NCBI Conserved Domain Search

Conserved domains on [gi|739227338|ref|WP_037090637|]

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MULTISPECIES: ATP-binding cassette domain-containing protein [Agrobacterium]

Protein Classification

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

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

Graphical summary

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List of domain hits

Name

Accession

Description

Interval

E-value

P-loop_NTPase super family

cl38936

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...

1-269

2.92e-155

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

The actual alignment was detected with superfamily member PRK11308:

Pssm-ID: 476819 [Multi-domain] Cd Length: 327 Bit Score: 435.93 E-value: 2.92e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHVPGGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:PRK11308   2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRRPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQ 160
Cdd:PRK11308  82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 161 RIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241

                        250       260
                 ....*....|....*....|....*....
gi 739227338 241 LFADPKHPYTRQLFAATPITDVDAIRARV 269
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNPDDRRERI 270

Name

Accession

Description

Interval

E-value

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

1-269

2.92e-155

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 435.93 E-value: 2.92e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHVPGGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:PRK11308   2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRRPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQ 160
Cdd:PRK11308  82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 161 RIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241

                        250       260
                 ....*....|....*....|....*....
gi 739227338 241 LFADPKHPYTRQLFAATPITDVDAIRARV 269
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNPDDRRERI 270

AppF

COG4608

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

4-269

1.18e-150

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 424.14 E-value: 1.18e-150

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   4 VVKGKGITRDYHVPGGLFGGAR-MVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIAR 82
Cdd:COG4608    7 LLEVRDLKKHFPVRGGLFGRTVgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  83 RRPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRI 162
Cdd:COG4608   87 GRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 163 AIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELF 242
Cdd:COG4608  167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246

                        250       260
                 ....*....|....*....|....*..
gi 739227338 243 ADPKHPYTRQLFAATPITDVDAIRARV 269
Cdd:COG4608  247 ARPLHPYTQALLSAVPVPDPERRRERI 273

ABC_NikE_OppD_transporters

cd03257

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

4-236

3.08e-105

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: 305.20 E-value: 3.08e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   4 VVKGKGITRDYHVPGGlfggarMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARR 83
Cdd:cd03257    1 LLEVKNLSVSFPTGGG------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  84 RPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAM-LVKVGLGPEHFNRYPHMFSGGQRQRI 162
Cdd:cd03257   75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGGQRQRV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338 163 AIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03257  155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228

nickel_nikE

TIGR02769

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

18-256

3.35e-71

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: 220.06 E-value: 3.35e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   18 GGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVF 97
Cdd:TIGR02769  15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   98 QNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:TIGR02769  95 QDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338  178 DEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADpKHPYTRQLFAA 256
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSA 252

ABC_tran

pfam00005

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

30-180

6.84e-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: 143.56 E-value: 6.84e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgteMRSKVQMVFQNPygSLNPRQK 109
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS---LRKEIGYVFQDP--QLFPRLT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338  110 VGDVLMEPLIInTKIPASERRERAEAMLVKVGLGP---EHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:pfam00005  76 VRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

29-218

2.38e-20

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 2.38e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDG--------QPVDIARRRPGTeMRSKVQMVFQNP 100
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpQRSEVPDSLPLT-VRDLVAMGRWAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YGSLNPrqkvgdvlmepliintkiPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:NF040873  86 RGLWRR------------------LTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVR 218
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183

GguA

NF040905

sugar ABC transporter ATP-binding protein;

8-234

1.08e-19

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 88.31 E-value: 1.08e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYhvPGglfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPAS--GGELKIDGQPV---DIAr 82
Cdd:NF040905   5 RGITKTF--PG--------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCrfkDIR- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  83 rrpGTEMRSKV---QMVFQNPYGSL-------NPRQKVGdvlmeplIINTkipaSERRERAEAMLVKVGLGPEHFNRYPH 152
Cdd:NF040905  74 ---DSEALGIViihQELALIPYLSIaeniflgNERAKRG-------VIDW----NETNRRARELLAKVGLDESPDTLVTD 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 153 MFSGGQrQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEA 232
Cdd:NF040905 140 IGVGKQ-QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRT 217


                 ..
gi 739227338 233 VE 234
Cdd:NF040905 218 IE 219

AAA

smart00382

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

39-231

4.36e-09

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

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 4.36e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    39 RGKTLAIVGESGSGKSTLARIIA-LIDPASGGELKIDGQPVDIARRrpgtemrskvqmvfqnpygslnprqkvgdvlmep 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALArELGPPGGGVIYIDGEDILEEVL---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   118 liintkipaserreraeamlvkVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLR 197
Cdd:smart00382  47 ----------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 739227338   198 D-----LQEEFELTYVFVSHDLSV-----VRYIADDVMVISKGE 231
Cdd:smart00382 105 LrllllLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148

