77e-34

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD--RAARARDVGMVFQNYALFpHLT 101
Cdd:COG1132 351 GDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDltLESLRRQIGVVPQDTFLF-SGT 429

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 102 ARENVeyplkvrrlpreerrrralEY-------------LERVHLSEWADRYP-----------RELSGGQQQRVALARS 157
Cdd:COG1132 430 IRENI-------------------RYgrpdatdeeveeaAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARA 490

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 158 LVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgITFVhVTHDqsealaLSSL-----VVIMRDGRLEQVGSPEQ 230
Cdd:COG1132 491 LLKDPPILILDEATSALDTETEALIQEALERLMKGR-TTIV-IAHR------LSTIrnadrILVLDDGRIVEQGTHEE 560

MglA

COG1129

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

10-222

1.72e-33

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 129.75 E-value: 1.72e-33

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV---TDRAARARD 86
Cdd:COG1129   1 AEPLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVrfrSPRDAQAAG 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 VGMVFQNYALFPHLTARENV---EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:COG1129  81 IAIIHQELNLVPNLSVAENIflgREPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSRDAR 160

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG1129 161 VLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISHRLDEVFEIADRVTVLRDGRL 218

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

31-235

2.53e-33

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 126.36 E-value: 2.53e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   31 GLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARaRDVGMVFQN--YALFPHLTA 102
Cdd:PRK15079  39 GVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGmkddewRAVR-SDIQMIFQDplASLNPRMTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  103 RENVEYPLKVRRLPREERRRRaleylERVH--------LSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PRK15079 118 GEIIAEPLRTYHPKLSRQEVK-----DRVKammlkvglLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSAL 192

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  175 DKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK15079 193 DVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNP 253

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

29-232

4.18e-33

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 124.36 E-value: 4.18e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA---RARdVGMVFQNY-ALFPHLTARE 104
Cdd:PRK13635  23 LKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEETVwdvRRQ-VGMVFQNPdNQFVGATVQD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  105 NVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQD 184
Cdd:PRK13635 102 DVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLE 181

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 14028433  185 FLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13635 182 TVRQLKEQKGITVLSITHDLDEA-AQADRVIVMNKGEILEEGTPEEIF 228

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

24-222

1.09e-32

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 128.69 E-value: 1.09e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT----DRAARAR--DVGMVFQNYALF 97
Cdd:PRK10535  19 EQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVAtldaDALAQLRreHFGFIFQRYHLL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   98 PHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKH 177
Cdd:PRK10535  99 SHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSH 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 14028433  178 LRGQMQDFLKELqRDLGITFVHVTHDQSEAlALSSLVVIMRDGRL 222
Cdd:PRK10535 179 SGEEVMAILHQL-RDRGHTVIIVTHDPQVA-AQAERVIEIRDGEI 221

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

23-209

1.09e-32

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 120.80 E-value: 1.09e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVsisgvdvtdRAARARDVGMVFQNYAL---FPh 99
Cdd:NF040873   2 YGGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTV---------RRAGGARVAYVPQRSEVpdsLP- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  100 LTARENVEY----PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:NF040873  72 LTVRDLVAMgrwaRRGLWRRLTRDDRAAVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                        170       180       190
                 ....*....|....*....|....*....|....
gi 14028433  176 KHLRGQMQDFLKELQRDlGITFVHVTHDQSEALA 209
Cdd:NF040873 152 AESRERIIALLAEEHAR-GATVVVVTHDLELVRR 184

YhaQ

COG4152

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

13-231

2.72e-32

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 122.52 E-value: 2.72e-32

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVtDRAARARdVGmvfq 92
Cdd:COG4152   1 MLELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPL-DPEDRRR-IG---- 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  93 nY-----ALFPHLTARENVEY-------PLKVRRLPREErrrraleYLERVHLSEWADRYPRELSGGQQQRVALARSLVY 160
Cdd:COG4152  75 -YlpeerGLYPKMKVGEQLVYlarlkglSKAEAKRRADE-------WLERLGLGDRANKKVEELSKGNQQKVQLIAALLH 146

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 161 RPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG4152 147 DPELLILDEPFSGLDPVNVELLKDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI 216

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

12-231

2.74e-32

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

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 126.84 E-value: 2.74e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    12 PAIQISRLKKCY-----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSI----SGVDVTDRA- 81
Cdd:TIGR03269 278 PIIKVRNVSKRYisvdrGVVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGp 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    82 ---ARA-RDVGMVFQNYALFPHLTAREN------VEYPLKVRRLPREERRRRALeyLERVHLSEWADRYPRELSGGQQQR 151
Cdd:TIGR03269 358 dgrGRAkRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITLKMVG--FDEEKAEEILDKYPDELSEGERHR 435

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   152 VALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:TIGR03269 436 VALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEI 515

cbiO

PRK13640

energy-coupling factor transporter ATPase;

28-232

3.03e-32

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 122.22 E-value: 3.03e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFA---SVSEGTVSISGVDVTDRAA-RARD-VGMVFQNY-ALFPHLT 101
Cdd:PRK13640  22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLlpdDNPNSKITVDGITLTAKTVwDIREkVGIVFQNPdNQFVGAT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  102 ARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ 181
Cdd:PRK13640 102 VGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQ 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 14028433  182 MQDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13640 182 ILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF 231

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

29-236

4.53e-32

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 122.05 E-value: 4.53e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSI------SGVDVTDRAARARDVGMVFQnyalFP-HLT 101
Cdd:PRK13634  23 LYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIgervitAGKKNKKLKPLRKKVGIVFQ----FPeHQL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  102 ARENVEY-----PLKVRRLPREERRRRALEyLERVHLSE-WADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:PRK13634  99 FEETVEKdicfgPMNFGVSEEDAKQKAREM-IELVGLPEeLLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  176 KHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADPD 238

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

16-244

5.53e-32

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 120.92 E-value: 5.53e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   16 ISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG--------VDVTDRAARARDV 87
Cdd:PRK14246  13 ISRLYLYINDKAILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGkvlyfgkdIFQIDAIKLRKEV 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 GMVFQNYALFPHLTARENVEYPLKVR-RLPREERRRRALEYLERVHLseWADRYPR------ELSGGQQQRVALARSLVY 160
Cdd:PRK14246  93 GMVFQQPNPFPHLSIYDNIAYPLKSHgIKEKREIKKIVEECLRKVGL--WKEVYDRlnspasQLSGGQQQRLTIARALAL 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  161 RPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlgITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFV 240
Cdd:PRK14246 171 KPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELT 248


                 ....
gi 14028433  241 AGFI 244
Cdd:PRK14246 249 EKYV 252

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

10-231

1.25e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 120.10 E-value: 1.25e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVE--VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR-ARD 86
Cdd:PRK13632   4 KSVMIKVENVSFSYPNSEnnALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKeIRK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   87 -VGMVFQNY-ALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:PRK13632  84 kIGIIFQNPdNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNPEI 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433  165 LLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALaLSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK13632 164 IIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAI-LADKVIVFSEGKLIAQGKPKEI 229

ABC_YhbG

cd03218

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...

19-232

4.45e-31

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: 117.64 E-value: 4.45e-31

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  19 LKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA--ARARDvGMVF--QNY 94
Cdd:cd03218   6 LSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPmhKRARL-GIGYlpQEA 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  95 ALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:cd03218  85 SIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLLDEPFAGV 164

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 175 DKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:cd03218 165 DPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIA 221

PRK14239

phosphate transporter ATP-binding protein; Provisional

10-235

6.05e-31

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 117.95 E-value: 6.05e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS-----EGTVSISGVDV----TDR 80
Cdd:PRK14239   2 TEPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMNDLNpevtiTGSIVYNGHNIysprTDT 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   81 AARARDVGMVFQNYALFPhLTARENVEYPLK--------VRRLPREERRRRALEYLE---RVHLSEWAdrypreLSGGQQ 149
Cdd:PRK14239  82 VDLRKEIGMVFQQPNPFP-MSIYENVVYGLRlkgikdkqVLDEAVEKSLKGASIWDEvkdRLHDSALG------LSGGQQ 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  150 QRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPE 229
Cdd:PRK14239 155 QRVCIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTK 232


                 ....*.
gi 14028433  230 QIYLEP 235
Cdd:PRK14239 233 QMFMNP 238

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

32-232

6.18e-31

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 120.36 E-value: 6.18e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   32 LDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG---VDVTDR---AARARDVGMVFQNYALFPHLTAREN 105
Cdd:PRK11144  17 VNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlFDAEKGiclPPEKRRIGYVFQDARLFPHYKVRGN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  106 VEYPLKvrrlpreerrRRALEYLERV-------HLsewADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:PRK11144  97 LRYGMA----------KSMVAQFDKIvallgiePL---LDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPR 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14028433  179 RGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK11144 164 KRELLPYLERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVW 217

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

36-232

7.70e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 117.93 E-value: 7.70e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   36 IPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQN-YALFPHLTARENVEYPLKV 112
Cdd:PRK13648  32 IPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKlrKHIGIVFQNpDNQFVGSIVKYDVAFGLEN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  113 RRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRD 192
Cdd:PRK13648 112 HAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSE 191

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 14028433  193 LGITFVHVTHDQSEALAlSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13648 192 HNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIF 230

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

14-238

1.23e-30

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 117.56 E-value: 1.23e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAARARdV 87
Cdd:PRK11831   8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAmsrsrlYTVRKR-M 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 GMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEY-LERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLL 166
Cdd:PRK11831  87 SMLFQSGALFTDMNVFDNVAYPLREHTQLPAPLLHSTVMMkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIM 166

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  167 LDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSR 238
Cdd:PRK11831 167 FDEPFVGQDPITMGVLVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPDPR 238

urea_trans_UrtE

TIGR03410

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...

15-241

4.03e-30

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: 114.93 E-value: 4.03e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    15 QISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA--ARARD-VGMVF 91
Cdd:TIGR03410   2 EVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPphERARAgIAYVP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    92 QNYALFPHLTARENVEYPLKVRRLPREERrrraleyLERVH-----LSEWADRYPRELSGGQQQRVALARSLVYRPKLLL 166
Cdd:TIGR03410  82 QGREIFPRLTVEENLLTGLAALPRRSRKI-------PDEIYelfpvLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433   167 LDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFVA 241
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDELDEDKVRRYLA 229

type_I_sec_LssB

TIGR03375

type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...

28-231

4.59e-30

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: 121.51 E-value: 4.59e-30

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFpHLTAREN 105
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRqiDPADLRRNIGYVPQDPRLF-YGTLRDN 558

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   106 VEYplkvrrLPREERRRRALEYLERVHLSEWADRYP-----------RELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:TIGR03375 559 IAL------GAPYADDEEILRAAELAGVTEFVRRHPdgldmqigergRSLSGGQRQAVALARALLRDPPILLLDEPTSAM 632

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433   175 DKhlrGQMQDFLKELQRDL-GITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:TIGR03375 633 DN---RSEERFKDRLKRWLaGKTLVLVTHRTS-LLDLVDRIIVMDNGRIVADGPKDQV 686

cbiO

PRK13650

energy-coupling factor transporter ATPase;

38-232

1.53e-29

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 114.83 E-value: 1.53e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   38 EGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA--RARDVGMVFQNY-ALFPHLTARENVEYPLKVRR 114
Cdd:PRK13650  32 QGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVwdIRHKIGMVFQNPdNQFVGATVEDDVAFGLENKG 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  115 LPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLG 194
Cdd:PRK13650 112 IPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQ 191

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 14028433  195 ITFVHVTHDQSEaLALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13650 192 MTVISITHDLDE-VALSDRVLVMKNGQVESTSTPRELF 228

cbiO

PRK13637

energy-coupling factor transporter ATPase;

29-234

2.11e-29

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 114.76 E-value: 2.11e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARD----VGMVFQ--NYALFPHlTA 102
Cdd:PRK13637  23 LDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLSDirkkVGLVFQypEYQLFEE-TI 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  103 RENVEYPLKVRRLPREERRRRALEYLERVHLS--EWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRG 180
Cdd:PRK13637 102 EKDIAFGPINLGLSEEEIENRVKRAMNIVGLDyeDYKDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRD 181

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14028433  181 QMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLE 234
Cdd:PRK13637 182 EILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKE 235

PRK10908

cell division ATP-binding protein FtsE;

14-222

2.48e-29

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 112.66 E-value: 2.48e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA-----RDV 87
Cdd:PRK10908   2 IRFEHVSKAYlGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpflrRQI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 GMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:PRK10908  82 GMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLA 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  168 DEPLSALDKHLRGQMQDFLKELQRdLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK10908 162 DEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

12-231

2.57e-29

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 116.86 E-value: 2.57e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGM 89
Cdd:PRK09536   2 PMIDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAasRRVAS 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQNYALFPHLTARENVE---YP-LKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLL 165
Cdd:PRK09536  82 VPQDTSLSFEFDVRQVVEmgrTPhRSRFDTWTETDRAAVERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433  166 LLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDD-GKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADV 226

PRK09984

phosphonate ABC transporter ATP-binding protein;

14-239

2.70e-29

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 113.95 E-value: 2.70e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFA---SVSEGTVSISGVDVTDRAARARDV--- 87
Cdd:PRK09984   5 IRVEKLAKTFNQHQALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLItgdKSAGSHIELLGRTVQREGRLARDIrks 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 ----GMVFQNYALFPHLTARENV------EYPLKVRRLPREERRRRALEY--LERVHLSEWADRYPRELSGGQQQRVALA 155
Cdd:PRK09984  85 rantGYIFQQFNLVNRLSVLENVligalgSTPFWRTCFSWFTREQKQRALqaLTRVGMVHFAHQRVSTLSGGQQQRVAIA 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  156 RSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIyleP 235
Cdd:PRK09984 165 RALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF---D 241


                 ....
gi 14028433  236 NSRF 239
Cdd:PRK09984 242 NERF 245

YejF

COG4172

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...

24-235

3.81e-29

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: 117.86 E-value: 3.81e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGsyTTF--LGPSGSGKT----TLLRIIAGFASVSEGTVSISGVDVTD------RAARARDVGMVF 91
Cdd:COG4172  21 GTVEAVKGVSFDIAAG--ETLalVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGlserelRRIRGNRIAMIF 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  92 QN--YALFPHLTARENVEYPLKV-RRLPREERRRRALEYLERVHLSEWA---DRYPRELSGGQQQRVALARSLVYRPKLL 165
Cdd:COG4172  99 QEpmTSLNPLHTIGKQIAEVLRLhRGLSGAAARARALELLERVGIPDPErrlDAYPHQLSGGQRQRVMIAMALANEPDLL 178

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433 166 LLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDqseaLAL----SSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:COG4172 179 IADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD----LGVvrrfADRVAVMRQGEIVEQGPTAELFAAP 248

fecE

PRK11231

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

14-231

5.65e-29

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 112.80 E-value: 5.65e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARDVGMVF 91
Cdd:PRK11231   3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRqlARRLALLP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   92 QNYALFPHLTARENVEY---P-LKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:PRK11231  83 QHHLTPEGITVRELVAYgrsPwLSLWGRLSAEDNARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433  168 DEPLSALDKHLRGQMQDFLKELQrDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK11231 163 DEPTTYLDINHQVELMRLMRELN-TQGKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEV 225

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

7-231

7.37e-29

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 113.75 E-value: 7.37e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    7 DCGSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARD 86
Cdd:PRK13537   1 GPMSVAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   87 -VGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLL 165
Cdd:PRK13537  81 rVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433  166 LLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK13537 161 VLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHAL 225

ModF

COG1119

ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...

11-231

7.78e-29

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: 112.10 E-value: 7.78e-29

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  11 PPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEG-TVSISG-----VDVTD----- 79
Cdd:COG1119   1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGerrggEDVWElrkri 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  80 ------------RAARARDVgmV----FQNYALFPHLTAREnveyplkvrrlpreerRRRALEYLERVHLSEWADRYPRE 143
Cdd:COG1119  81 glvspalqlrfpRDETVLDV--VlsgfFDSIGLYREPTDEQ----------------RERARELLELLGLAHLADRPFGT 142

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 144 LSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLE 223
Cdd:COG1119 143 LSQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIPPGITHVLLLKDGRVV 222


                ....*...
gi 14028433 224 QVGSPEQI 231
Cdd:COG1119 223 AAGPKEEV 230

CP_lyasePhnK

TIGR02323

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...

11-235

8.44e-29

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: 112.23 E-value: 8.44e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    11 PPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDR-------AAR 83
Cdd:TIGR02323   1 KPLLQVSGLSKSYGGGKGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYIMRSGAELelyqlseAER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    84 AR----DVGMVFQNYA--LFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSE-WADRYPRELSGGQQQRVALA 155
Cdd:TIGR02323  81 RRlmrtEWGFVHQNPRdgLRMRVSAGANIgERLMAIGARHYGNIRATAQDWLEEVEIDPtRIDDLPRAFSGGMQQRLQIA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   156 RSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:TIGR02323 161 RNLVTRPRLVFMDEPTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDP 240

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

28-222

1.22e-28

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.

Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 109.61 E-value: 1.22e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFPHlTAREN 105
Cdd:cd03246  17 VLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISqwDPNELGDHVGYLPQDDELFSG-SIAEN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 106 VeyplkvrrlpreerrrraleylervhlsewadrypreLSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDF 185
Cdd:cd03246  96 I-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQA 138

                       170       180       190
                ....*....|....*....|....*....|....*..
gi 14028433 186 LKELQRDlGITFVHVTHdQSEALALSSLVVIMRDGRL 222
Cdd:cd03246 139 IAALKAA-GATRIVIAH-RPETLASADRILVLEDGRV 173

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

10-231

1.46e-28

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 113.77 E-value: 1.46e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA--ARARdV 87
Cdd:PRK13536  38 STVAIDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARArlARAR-I 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 GMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:PRK13536 117 GVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLIL 196

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433  168 DEPLSALDKHLRGQMQDFLKELQRdLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK13536 197 DEPTTGLDPHARHLIWERLRSLLA-RGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259

nickel_nikD

TIGR02770

nickel import ATP-binding protein NikD; This family represents the NikD subunit of a ...

31-237

1.54e-28

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: 110.92 E-value: 1.54e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    31 GLDLVIPEGSYTTFLGPSGSGKTT----LLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQN--YALFPHLTARE 104
Cdd:TIGR02770   4 DLNLSLKRGEVLALVGESGSGKSLtclaILGLLPPGLTQTSGEILLDGRPLLPLSIRGRHIATIMQNprTAFNPLFTMGN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   105 NVEYPLKVRRLPREERRRRALEYLERVHLSEWA---DRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ 181
Cdd:TIGR02770  84 HAIETLRSLGKLSKQARALILEALEAVGLPDPEevlKKYPFQLSGGMLQRVMIALALLLEPPFLIADEPTTDLDVVNQAR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433   182 MQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNS 237
Cdd:TIGR02770 164 VLKLLRELRQLFGTGILLITHDLGVVARIADEVAVMDDGRIVERGTVKEIFYNPKH 219

cbiO

PRK13641

energy-coupling factor transporter ATPase;

30-236

1.78e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 112.23 E-value: 1.78e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   30 RGLDLV---IPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA------RDVGMVFQnyalFPHL 100
Cdd:PRK13641  21 KGLDNIsfeLEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNKnlkklrKKVSLVFQ----FPEA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  101 -----TARENVEYPLKVRRLPREERRRRALEYLERVHLSE-WADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PRK13641  97 qlfenTVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEdLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGL 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  175 DKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:PRK13641 177 DPEGRKEMMQLFKDYQKA-GHTVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

5-222

2.90e-28

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: 110.11 E-value: 2.90e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   5 SKDCGSPPAIQiSRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG-VDVTDRAAR 83
Cdd:cd03267  14 SKEPGLIGSLK-SLFKRKYREVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGlVPWKRRKKF 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  84 ARDVGMVF-QNYALFPHLTARENVE-----YPLKvrrlpreerrrrALEYLERV-HLSEWADRYP------RELSGGQQQ 150
Cdd:cd03267  93 LRRIGVVFgQKTQLWWDLPVIDSFYllaaiYDLP------------PARFKKRLdELSELLDLEElldtpvRQLSLGQRM 160

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 151 RVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03267 161 RAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRL 232

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

27-222

6.00e-28

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: 108.02 E-value: 6.00e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS--EGTVSISGVDVTDRAARARdVGMVFQNYALFPHLTARE 104
Cdd:cd03213  23 QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLgvSGEVLINGRPLDKRSFRKI-IGYVPQDDILHPTLTVRE 101

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 105 NVEYPLKVrrlpreerrrraleylervhlsewadrypRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQD 184
Cdd:cd03213 102 TLMFAAKL-----------------------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMS 152

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 14028433 185 FLKELqRDLGITFVHVTHD-QSEALALSSLVVIMRDGRL 222
Cdd:cd03213 153 LLRRL-ADTGRTIICSIHQpSSEIFELFDKLLLLSQGRV 190

cbiO

PRK13649

energy-coupling factor transporter ATPase;

29-234

6.71e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 110.60 E-value: 6.71e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA------RDVGMVFQnyalFPHL-- 100
Cdd:PRK13649  23 LFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKNKdikqirKKVGLVFQ----FPESql 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  101 ---TARENVEYPLKVRRLPREERRRRALEYLERVHLSE-WADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:PRK13649  99 feeTVLKDVAFGPQNFGVSQEEAEALAREKLALVGISEsLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDP 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433  177 HLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLE 234
Cdd:PRK13649 179 KGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

26-222

1.26e-27

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: 108.06 E-value: 1.26e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFpHLTAR 103
Cdd:cd03245  17 IPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRqlDPADLRRNIGYVPQDVTLF-YGTLR 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 104 ENVEYplkvrrLPREERRRRALEYLERVHLSEWADRYP-----------RELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:cd03245  96 DNITL------GAPLADDERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVALARALLNDPPILLLDEPTS 169

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 14028433 173 ALDKHLRGQMQDFLKELQRDlgITFVHVTHDQSeALALSSLVVIMRDGRL 222
Cdd:cd03245 170 AMDMNSEERLKERLRQLLGD--KTLIIITHRPS-LLDLVDRIIVMDSGRI 216

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

13-229

2.71e-27

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 108.67 E-value: 2.71e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARDVGM 89
Cdd:PRK13647   4 IIEVEDLHFRYkDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKwvRSKVGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQNY--ALFPhLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:PRK13647  84 VFQDPddQVFS-STVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  168 DEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPE 229
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDRLHNQ-GKTVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKS 223

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

26-230

3.07e-27

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: 107.63 E-value: 3.07e-27

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFPhLTAR 103
Cdd:cd03249  16 VPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWlrSQIGLVSQEPVLFD-GTIA 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 104 ENVEY---PLKVRRLPREERRRRALEYLErvhlsEWADRY-----PR--ELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03249  95 ENIRYgkpDATDEEVEEAAKKANIHDFIM-----SLPDGYdtlvgERgsQLSGGQKQRIAIARALLRNPKILLLDEATSA 169

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 174 LDKHLRGQMQDFLKELQRdlGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:cd03249 170 LDAESEKLVQEALDRAMK--GRTTIVIAHRLS-TIRNADLIAVLQNGQVVEQGTHDE 223

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

10-235

9.15e-27

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 106.93 E-value: 9.15e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDR------AAR 83
Cdd:PRK11701   3 DQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRdlyalsEAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   84 AR-----DVGMVFQNYA--LFPHLTARENV-EYPLKVRRLPREERRRRALEYLERVHLSewADR---YPRELSGGQQQRV 152
Cdd:PRK11701  83 RRrllrtEWGFVHQHPRdgLRMQVSAGGNIgERLMAVGARHYGDIRATAGDWLERVEID--AARiddLPTTFSGGMQQRL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  153 ALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK11701 161 QIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTDQVL 240


                 ...
gi 14028433  233 LEP 235
Cdd:PRK11701 241 DDP 243

PhnK

COG1101

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

14-221

1.15e-26

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 106.71 E-value: 1.15e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGA-----VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA--RARD 86
Cdd:COG1101   2 LELKNLSKTFNPgtvneKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPEykRAKY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 VGMVFQNYAL--FPHLTARENV--------EYPLKvrRLPREERRRRALEYLERVHLS-EwaDRYPRE---LSGGQQQRV 152
Cdd:COG1101  82 IGRVFQDPMMgtAPSMTIEENLalayrrgkRRGLR--RGLTKKRRELFRELLATLGLGlE--NRLDTKvglLSGGQRQAL 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 153 ALARSLVYRPKLLLLDEPLSALDKhlrgQMQDFLKELQRDL----GITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:COG1101 158 SLLMATLTKPKLLLLDEHTAALDP----KTAALVLELTEKIveenNLTTLMVTHNMEQALDYGNRLIMMHEGR 226

PRK10261

glutathione transporter ATP-binding protein; Provisional

39-235

1.66e-26

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 110.72 E-value: 1.66e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   39 GSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA-----RDVGMVFQN-YA-LFPHLTARENVEYPLK 111
Cdd:PRK10261 350 GETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKlqalrRDIQFIFQDpYAsLDPRQTVGDSIMEPLR 429

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  112 VRRLPREERRRRALEYL-ERVHL-SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKEL 189
Cdd:PRK10261 430 VHGLLPGKAAAARVAWLlERVGLlPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQIINLLLDL 509

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 14028433  190 QRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK10261 510 QRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENP 555

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

9-227

1.72e-26

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.12 E-value: 1.72e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   9 GSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG--VDVTD-RAARAR 85
Cdd:COG3845   1 MMPPALELRGITKRFGGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGkpVRIRSpRDAIAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  86 DVGMVFQNYALFPHLTARENV----EyPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYR 161
Cdd:COG3845  81 GIGMVHQHFMLVPNLTVAENIvlglE-PTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKALYRG 159

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 162 PKLLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLeqVGS 227
Cdd:COG3845 160 ARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITHKLREVMAIADRVTVLRRGKV--VGT 222

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

28-231

2.29e-26

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: 110.22 E-value: 2.29e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARAR-------DV----GMVFQNY 94
Cdd:COG4618 347 ILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSqwDREELGRhigylpqDVelfdGTIAENI 426

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  95 ALFPHLTARENVEYPLKVrrlpreerrrraleyleRVHlsEWADRYP-----------RELSGGQQQRVALARSLVYRPK 163
Cdd:COG4618 427 ARFGDADPEKVVAAAKLA-----------------GVH--EMILRLPdgydtrigeggARLSGGQRQRIGLARALYGDPR 487

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433 164 LLLLDEPLSALD----KHLRGQMQDFlkelqRDLGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG4618 488 LVVLDEPNSNLDdegeAALAAAIRAL-----KARGATVVVITHRPS-LLAAVDKLLVLRDGRVQAFGPRDEV 553

LPS_export_lptB

TIGR04406

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...

14-240

4.01e-26

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]

Pssm-ID: 275199 [Multi-domain] Cd Length: 239 Bit Score: 104.66 E-value: 4.01e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA--ARAR-DVGMV 90
Cdd:TIGR04406   2 LVAENLIKSYKKRKVVNDVSLSVKSGEIVGLLGPNGAGKTTSFYMIVGLVRPDAGKILIDGQDITHLPmhERARlGIGYL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    91 FQNYALFPHLTARENVEYPLKVRR-LPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:TIGR04406  82 PQEASIFRKLTVEENIMAVLEIRKdLDRAEREERLEALLEEFQISHLRDNKAMSLSGGERRRVEIARALATNPKFILLDE 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433   170 PLSALDKHLRGQMQDFLKEL-QRDLGITfvhVT-HDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFV 240
Cdd:TIGR04406 162 PFAGVDPIAVGDIKKIIKHLkERGIGVL---ITdHNVRETLDICDRAYIISDGKVLAEGTPAEIVANEKVRRV 231

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

9-216

4.63e-26

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: 108.91 E-value: 4.63e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     9 GSPPAIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARAR 85
Cdd:TIGR02857 317 APASSLEFSGVSVAYpGRRPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLAdaDADSWRD 396

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    86 DVGMVFQNYALFPHlTARENVEYPLKVRRLPREERRrraleyLERVHLSEWADRYP-----------RELSGGQQQRVAL 154
Cdd:TIGR02857 397 QIAWVPQHPFLFAG-TIAENIRLARPDASDAEIREA------LERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLAL 469

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433   155 ARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRdlGITFVHVTHDQSEALALSSLVVI 216
Cdd:TIGR02857 470 ARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVVL 529

PRK13633

energy-coupling factor transporter ATPase;

28-232

6.08e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 105.17 E-value: 6.08e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA----ARARdVGMVFQN---------- 93
Cdd:PRK13633  25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEnlwdIRNK-AGMVFQNpdnqivativ 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   94 ---YALFPH------LTARENVEYPLKvrrlpreerrrraleyleRVHLSEWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:PRK13633 104 eedVAFGPEnlgippEEIRERVDESLK------------------KVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPEC 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433  165 LLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13633 166 IIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEA-VEADRIIVMDSGKVVMEGTPKEIF 232

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

27-239

6.19e-26

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: 103.85 E-value: 6.19e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD---RAARaRDVGMVFQNYALFpHLTAR 103
Cdd:cd03253  15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREvtlDSLR-RAIGVVPQDTVLF-NDTIG 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 104 ENVEYPlKVRRLPREERRRRALEYLERVHLSeWADRYPRE-------LSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:cd03253  93 YNIRYG-RPDATDEEVIEAAKAAQIHDKIMR-FPDGYDTIvgerglkLSGGEKQRVAIARAILKNPPILLLDEATSALDT 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 177 HLRGQMQDFLKELQRdlGITFVHVTHDQSEaLALSSLVVIMRDGRLEQVGSPEQIyLEPNSRF 239
Cdd:cd03253 171 HTEREIQAALRDVSK--GRTTIVIAHRLST-IVNADKIIVLKDGRIVERGTHEEL-LAKGGLY 229

cbiO

PRK13642

energy-coupling factor transporter ATPase;

26-232

7.11e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 104.79 E-value: 7.11e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAA--RARDVGMVFQNY-ALFPHLTA 102
Cdd:PRK13642  20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVwnLRRKIGMVFQNPdNQFVGATV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  103 RENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQM 182
Cdd:PRK13642 100 EDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEI 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 14028433  183 QDFLKELQRDLGITFVHVTHDQSEAlALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13642 180 MRVIHEIKEKYQLTVLSITHDLDEA-ASSDRILVMKAGEIIKEAAPSELF 228

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

14-238

7.27e-26

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 103.96 E-value: 7.27e-26

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA--ARARdVGMVF 91
Cdd:COG1137   4 LEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPmhKRAR-LGIGY 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  92 --QNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:COG1137  83 lpQEASIFRKLTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFILLDE 162

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 170 PLSALDKHLRGQMQDFLKEL-QRDLGITfvhVT-HDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSR 238
Cdd:COG1137 163 PFAGVDPIAVADIQKIIRHLkERGIGVL---ITdHNVRETLGICDRAYIISEGKVLAEGTPEEILNNPLVR 230

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

23-231

7.31e-26

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 104.68 E-value: 7.31e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARDVGMVFQNYALFPHL 100
Cdd:PRK10253  17 YGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKevARRIGLLAQNATTPGDI 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  101 TARENV---EYPLK-VRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:PRK10253  97 TVQELVargRYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDI 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  177 HLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK10253 177 SHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

24-206

1.86e-25

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 102.48 E-value: 1.86e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFPHlT 101
Cdd:PRK10247  18 GDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIyrQQVSYCAQTPTLFGD-T 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  102 ARENVEYPLKVRRLPREERRRRALeyLERVHLSEWA-DRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRG 180
Cdd:PRK10247  97 VYDNLIFPWQIRNQQPDPAIFLDD--LERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKH 174

                        170       180
                 ....*....|....*....|....*.
gi 14028433  181 QMQDFLKELQRDLGITFVHVTHDQSE 206
Cdd:PRK10247 175 NVNEIIHRYVREQNIAVLWVTHDKDE 200

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

19-239

2.30e-25

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 107.10 E-value: 2.30e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   19 LKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTT----LLRIIAgfasvSEGTVSISGVDVTDRAARA-----RDVGM 89
Cdd:PRK15134 292 LKRTVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQllpvrHRIQV 366

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQ--NYALFPHLTARENVEYPLKV--RRLPREERRRRALEYLERVHLS-EWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:PRK15134 367 VFQdpNSSLNPRLNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDpETRHRYPAEFSGGQRQRIAIARALILKPSL 446

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  165 LLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRF 239
Cdd:PRK15134 447 IILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEY 521

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

28-232

2.88e-25

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: 101.92 E-value: 2.88e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFpHLTAREN 105
Cdd:cd03251  17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASlrRQIGLVSQDVFLF-NDTVAEN 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 106 VEYplkvrrLPREERRRRALEYLERVHLSEWADRYPR-----------ELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:cd03251  96 IAY------GRPGATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIAIARALLKDPPILILDEATSAL 169

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 175 DKHLRGQMQDFLKELQRDLgITFVhVTHdqsealALSSL-----VVIMRDGRLEQVGSPEQIY 232
Cdd:cd03251 170 DTESERLVQAALERLMKNR-TTFV-IAH------RLSTIenadrIVVLEDGKIVERGTHEELL 224

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

24-177

2.99e-25

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 101.49 E-value: 2.99e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQNyALFPHLTAR 103
Cdd:PRK13539  13 GGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHYLGHRN-AMKPALTVA 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433  104 ENVEYPLKVRRLPREERRRRaleyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKH 177
Cdd:PRK13539  92 ENLEFWAAFLGGEELDIAAA----LEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDEPTAALDAA 161

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

2-246

3.97e-25

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 102.87 E-value: 3.97e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    2 SNASKDCGSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRI-------IAGFASvsEGTVSISG 74
Cdd:PRK14271  10 SGAADVDAAAPAMAAVNLTLGFAGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGG 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   75 VDV---TDRAARARDVGMVFQNYALFPhLTARENVEYPLKVRRLPREERRRRaleyLERVHLSE---W---ADRY---PR 142
Cdd:PRK14271  88 RSIfnyRDVLEFRRRVGMLFQRPNPFP-MSIMDNVLAGVRAHKLVPRKEFRG----VAQARLTEvglWdavKDRLsdsPF 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  143 ELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK14271 163 RLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADRL--TVIIVTHNLAQAARISDRAALFFDGRL 240