40850658_otr

NF000106

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

27-241

1.04e-08

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 1.04e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGelkidgQPVDI----ARRRPGTEMRSKVQMVFQNPYG 102
Cdd:NF000106  26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR------RPWRF*twcANRRALRRTIG*HRPVR*GRRE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVgdvlmepLIINTKIPASER--RERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:NF000106 100 SFSGRENL-------YMIGR*LDLSRKdaRARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

33-185

1.22e-08

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.22e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV---DIA-RRRPGTEMRSkvqmvFqNPYGSLNPRQ 108
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagDIAtRRRVGYMSQA-----F-SLYGELTVRQ 358

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 109 KVgdVLMEPLIintKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:NF033858 359 NL--ELHARLF---HLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

27-180

1.74e-04

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.74e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLariIALIdpaSG------GELKIDGQpvDIARRRpgteMRSKVQmvfqnp 100
Cdd:NF033858  14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSL---LSLI---AGarkiqqGRVEVLGG--DMADAR----HRRAVC------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ygslnPR-----QKVGDVLMEPLIINTKI---------PASERRERAEAMLVKVGLGPehF-NRYPHMFSGGQRQRIAIA 165
Cdd:NF033858  76 -----PRiaympQGLGKNLYPTLSVFENLdffgrlfgqDAAERRRRIDELLRATGLAP--FaDRPAGKLSGGMKQKLGLC 148

                        170
                 ....*....|....*
gi 739227338 166 RALMLNPALLVLDEP 180
Cdd:NF033858 149 CALIHDPDLLILDEP 163

Name

Accession

Description

Interval

E-value

dppF

PRK11308

dipeptide transporter ATP-binding subunit; Provisional

1-269

2.92e-155

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 236898 [Multi-domain] Cd Length: 327 Bit Score: 435.93 E-value: 2.92e-155

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHVPGGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:PRK11308   2 QQPLLQAIDLKKHYPVKRGLFKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRRPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQ 160
Cdd:PRK11308  82 ADPEAQKLLRQKIQIVFQNPYGSLNPRKKVGQILEEPLLINTSLSAAERREKALAMMAKVGLRPEHYDRYPHMFSGGQRQ 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 161 RIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:PRK11308 162 RIAIARALMLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQ 241

                        250       260
                 ....*....|....*....|....*....
gi 739227338 241 LFADPKHPYTRQLFAATPITDVDAIRARV 269
Cdd:PRK11308 242 IFNNPRHPYTQALLSATPRLNPDDRRERI 270

AppF

COG4608

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

4-269

1.18e-150

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

Pssm-ID: 443658 [Multi-domain] Cd Length: 329 Bit Score: 424.14 E-value: 1.18e-150

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   4 VVKGKGITRDYHVPGGLFGGAR-MVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIAR 82
Cdd:COG4608    7 LLEVRDLKKHFPVRGGLFGRTVgVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLS 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  83 RRPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRI 162
Cdd:COG4608   87 GRELRPLRRRMQMVFQDPYASLNPRMTVGDIIAEPLRIHGLASKAERRERVAELLELVGLRPEHADRYPHEFSGGQRQRI 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 163 AIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELF 242
Cdd:COG4608  167 GIARALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELY 246

                        250       260
                 ....*....|....*....|....*..
gi 739227338 243 ADPKHPYTRQLFAATPITDVDAIRARV 269
Cdd:COG4608  247 ARPLHPYTQALLSAVPVPDPERRRERI 273

GsiA

COG1123

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

4-263

5.22e-131

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: 381.17 E-value: 5.22e-131

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   4 VVKGKGITRDYHVPGGlfggaRMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARR 83
Cdd:COG1123  260 LLEVRNLSKRYPVRGK-----GGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  84 RPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIA 163
Cdd:COG1123  335 RSLRELRRRVQMVFQDPYSSLNPRMTVGDIIAEPLRLHGLLSRAERRERVAELLERVGLPPDLADRYPHELSGGQRQRVA 414

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 164 IARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFA 243
Cdd:COG1123  415 IARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFA 494

                        250       260
                 ....*....|....*....|
gi 739227338 244 DPKHPYTRQLFAATPITDVD 263
Cdd:COG1123  495 NPQHPYTRALLAAVPSLDPA 514

YejF

COG4172

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

3-261

8.31e-127

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: 370.94 E-value: 8.31e-127

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   3 IVVKGKGITRDYHVPGGLFG-GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDpaSGGELKIDGQPVDI 80
Cdd:COG4172  274 PLLEARDLKVWFPIKRGLFRrTVGHVKAVDGVSLTLRRGETLGLVGESGSGKSTLGLaLLRLIP--SEGEIRFDGQDLDG 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRRPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLII-NTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQR 159
Cdd:COG4172  352 LSRRALRPLRRRMQVVFQDPFGSLSPRMTVGQIIAEGLRVhGPGLSAAERRARVAEALEEVGLDPAARHRYPHEFSGGQR 431

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 160 QRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTRE 239
Cdd:COG4172  432 QRIAIARALILEPKLLVLDEPTSALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTE 511

                        250       260
                 ....*....|....*....|..
gi 739227338 240 ELFADPKHPYTRQLFAATPITD 261
Cdd:COG4172  512 QVFDAPQHPYTRALLAAAPLLE 533

DppD

COG0444

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

4-266

4.59e-122

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: 351.28 E-value: 4.59e-122

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   4 VVKGKGITRDYHVPGGLfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPA--SGGELKIDGQpvDI 80
Cdd:COG0444    1 LLEVRNLKVYFPTRRGV------VKAVDGVSFDVRRGETLGLVGESGSGKSTLARAILgLLPPPgiTSGEILFDGE--DL 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRrPGTEMRS----KVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGP--EHFNRYPHMF 154
Cdd:COG0444   73 LKL-SEKELRKirgrEIQMIFQDPMTSLNPVMTVGDQIAEPLRIHGGLSKAEARERAIELLERVGLPDpeRRLDRYPHEL 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVE 234
Cdd:COG0444  152 SGGMRQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVE 231

                        250       260       270
                 ....*....|....*....|....*....|..
gi 739227338 235 QGTREELFADPKHPYTRQLFAATPITDVDAIR 266
Cdd:COG0444  232 EGPVEELFENPRHPYTRALLSSIPRLDPDGRR 263

DppF

COG1124

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

23-259

3.76e-115

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: 331.00 E-value: 3.76e-115

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPYG 102
Cdd:COG1124   14 GGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK---AFRRRVQMVFQDPYA 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEPLIINTKipaSERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:COG1124   91 SLHPRHTVDRILAEPLRIHGL---PDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTS 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATPI 259
Cdd:COG1124  168 ALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHPYTRELLAASLA 244

SapF

COG4167

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

1-253

7.53e-106

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

Pssm-ID: 443328 [Multi-domain] Cd Length: 265 Bit Score: 308.30 E-value: 7.53e-106

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHVPGGLFGgARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-- 78
Cdd:COG4167    1 MSALLEVRNLSKTFKYRTGLFR-RQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLey 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  79 -DIARRrpgtemrSK-VQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSG 156
Cdd:COG4167   80 gDYKYR-------CKhIRMIFQDPNTSLNPRLNIGQILEEPLRLNTDLTAEEREERIFATLRLVGLLPEHANFYPHMLSS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 157 GQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:COG4167  153 GQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYG 232

                        250
                 ....*....|....*..
gi 739227338 237 TREELFADPKHPYTRQL 253
Cdd:COG4167  233 KTAEVFANPQHEVTKRL 249

ABC_NikE_OppD_transporters

cd03257

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

4-236

3.08e-105

Pssm-ID: 213224 [Multi-domain] Cd Length: 228 Bit Score: 305.20 E-value: 3.08e-105

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   4 VVKGKGITRDYHVPGGlfggarMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARR 83
Cdd:cd03257    1 LLEVKNLSVSFPTGGG------SVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSR 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  84 RPGTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAM-LVKVGLGPEHFNRYPHMFSGGQRQRI 162
Cdd:cd03257   75 RLRKIRRKEIQMVFQDPMSSLNPRMTIGEQIAEPLRIHGKLSKKEARKEAVLLlLVGVGLPEEVLNRYPHELSGGQRQRV 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338 163 AIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03257  155 AIARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228

PRK15079

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

28-273

6.02e-100

oligopeptide ABC transporter ATP-binding protein OppF; Provisional

Pssm-ID: 185037 [Multi-domain] Cd Length: 331 Bit Score: 295.46 E-value: 6.02e-100

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIdPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNPYGSLNP 106
Cdd:PRK15079  35 KAVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLV-KATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDPLASLNP 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLII-NTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK15079 114 RMTIGEIIAEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALD 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATPITDVDai 265
Cdd:PRK15079 194 VSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAVPIPDPD-- 271


                 ....*...
gi 739227338 266 rarVERRK 273
Cdd:PRK15079 272 ---LERNK 276

YejF

COG4172

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

22-258

2.19e-83

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: 259.62 E-value: 2.19e-83

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDPAS---GGELKIDGQPVDIArrrPGTEMR----SKV 93
Cdd:COG4172   18 QGGGTVEAVKGVSFDIAAGETLALVGESGSGKSVTALsILRLLPDPAahpSGSILFDGQDLLGL---SERELRrirgNRI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  94 QMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLgPE---HFNRYPHMFSGGQRQRIAIARALML 170
Cdd:COG4172   95 AMIFQEPMTSLNPLHTIGKQIAEVLRLHRGLSGAAARARALELLERVGI-PDperRLDAYPHQLSGGQRQRVMIAMALAN 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYT 250
Cdd:COG4172  174 EPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTAELFAAPQHPYT 253