                        250       260
                 ....*....|....*....|....*...
gi 14028433  223 EQVGSPEQIYLEP----NSRFVAGFIGN 246
Cdd:PRK14271 241 VEEGPTEQLFSSPkhaeTARYVAGLSGD 268

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

28-202

4.88e-25

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 106.04 E-value: 4.88e-25

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVsisgvdvtdraARARDVGMVF---QNYalFPHLTARE 104
Cdd:COG4178 378 LLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-----------ARPAGARVLFlpqRPY--LPLGTLRE 444

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 105 NVEYPlkvrRLPREERRRRALEYLERVHLSEWADRY------PRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:COG4178 445 ALLYP----ATAEAFSDAELREALEAVGLGHLAERLdeeadwDQVLSLGEQQRLAFARLLLHKPDWLFLDEATSALDEEN 520

                       170       180
                ....*....|....*....|....*
gi 14028433 179 RGQMqdfLKELQRDL-GITFVHVTH 202
Cdd:COG4178 521 EAAL---YQLLREELpGTTVISVGH 542

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

24-236

4.91e-25

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 102.57 E-value: 4.91e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNY--ALFPH 99
Cdd:PRK13652  15 GSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREvrKFVGLVFQNPddQIFSP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  100 lTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:PRK13652  95 -TVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGV 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433  180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:PRK13652 174 KELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQPD 230

cbiO

PRK13643

energy-coupling factor transporter ATPase;

25-234

5.47e-25

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 102.89 E-value: 5.47e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   25 AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA------RDVGMVFQ--NYAL 96
Cdd:PRK13643  18 ASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpvrKKVGVVFQfpESQL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   97 FPHlTARENVEYPLKVRRLPREERRRRALEYLERVHLS-EWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:PRK13643  98 FEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLAdEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLD 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433  176 KHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLE 234
Cdd:PRK13643 177 PKARIEMMQLFESIHQS-GQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

27-236

1.55e-24

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 101.31 E-value: 1.55e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG----VDVTDRAARARDVGMVFQNY--ALF-Ph 99
Cdd:PRK13639  16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGepikYDKKSLLEVRKTVGIVFQNPddQLFaP- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  100 lTARENVEY-PLKVRRLPREERRRRALEyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:PRK13639  95 -TVEEDVAFgPLNLGLSKEEVEKRVKEA-LKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMG 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433  179 RGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:PRK13639 173 ASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

24-203

1.69e-24

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: 104.36 E-value: 1.69e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFpHLT 101
Cdd:TIGR02868 346 GAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSslDQDEVRRRVSVCAQDAHLF-DTT 424

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   102 ARENveyplkVRRLPREERRRRALEYLERVHLSEWADRYP-----------RELSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:TIGR02868 425 VREN------LRLARPDATDEELWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDEP 498

                         170       180       190
                  ....*....|....*....|....*....|...
gi 14028433   171 LSALDKHLRGQMQDFLkeLQRDLGITFVHVTHD 203
Cdd:TIGR02868 499 TEHLDAETADELLEDL--LAALSGRTVVLITHH 529

PRK15112

peptide ABC transporter ATP-binding protein SapF;

26-247

3.69e-24

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 99.86 E-value: 3.69e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQN--YALFPHLT 101
Cdd:PRK15112  26 VEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfgDYSYRSQRIRMIFQDpsTSLNPRQR 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  102 ARENVEYPLKVRRLPREERRRRA-LEYLERVHL-SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:PRK15112 106 ISQILDFPLRLNTDLEPEQREKQiIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMR 185

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP----NSRFVAGFIGNS 247
Cdd:PRK15112 186 SQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPlhelTKRLIAGHFGEA 257

PRK14243

phosphate transporter ATP-binding protein; Provisional

23-245

5.03e-24

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 99.47 E-value: 5.03e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLR-------IIAGFASvsEGTVSISGVDV----TDRAARARDVGMVF 91
Cdd:PRK14243  20 YGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyapdVDPVEVRRRIGMVF 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   92 QNYALFPHlTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRE---LSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:PRK14243  98 QKPNPFPK-SIYDNIAYGARINGYKGDMDELVERSLRQAALWDEVKDKLKQSglsLSGGQQQRLCIARAIAVQPEVILMD 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  169 EPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALALSSLVVIM---------RDGRLEQVGSPEQIYLEPNSR- 238
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFnveltegggRYGYLVEFDRTEKIFNSPQQQa 254

                        250
                 ....*....|
gi 14028433  239 ---FVAGFIG 245
Cdd:PRK14243 255 trdYVSGRFG 264

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

26-222

6.61e-24

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: 98.11 E-value: 6.61e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAG---FASVSEGTVSISGVDVtDRAARARDVGMVFQNYALFPHLTA 102
Cdd:cd03234  20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGrveGGGTTSGQILFNGQPR-KPDQFQKCVAYVRQDDILLPGLTV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 103 RENVEY----PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:cd03234  99 RETLTYtailRLPRKSSDAIRKKRVEDVLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....
gi 14028433 179 RGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03234 179 ALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEI 222

livG

PRK11300

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

10-231

7.06e-24

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 98.91 E-value: 7.06e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARdV 87
Cdd:PRK11300   2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHqiAR-M 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 GMV--FQNYALFPHLTAREN--VEYPLKVRRL-------------PREERRRRALEYLERVHLSEWADRYPRELSGGQQQ 150
Cdd:PRK11300  81 GVVrtFQHVRLFREMTVIENllVAQHQQLKTGlfsgllktpafrrAESEALDRAATWLERVGLLEHANRQAGNLAYGQQR 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  151 RVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEE 240


                 .
gi 14028433  231 I 231
Cdd:PRK11300 241 I 241

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

28-205

7.70e-24

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: 96.45 E-value: 7.70e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSIsgvdvtdraARARDVGMVFQNyALFPHLTARENVE 107
Cdd:cd03223  16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM---------PEGEDLLFLPQR-PYLPLGTLREQLI 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 108 YPlkvrrlpreerrrraleylervhlseWADryprELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKhlrgQMQDFLK 187
Cdd:cd03223  86 YP--------------------------WDD----VLSGGEQQRLAFARLLLHKPKFVFLDEATSALDE----ESEDRLY 131

                       170
                ....*....|....*...
gi 14028433 188 ELQRDLGITFVHVTHDQS 205
Cdd:cd03223 132 QLLKELGITVISVGHRPS 149

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

27-234

1.18e-23

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 98.77 E-value: 1.18e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVtDRAARA-----RDVGMVFQ--NYALFPh 99
Cdd:PRK13636  20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGlmklrESVGMVFQdpDNQLFS- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  100 LTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:PRK13636  98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLE 234
Cdd:PRK13636 178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

28-230

1.93e-23

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: 96.91 E-value: 1.93e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD--RAARARDVGMVFQNYALFPHlTAREN 105
Cdd:cd03254  18 VLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDisRKSLRSMIGVVLQDTFLFSG-TIMEN 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 106 VEY--PLKVRRLPREERRRRALEYLERvHLSEWADRYPRE----LSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:cd03254  97 IRLgrPNATDEEVIEAAKEAGAHDFIM-KLPNGYDTVLGEnggnLSQGERQLLAIARAMLRDPKILILDEATSNIDTETE 175

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14028433 180 GQMQDFLKELQRdlGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:cd03254 176 KLIQEALEKLMK--GRTSIIIAHRLS-TIKNADKILVLDDGKIIEEGTHDE 223

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

24-231

3.69e-23

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

Pssm-ID: 200134 [Multi-domain] Cd Length: 544 Bit Score: 100.50 E-value: 3.69e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFPHLT 101
Cdd:TIGR01842 329 GKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKqwDRETFGKHIGYLPQDVELFPGTV 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   102 A------RENVEyPLKVRRLPReerrrraleyLERVHlsEWADRYPR-----------ELSGGQQQRVALARSLVYRPKL 164
Cdd:TIGR01842 409 AeniarfGENAD-PEKIIEAAK----------LAGVH--ELILRLPDgydtvigpggaTLSGGQRQRIALARALYGDPKL 475

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433   165 LLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:TIGR01842 476 VVLDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPS-LLGCVDKILVLQDGRIARFGERDEV 540

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

9-228

4.79e-23

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: 101.24 E-value: 4.79e-23

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433      9 GSPPAIQISRLKKC---YGAVEVLRgLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARA 84
Cdd:TIGR01257  924 GLVPGVCVKNLVKIfepSGRPAVDR-LNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDAVR 1002

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     85 RDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:TIGR01257 1003 QSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKV 1082

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433    165 LLLDEPLSALDKHLRGQMQDFLkeLQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSP 228
Cdd:TIGR01257 1083 VVLDEPTSGVDPYSRRSIWDLL--LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGTP 1144

cbiO

PRK13644

energy-coupling factor transporter ATPase;

14-240

5.37e-23

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 96.98 E-value: 5.37e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA---RDVGM 89
Cdd:PRK13644   2 IRLENVSYSYpDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKLQgirKLVGI 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQN-YALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:PRK13644  82 VFQNpETQFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  169 EPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEaLALSSLVVIMRDGRLEQVGSPEQIYLEPNSRFV 240
Cdd:PRK13644 162 EVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHNLEE-LHDADRIIVMDRGKIVLEGEPENVLSDVSLQTL 231

cbiO

PRK13646

energy-coupling factor transporter ATPase;

27-232

6.41e-23

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 96.77 E-value: 6.41e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-------RAARARdVGMVFQ--NYALF 97
Cdd:PRK13646  21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkyiRPVRKR-IGMVFQfpESQLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   98 PHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKH 177
Cdd:PRK13646 100 EDTVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQ 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  178 LRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13646 180 SKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELF 234

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

9-226

8.18e-23

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: 95.29 E-value: 8.18e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   9 GSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdraaraRDVG 88
Cdd:cd03220  18 SSLKKLGILGRKGEVGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG----------RVSS 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  89 MVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:cd03220  88 LLGLGGGFNPELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSSGMKARLAFAIATALEPDILLID 167

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 169 EPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:cd03220 168 EVLAVGDAAFQEKCQRRLRELLKQ-GKTVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

12-238

1.09e-22

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 95.87 E-value: 1.09e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS-----EGTVSISGVDVTDRAARA-- 84
Cdd:PRK14258   6 PAIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELEsevrvEGRVEFFNQNIYERRVNLnr 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   85 --RDVGMVFQNYALFPhLTARENVEYPLK-VRRLPREERRRRALEYLERVHLseWAD------RYPRELSGGQQQRVALA 155
Cdd:PRK14258  86 lrRQVSMVHPKPNLFP-MSVYDNVAYGVKiVGWRPKLEIDDIVESALKDADL--WDEikhkihKSALDLSGGQQQRLCIA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  156 RSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIM-----RDGRLEQVGSPEQ 230
Cdd:PRK14258 163 RALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFkgnenRIGQLVEFGLTKK 242


                 ....*....
gi 14028433  231 IYLEP-NSR 238
Cdd:PRK14258 243 IFNSPhDSR 251

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

24-176

1.80e-22

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: 93.58 E-value: 1.80e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDVGMVFQNYALFPHLTA 102
Cdd:TIGR01189  11 GERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLaEQRDEPHENILYLGHLPGLKPELSA 90

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433   103 RENveypLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:TIGR01189  91 LEN----LHFWAAIHGGAQRTIEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDK 160

COG4586

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

17-222

3.31e-22

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 95.54 E-value: 3.31e-22

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  17 SRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVD-VTDRAARARDVGMVF-QNY 94
Cdd:COG4586  26 GLFRREYREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVpFKRRKEFARRIGVVFgQRS 105

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  95 ALFPHLTARENVE-----YPLkvrrlpreerrrRALEYLERVH-------LSEWADRYPRELSGGQQQRVALARSLVYRP 162
Cdd:COG4586 106 QLWWDLPAIDSFRllkaiYRI------------PDAEYKKRLDelvelldLGELLDTPVRQLSLGQRMRCELAAALLHRP 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 163 KLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG4586 174 KILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDRVIVIDHGRI 233

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

30-177

3.65e-22

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 92.94 E-value: 3.65e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   30 RGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDvgMVF---QNyALFPHLTAREN 105
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIrRQRDEYHQD--LLYlghQP-GIKTELTALEN 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  106 VEYPLKVRRLPREERRRRaleYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKH 177
Cdd:PRK13538  95 LRFYQRLHGPGDDEALWE---ALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAIDKQ 163

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

26-231

1.65e-21

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

Pssm-ID: 131258 [Multi-domain] Cd Length: 571 Bit Score: 95.94 E-value: 1.65e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFPHlTAR 103
Cdd:TIGR02203 345 RPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLASlrRQVALVSQDVVLFND-TIA 423

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   104 ENVEYplkvrRLPREERRRRALEYLERVHLSEWADRYPR-----------ELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:TIGR02203 424 NNIAY-----GRTEQADRAEIERALAAAYAQDFVDKLPLgldtpigengvLLSGGQRQRLAIARALLKDAPILILDEATS 498

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433   173 ALDKHLRGQMQDFLKELQRdlGITFVHVTHdqsealALSSL-----VVIMRDGRLEQVGSPEQI 231
Cdd:TIGR02203 499 ALDNESERLVQAALERLMQ--GRTTLVIAH------RLSTIekadrIVVMDDGRIVERGTHNEL 554

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

16-203

1.95e-21

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 95.52 E-value: 1.95e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  16 ISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvDVTdraarardVGMVFQNYA 95
Cdd:COG0488   1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPK-GLR--------IGYLPQEPP 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  96 LFPHLTARENVE------YPLKVRRLPREERRRRALEYLERV--------HLSEWA-------------------DRYPR 142
Cdd:COG0488  72 LDDDLTVLDTVLdgdaelRALEAELEELEAKLAEPDEDLERLaelqeefeALGGWEaearaeeilsglgfpeedlDRPVS 151

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 143 ELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQrdlgITFVHVTHD 203
Cdd:COG0488 152 ELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKNYP----GTVLVVSHD 208

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

26-221

2.09e-21

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: 91.34 E-value: 2.09e-21

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSI----SGVDVT---DR---AARARDVGMVFQnya 95
Cdd:COG4778  24 LPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAqasPReilALRRRTIGYVSQ--- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  96 lF----PHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSE--WaDRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:COG4778 101 -FlrviPRVSALDVVAEPLLERGVDREEARARARELLARLNLPErlW-DLPPATFSGGEQQRVNIARGFIADPPLLLLDE 178

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14028433 170 PLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:COG4778 179 PTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPFS 229

PRK11174

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

32-236

2.55e-21

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 95.30 E-value: 2.55e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   32 LDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVsEGTVSISGVDVT--DRAARARDVGMVFQNYALFpHLTARENVeyp 109
Cdd:PRK11174 369 LNFTLPAGQRIALVGPSGAGKTSLLNALLGFLPY-QGSLKINGIELRelDPESWRKHLSWVGQNPQLP-HGTLRDNV--- 443

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  110 lkvRRLPREERRRRALEYLERVHLSEWADRYPR-----------ELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:PRK11174 444 ---LLGNPDASDEQLQQALENAWVSEFLPLLPQgldtpigdqaaGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHS 520

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433  179 RGQMQDFLKELQRDLgiTFVHVTHdQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:PRK11174 521 EQLVMQALNAASRRQ--TTLMVTH-QLEDLAQWDQIWVMQDGQIVQQGDYAELSQAGG 575

livF

PRK11614

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

12-227

4.21e-21

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 90.71 E-value: 4.21e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-RAARA--RDVG 88
Cdd:PRK11614   4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDwQTAKImrEAVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   89 MVFQNYALFPHLTARENVeyplkvrrlPREERRRRALEYLERVhlsEWA-DRYPR----------ELSGGQQQRVALARS 157
Cdd:PRK11614  84 IVPEGRRVFSRMTVEENL---------AMGGFFAERDQFQERI---KWVyELFPRlherriqragTMSGGEQQMLAIGRA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  158 LVYRPKLLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGR--LEQVGS 227
Cdd:PRK11614 152 LMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHvvLEDTGD 222

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

19-231

6.33e-21

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 90.34 E-value: 6.33e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   19 LKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARA-RDVGMVFQNYA 95
Cdd:PRK10895   9 LAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISllPLHARArRGIGYLPQEAS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   96 LFPHLTARENVEYPLKVRRLPREERRRRALEYL-ERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PRK10895  89 IFRRLSVYDNLMAVLQIRDDLSAEQREDRANELmEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGV 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433  175 DKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK10895 169 DPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEI 224

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

11-220

6.57e-21

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.96 E-value: 6.57e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   11 PPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-RAARARDVG- 88
Cdd:PRK15439   9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARlTPAKAHQLGi 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   89 -MVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYleRVHLSewADRYPRELSGGQQQRVALARSLVYRPKLLLL 167
Cdd:PRK15439  89 yLVPQEPLLFPNLSVKENILFGLPKRQASMQKMKQLLAAL--GCQLD--LDSSAGSLEVADRQIVEILRGLMRDSRILIL 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433  168 DEPLSALDKH----LRGQMQDFlkeLQRDLGITFvhVTHDQSEALALSSLVVIMRDG 220
Cdd:PRK15439 165 DEPTASLTPAeterLFSRIREL---LAQGVGIVF--ISHKLPEIRQLADRISVMRDG 216

met_CoM_red_A2

TIGR03269

methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...

14-231

1.54e-20

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 92.94 E-value: 1.54e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF------------------------------- 62
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqyeptsgriiyhvalcekcgyverpskvge 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    63 -ASVSEGTVSISGVDVTD------RAARARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSE 135
Cdd:TIGR03269  81 pCPVCGGTLEPEEVDFWNlsdklrRRIRKRIAIMLQRTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   136 WADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVhVTHDQSEALA-LSSLV 214
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMV-LTSHWPEVIEdLSDKA 239

                         250
                  ....*....|....*..
gi 14028433   215 VIMRDGRLEQVGSPEQI 231
Cdd:TIGR03269 240 IWLENGEIKEEGTPDEV 256

cbiO

PRK13645

energy-coupling factor transporter ATPase;

20-232

1.90e-20

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 90.07 E-value: 1.90e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   20 KKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSI------SGVDVTDRAARAR-DVGMVFQ 92
Cdd:PRK13645  18 KKTPFEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVgdyaipANLKKIKEVKRLRkEIGLVFQ 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   93 --NYALFPHLTARENVEYPLKVRRLPREERRRRALEyLERVHL-SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:PRK13645  98 fpEYQLFQETIEKDIAFGPVNLGENKQEAYKKVPEL-LKLVQLpEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDE 176

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433  170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13645 177 PTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIF 239

ABC_Carb_Monos_II

cd03215

Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...

28-222

2.35e-20

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

Pssm-ID: 213182 [Multi-domain] Cd Length: 182 Bit Score: 87.10 E-value: 2.35e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR-ARDVGMVF-----QNYALFPHLT 101
Cdd:cd03215  15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRdAIRAGIAYvpedrKREGLVLDLS 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 102 ARENVeyplkvrrlpreerrrraleylervhlsewadRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ 181
Cdd:cd03215  95 VAENI--------------------------------ALSSLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDVGAKAE 142

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 14028433 182 MQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:cd03215 143 IYRLIREL-ADAGKAVLLISSELDELLGLCDRILVMYEGRI 182

PRK13651

cobalt transporter ATP-binding subunit; Provisional

20-231

4.21e-20

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 89.37 E-value: 4.21e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   20 KKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--------------- 84
Cdd:PRK13651  14 KKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTKekekvleklviqktr 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   85 -----------RDVGMVFQ--NYALFPHlTARENVEYPLKVRRLPREERRRRALEYLERVHLSE-WADRYPRELSGGQQQ 150
Cdd:PRK13651  94 fkkikkikeirRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLDEsYLQRSPFELSGGQKR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  151 RVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:PRK13651 173 RVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYD 251


                 .
gi 14028433  231 I 231
Cdd:PRK13651 252 I 252

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

45-235

1.04e-19

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 88.37 E-value: 1.04e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   45 LGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARD------------------VGMVFQ--NYALFPHlTARE 104
Cdd:PRK13631  58 IGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIGDKKNNHELitnpyskkiknfkelrrrVSMVFQfpEYQLFKD-TIEK 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  105 NVEYPLKVRRLPREERRRRALEYLERVHLSE-WADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQ 183
Cdd:PRK13631 137 DIMFGPVALGVKKSEAKKLAKFYLNKMGLDDsYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMM 216

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 14028433  184 DFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK13631 217 QLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ 267

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

27-192

2.35e-19

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 89.49 E-value: 2.35e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RAArardVGMVFQNYALFpHL 100
Cdd:COG5265 372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDvtqaslRAA----IGIVPQDTVLF-ND 446

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 101 TARENVEY------PLKVRRLPreerrrraleylERVHLSEWADRYPR-----------ELSGGQQQRVALARSLVYRPK 163
Cdd:COG5265 447 TIAYNIAYgrpdasEEEVEAAA------------RAAQIHDFIESLPDgydtrvgerglKLSGGEKQRVAIARTLLKNPP 514

                       170       180
                ....*....|....*....|....*....
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQRD 192
Cdd:COG5265 515 ILIFDEATSALDSRTERAIQAALREVARG 543

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

14-229

2.55e-19

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: 84.89 E-value: 2.55e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFAS--VSEGTVSISGVDVTDRAA--RAR-DVG 88
Cdd:cd03217   1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPKyeVTEGEILFKGEDITDLPPeeRARlGIF 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  89 MVFQNYALFPHLTAREnveyplkvrrlpreerrrraleYLervhlsewadRYPRE-LSGGQQQRVALARSLVYRPKLLLL 167
Cdd:cd03217  81 LAFQYPPEIPGVKNAD----------------------FL----------RYVNEgFSGGEKKRNEILQLLLLEPDLAIL 128

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433 168 DEPLSALD-KHLRgQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVV-IMRDGRLEQVGSPE 229
Cdd:cd03217 129 DEPDSGLDiDALR-LVAEVINKL-REEGKSVLIITHYQRLLDYIKPDRVhVLYDGRIVKSGDKE 190

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

24-235

2.66e-19

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 87.47 E-value: 2.66e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKT-TLLRIIAGFAS--VSEGTVSISGVDVTD------RAARARDVGMVFQN- 93
Cdd:PRK09473  27 GDVTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAAngRIGGSATFNGREILNlpekelNKLRAEQISMIFQDp 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   94 -YALFPHLTARENVEYPLKVRRLPREERR-RRALEYLERVHLSEWADR---YPRELSGGQQQRVALARSLVYRPKLLLLD 168
Cdd:PRK09473 107 mTSLNPYMRVGEQLMEVLMLHKGMSKAEAfEESVRMLDAVKMPEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433  169 EPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

14-221

6.08e-19

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: 87.96 E-value: 6.08e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF--ASVSEGTVSISGVDVTDRAAR---ARDVG 88
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVypHGTWDGEIYWSGSPLKASNIRdteRAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    89 MVFQNYALFPHLTARENV----EYPLKVRRLPREERRRRALEYLERVHLSEWADRYP-RELSGGQQQRVALARSLVYRPK 163
Cdd:TIGR02633  82 IIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIAKALNKQAR 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433   164 LLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:TIGR02633 162 LLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQ 218

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

27-239

1.17e-18

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: 84.07 E-value: 1.17e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV--TDRAARARDVGMVFQNYALFpHLTARE 104
Cdd:cd03252  16 VILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLalADPAWLRRQVGVVLQENVLF-NRSIRD 94

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 105 NVeyplKVRRLPREERRRRALEYLERVH-----LSEWADRYPRE----LSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:cd03252  95 NI----ALADPGMSMERVIEAAKLAGAHdfiseLPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALD 170

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433 176 ----KHLRGQMQDFLKelqrdlGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQIyLEPNSRF 239
Cdd:cd03252 171 yeseHAIMRNMHDICA------GRTVIIIAHRLS-TVKNADRIIVMEKGRIVEQGSHDEL-LAENGLY 230

BtuD

COG4138

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

29-236

1.19e-18

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

Pssm-ID: 443313 [Multi-domain] Cd Length: 248 Bit Score: 84.12 E-value: 1.19e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASvSEGTVSISGVDVTD----RAARARDV---------GM-VFQNY 94
Cdd:COG4138  12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLLP-GQGEILLNGRPLSDwsaaELARHRAYlsqqqsppfAMpVFQYL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  95 ALF-PHLTARENVEYPLkvrrlpreerrrralEYL-ERVHLsewADRYPR---ELSGGQQQRVALARSLVY-------RP 162
Cdd:COG4138  91 ALHqPAGASSEAVEQLL---------------AQLaEALGL---EDKLSRpltQLSGGEWQRVRLAAVLLQvwptinpEG 152

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433 163 KLLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:COG4138 153 QLLLLDEPMNSLDVAQQAALDRLLREL-CQQGITVVMSSHDLNHTLRHADRVWLLKQGKLVASGETAEVMTPEN 225

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

27-221

2.86e-18

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 85.91 E-value: 2.86e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   27 EVLRGLDLVIPEGSYTTFLGPSGSGKT----TLLRIIAGFASV-SEGTVSISGVDV------TDRAARARDVGMVFQN-- 93
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSvtalSILRLLPSPPVVyPSGDIRFHGESLlhaseqTLRGVRGNKIAMIFQEpm 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   94 YALFP-HLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADR---YPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:PRK15134 103 VSLNPlHTLEKQLYEVLSLHRGMRREAARGEILNCLDRVGIRQAAKRltdYPHQLSGGERQRVMIAMALLTRPELLIADE 182

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 14028433  170 PLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:PRK15134 183 PTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGR 234

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

28-176

3.79e-18

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

Pssm-ID: 213198 [Multi-domain] Cd Length: 201 Bit Score: 81.77 E-value: 3.79e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGV-DVTDRAARARDVGMVFQNYALFPHLTARENV 106
Cdd:cd03231  15 LFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGpLDFQRDSIARGLLYLGHAPGIKTTLSVLENL 94

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 107 EYplkvrrLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:cd03231  95 RF------WHADHSDEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTALDK 158

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

28-221

4.61e-18

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: 81.36 E-value: 4.61e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdraararDVGMVFQNYALFPhLTARENV- 106
Cdd:cd03250  20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG-----------SIAYVSQEPWIQN-GTIRENIl 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 107 ---EYplkvrrlpreerrrRALEYLERVH-------LSEWADRYPRE-------LSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:cd03250  88 fgkPF--------------DEERYEKVIKacalepdLEILPDGDLTEigekginLSGGQKQRISLARAVYSDADIYLLDD 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 170 PLSALDKH---------LRGQMQDflkelqrdlGITFVHVTHdQSEALALSSLVVIMRDGR 221
Cdd:cd03250 154 PLSAVDAHvgrhifencILGLLLN---------NKTRILVTH-QLQLLPHADQIVVLDNGR 204

3a01208

TIGR00958

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

26-235

5.78e-18

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 85.54 E-value: 5.78e-18

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFPHlTAR 103
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYlhRQVALVGQEPVLFSG-SVR 572

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   104 ENVEYPLKVRRLPREERRRRALEylerVH--LSEWADRYPRE-------LSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:TIGR00958 573 ENIAYGLTDTPDEEIMAAAKAAN----AHdfIMEFPNGYDTEvgekgsqLSGGQKQRIAIARALVRKPRVLILDEATSAL 648

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433   175 DkhlrGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVImRDGRLEQVGSPEQIYLEP 235
Cdd:TIGR00958 649 D----AECEQLLQESRSRASRTVLLIAHRLSTVERADQILVL-KKGSVVEMGTHKQLMEDQ 704

PRK10261

glutathione transporter ATP-binding protein; Provisional

26-235

6.87e-18

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 84.91 E-value: 6.87e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   26 VEVLRGLDLVIPEGSYTTFLGPSGSGKT----TLLRII--AGFASVSEGTV-------SISGVDVTD---RAARARDVGM 89
Cdd:PRK10261  29 IAAVRNLSFSLQRGETLAIVGESGSGKSvtalALMRLLeqAGGLVQCDKMLlrrrsrqVIELSEQSAaqmRHVRGADMAM 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQN--YALFPHLTARENVEYPLKV-RRLPREERRRRALEYLERVHLSEWA---DRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:PRK10261 109 IFQEpmTSLNPVFTVGEQIAESIRLhQGASREEAMVEAKRMLDQVRIPEAQtilSRYPHQLSGGMRQRVMIAMALSCRPA 188

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK10261 189 VLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAP 260

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

28-226

9.44e-18

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: 80.05 E-value: 9.44e-18

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-RAARARDVGMVFQNyalfPHL---TAR 103
Cdd:cd03247  17 VLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDlEKALSSLISVLNQR----PYLfdtTLR 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 104 ENVEyplkvrrlpreerrrraleylervhlsewadrypRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQ 183
Cdd:cd03247  93 NNLG----------------------------------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLL 138

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14028433 184 DFLKELQRDLgiTFVHVTHDQSeALALSSLVVIMRDGRLEQVG 226
Cdd:cd03247 139 SLIFEVLKDK--TLIWITHHLT-GIEHMDKILFLENGKIIMQG 178

PRK13549

xylose transporter ATP-binding subunit; Provisional

10-221

1.20e-17

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 84.21 E-value: 1.20e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS--EGTVSISGVDVtdRAARARD- 86
Cdd:PRK13549   2 MEYLLEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL--QASNIRDt 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   87 ----VGMVFQNYALFPHLTARENV---EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLV 159
Cdd:PRK13549  80 eragIAIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALN 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  160 YRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:PRK13549 160 KQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGR 220

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

14-204

1.27e-17

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: 78.64 E-value: 1.27e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVdvtdraarardvgmvfqn 93
Cdd:cd03221   1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST------------------ 62

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 yalfphltarenveypLKVRrlpreerrrraleYLERvhlsewadrypreLSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03221  63 ----------------VKIG-------------YFEQ-------------LSGGEKMRLALAKLLLENPNLLLLDEPTNH 100

                       170       180       190
                ....*....|....*....|....*....|.
gi 14028433 174 LDKHLRGQMQDFLKELQRdlgiTFVHVTHDQ 204
Cdd:cd03221 101 LDLESIEALEEALKEYPG----TVILVSHDR 127

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

23-243

1.72e-17

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 80.93 E-value: 1.72e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVsisgvdvtDRAARARdVGMVFQNYALFPHLta 102
Cdd:PRK09544  14 FGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------KRNGKLR-IGYVPQKLYLDTTL-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  103 renveyPLKVRRLPREERRRRALEY---LERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:PRK09544  83 ------PLTVNRFLRLRPGTKKEDIlpaLKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433  180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMrDGRLEQVGSPEQIYLEPNsrFVAGF 243
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVLCL-NHHICCSGTPEVVSLHPE--FISMF 217

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

36-235

2.69e-17

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 81.71 E-value: 2.69e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   36 IPEGSYTTFLGPSGSGKTTLLRIIAGF----ASVSEGTVSISGVDVTDRAARAR------DVGMVFQN--YALFPHLTAR 103
Cdd:PRK11022  30 VKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKERrnlvgaEVAMIFQDpmTSLNPCYTVG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  104 ENVEYPLKV-RRLPREERRRRALEYLERVHLSEWADR---YPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:PRK11022 110 FQIMEAIKVhQGGNKKTRRQRAIDLLNQVGIPDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIADEPTTALDVTIQ 189

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433  180 GQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK11022 190 AQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAP 245

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

11-232

3.29e-17

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: 79.23 E-value: 3.29e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  11 PPAIQISRLKKcYGAVE--VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAG----FASVsEGTVSISGVDVTDRAARA 84
Cdd:cd03233   4 LSWRNISFTTG-KGRSKipILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSV-EGDIHYNGIPYKEFAEKY 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  85 -RDVGMVFQNYALFPHLTARENVEYPLKVRrlpreerrrraleylervhlsewADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:cd03233  82 pGEIIYVSEEDVHFPTLTVRETLDFALRCK-----------------------GNEFVRGISGGERKRVSIAEALVSRAS 138

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 164 LLLLDEPLSALDKHLRGQMQDFLKELQRDLGIT-FVHVTHDQSEALALSSLVVIMRDGRleqvgspeQIY 232
Cdd:cd03233 139 VLCWDNSTRGLDSSTALEILKCIRTMADVLKTTtFVSLYQASDEIYDLFDKVLVLYEGR--------QIY 200

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

28-219

5.54e-17

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 78.85 E-value: 5.54e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASvseGTVSISGVDVTDRAarardvgmVFQNYALFPHLTARENVE 107
Cdd:COG2401  45 VLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALK---GTPVAGCVDVPDNQ--------FGREASLIDAIGRKGDFK 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 108 YPLKVrrlpreerrrraleyLERVHLSE---WADRYpRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQD 184
Cdd:COG2401 114 DAVEL---------------LNAVGLSDavlWLRRF-KELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVAR 177

                       170       180       190
                ....*....|....*....|....*....|....*
gi 14028433 185 FLKELQRDLGITFVHVTHDQSEALALSSLVVIMRD 219
Cdd:COG2401 178 NLQKLARRAGITLVVATHHYDVIDDLQPDLLIFVG 212

PRK13543

heme ABC exporter ATP-binding protein CcmA;

10-175

8.58e-17

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 78.35 E-value: 8.58e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTdRAARARDVGM 89
Cdd:PRK13543   8 APPLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAT-RGDRSRFMAY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   90 VFQNYALFPHLTARENVEYplkVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:PRK13543  87 LGHLPGLKADLSTLENLHF---LCGLHGRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDE 163


                 ....*.
gi 14028433  170 PLSALD 175
Cdd:PRK13543 164 PYANLD 169

PRK10575

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

28-231

8.73e-17

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 79.45 E-value: 8.73e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG--VDVTDRAARARDVGMVFQNYALFPHLTAREN 105
Cdd:PRK10575  26 LLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAqpLESWSSKAFARKVAYLPQQLPAAEGMTVREL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  106 V---EYPLK-VRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ 181
Cdd:PRK10575 106 VaigRYPWHgALGRFGAADREKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 14028433  182 MQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK10575 186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

23-231

1.83e-16

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 77.81 E-value: 1.83e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdraaraR-----DVGMVFQnyalf 97
Cdd:COG1134  36 REEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG----------RvsallELGAGFH----- 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  98 PHLTARENVeyplkvrrlpreerrrraleYL-------------ERVH-------LSEWADRyP-RELSGGQQQRVALAR 156
Cdd:COG1134 101 PELTGRENI--------------------YLngrllglsrkeidEKFDeivefaeLGDFIDQ-PvKTYSSGMRARLAFAV 159