                 ....*...
gi 739227338 251 RQLFAATP 258
Cdd:COG4172  254 RKLLAAEP 261

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

28-257

3.02e-78

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 246.54 E-value: 3.02e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKST----LARIIAlidpaSGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNPYGS 103
Cdd:PRK15134 300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNSS 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 LNPRQKVGDVLMEPLIINTK-IPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK15134 375 LNPRLNVLQIIEEGLRVHQPtLSAAQREQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAAT 257
Cdd:PRK15134 455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTRQLLALS 529

PRK10261

glutathione transporter ATP-binding protein; Provisional

10-261

2.55e-74

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 238.60 E-value: 2.55e-74

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  10 ITRdYHVPGGLFGG-ARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTE 88
Cdd:PRK10261 320 VTR-FPLRSGLLNRvTREVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQA 398

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  89 MRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARAL 168
Cdd:PRK10261 399 LRRDIQFIFQDPYASLDPRQTVGDSIMEPLRVHGLLPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARAL 478

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 169 MLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHP 248
Cdd:PRK10261 479 ALNPKVIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHP 558

                        250
                 ....*....|...
gi 739227338 249 YTRQLFAATPITD 261
Cdd:PRK10261 559 YTRKLMAAVPVAD 571

PRK15112

peptide ABC transporter ATP-binding protein SapF;

8-256

3.65e-72

peptide ABC transporter ATP-binding protein SapF;

Pssm-ID: 185067 [Multi-domain] Cd Length: 267 Bit Score: 222.74 E-value: 3.65e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYHVPGGLFGgARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgt 87
Cdd:PRK15112   8 RNLSKTFRYRTGWFR-RQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGDYS--- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  88 eMRS-KVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIAR 166
Cdd:PRK15112  84 -YRSqRIRMIFQDPSTSLNPRQRISQILDFPLRLNTDLEPEQREKQIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLAR 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:PRK15112 163 ALILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPL 242

                        250
                 ....*....|
gi 739227338 247 HPYTRQLFAA 256
Cdd:PRK15112 243 HELTKRLIAG 252

GsiA

COG1123

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

23-275

8.88e-72

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: 229.02 E-value: 8.88e-72

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG---GELKIDGQPVdiaRRRPGTEMRSKVQMVFQN 99
Cdd:COG1123   15 PGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDL---LELSEALRGRRIGMVFQD 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PYGSLNPrQKVGDVLMEPLIiNTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:COG1123   92 PMTQLNP-VTVGDQIAEALE-NLGLSRAEARARVLELLEAVGL-ERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADE 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 180 PVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPkhpytrQLFAATPI 259
Cdd:COG1123  169 PTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAP------QALAAVPR 242

                        250
                 ....*....|....*.
gi 739227338 260 TDVDAIRARVERRKAA 275
Cdd:COG1123  243 LGAARGRAAPAAAAAE 258

nickel_nikE

TIGR02769

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

18-256

3.35e-71

Pssm-ID: 131816 [Multi-domain] Cd Length: 265 Bit Score: 220.06 E-value: 3.35e-71

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   18 GGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVF 97
Cdd:TIGR02769  15 GGLFGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAFRRDVQLVF 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   98 QNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:TIGR02769  95 QDSPSAVNPRMTVRQIIGEPLRHLTSLDESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQRINIARALAVKPKLIVL 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338  178 DEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADpKHPYTRQLFAA 256
Cdd:TIGR02769 175 DEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQIVEECDVAQLLSF-KHPAGRNLQSA 252

AbcC

COG1135

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

8-273

2.28e-68

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

Pssm-ID: 440750 [Multi-domain] Cd Length: 339 Bit Score: 215.33 E-value: 2.28e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYHVPGGLfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPG- 86
Cdd:COG1135    5 ENLSKTFPTKGGP------VTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGV--DLTALSERe 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  87 -TEMRSKVQMVFQNPygSLNPRQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIA 165
Cdd:COG1135   77 lRAARRKIGMIFQHF--NLLSSRTVAENVALPLEI-AGVPKAEIRKRVAELLELVGLS-DKADAYPSQLSGGQKQRVGIA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 166 RALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:COG1135  153 RALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANP 232

                        250       260
                 ....*....|....*....|....*....
gi 739227338 246 KHPYTRQLFAATPITDV-DAIRARVERRK 273
Cdd:COG1135  233 QSELTRRFLPTVLNDELpEELLARLREAA 261

GlnQ

COG1126

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

21-252

3.82e-68

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

Pssm-ID: 440743 [Multi-domain] Cd Length: 239 Bit Score: 211.39 E-value: 3.82e-68