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433 157 SLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:COG1134 160 ATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRES-GRTVIFVSHSMGAVRRLCDRAIWLEKGRLVMDGDPEEV 233

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

27-229

1.90e-16

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 77.80 E-value: 1.90e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFAS--VSEGTVSISGVDVTDRAA--RARD-VGMVFQNYALFPHLT 101
Cdd:COG0396  14 EILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPKyeVTSGSILLDGEDILELSPdeRARAgIFLAFQYPVEIPGVS 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 102 ARE--------NVEYPLKVRRLPREERRrraleYLERVHLSE-WADRYPRE-LSGGQQQRVALARSLVYRPKLLLLDEPL 171
Cdd:COG0396  94 VSNflrtalnaRRGEELSAREFLKLLKE-----KMKELGLDEdFLDRYVNEgFSGGEKKRNEILQMLLLEPKLAILDETD 168

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 172 SALD----KHLRGQMQDFLKElqrdlGITFVHVTHdqSEALaLSSL----VVIMRDGRLEQVGSPE 229
Cdd:COG0396 169 SGLDidalRIVAEGVNKLRSP-----DRGILIITH--YQRI-LDYIkpdfVHVLVDGRIVKSGGKE 226

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

25-192

2.48e-16

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: 77.13 E-value: 2.48e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  25 AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARDVGMVFQNYALFPHlTA 102
Cdd:cd03248  26 DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKylHSKVSLVGQEPVLFAR-SL 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 103 RENVEYPLkvRRLPREERRRRALEYLERVHLSEWADRYPRE-------LSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:cd03248 105 QDNIAYGL--QSCSFECVKEAAQKAHAHSFISELASGYDTEvgekgsqLSGGQKQRVAIARALIRNPQVLILDEATSALD 182

                       170
                ....*....|....*..
gi 14028433 176 KHLRGQMQDFLKELQRD 192
Cdd:cd03248 183 AESEQQVQQALYDWPER 199

PRK15056

manganese/iron ABC transporter ATP-binding protein;

10-203

2.88e-16

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 78.00 E-value: 2.88e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDvTDRAARARDVG 88
Cdd:PRK15056   3 QQAGIVVNDVTVTWrNGHTALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQP-TRQALQKNLVA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   89 MVFQNYAL---FPHLTarENV----EYP-LKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVY 160
Cdd:PRK15056  82 YVPQSEEVdwsFPVLV--EDVvmmgRYGhMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARAIAQ 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 14028433  161 RPKLLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHD 203
Cdd:PRK15056 160 QGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHN 201

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

12-223

2.92e-16

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 79.72 E-value: 2.92e-16

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSIsGVDVTdraarardVGMVF 91
Cdd:COG0488 314 KVLELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVK--------IGYFD 384

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  92 QNYALF-PHLTARENVEYplkvrrLPREERRRRALEYLERVHLS-EWADRYPRELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:COG0488 385 QHQEELdPDKTVLDELRD------GAPGGTEQEVRGYLGRFLFSgDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDE 458

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 170 PLSALDKHLRGQMQDFLKELQrdlGiTFVHVTHDQSealALSSLV---VIMRDGRLE 223
Cdd:COG0488 459 PTNHLDIETLEALEEALDDFP---G-TVLLVSHDRY---FLDRVAtriLEFEDGGVR 508

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

12-220

3.10e-16

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 79.83 E-value: 3.10e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVD---VTDRAARARDVG 88
Cdd:PRK09700   4 PYISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINynkLDHKLAAQLGIG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   89 MVFQNYALFPHLTARENV---EYPLK----VRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYR 161
Cdd:PRK09700  84 IIYQELSVIDELTVLENLyigRHLTKkvcgVNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433  162 PKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDG 220
Cdd:PRK09700 164 AKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDG 221

PRK11160

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

10-230

4.14e-16

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 79.48 E-value: 4.14e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCY--GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD------RA 81
Cdd:PRK11160 335 DQVSLTLNNVSFTYpdQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADyseaalRQ 414

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   82 ArardVGMVFQNYALFPHlTARENveypLKVRRLPREERRRRALeyLERVHLSEWADRYP----------RELSGGQQQR 151
Cdd:PRK11160 415 A----ISVVSQRVHLFSA-TLRDN----LLLAAPNASDEALIEV--LQQVGLEKLLEDDKglnawlgeggRQLSGGEQRR 483

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  152 VALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgiTFVHVTHdqsEALALSSL--VVIMRDGRLEQVGSPE 229
Cdd:PRK11160 484 LGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQNK--TVLMITH---RLTGLEQFdrICVMDNGQIIEQGTHQ 558


                 .
gi 14028433  230 Q 230
Cdd:PRK11160 559 E 559

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

10-238

4.60e-16

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 77.05 E-value: 4.60e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKkCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKT----TLLRIIAGFASVSEGTVSISGVDVTDRAARAR 85
Cdd:PRK10418   1 MPQQIELRNIA-LQAAQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVAPCALRGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   86 DVGMVFQN--YALFPHLTARENVEYPLKVRRLPREERRRRALeyLERVHLSEWA---DRYPRELSGGQQQRVALARSLVY 160
Cdd:PRK10418  80 KIATIMQNprSAFNPLHTMHTHARETCLALGKPADDATLTAA--LEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLC 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433  161 RPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSR 238
Cdd:PRK10418 158 EAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHA 235

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

13-170

1.54e-15

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 78.24 E-value: 1.54e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARdvgmVFQ 92
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMADARHRRA----VCP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   93 NYA---------LFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:NF033858  77 RIAympqglgknLYPTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPD 156


                 ....*..
gi 14028433  164 LLLLDEP 170
Cdd:NF033858 157 LLILDEP 163

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

12-228

2.10e-15

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

Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 74.45 E-value: 2.10e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  12 PAIQISRLKKCY--GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD---RAARARd 86
Cdd:cd03244   1 GDIEFKNVSLRYrpNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKiglHDLRSR- 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 VGMVFQNYALFPHlTARENVEyPLKvrrlprEERRRRALEYLERVHLSEWADRYP-----------RELSGGQQQRVALA 155
Cdd:cd03244  80 ISIIPQDPVLFSG-TIRSNLD-PFG------EYSDEELWQALERVGLKEFVESLPggldtvveeggENLSVGQRQLLCLA 151

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 156 RSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlgITFVHVTHdQSEALALSSLVVIMRDGRLEQVGSP 228
Cdd:cd03244 152 RALLRKSKILVLDEATASVDPETDALIQKTIREAFKD--CTVLTIAH-RLDTIIDSDRILVLDKGRVVEFDSP 221

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

14-234

2.18e-15

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: 77.47 E-value: 2.18e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYG-AVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMV 90
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKdiDRHTLRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    91 FQNYALFPH-------LTARENVEyplkvrrlpreerrrrALEYLERVHLSEWADR-------YPREL-------SGGQQ 149
Cdd:TIGR01193 554 PQEPYIFSGsilenllLGAKENVS----------------QDEIWAACEIAEIKDDienmplgYQTELseegssiSGGQK 617

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   150 QRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlgiTFVHVTHDQSEAlALSSLVVIMRDGRLEQVGSPE 229
Cdd:TIGR01193 618 QRIALARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVA-KQSDKIIVLDHGKIIEQGSHD 693


                  ....*
gi 14028433   230 QIYLE 234
Cdd:TIGR01193 694 ELLDR 698

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

39-208

2.85e-15

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: 73.43 E-value: 2.85e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  39 GSYTTFLGPSGSGKTTLLRIIAG--FASVSEGTVSISGVDVTDraARARDVGMVFQNYALFPHLTARENVEYPLKVrrlp 116
Cdd:cd03232  33 GTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDK--NFQRSTGYVEQQDVHSPNLTVREALRFSALL---- 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 117 reerrrraleylervhlsewadrypRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGIT 196
Cdd:cd03232 107 -------------------------RGLSVEQRKRLTIGVELAAKPSILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQA 160

                       170
                ....*....|..
gi 14028433 197 FVHVTHDQSEAL 208
Cdd:cd03232 161 ILCTIHQPSASI 172

3a01204

TIGR00955

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

14-230

4.16e-15

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 76.62 E-value: 4.16e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCY----GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF---ASVSEGTVSISGVDVTDRAARARD 86
Cdd:TIGR00955  22 QLVSRLRGCFcrerPRKHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRspkGVKGSGSVLLNGMPIDAKEMRAIS 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    87 vGMVFQNYALFPHLTARENVEYPLKV---RRLPREERRRRALEYLERVHLSEWAD------RYPRELSGGQQQRVALARS 157
Cdd:TIGR00955 102 -AYVQQDDLFIPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANtrigvpGRVKGLSGGERKRLAFASE 180

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433   158 LVYRPKLLLLDEPLSALDKHLRGQMQDFLKEL-QRdlGITFVHVTHD-QSEALALSSLVVIMRDGRLEQVGSPEQ 230
Cdd:TIGR00955 181 LLTDPPLLFCDEPTSGLDSFMAYSVVQVLKGLaQK--GKTIICTIHQpSSELFELFDKIILMAEGRVAYLGSPDQ 253

PRK11176

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

29-192

5.11e-15

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 76.21 E-value: 5.11e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD-RAARARD-VGMVFQNYALFpHLTARENV 106
Cdd:PRK11176 359 LRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDyTLASLRNqVALVSQNVHLF-NDTIANNI 437

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  107 EYPLKvrrlpreerrrraleylervhlsewaDRYPRE--------------------------------LSGGQQQRVAL 154
Cdd:PRK11176 438 AYART--------------------------EQYSREqieeaarmayamdfinkmdngldtvigengvlLSGGQRQRIAI 491

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 14028433  155 ARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRD 192
Cdd:PRK11176 492 ARALLRDSPILILDEATSALDTESERAIQAALDELQKN 529

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

28-176

6.82e-15

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 72.68 E-value: 6.82e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDVGMVFQNYALFPHLTARENV 106
Cdd:PRK13540  16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIkKDLCTYQKQLCFVGHRSGINPYLTLRENC 95

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  107 EYPLKVRRLPREERRRRALEYLErvHLSEwadrYP-RELSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:PRK13540  96 LYDIHFSPGAVGITELCRLFSLE--HLID----YPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160

MglA

COG1129

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

49-222

1.42e-14

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 74.67 E-value: 1.42e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  49 GSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR-ARDVGMVF-----QNYALFPHLTARENVEYPL--KVRRLPREER 120
Cdd:COG1129 288 GAGRTELARALFGADPADSGEIRLDGKPVRIRSPRdAIRAGIAYvpedrKGEGLVLDLSIRENITLASldRLSRGGLLDR 367

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 121 RRraleylERVHLSEWAD----RYP------RELSGGQQQRVALARSLVYRPKLLLLDEPlsaldkhLRG-------QMQ 183
Cdd:COG1129 368 RR------ERALAEEYIKrlriKTPspeqpvGNLSGGNQQKVVLAKWLATDPKVLILDEP-------TRGidvgakaEIY 434

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 14028433 184 DFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG1129 435 RLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRI 472

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

7-207

1.47e-14

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 75.16 E-value: 1.47e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    7 DCGSPPAIQISRLKKCYG---AVEvlrGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG--VDVTDRA 81
Cdd:NF033858 260 DDDDEPAIEARGLTMRFGdftAVD---HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGqpVDAGDIA 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   82 ARARdVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYR 161
Cdd:NF033858 337 TRRR-VGYMSQAFSLYGELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHK 415

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 14028433  162 PKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGIT-FVHvTHDQSEA 207
Cdd:NF033858 416 PELLILDEPTSGVDPVARDMFWRLLIELSREDGVTiFIS-THFMNEA 461

PTZ00243

ABC transporter; Provisional

27-227

2.28e-14

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 74.82 E-value: 2.28e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTV----SISGV-------DVT----------DRAARAR 85
Cdd:PTZ00243  674 VLLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVwaerSIAYVpqqawimNATvrgnilffdeEDAARLA 753

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    86 DVGMVFQNYALFPHLTARENVEYPLKVRrlpreerrrraleylervhlsewadryprELSGGQQQRVALARSLVYRPKLL 165
Cdd:PTZ00243  754 DAVRVSQLEADLAQLGGGLETEIGEKGV-----------------------------NLSGGQKARVSLARAVYANRDVY 804

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433   166 LLDEPLSALDKHLrGQ--MQD-FLKELQrdlGITFVHVTHdQSEALALSSLVVIMRDGRLEQVGS 227
Cdd:PTZ00243  805 LLDDPLSALDAHV-GErvVEEcFLGALA---GKTRVLATH-QVHVVPRADYVVALGDGRVEFSGS 864

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

10-222

2.30e-14

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 74.18 E-value: 2.30e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV---TDRAARARD 86
Cdd:PRK11288   1 SSPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMrfaSTTAALAAG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   87 VGMVFQNYALFPHLTARENV---EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPK 163
Cdd:PRK11288  81 VAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNAR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433  164 LLLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK11288 161 VIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFKDGRY 218

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

11-227

2.67e-14

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 73.84 E-value: 2.67e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   11 PPAIQISRLKkcyGAVEV-------------LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV 77
Cdd:PRK13657 323 PGAIDLGRVK---GAVEFddvsfsydnsrqgVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDI 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   78 TD--RAARARDVGMVFQNYALFPHlTARENveypLKVRRLPREERRRRALeyLERVHLSEWADRYP-----------REL 144
Cdd:PRK13657 400 RTvtRASLRRNIAVVFQDAGLFNR-SIEDN----IRVGRPDATDEEMRAA--AERAQAHDFIERKPdgydtvvgergRQL 472

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  145 SGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgITFVhVTHDQSeALALSSLVVIMRDGRLEQ 224
Cdd:PRK13657 473 SGGERQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKGR-TTFI-IAHRLS-TVRNADRILVFDNGRVVE 549


                 ...
gi 14028433  225 VGS 227
Cdd:PRK13657 550 SGS 552

PLN03211

ABC transporter G-25; Provisional

28-175

3.36e-14

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 73.76 E-value: 3.36e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAG--FASVSEGTVSISGVDVTDRAARArdVGMVFQNYALFPHLTAREN 105
Cdd:PLN03211  83 ILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQILKR--TGFVTQDDILYPHLTVRET 160

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433  106 VEY--------PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:PLN03211 161 LVFcsllrlpkSLTKQEKILVAESVISELGLTKCENTIIGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLD 238

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

15-203

3.37e-14

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

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 73.82 E-value: 3.37e-14

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    15 QISRLKKCYGA-VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVsisgvdvtdRAARARDVGMVFQN 93
Cdd:TIGR03719   6 TMNRVSKVVPPkKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEA---------RPQPGIKVGYLPQE 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    94 YALFPHLTARENVEYPLKVRRLPREERRRRALEYLE-----------------------------RVHLSEWADRYP--- 141
Cdd:TIGR03719  77 PQLDPTKTVRENVEEGVAEIKDALDRFNEISAKYAEpdadfdklaaeqaelqeiidaadawdldsQLEIAMDALRCPpwd 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433   142 ---RELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQrdlGiTFVHVTHD 203
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQEYP---G-TVVAVTHD 217

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

29-246

4.12e-14

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

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 73.83 E-value: 4.12e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdraararDVGMVFQNyALFPHLTARENVEY 108
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-----------SVAYVPQQ-AWIQNDSLRENILF 721

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    109 --PLKVRRLPREERRRRALEYLE------RVHLSEWAdrypRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRG 180
Cdd:TIGR00957  722 gkALNEKYYQQVLEACALLPDLEilpsgdRTEIGEKG----VNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHVGK 797

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433    181 QMQDFLKELQRDL-GITFVHVTHDQSeALALSSLVVIMRDGRLEQVGsPEQIYLEPNSRFvAGFIGN 246
Cdd:TIGR00957  798 HIFEHVIGPEGVLkNKTRILVTHGIS-YLPQVDVIIVMSGGKISEMG-SYQELLQRDGAF-AEFLRT 861

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

23-232

4.33e-14

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 71.58 E-value: 4.33e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISG--VDVTDRA--ARARDVGMVFQN--YAL 96
Cdd:PRK13638  11 YQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGkpLDYSKRGllALRQQVATVFQDpeQQI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   97 FpHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDK 176
Cdd:PRK13638  91 F-YTDIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRHQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDP 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433  177 HLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIY 232
Cdd:PRK13638 170 AGRTQMIAIIRRIVAQ-GNHVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVF 224

40850658_otr

NF000106

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

1-238

5.40e-14

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 72.08 E-value: 5.40e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    1 MSNASKDCGSPPAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGsgkttllriiagfASVSEGTVS--ISGVDV- 77
Cdd:NF000106   1 MTRKTISNGARNAVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*G-------------AA**RGALPahV*GPDAg 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   78 ----------TDRAARARDVGMVFQ-NYALFPHLTARENVEYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSG 146
Cdd:NF000106  68 rrpwrf*twcANRRALRRTIG*HRPvR*GRRESFSGRENLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  147 GQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVG 226
Cdd:NF000106 148 GMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADG 226

                        250
                 ....*....|..
gi 14028433  227 SPEQIYLEPNSR 238
Cdd:NF000106 227 KVDELKTKVGGR 238

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

44-244

6.08e-14

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 73.51 E-value: 6.08e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     44 FLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV-TDRAARARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRR 122
Cdd:TIGR01257 1970 LLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNISDVHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEK 2049

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    123 RALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTH 202
Cdd:TIGR01257 2050 VANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSH 2128

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 14028433    203 DQSEALALSSLVVIMRDGRLEQVGSPEQIylepNSRFVAGFI 244
Cdd:TIGR01257 2129 SMEECEALCTRLAIMVKGAFQCLGTIQHL----KSKFGDGYI 2166

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

32-205

1.02e-13

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

Pssm-ID: 273360 [Multi-domain] Cd Length: 659 Bit Score: 72.47 E-value: 1.02e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    32 LDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISgvdvtdraaraRDVGMVF--QNyalfPHL---TARENV 106
Cdd:TIGR00954 471 LSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP-----------AKGKLFYvpQR----PYMtlgTLRDQI 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   107 EYPLKVRRLPREERR-RRALEYLERVHLS-------------EWADryprELSGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:TIGR00954 536 IYPDSSEDMKRRGLSdKDLEQILDNVQLThilereggwsavqDWMD----VLSGGEKQRIAMARLFYHKPQFAILDECTS 611

                         170       180       190
                  ....*....|....*....|....*....|...
gi 14028433   173 ALDKhlrgQMQDFLKELQRDLGITFVHVTHDQS 205
Cdd:TIGR00954 612 AVSV----DVEGYMYRLCREFGITLFSVSHRKS 640

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

28-228

1.34e-13

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 70.24 E-value: 1.34e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAG--FASVSEGTVSISGvDVT-----------DRAARARDVgMVFQNY 94
Cdd:PRK13547  16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGdlTGGGAPRGARVTG-DVTlngeplaaidaPRLARLRAV-LPQAAQ 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   95 ALFPhLTARENV---EYP-LKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSL---------VYR 161
Cdd:PRK13547  94 PAFA-FSAREIVllgRYPhARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQP 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433  162 PKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSP 228
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAP 239

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

29-220

1.45e-13

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The sulfonylurea receptor SUR is an ATP transporter of the ABCC/MRP family with tandem ATPase binding domains. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.

Pssm-ID: 213257 [Multi-domain] Cd Length: 218 Bit Score: 69.28 E-value: 1.45e-13

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARARD------VGMVFQNYALFpHLTA 102
Cdd:cd03290  17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRsrnrysVAYAAQKPWLL-NATV 95

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 103 RENVEY--PLKVRRLPREERRRRALEYLERVHLSEWADRYPR--ELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHL 178
Cdd:cd03290  96 EENITFgsPFNKQRYKAVTDACSLQPDIDLLPFGDQTEIGERgiNLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHL 175

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 14028433 179 RGQ-MQDFLKELQRDLGITFVHVTHdQSEALALSSLVVIMRDG 220
Cdd:cd03290 176 SDHlMQEGILKFLQDDKRTLVLVTH-KLQYLPHADWIIAMKDG 217

PRK10790

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

28-239

3.05e-12

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 67.82 E-value: 3.05e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFPHlTAREN 105
Cdd:PRK10790 356 VLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVlrQGVAMVQQDPVVLAD-TFLAN 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  106 VEYPLKVRRLPREERrrraleyLERVHLSEWADRYP-----------RELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PRK10790 435 VTLGRDISEEQVWQA-------LETVQLAELARSLPdglytplgeqgNNLSVGQKQLLALARVLVQTPQILILDEATANI 507

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433  175 DKHLRGQMQDFLKELQRDlgITFVHVTHDQSEALALSSLVVIMRDGRLEQvGSPEQIyLEPNSRF 239
Cdd:PRK10790 508 DSGTEQAIQQALAAVREH--TTLVVIAHRLSTIVEADTILVLHRGQAVEQ-GTHQQL-LAAQGRY 568

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

27-228

3.33e-12

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: 65.13 E-value: 3.33e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFPHlTARE 104
Cdd:cd03369  22 PVLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIStiPLEDLRSSLTIIPQDPTLFSG-TIRS 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 105 NV----EYplkvrrlpreerrrRALEYLERVHLSEWADryprELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRG 180
Cdd:cd03369 101 NLdpfdEY--------------SDEEIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDA 162

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*....
gi 14028433 181 QMQDFLKELQRDLGI-TFVHVTHdqseALALSSLVVIMRDGRLEQVGSP 228
Cdd:cd03369 163 LIQKTIREEFTNSTIlTIAHRLR----TIIDYDKILVMDAGEVKEYDHP 207

PRK10762

D-ribose transporter ATP binding protein; Provisional

12-220

4.31e-12

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.95 E-value: 4.31e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT---DRAARARDVG 88
Cdd:PRK10762   3 ALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTfngPKSSQEAGIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   89 MVFQNYALFPHLTARENV----EYPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKL 164
Cdd:PRK10762  83 IIHQELNLIPQLTIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKV 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433  165 LLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDG 220
Cdd:PRK10762 163 IIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISHRLKEIFEICDDVTVFRDG 217

PLN03232

ABC transporter C family member; Provisional

29-302

2.10e-11

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 65.38 E-value: 2.10e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTvsisGVDVTDRAARARDVGMVFqnyalfpHLTARENVEY 108
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAETS----SVVIRGSVAYVPQVSWIF-------NATVRENILF 701

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   109 -----PLKVRRLPREERRRRALEYLERVHLSEWADRyPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQ 183
Cdd:PLN03232  702 gsdfeSERYWRAIDVTALQHDLDLLPGRDLTEIGER-GVNISGGQKQRVSMARAVYSNSDIYIFDDPLSALDAHVAHQVF 780

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   184 D--FLKELQrdlGITFVHVThDQSEALALSSLVVIMRDGRLEQVGSPEQiyLEPNSRFVAGFIGNSNIVCCSVTARNGRL 261
Cdd:PLN03232  781 DscMKDELK---GKTRVLVT-NQLHFLPLMDRIILVSEGMIKEEGTFAE--LSKSGSLFKKLMENAGKMDATQEVNTNDE 854

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 14028433   262 ATVKLGDGTEVGVPIPAGVTERLGVGEKSlLLLRPEKAETG 302
Cdd:PLN03232  855 NILKLGPTVTIDVSERNLGSTKQGKRGRS-VLVKQEERETG 894

PRK11147

ABC transporter ATPase component; Reviewed

23-205

2.82e-11

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 64.59 E-value: 2.82e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   23 YGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDR-----------------AARAR 85
Cdd:PRK11147  13 FSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLIVARlqqdpprnvegtvydfvAEGIE 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   86 DVGMVFQNYALFPHLTARENVEYPLKvrrlpreerrrraleYLERV-----HLSEW----------------ADRYPREL 144
Cdd:PRK11147  93 EQAEYLKRYHDISHLVETDPSEKNLN---------------ELAKLqeqldHHNLWqlenrinevlaqlgldPDAALSSL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  145 SGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQrdlGiTFVHVTHDQS 205
Cdd:PRK11147 158 SGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKTFQ---G-SIIFISHDRS 214

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

26-222

3.24e-11

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 64.28 E-value: 3.24e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA-RDVGMVF-----QNYALFPH 99
Cdd:COG3845 271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRErRRLGVAYipedrLGRGLVPD 350

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 100 LTARENVeyplkvRRLPREERRRRALEYLERVHLSEWAD--------RYP------RELSGGQQQRVALARSLVYRPKLL 165
Cdd:COG3845 351 MSVAENL------ILGRYRRPPFSRGGFLDRKAIRAFAEelieefdvRTPgpdtpaRSLSGGNQQKVILARELSRDPKLL 424

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433 166 LLDEPLSALD----KHLRGQMQDflkelQRDLGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:COG3845 425 IAAQPTRGLDvgaiEFIHQRLLE-----LRDAGAAVLLISEDLDEILALSDRIAVMYEGRI 480

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

21-221

3.74e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 64.37 E-value: 3.74e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   21 KCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDV---TDRAARARDVGMVFQNYALF 97
Cdd:PRK10982   6 KSFPGVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIdfkSSKEALENGISMVHQELNLV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   98 PHLTARENV---EYPLKVRRLPREERRRRALEYLERVHLsewaDRYPRE----LSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:PRK10982  86 LQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDI----DIDPRAkvatLSVSQMQMIEIAKAFSYNAKIVIMDEP 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 14028433  171 LSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:PRK10982 162 TSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQ 211

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

46-231

3.92e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 64.30 E-value: 3.92e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   46 GPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARAR-DVGMVF-----QNYALFPHLTARENVeYPLKVRRLPREE 119
Cdd:PRK15439 296 GVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRlARGLVYlpedrQSSGLYLDAPLAWNV-CALTHNRRGFWI 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  120 RRRRALEYLERVHLS-----EWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlG 194
Cdd:PRK15439 375 KPARENAVLERYRRAlnikfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLIRSIAAQ-N 453

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 14028433  195 ITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK15439 454 VAVLFISSDLEEIEQMADRVLVMHQGEISGALTGAAI 490

PRK03695

vitamin B12-transporter ATPase; Provisional

44-236

8.59e-11

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 61.49 E-value: 8.59e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   44 FLGPSGSGKTTLLRIIAGFASvSEGTVSISGVDVTDRAAR--ARDVG-----------M-VFQNYALfpHLTARENVEYP 109
Cdd:PRK03695  27 LVGPNGAGKSTLLARMAGLLP-GSGSIQFAGQPLEAWSAAelARHRAylsqqqtppfaMpVFQYLTL--HQPDKTRTEAV 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  110 LKVRRLPReerrrraleylERVHLSEWADRYPRELSGGQQQRVALA-------RSLVYRPKLLLLDEPLSALDKHLRGQM 182
Cdd:PRK03695 104 ASALNEVA-----------EALGLDDKLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSLDVAQQAAL 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14028433  183 QDFLKELQRdLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPN 236
Cdd:PRK03695 173 DRLLSELCQ-QGIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDEVLTPEN 225

PRK10762

D-ribose transporter ATP binding protein; Provisional

144-222

1.83e-10

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 61.94 E-value: 1.83e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  144 LSGGQQQRVALARSLVYRPKLLLLDEPLSALD----KHLRGQMQDFLKElqrdlGITFVHVTHDQSEALALSSLVVIMRD 219
Cdd:PRK10762 396 LSGGNQQKVAIARGLMTRPKVLILDEPTRGVDvgakKEIYQLINQFKAE-----GLSIILVSSEMPEVLGMSDRILVMHE 470


                 ...
gi 14028433  220 GRL 222
Cdd:PRK10762 471 GRI 473

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

45-203

2.78e-10

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 61.67 E-value: 2.78e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   45 LGPSGSGKTTLLRIIAGFASVSEGTVsisgvdvtdRAARARDVGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRA 124
Cdd:PRK11819  39 LGLNGAGKSTLLRIMAGVDKEFEGEA---------RPAPGIKVGYLPQEPQLDPEKTVRENVEEGVAEVKAALDRFNEIY 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  125 LEYLERV------------------HLSEW-----------ADRYP------RELSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:PRK11819 110 AAYAEPDadfdalaaeqgelqeiidAADAWdldsqleiamdALRCPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDE 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 14028433  170 PLSALDKHLRGQMQDFLKELQrdlGiTFVHVTHD 203
Cdd:PRK11819 190 PTNHLDAESVAWLEQFLHDYP---G-TVVAVTHD 219

3a01205

TIGR00956

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

26-238

5.66e-10

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 60.89 E-value: 5.66e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIA----GFASVSEGTVSISGVDVTDRAARAR-DVGMVFQNYALFPHL 100
Cdd:TIGR00956   74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRgDVVYNAETDVHFPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    101 TARENVEYPLKVRRLPREERRRRALEYLErvHLSEWA---------------DRYPRELSGGQQQRVALARSLVYRPKLL 165
Cdd:TIGR00956  154 TVGETLDFAARCKTPQNRPDGVSREEYAK--HIADVYmatyglshtrntkvgNDFVRGVSGGERKRVSIAEASLGGAKIQ 231

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433    166 LLDEPLSALDKHLRGQMQDFLKELQRDLGIT-FVHVTHDQSEALALSSLVVIMRDGRleqvgspeQIYLEPNSR 238
Cdd:TIGR00956  232 CWDNATRGLDSATALEFIRALKTSANILDTTpLVAIYQCSQDAYELFDKVIVLYEGY--------QIYFGPADK 297

ycf16

CHL00131

sulfate ABC transporter protein; Validated

12-234

8.70e-10

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 58.50 E-value: 8.70e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFAS--VSEGTVSISGVDVTDRAARARD--- 86
Cdd:CHL00131   6 PILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPAykILEGDILFKGESILDLEPEERAhlg 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   87 VGMVFQNYALFPHLTARENVEYPLKVRRLPREERRRRALEYLE-------RVHLSE-WADRYPRE-LSGGQQQRVALARS 157
Cdd:CHL00131  86 IFLAFQYPIEIPGVSNADFLRLAYNSKRKFQGLPELDPLEFLEiineklkLVGMDPsFLSRNVNEgFSGGEKKRNEILQM 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  158 LVYRPKLLLLDEPLSALDKhlrgqmqDFLKELQ------RDLGITFVHVTHDQSealaL-----SSLVVIMRDGRLEQVG 226
Cdd:CHL00131 166 ALLDSELAILDETDSGLDI-------DALKIIAeginklMTSENSIILITHYQR----LldyikPDYVHVMQNGKIIKTG 234


                 ....*....
gi 14028433  227 SPE-QIYLE 234
Cdd:CHL00131 235 DAElAKELE 243

PRK10789

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

28-235

2.61e-09

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 58.57 E-value: 2.61e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD---RAARARdVGMVFQNYALFPHLTA-- 102
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKlqlDSWRSR-LAVVSQTPFLFSDTVAnn 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  103 ---------RENVEYPLKvrrlpreerrrraleyLERVH-----LSEWADRYPRE----LSGGQQQRVALARSLVYRPKL 164
Cdd:PRK10789 409 ialgrpdatQQEIEHVAR----------------LASVHddilrLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEI 472

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433  165 LLLDEPLSALDKHLRGQMQDFLKELQRdlGITFVHVTHDQSeALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:PRK10789 473 LILDDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLS-ALTEASEILVMQHGHIAQRGNHDQLAQQS 540

PLN03130

ABC transporter C family member; Provisional

29-231

2.63e-09

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 58.98 E-value: 2.63e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAG-FASVSEGTVSISGvdvtdRAARARDVGMVFqnyalfpHLTARENVE 107
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGeLPPRSDASVVIRG-----TVAYVPQVSWIF-------NATVRDNIL 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   108 Y-----PLKVRRLPREERRRRALEYLERVHLSEWADRyPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQM 182
Cdd:PLN03130  701 FgspfdPERYERAIDVTALQHDLDLLPGGDLTEIGER-GVNISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQV 779

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 14028433   183 qdFLKELQRDL-GITFVHVThDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PLN03130  780 --FDKCIKDELrGKTRVLVT-NQLHFLSQVDRIILVHEGMIKEEGTYEEL 826

AAA

smart00382

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...

44-223

3.13e-09

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 55.07 E-value: 3.13e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     44 FLGPSGSGKTTLLRIIAGFASVSEGTVSIsgVDVTDRAARARDVGMVFQNYalfphltarenveyplkvrrlpreerrrr 123
Cdd:smart00382   7 IVGPPGSGKTTLARALARELGPPGGGVIY--IDGEDILEEVLDQLLLIIVG----------------------------- 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    124 aleylervhlsewadRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQD-----FLKELQRDLGITFV 198
Cdd:smart00382  56 ---------------GKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLleelrLLLLLKSEKNLTVI 120

                          170       180
                   ....*....|....*....|....*
gi 14028433    199 HVTHDQSEalALSSLVVIMRDGRLE 223
Cdd:smart00382 121 LTTNDEKD--LGPALLRRRFDRRIV 143

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

144-223

5.19e-09

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 57.53 E-value: 5.19e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   144 LSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLE 223
Cdd:TIGR02633 404 LSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKLK 482

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

38-225

5.36e-09

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 57.49 E-value: 5.36e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   38 EGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRA---ARARDVGMVFQNY---ALFPHLTARENVEYP-- 109
Cdd:PRK09700 288 RGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSpldAVKKGMAYITESRrdnGFFPNFSIAQNMAISrs 367

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  110 -----LKVRRLPREERRRRALEYLERVHLS---EWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQ 181
Cdd:PRK09700 368 lkdggYKGAMGLFHEVDEQRTAENQRELLAlkcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAE 447

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 14028433  182 MQDFLKELQrDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQV 225
Cdd:PRK09700 448 IYKVMRQLA-DDGKVILMVSSELPEIITVCDRIAVFCEGRLTQI 490

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

17-179

6.32e-09

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.