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgTEMRSKVQMVFQNP 100
Cdd:COG1126   11 FGD---LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTDSKKDI-NKLRRKVGMVFQQF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ygSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:COG1126   87 --NLFPHLTVLENVTLAPIKVKKMSKAEAEERAMELLERVGLA-DKADAYPAQLSGGQQQRVAIARALAMEPKVMLFDEP 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ 252
Cdd:COG1126  164 TSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234

MlaF

COG1127

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

23-254

5.11e-67

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: 208.29 E-value: 5.11e-67

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNP-- 100
Cdd:COG1127   16 GDRVV--LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYELRRRIGMLFQGGal 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YGSLNprqkVGDVLMEPLIINTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:COG1127   94 FDSLT----VFENVAFPLREHTDLSEAEIRELVLEKLELVGL-PGAADKMPSELSGGMRKRVALARALALDPEILLYDEP 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 181 VSALD-LSVqAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPkHPYTRQLF 254
Cdd:COG1127  169 TAGLDpITS-AVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEGTPEELLASD-DPWVRQFL 241

nikE

PRK10419

nickel ABC transporter ATP-binding protein NikE;

18-256

1.17e-66

nickel ABC transporter ATP-binding protein NikE;

Pssm-ID: 236689 [Multi-domain] Cd Length: 268 Bit Score: 208.39 E-value: 1.17e-66

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  18 GGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVF 97
Cdd:PRK10419  16 GGLSGKHQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAQRKAFRRDIQMVF 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  98 QNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:PRK10419  96 QDSISAVNPRKTVREIIREPLRHLLSLDKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVCLARALAVEPKLLIL 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAdPKHPYTRQLFAA 256
Cdd:PRK10419 176 DEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKLT-FSSPAGRVLQNA 253

PhnK

COG4107

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

20-253

1.68e-65

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

Pssm-ID: 443283 [Multi-domain] Cd Length: 262 Bit Score: 205.43 E-value: 1.68e-65

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  20 LFG-GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKI---DGQPVDI-----ARRRpgTEMR 90
Cdd:COG4107   17 RYGpGCGTVVACRDVSFDLYPGEVLGIVGESGSGKSTLLKCLYFDLAPTSGSVYYrdrDGGPRDLfalseAERR--RLRR 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  91 SKVQMVFQNPYGSLNPRQKVGDVLMEPLIIntkipASER-----RERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIA 165
Cdd:COG4107   95 TDWGMVYQNPRDGLRMDVSAGGNIAERLMA-----AGERhygdiRARALEWLERVEIPLERIDDLPRTFSGGMQQRVQIA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 166 RALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:COG4107  170 RALVTNPRLLFLDEPTTGLDVSVQARLLDLIRRLQRELGLSMIVVTHDLGVIRLLADRTMVMKNGRVVESGLTDQVLEDP 249


                 ....*...
gi 739227338 246 KHPYTRQL 253
Cdd:COG4107  250 QHPYTQLL 257

ABC_MetN_methionine_transporter

cd03258

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

8-246

3.16e-64

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: 201.27 E-value: 3.16e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYHvpgglfGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGT 87
Cdd:cd03258    5 KNVSKVFG------DTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  88 EMRSKVQMVFQNpYGSLNPRqKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGPEHfNRYPHMFSGGQRQRIAIARA 167
Cdd:cd03258   79 KARRRIGMIFQH-FNLLSSR-TVFENVALPLEI-AGVPKAEIEERVLELLELVGLEDKA-DAYPAQLSGGQKQRVGIARA 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 168 LMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:cd03258  155 LANNPKVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233

oppD

PRK09473

oligopeptide transporter ATP-binding component; Provisional

27-263

8.03e-64

oligopeptide transporter ATP-binding component; Provisional

Pssm-ID: 181888 [Multi-domain] Cd Length: 330 Bit Score: 203.42 E-value: 8.03e-64

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLA-RIIALIdpAS----GGELKIDGQPVDIARRRPGTEMRS-KVQMVFQNP 100
Cdd:PRK09473  29 VTAVNDLNFSLRAGETLGIVGESGSGKSQTAfALMGLL--AAngriGGSATFNGREILNLPEKELNKLRAeQISMIFQDP 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLgPEHFNR---YPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:PRK09473 107 MTSLNPYMRVGEQLMEVLMLHKGMSKAEAFEESVRMLDAVKM-PEARKRmkmYPHEFSGGMRQRVMIAMALLCRPKLLIA 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAAT 257
Cdd:PRK09473 186 DEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQPSHPYSIGLLNAV 265


                 ....*.
gi 739227338 258 PITDVD 263
Cdd:PRK09473 266 PRLDAE 271

ABC_Org_Solvent_Resistant

cd03261

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

21-252

1.87e-63

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: 199.27 E-value: 1.87e-63

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMvqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNP 100
Cdd:cd03261   10 FGGRTV---LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLRRRMGMLFQSG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 --YGSLNprqkVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHfNRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:cd03261   87 alFDSLT----VFENVAFPLREHTRLSEEEIREIVLEKLEAVGLRGAE-DLYPAELSGGMKKRVALARALALDPELLLYD 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPkHPYTRQ 252
Cdd:cd03261  162 EPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEGTPEELRASD-DPLVRQ 234

LolD

COG1136

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

1-235

1.30e-62

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

Pssm-ID: 440751 [Multi-domain] Cd Length: 227 Bit Score: 196.80 E-value: 1.30e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHVpgglfgGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-- 78
Cdd:COG1136    1 MSPLLELRNLTKSYGT------GEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDIss 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  79 ----DIARRRpgtemRSKVQMVFQNPYgsLNPRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMF 154
Cdd:COG1136   75 lserELARLR-----RRHIGFVFQFFN--LLPELTALENVALPLLLA-GVSRKERRERARELLERVGLG-DRLDHRPSQL 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVE 234
Cdd:COG1136  146 SGGQQQRVAIARALVNRPKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAAR-ADRVIRLRDGRIVS 224


                 .
gi 739227338 235 Q 235
Cdd:COG1136  225 D 225

ABC_MJ0796_LolCDE_FtsE

cd03255

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

5-231

6.48e-62

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: 194.63 E-value: 6.48e-62

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   5 VKGKGITRDYHvpgglfGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRR 84
Cdd:cd03255    1 IELKNLSKTYG------GGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEK 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  85 PGTEMR-SKVQMVFQNPYgsLNPRQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIA 163
Cdd:cd03255   75 ELAAFRrRHIGFVFQSFN--LLPDLTALENVELPLLL-AGVPKKERRERAEELLERVGLG-DRLNHYPSELSGGQQQRVA 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 164 IARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGE 231
Cdd:cd03255  151 IARALANDPKIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEY-ADRIIELRDGK 217

EcfA2

COG1122

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

27-246

1.05e-61

Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and metabolism, General function prediction only];

Pssm-ID: 440739 [Multi-domain] Cd Length: 230 Bit Score: 194.47 E-value: 1.05e-61

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQNPygslnP 106
Cdd:COG1122   14 TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDI---TKKNLRELRRKVGLVFQNP-----D 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLME-----PLiiNTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:COG1122   86 DQLFAPTVEEdvafgPE--NLGLPREEIRERVEEALELVGL--EHLaDRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEP 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:COG1122  162 TAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYE 226

PotA

COG3842

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

21-276

2.75e-57

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

Pssm-ID: 443052 [Multi-domain] Cd Length: 353 Bit Score: 187.23 E-value: 2.75e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPgtEMRsKVQMVFQNP 100
Cdd:COG3842   15 YGD---VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGR--DVTGLPP--EKR-NVGMVFQDY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 -------------YGslnPRQKvgdvlmepliintKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIAR 166
Cdd:COG3842   87 alfphltvaenvaFG---LRMR-------------GVPKAEIRARVAELLELVGL--EGLaDRYPHQLSGGQQQRVALAR 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHD----LSvvryIADDVMVISKGEAVEQGTREELF 242
Cdd:COG3842  149 ALAPEPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDqeeaLA----LADRIAVMNDGRIEQVGTPEEIY 224

                        250       260       270
                 ....*....|....*....|....*....|....
gi 739227338 243 ADPKHPytrqlFAATPITDVDAIRARVERRKAAR 276
Cdd:COG3842  225 ERPATR-----FVADFIGEANLLPGTVLGDEGGG 253

PRK15134

microcin C ABC transporter ATP-binding protein YejF; Provisional

28-258

5.30e-57

microcin C ABC transporter ATP-binding protein YejF; Provisional

Pssm-ID: 237917 [Multi-domain] Cd Length: 529 Bit Score: 191.07 E-value: 5.30e-57

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPAS-----GGELKIDGQPVDIARRRPGTEMR-SKVQMVFQNPY 101
Cdd:PRK15134  23 TVVNDVSLQIEAGETLALVGESGSGKSVTALSILRLLPSPpvvypSGDIRFHGESLLHASEQTLRGVRgNKIAMIFQEPM 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 GSLNPRQKVGDVLMEPLIINTKIpaseRRE--RAEAM--LVKVGL--GPEHFNRYPHMFSGGQRQRIAIARALMLNPALL 175
Cdd:PRK15134 103 VSLNPLHTLEKQLYEVLSLHRGM----RREaaRGEILncLDRVGIrqAAKRLTDYPHQLSGGERQRVMIAMALLTRPELL 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFA 255
Cdd:PRK15134 179 IADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAATLFSAPTHPYTQKLLN 258


                 ...
gi 739227338 256 ATP 258
Cdd:PRK15134 259 SEP 261

metN

PRK11153

DL-methionine transporter ATP-binding subunit; Provisional

22-257

2.18e-56

DL-methionine transporter ATP-binding subunit; Provisional

Pssm-ID: 236863 [Multi-domain] Cd Length: 343 Bit Score: 184.62 E-value: 2.18e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNpY 101
Cdd:PRK11153  13 QGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKARRQIGMIFQH-F 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 GSLNPRQKVGDVLMePLIInTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:PRK11153  92 NLLSSRTVFDNVAL-PLEL-AGTPKAEIKARVTELLELVGLS-DKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEAT 168

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 182 SALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAAT 257
Cdd:PRK11153 169 SALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREFIQST 244

TauB

COG1116

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

8-230

5.47e-56

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

Pssm-ID: 440733 [Multi-domain] Cd Length: 260 Bit Score: 181.06 E-value: 5.47e-56

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYHVPGGlfggarMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGt 87
Cdd:COG1116   11 RGVSKRFPTGGG------GVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGPDRG- 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  88 emrskvqMVFQNPygSLNPRQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARA 167
Cdd:COG1116   84 -------VVFQEP--ALLPWLTVLDNVALGLEL-RGVPKAERRERARELLELVGLA-GFEDAYPHQLSGGMRQRVAIARA 152

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 168 LMLNPALLVLDEPVSALD----LSVQaqvlNLLRDLQEEFELTYVFVSHDLS--VvrYIADDVMVISKG 230
Cdd:COG1116  153 LANDPEVLLMDEPFGALDaltrERLQ----DELLRLWQETGKTVLFVTHDVDeaV--FLADRVVVLSAR 215

ABC_NrtD_SsuB_transporters

cd03293

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

22-229

2.73e-55

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: 177.66 E-value: 2.73e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGtemrskvqMVFQNPy 101
Cdd:cd03293   12 GGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGPDRG--------YVFQQD- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 gSLNPRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:cd03293   83 -ALLPWLTVLDNVALGLELQ-GVPKAEARERAEELLELVGLS-GFENAYPHQLSGGMRQRVALARALAVDPDVLLLDEPF 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 739227338 182 SALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISK 229
Cdd:cd03293  160 SALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSA 207

ABC_HisP_GlnQ

cd03262

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

28-231

3.38e-55

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: 177.34 E-value: 3.38e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiARRRPGTEMRSKVQMVFQNPYgsLNPR 107
Cdd:cd03262   14 HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLT-DDKKNINELRQKVGMVFQQFN--LFPH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:cd03262   91 LTVLENITLAPIKVKGMSKAEAEERALELLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSALDPE 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 739227338 188 VQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03262  170 LVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGR 212

ABC_cobalt_CbiO_domain1

cd03225

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

28-231

7.47e-55

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: 176.50 E-value: 7.47e-55

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPygslnPR 107
Cdd:cd03225   15 PALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLK---ELRRKVGLVFQNP-----DD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLII---NTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:cd03225   87 QFFGPTVEEEVAFgleNLGLPEEEIEERVEEALELVGLE-GLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGL 165

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 739227338 185 DLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03225  166 DPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211

ABC_Carb_Solutes_like

cd03259

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

27-236

3.13e-54

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: 175.02 E-value: 3.13e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGtemRSKVQMVFQNPygSLNP 106
Cdd:cd03259   13 VRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGR--DVTGVPPE---RRNIGMVFQDY--ALFP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03259   86 HLTVAENIAFGLKLR-GVPKAEIRARVRELLELVGL-EGLLNRYPHELSGGQQQRVALARALAREPSLLLLDEPLSALDA 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03259  164 KLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213

CysA

COG1118

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

1-253

9.78e-54

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

Pssm-ID: 440735 [Multi-domain] Cd Length: 348 Bit Score: 177.65 E-value: 9.78e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGkgITRDyhvpgglFGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:COG1118    1 MSIEVRN--ISKR-------FGS---FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFT 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ---ARRRpgtemrsKVQMVFQN----PYgsLNPRQKVG---DVLmepliintKIPASERRERAEAMLVKVGLgpEHF-NR 149
Cdd:COG1118   69 nlpPRER-------RVGFVFQHyalfPH--MTVAENIAfglRVR--------PPSKAEIRARVEELLELVQL--EGLaDR 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 150 YPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISK 229
Cdd:COG1118  130 YPSQLSGGQRQRVALARALAVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQ 209

                        250       260
                 ....*....|....*....|....
gi 739227338 230 GEAVEQGTREELFADPKHPYTRQL 253
Cdd:COG1118  210 GRIEQVGTPDEVYDRPATPFVARF 233