Pssm-ID: 213204 [Multi-domain] Cd Length: 246 Bit Score: 55.88 E-value: 6.32e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  17 SRLKKCYGavevlrGLDLVIPEGSYT-----TFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--------DRAAR 83
Cdd:cd03237   4 PTMKKTLG------EFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqyikaDYEGT 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  84 ARDVGM-VFQNYALFPHLtaRENVEYPLKvrrlpreerrrraleyLERVHlsewaDRYPRELSGGQQQRVALARSLVYRP 162
Cdd:cd03237  78 VRDLLSsITKDFYTHPYF--KTEIAKPLQ----------------IEQIL-----DREVPELSGGELQRVAIAACLSKDA 134

                       170
                ....*....|....*..
gi 14028433 163 KLLLLDEPLSALDKHLR 179
Cdd:cd03237 135 DIYLLDEPSAYLDVEQR 151

PTZ00265

multidrug resistance protein (mdr1); Provisional

26-175

7.07e-09

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 57.73 E-value: 7.07e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGV----DVTDRAARARdVGMVFQNYALFPHlT 101
Cdd:PTZ00265  398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDShnlkDINLKWWRSK-IGVVSQDPLLFSN-S 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   102 ARENVEYPL------------------------------KVRRLPREERRRRALEYLERVHL------------------ 133
Cdd:PTZ00265  476 IKNNIKYSLyslkdlealsnyynedgndsqenknkrnscRAKCAGDLNDMSNTTDSNELIEMrknyqtikdsevvdvskk 555

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433   134 -------SEWADRY-------PRELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:PTZ00265  556 vlihdfvSALPDKYetlvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLD 611

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

14-175

7.43e-09

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 57.25 E-value: 7.43e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSIsGVDVtdraararDVGMVFQN 93
Cdd:TIGR03719 323 IEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV--------KLAYVDQS 393

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    94 Y-ALFPHLTARE------------NVEYPLKvrrlpreerrrralEYLERVHLSEwADRYPR--ELSGGQQQRVALARSL 158
Cdd:TIGR03719 394 RdALDPNKTVWEeisggldiiklgKREIPSR--------------AYVGRFNFKG-SDQQKKvgQLSGGERNRVHLAKTL 458

                         170
                  ....*....|....*..
gi 14028433   159 VYRPKLLLLDEPLSALD 175
Cdd:TIGR03719 459 KSGGNVLLLDEPTNDLD 475

PLN03232

ABC transporter C family member; Provisional

28-239

9.09e-09

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 57.29 E-value: 9.09e-09

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARDVGMVFQNYALFPHlTAREN 105
Cdd:PLN03232 1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTdlRRVLSIIPQSPVLFSG-TVRFN 1329

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   106 VEyPLKvrrlprEERRRRALEYLERVHLSEWADRYP-----------RELSGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PLN03232 1330 ID-PFS------EHNDADLWEALERAHIKDVIDRNPfgldaevseggENFSVGQRQLLSLARALLRRSKILVLDEATASV 1402

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 14028433   175 DKHLRGQMQDFLKELQRDlgITFVHVTHDQSEALALSSLVViMRDGRLEQVGSPEQIYLEPNSRF 239
Cdd:PLN03232 1403 DVRTDSLIQRTIREEFKS--CTMLVIAHRLNTIIDCDKILV-LSSGQVLEYDSPQELLSRDTSAF 1464

SapD

COG4170

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

24-235

9.22e-09

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 56.07 E-value: 9.22e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFAS----VSEGTVSISGVDVTDRAARAR------DVGMVFQN 93
Cdd:COG4170  18 GRVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKAICGITKdnwhVTADRFRWNGIDLLKLSPRERrkiigrEIAMIFQE 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  94 yalfP--HLTARENVEYPLKVRRLPREER----------RRRALEYLERVHLSEWAD---RYPRELSGGQQQRVALARSL 158
Cdd:COG4170  98 ----PssCLDPSAKIGDQLIEAIPSWTFKgkwwqrfkwrKKRAIELLHRVGIKDHKDimnSYPHELTEGECQKVMIAMAI 173

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 159 VYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEP 235
Cdd:COG4170 174 ANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSP 250

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

44-222

9.89e-09

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 56.84 E-value: 9.89e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   44 FLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR-ARDVGMVF-----QNYALFPHLTARENVEYPLKvrrlpr 117
Cdd:PRK11288 284 LFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPRdAIRAGIMLcpedrKAEGIIPVHSVADNINISAR------ 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  118 eERRRRALEYLERVHLSEWADRYPRE--------------LSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQ 183
Cdd:PRK11288 358 -RHHLRAGCLINNRWEAENADRFIRSlniktpsreqlimnLSGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIY 436

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 14028433  184 DFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK11288 437 NVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRI 474

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

32-222

1.33e-08

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.52 E-value: 1.33e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   32 LDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT--DRAARARDVGMVFQNYALFPHLTARENVEyp 109
Cdd:PRK10522 342 INLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTaeQPEDYRKLFSAVFTDFHLFDQLLGPEGKP-- 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  110 lkvrrlpreERRRRALEYLER------VHLSEWADRYPReLSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRgqmQ 183
Cdd:PRK10522 420 ---------ANPALVEKWLERlkmahkLELEDGRISNLK-LSKGQKKRLALLLALAEERDILLLDEWAADQDPHFR---R 486

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 14028433  184 DFLKEL---QRDLGITFVHVTHDQSEALALSSLvVIMRDGRL 222
Cdd:PRK10522 487 EFYQVLlplLQEMGKTIFAISHDDHYFIHADRL-LEMRNGQL 527

PTZ00265

multidrug resistance protein (mdr1); Provisional

140-202

3.18e-08

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 55.42 E-value: 3.18e-08

                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433   140 YPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTH 202
Cdd:PTZ00265 1355 YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAH 1417

PRK15093

peptide ABC transporter ATP-binding protein SapD;

24-244

6.78e-08

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 53.65 E-value: 6.78e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFA----SVSEGTVSISGVDVTDRAARAR------DVGMVFQN 93
Cdd:PRK15093  18 GWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERrklvghNVSMIFQE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   94 yalfPH--LTARENVEYPLKVRR----------LPREERRRRALEYLERVHLSEWAD---RYPRELSGGQQQRVALARSL 158
Cdd:PRK15093  98 ----PQscLDPSERVGRQLMQNIpgwtykgrwwQRFGWRKRRAIELLHRVGIKDHKDamrSFPYELTEGECQKVMIAIAL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  159 VYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQIYLEPNSR 238
Cdd:PRK15093 174 ANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTPHHP 253


                 ....*.
gi 14028433  239 FVAGFI 244
Cdd:PRK15093 254 YTQALI 259

PLN03140

ABC transporter G family member; Provisional

26-175

8.18e-08

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 54.47 E-value: 8.18e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    26 VEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVS--EGTVSISGVDvTDRAARARDVGMVFQNYALFPHLTAR 103
Cdd:PLN03140  893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGGyiEGDIRISGFP-KKQETFARISGYCEQNDIHSPQVTVR 971

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   104 ENVEY------PLKVRRLPREERRRRALEYLERVHLSEWADRYP--RELSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:PLN03140  972 ESLIYsaflrlPKEVSKEEKMMFVDEVMELVELDNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051

3a01205

TIGR00956

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

28-175

9.82e-08

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 53.96 E-value: 9.82e-08

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGfaSVSEGTVSISGVDVTDR---AARARDVGMVFQNYALFPHLTARE 104
Cdd:TIGR00956  778 ILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAE--RVTTGVITGGDRLVNGRpldSSFQRSIGYVQQQDLHLPTSTVRE 855

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    105 NVEY------PLKVrrlpreeRRRRALEYLERV----HLSEWADRY---PRE-LSGGQQQRVALARSLVYRPKLLL-LDE 169
Cdd:TIGR00956  856 SLRFsaylrqPKSV-------SKSEKMEYVEEVikllEMESYADAVvgvPGEgLNVEQRKRLTIGVELVAKPKLLLfLDE 928


                   ....*.
gi 14028433    170 PLSALD 175
Cdd:TIGR00956  929 PTSGLD 934

GguA

NF040905

sugar ABC transporter ATP-binding protein;

21-221

1.31e-07

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 53.25 E-value: 1.31e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   21 KCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGF--ASVSEGTVSISGVDVTDRAARA-RDVGMVF--QNYA 95
Cdd:NF040905   9 KTFPGVKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVypHGSYEGEILFDGEVCRFKDIRDsEALGIVIihQELA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   96 LFPHLTARENV----EyPLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPL 171
Cdd:NF040905  89 LIPYLSIAENIflgnE-RAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPT 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 14028433  172 SALDKHLRGQMQDFLKELqRDLGITFVHVTHDQSEALALSSLVVIMRDGR 221
Cdd:NF040905 168 AALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGR 216

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

32-203

3.24e-07

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

Pssm-ID: 443659 [Multi-domain] Cd Length: 547 Bit Score: 52.11 E-value: 3.24e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  32 LDLVIPEGSyTTFL-GPSGSGKTTLLRIIAGFASVSEGTVSISGVDVT-DRAARARD---VgmVFQNYALFPHLTARENV 106
Cdd:COG4615 351 IDLTIRRGE-LVFIvGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTaDNREAYRQlfsA--VFSDFHLFDRLLGLDGE 427

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 107 EYPLKVrrlpreerrrraLEYLERVHLSE----WADRY-PRELSGGQQQRVALArsLVY---RPkLLLLDEplSALDkhl 178
Cdd:COG4615 428 ADPARA------------RELLERLELDHkvsvEDGRFsTTDLSQGQRKRLALL--VALledRP-ILVFDE--WAAD--- 487

                       170       180       190
                ....*....|....*....|....*....|....*
gi 14028433 179 rgqmQD----------FLKELQRdLGITFVHVTHD 203
Cdd:COG4615 488 ----QDpefrrvfyteLLPELKA-RGKTVIAISHD 517

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

29-231

3.38e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.97 E-value: 3.38e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdraararDVGMVFQNYALFPHLTARENVEY 108
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----------EVSVIAISAGLSGQLTGIENIEF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  109 PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKE 188
Cdd:PRK13546 109 KMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQKCLDKIYE 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 14028433  189 LqRDLGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK13546 189 F-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDV 230

PRK13549

xylose transporter ATP-binding subunit; Provisional

144-222

4.22e-07

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 51.47 E-value: 4.22e-07

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433  144 LSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK13549 406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

28-175

5.78e-07

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

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 51.45 E-value: 5.78e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASvSEGTVSISGVD---VTDRAARaRDVGMVFQNYALFPHlTARE 104
Cdd:TIGR01271 1234 VLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSwnsVTLQTWR-KAFGVIPQKVFIFSG-TFRK 1310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    105 NV--------EYPLKVRrlpreerrrraleylERVHLSEWADRYPREL-----------SGGQQQRVALARSLVYRPKLL 165
Cdd:TIGR01271 1311 NLdpyeqwsdEEIWKVA---------------EEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKIL 1375

                          170
                   ....*....|
gi 14028433    166 LLDEPLSALD 175
Cdd:TIGR01271 1376 LLDEPSAHLD 1385

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

34-217

1.15e-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: 50.17 E-value: 1.15e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  34 LVIP-EGSYTTFLGPSGSGKTTLLRIIAG------------------------------FASVSEGTVSIS----GVDVt 78
Cdd:COG1245  93 LPVPkKGKVTGILGPNGIGKSTALKILSGelkpnlgdydeepswdevlkrfrgtelqdyFKKLANGEIKVAhkpqYVDL- 171

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  79 draarardVGMVFQNyalfphlTARENVEyplKVRRLPREERrrraleYLERVHLSEWADRYPRELSGGQQQRVALARSL 158
Cdd:COG1245 172 --------IPKVFKG-------TVRELLE---KVDERGKLDE------LAEKLGLENILDRDISELSGGELQRVAIAAAL 227

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433 159 VYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVhVTHDqseaLA----LSSLVVIM 217
Cdd:COG1245 228 LRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEGKYVLV-VEHD----LAildyLADYVHIL 285

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

127-207

1.22e-06

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 50.01 E-value: 1.22e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  127 YLERVHLSEW-ADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHDQS 205
Cdd:PRK10938 384 WLDILGIDKRtADAPFHSLSWGQQRLALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHHAE 463


                 ..
gi 14028433  206 EA 207
Cdd:PRK10938 464 DA 465

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

34-217

1.54e-06

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 49.81 E-value: 1.54e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   34 LVIP-EGSYTTFLGPSGSGKTTLLRIIAG-----FASVsEGTVSISgvDVTDRAArardvGMVFQNYalFPHLTARE--- 104
Cdd:PRK13409  93 LPIPkEGKVTGILGPNGIGKTTAVKILSGelipnLGDY-EEEPSWD--EVLKRFR-----GTELQNY--FKKLYNGEikv 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  105 -----NVEYPLKVRR------LPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:PRK13409 163 vhkpqYVDLIPKVFKgkvrelLKKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 14028433  174 LDKHLRGQMQDFLKELQRdlGITFVHVTHDqseaLA----LSSLVVIM 217
Cdd:PRK13409 243 LDIRQRLNVARLIRELAE--GKYVLVVEHD----LAvldyLADNVHIA 284

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

34-217

1.56e-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: 48.90 E-value: 1.56e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  34 LVIP-EGSYTTFLGPSGSGKTTLLRIIAG--------FASVSEGTVSIS---GVDVTDRAARARD----VGMVFQNYALF 97
Cdd:cd03236  20 LPVPrEGQVLGLVGPNGIGKSTALKILAGklkpnlgkFDDPPDWDEILDefrGSELQNYFTKLLEgdvkVIVKPQYVDLI 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  98 PHlTARENVEYPLKvrrlpREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKH 177
Cdd:cd03236 100 PK-AVKGKVGELLK-----KKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 14028433 178 LRGQMQDFLKELQRDLGITFVhVTHDQSEALALSSLVVIM 217
Cdd:cd03236 174 QRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCL 212

PRK13541

cytochrome c biogenesis protein CcmA; Provisional

28-179

1.58e-06

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184128 [Multi-domain] Cd Length: 195 Bit Score: 48.33 E-value: 1.58e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARArdVGMVFQNYALFPHLTARENVE 107
Cdd:PRK13541  15 NLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPY--CTYIGHNLGLKLEMTVFENLK 92

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 14028433  108 YPLKVRRLPREERRRraleyLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLR 179
Cdd:PRK13541  93 FWSEIYNSAETLYAA-----IHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENR 159

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

28-175

1.66e-06

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: 49.08 E-value: 1.66e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdRAARARDVGMVFQNyalfphlTARENV- 106
Cdd:cd03291  52 VLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG-----RISFSSQFSWIMPG-------TIKENIi 119

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 107 ------EYPLKvrrlpreerrrralEYLERVHLSEWADRYPRE-----------LSGGQQQRVALARSLVYRPKLLLLDE 169
Cdd:cd03291 120 fgvsydEYRYK--------------SVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDS 185


                ....*.
gi 14028433 170 PLSALD 175
Cdd:cd03291 186 PFGYLD 191

PRK10636

putative ABC transporter ATP-binding protein; Provisional

12-223

1.91e-06

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 49.78 E-value: 1.91e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   12 PAIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSIsgvdvtdraARARDVGMVF 91
Cdd:PRK10636 311 PLLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL---------AKGIKLGYFA 381

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   92 QNYALFphLTARENveyPLKvrrlpreerrrraleylervHLSEWADRYP----------------------RELSGGQQ 149
Cdd:PRK10636 382 QHQLEF--LRADES---PLQ--------------------HLARLAPQELeqklrdylggfgfqgdkvteetRRFSGGEK 436

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 14028433  150 QRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLgitfVHVTHDQSEALALSSLVVIMRDGRLE 223
Cdd:PRK10636 437 ARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALIDFEGAL----VVVSHDRHLLRSTTDDLYLVHDGKVE 506

PLN03073

ABC transporter F family; Provisional

7-175

2.01e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 49.86 E-value: 2.01e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    7 DCGSPPAIQISRLKKCY-GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSisgvdvtdRAARAR 85
Cdd:PLN03073 502 DRPGPPIISFSDASFGYpGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVF--------RSAKVR 573

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   86 DVgmVFQNYalfpHLTARENVEYPLKVRRLPREERRRRALeyleRVHLSEW------ADRYPRELSGGQQQRVALARSLV 159
Cdd:PLN03073 574 MA--VFSQH----HVDGLDLSSNPLLYMMRCFPGVPEQKL----RAHLGSFgvtgnlALQPMYTLSGGQKSRVAFAKITF 643

                        170
                 ....*....|....*.
gi 14028433  160 YRPKLLLLDEPLSALD 175
Cdd:PLN03073 644 KKPHILLLDEPSNHLD 659

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

10-203

2.44e-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: 49.40 E-value: 2.44e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  10 SPPAIQISRLKKCYGA--VEVLRGldlVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSiSGVDV--------TD 79
Cdd:COG1245 338 EETLVEYPDLTKSYGGfsLEVEGG---EIREGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD-EDLKIsykpqyisPD 413

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  80 RAARARDVgmvfqnyaLFPHLTARENVEY-------PLKvrrlpreerrrraleyLERVHlsewaDRYPRELSGGQQQRV 152
Cdd:COG1245 414 YDGTVEEF--------LRSANTDDFGSSYykteiikPLG----------------LEKLL-----DKNVKDLSGGELQRV 464

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 14028433 153 ALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDLGITFVHVTHD 203
Cdd:COG1245 465 AIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHD 515

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

10-175

3.82e-06

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 48.65 E-value: 3.82e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   10 SPPAIQISRLKKCYGA--VEVLRGldlVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISgVDV--------TD 79
Cdd:PRK13409 337 RETLVEYPDLTKKLGDfsLEVEGG---EIYEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE-LKIsykpqyikPD 412

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   80 RAARARDV-GMVFQNYAlfphlTARENVEY--PLKvrrlpreerrrraleyLERVHlsewaDRYPRELSGGQQQRVALAR 156
Cdd:PRK13409 413 YDGTVEDLlRSITDDLG-----SSYYKSEIikPLQ----------------LERLL-----DKNVKDLSGGELQRVAIAA 466

                        170
                 ....*....|....*....
gi 14028433  157 SLVYRPKLLLLDEPLSALD 175
Cdd:PRK13409 467 CLSRDADLYLLDEPSAHLD 485

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

27-204

4.00e-06

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 47.48 E-value: 4.00e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   27 EVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFA--SVSEGTVSISGVDVTDRAARAR---DVGMVFQNYALFPHLT 101
Cdd:PRK09580  15 AILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRageGIFMAFQYPVEIPGVS 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  102 ARENVEYPLKVRRLPREERRRRALEYL----ERVHLSEW-ADRYPREL----SGGQQQRVALARSLVYRPKLLLLDEPLS 172
Cdd:PRK09580  95 NQFFLQTALNAVRSYRGQEPLDRFDFQdlmeEKIALLKMpEDLLTRSVnvgfSGGEKKRNDILQMAVLEPELCILDESDS 174

                        170       180       190
                 ....*....|....*....|....*....|..
gi 14028433  173 ALDKHLRGQMQDFLKELqRDLGITFVHVTHDQ 204
Cdd:PRK09580 175 GLDIDALKIVADGVNSL-RDGKRSFIIVTHYQ 205

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

144-222

4.18e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 48.57 E-value: 4.18e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  144 LSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKEL-QRDLGItfVHVTHDQSEALALSSLVVIMRDGRL 222
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELaKKDKGI--IIISSEMPELLGITDRILVMSNGLV 469

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

28-231

5.97e-06

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 48.40 E-value: 5.97e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD---RAARARdVGMVFQNYALFPHlTARE 104
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKiglHDLRFK-ITIIPQDPVLFSG-SLRM 1378

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    105 NVEyPLkvrrlpREERRRRALEYLERVHLSEWADRYP-----------RELSGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:TIGR00957 1379 NLD-PF------SQYSDEEVWWALELAHLKTFVSALPdkldhecaeggENLSVGQRQLVCLARALLRKTKILVLDEATAA 1451

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433    174 LDKHLRGQMQDFLKELQRDlgITFVHVTHDQSEALALSSlVVIMRDGRLEQVGSPEQI 231
Cdd:TIGR00957 1452 VDLETDNLIQSTIRTQFED--CTVLTIAHRLNTIMDYTR-VIVLDKGEVAEFGAPSNL 1506

PLN03073

ABC transporter F family; Provisional

134-202

6.38e-06

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 47.93 E-value: 6.38e-06

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433  134 SEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRdlgiTFVHVTH 202
Cdd:PLN03073 335 PEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWPK----TFIVVSH 399

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

29-231

6.70e-06

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 47.96 E-value: 6.70e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdraararDVGMVFQNYALFPHLTARENVEY 108
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKG-----------SAALIAISSGLNGQLTGIENIEL 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  109 PLKVRRLPREERRRRALEYLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKE 188
Cdd:PRK13545 109 KGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKMNE 188

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 14028433  189 LQRDlGITFVHVTHDQSEALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK13545 189 FKEQ-GKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

127-231

6.90e-06

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 47.70 E-value: 6.90e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  127 YLERVHLSEWADRYPRELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRDlGITFVHVTHDQSE 206
Cdd:PRK10938 119 LAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDE 197

                         90       100
                 ....*....|....*....|....*
gi 14028433  207 ALALSSLVVIMRDGRLEQVGSPEQI 231
Cdd:PRK10938 198 IPDFVQFAGVLADCTLAETGEREEI 222

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

28-175

8.28e-06

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 47.98 E-value: 8.28e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433     28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGvdvtdRAARARDVGMVFQNyalfphlTARENVE 107
Cdd:TIGR01271  441 VLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG-----RISFSPQTSWIMPG-------TIKDNII 508

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433    108 YPLKVRRLPREERrrraleyLERVHLSEWADRYPRE-----------LSGGQQQRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:TIGR01271  509 FGLSYDEYRYTSV-------IKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFTHLD 580

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

28-239

9.83e-06

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: 46.44 E-value: 9.83e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTD---RAARARdVGMVFQNYALFPHlTARE 104
Cdd:cd03288  36 VLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKlplHTLRSR-LSIILQDPILFSG-SIRF 113

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 105 NVEYPLKVRRLPREERrrraleyLERVHLSEWADRYPREL-----------SGGQQQRVALARSLVYRPKLLLLDEPLSA 173
Cdd:cd03288 114 NLDPECKCTDDRLWEA-------LEIAQLKNMVKSLPGGLdavvteggenfSVGQRQLFCLARAFVRKSSILIMDEATAS 186

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433 174 LDKHLRGQMQDFLKELQRDLgiTFVHVTHDQSEALAlSSLVVIMRDGRLEQVGSPEQIYLEPNSRF 239
Cdd:cd03288 187 IDMATENILQKVVMTAFADR--TVVTIAHRVSTILD-ADLVLVLSRGILVECDTPENLLAQEDGVF 249

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

24-175

1.13e-05

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: 46.39 E-value: 1.13e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  24 GAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASvSEGTVSISGVD---VTDRAARaRDVGMVFQNYALFPHl 100
Cdd:cd03289  15 GGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSwnsVPLQKWR-KAFGVIPQKVFIFSG- 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 101 TARENV--------EYPLKVRrlpreerrrraleylERVHLSEWADRYPRE-----------LSGGQQQRVALARSLVYR 161
Cdd:cd03289  92 TFRKNLdpygkwsdEEIWKVA---------------EEVGLKSVIEQFPGQldfvlvdggcvLSHGHKQLMCLARSVLSK 156

                       170
                ....*....|....
gi 14028433 162 PKLLLLDEPLSALD 175
Cdd:cd03289 157 AKILLLDEPSAHLD 170

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

29-204

1.79e-05

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

Pssm-ID: 213237 [Multi-domain] Cd Length: 226 Bit Score: 45.33 E-value: 1.79e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  29 LRGLDLVIPEGSYTTFLGPSGSGKTTL-------------LRIIAGFA-----SVSEGTV-SISGVDVT---DRAARARD 86
Cdd:cd03270  11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqrryVESLSAYArqflgQMDKPDVdSIEGLSPAiaiDQKTTSRN 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  87 ----VGMVFQNYALFPHLTARENVEYPLKvrrlpreerrrraleYLERV---HLSewADRYPRELSGGQQQRVALARSL- 158
Cdd:cd03270  91 prstVGTVTEIYDYLRLLFARVGIRERLG---------------FLVDVglgYLT--LSRSAPTLSGGEAQRIRLATQIg 153

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|..
gi 14028433 159 ------VYrpkllLLDEPLSALDKHLRGQMQDFLKELqRDLGITFVHVTHDQ 204
Cdd:cd03270 154 sgltgvLY-----VLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDE 199

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

18-243

1.86e-05

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: 44.87 E-value: 1.86e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  18 RLKKCYGAVEVLRGLDlVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRaarardvgmvfqnyalf 97
Cdd:cd03222   5 DCVKRYGVFFLLVELG-VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPVYK----------------- 66

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  98 phltarenveyPLKVrrlpreerrrraleylervhlsewadryprELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKH 177
Cdd:cd03222  67 -----------PQYI------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIE 105

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433 178 LRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVIMR-DGRLEQVGSPEQIYLEPNSRFVAGF 243
Cdd:cd03222 106 QRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVFEgEPGVYGIASQPKGTREGINRFLRGY 172

PTZ00243

ABC transporter; Provisional

28-239

2.03e-05

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 46.70 E-value: 2.03e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAARA--RDVGMVFQNYALFPHlTAREN 105
Cdd:PTZ00243 1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRElrRQFSMIPQDPVLFDG-TVRQN 1403

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   106 VEYPLKVRRLPREERrrraleyLERVHL-------SEWADryPRELSG------GQQQRVALARSLVYR-PKLLLLDEPL 171
Cdd:PTZ00243 1404 VDPFLEASSAEVWAA-------LELVGLrervaseSEGID--SRVLEGgsnysvGQRQLMCMARALLKKgSGFILMDEAT 1474

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 14028433   172 SALDKHLRGQMQD-FLKELQRDLGITFVHVTHdqseALALSSLVVIMRDGRLEQVGSPEQIYLEPNSRF 239
Cdd:PTZ00243 1475 ANIDPALDRQIQAtVMSAFSAYTVITIAHRLH----TVAQYDKIIVMDHGAVAEMGSPRELVMNRQSIF 1539

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

29-203

2.44e-05

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

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 44.24 E-value: 2.44e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLRiiAGFASvsegtvsisgvdvtdrAARARDVGmvfqnyalfphltARENVEY 108
Cdd:cd03238  11 LQNLDVSIPLNVLVVVTGVSGSGKSTLVN--EGLYA----------------SGKARLIS-------------FLPKFSR 59

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 109 PLKVRRLPREERRRRALEYLErvhlsewADRYPRELSGGQQQRVALARSLVYRPK--LLLLDEPLSALDKHLRGQMQDFL 186
Cdd:cd03238  60 NKLIFIDQLQFLIDVGLGYLT-------LGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132

                       170
                ....*....|....*..
gi 14028433 187 KELqRDLGITFVHVTHD 203
Cdd:cd03238 133 KGL-IDLGNTVILIEHN 148

PLN03130

ABC transporter C family member; Provisional

28-239

6.61e-05

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 45.11 E-value: 6.61e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433    28 VLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTVSISGVDVTDRAAR--ARDVGMVFQNYALFPHlTAREN 105
Cdd:PLN03130 1254 VLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMdlRKVLGIIPQAPVLFSG-TVRFN 1332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   106 VEyPLKVRRLPREERRrraleyLERVHLSEWADRYPREL-----------SGGQQQRVALARSLVYRPKLLLLDEPLSAL 174
Cdd:PLN03130 1333 LD-PFNEHNDADLWES------LERAHLKDVIRRNSLGLdaevseagenfSVGQRQLLSLARALLRRSKILVLDEATAAV 1405

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 14028433   175 DKHLRGQMQDFLKELQRdlGITFVHVTH------DQSEALALSSlvvimrdGRLEQVGSPEQIYLEPNSRF 239
Cdd:PLN03130 1406 DVRTDALIQKTIREEFK--SCTMLIIAHrlntiiDCDRILVLDA-------GRVVEFDTPENLLSNEGSAF 1467

PRK15064

ABC transporter ATP-binding protein; Provisional

13-70

8.99e-05

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 44.11 E-value: 8.99e-05

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 14028433   13 AIQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEGTV 70
Cdd:PRK15064 319 ALEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTV 376

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

144-221

9.57e-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: 42.98 E-value: 9.57e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 144 LSGGQQQ------RVALARSLVYRPKLLLLDEPLSALDK-HLRGQMQDFLKELQRDLGITFVHVTHDQSEALALSSLVVI 216
Cdd:cd03240 116 CSGGEKVlasliiRLALAETFGSNCGILALDEPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDAADHIYRV 195


                ....*
gi 14028433 217 MRDGR 221
Cdd:cd03240 196 EKDGR 200

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

14-175

3.11e-04

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 42.41 E-value: 3.11e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   14 IQISRLKKCYGAVEVLRGLDLVIPEGSYTTFLGPSGSGKTTLLRIIAGFASVSEG------TVSISGVDvtdraaRARDv 87
Cdd:PRK11819 325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGtikigeTVKLAYVD------QSRD- 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   88 gmvfqnyALFPHLTARE------------NVEYPlkvrrlpreerrrraleylERVHLSEW----ADRYPR--ELSGGQQ 149
Cdd:PRK11819 398 -------ALDPNKTVWEeisggldiikvgNREIP-------------------SRAYVGRFnfkgGDQQKKvgVLSGGER 451

                        170       180
                 ....*....|....*....|....*.
gi 14028433  150 QRVALARSLVYRPKLLLLDEPLSALD 175
Cdd:PRK11819 452 NRLHLAKTLKQGGNVLLLDEPTNDLD 477

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

138-237

4.78e-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: 42.31 E-value: 4.78e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433   138 DRYPRELSGGQQQRVALARSL------VyrpkLLLLDEPLSALdkHLRGQMQ--DFLKELqRDLGITFVHVTHDqSEALA 209
Cdd:TIGR00630 483 SRAAGTLSGGEAQRIRLATQIgsgltgV----LYVLDEPSIGL--HQRDNRRliNTLKRL-RDLGNTLIVVEHD-EDTIR 554

                          90       100       110
                  ....*....|....*....|....*....|....
gi 14028433   210 LSSLVVIM------RDGRLEQVGSPEQIYLEPNS 237
Cdd:TIGR00630 555 AADYVIDIgpgageHGGEVVASGTPEEILANPDS 588

AAA

cd00009

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...

44-89

6.88e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.

Pssm-ID: 99707 [Multi-domain] Cd Length: 151 Bit Score: 39.82 E-value: 6.88e-04

                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 14028433  44 FLGPSGSGKTTLLRIIAGFASVSEGTV-SISGVDVTDRAARARDVGM 89
Cdd:cd00009  24 LYGPPGTGKTTLARAIANELFRPGAPFlYLNASDLLEGLVVAELFGH 70

TOBE_2

pfam08402

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the ...

292-363

9.71e-04

TOBE domain; The TOBE domain (Transport-associated OB) always occurs as a dimer as the C-terminal strand of each domain is supplied by the partner. Probably involved in the recognition of small ligands such as molybdenum and sulphate. Found in ABC transporters immediately after the ATPase domain. In this family a strong RPE motif is found at the presumed N-terminus of the domain.

Pssm-ID: 462465 [Multi-domain] Cd Length: 73 Bit Score: 37.21 E-value: 9.71e-04

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 14028433   292 LLLRPEKAetgyRIDTSVVAMSGPVLSTTFMGTHYQVVFSTRHGE-ITAHLNN----DYAPGQSVDVAWRAGNLIVL 363
Cdd:pfam08402   1 LAIRPEKI----RLAAAANGLSGTVTDVEYLGDHTRYHVELAGGEeLVVRVPNaharPPAPGDRVGLGWDPEDAHVL 73

GguA

NF040905

sugar ABC transporter ATP-binding protein;

144-170

1.76e-03

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 40.16 E-value: 1.76e-03

                         10        20
                 ....*....|....*....|....*..
gi 14028433  144 LSGGQQQRVALARSLVYRPKLLLLDEP 170
Cdd:NF040905 405 LSGGNQQKVVLSKWLFTDPDVLILDEP 431

PRK10636

putative ABC transporter ATP-binding protein; Provisional

142-204

2.97e-03

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 39.38 E-value: 2.97e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 14028433  142 RELSGGQQQRVALARSLVYRPKLLLLDEPLSALDKHLRGQMQDFLKELQRdlgiTFVHVTHDQ 204
Cdd:PRK10636 148 SDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDAVIWLEKWLKSYQG----TLILISHDR 206

PRK13342

recombination factor protein RarA; Reviewed

44-88

3.74e-03

recombination factor protein RarA; Reviewed

Pssm-ID: 237355 [Multi-domain] Cd Length: 413 Bit Score: 38.91 E-value: 3.74e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 14028433   44 FLGPSGSGKTTLLRIIAG-----FASVSegtVSISGV----DVTDRAARARDVG 88
Cdd:PRK13342  41 LWGPPGTGKTTLARIIAGatdapFEALS---AVTSGVkdlrEVIEEARQRRSAG 91

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

29-204

6.84e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 36.95 E-value: 6.84e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433  29 LRGLDLVIPEGSYTTFLGPSGSGKTTLLR---IIAGFASVSEGTVSISGVDVTDRAARARDVGMVFQnyalfphltaren 105
Cdd:cd03227  11 FVPNDVTFGEGSLTIITGPNGSGKSTILDaigLALGGAQSATRRRSGVKAGCIVAAVSAELIFTRLQ------------- 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 14028433 106 veyplkvrrlpreerrrraleylervhlsewadrypreLSGGQQQRVALA-----RSLVYRPkLLLLDEPLSALDKHLRG 180
Cdd:cd03227  78 --------------------------------------LSGGEKELSALAlilalASLKPRP-LYILDEIDRGLDPRDGQ 118

                       170       180
                ....*....|....*....|....
gi 14028433 181 QMQDFLKElQRDLGITFVHVTHDQ 204
Cdd:cd03227 119 ALAEAILE-HLVKGAQVIVITHLP 141

SpoIIIAA

COG3854

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome ...

14-77

8.25e-03

Stage III sporulation protein SpoIIIAA [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 443063 Cd Length: 309 Bit Score: 37.82 E-value: 8.25e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 14028433  14 IQISRLKKcyGAVEVLrgLDLVIPEGSY--TTFLGPSGSGKTTLLRIIAgfASVSEGTVSISGVDV 77
Cdd:COG3854 117 IRIAREVK--GTADPI--LPYIISGGRIynTLIISPPGCGKTTLLRDIA--RVLSDGLLGFPGKRV 176

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