PRK10261

glutathione transporter ATP-binding protein; Provisional

24-258

9.90e-54

glutathione transporter ATP-binding protein; Provisional

Pssm-ID: 182342 [Multi-domain] Cd Length: 623 Bit Score: 183.90 E-value: 9.90e-54

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  24 ARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvdIARRR----------PGTEMR--- 90
Cdd:PRK10261  26 QQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDKM---LLRRRsrqvielseqSAAQMRhvr 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  91 -SKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAML--VKVGLGPEHFNRYPHMFSGGQRQRIAIARA 167
Cdd:PRK10261 103 gADMAMIFQEPMTSLNPVFTVGEQIAESIRLHQGASREEAMVEAKRMLdqVRIPEAQTILSRYPHQLSGGMRQRVMIAMA 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 168 LMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKH 247
Cdd:PRK10261 183 LSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEAVETGSVEQIFHAPQH 262

                        250
                 ....*....|.
gi 739227338 248 PYTRQLFAATP 258
Cdd:PRK10261 263 PYTRALLAAVP 273

PRK11264

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

28-252

1.13e-53

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

Pssm-ID: 183063 [Multi-domain] Cd Length: 250 Bit Score: 174.55 E-value: 1.13e-53

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIAR-----RRPGTEMRSKVQMVFQNpyG 102
Cdd:PRK11264  17 TVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARslsqqKGLIRQLRQHVGFVFQN--F 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGL-GPEhfNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:PRK11264  95 NLFPHRTVLENIIEGPVIVKGEPKEEATARARELLAKVGLaGKE--TSYPRRLSGGQQQRVAIARALAMRPEVILFDEPT 172

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 182 SALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ 252
Cdd:PRK11264 173 SALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQPRTRQ 242

ECF_ATPase_1

TIGR04520

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

27-244

1.24e-51

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: 169.92 E-value: 1.24e-51

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   27 VQALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDPASgGELKIDGQpvDIARRRPGTEMRSKVQMVFQNPygsln 105
Cdd:TIGR04520  15 KPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKlLNGLLLPTS-GKVTVDGL--DTLDEENLWEIRKKVGMVFQNP----- 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  106 PRQKVG-----DVL--MEpliiNTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:TIGR04520  87 DNQFVGatvedDVAfgLE----NLGVPREEMRKRVDEALKLVGM--EDFrDREPHLLSGGQKQRVAIAGVLAMRPDIIIL 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  178 DEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFAD 244
Cdd:TIGR04520 161 DEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVL-ADRVIVMNKGKIVAEGTPREIFSQ 226

ABC_Class3

cd03229

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

27-231

2.11e-51

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: 166.59 E-value: 2.11e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEmRSKVQMVFQNPygSLNP 106
Cdd:cd03229   13 KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDELPPL-RRRIGMVFQDF--ALFP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLiintkipaserreraeamlvkvglgpehfnryphmfSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03229   90 HLTVLENIALGL------------------------------------SGGQQQRVALARALAMDPDVLLLDEPTSALDP 133

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03229  134 ITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178

dppD

PRK11022

dipeptide transporter ATP-binding subunit; Provisional

28-266

4.04e-51

dipeptide transporter ATP-binding subunit; Provisional

Pssm-ID: 182906 [Multi-domain] Cd Length: 326 Bit Score: 170.31 E-value: 4.04e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKS--TLArIIALID---PASGGELKIDGQPV-DIARRRPGTEMRSKVQMVFQNPY 101
Cdd:PRK11022  21 RAVDRISYSVKQGEVVGIVGESGSGKSvsSLA-IMGLIDypgRVMAEKLEFNGQDLqRISEKERRNLVGAEVAMIFQDPM 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 GSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLgPEHFNR---YPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK11022 100 TSLNPCYTVGFQIMEAIKVHQGGNKKTRRQRAIDLLNQVGI-PDPASRldvYPHQLSGGMSQRVMIAMAIACRPKLLIAD 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATP 258
Cdd:PRK11022 179 EPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHDIFRAPRHPYTQALLRALP 258


                 ....*...
gi 739227338 259 ITDVDAIR 266
Cdd:PRK11022 259 EFAQDKAR 266

CcmA

COG1131

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

21-241

4.44e-51

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

Pssm-ID: 440746 [Multi-domain] Cd Length: 236 Bit Score: 167.55 E-value: 4.44e-51

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarRRPGTEMRSKVQMVFQNP 100
Cdd:COG1131   10 YGD---KTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVRRRIGYVPQEP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 --YGSLNPRQKVgdVLMEPLiinTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:COG1131   83 alYPDLTVRENL--RFFARL---YGLPRKEARERIDELLELFGLT-DAADRKVGTLSGGMKQRLGLALALLHDPELLILD 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:COG1131  157 EPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTPDEL 218

ECF_ATPase_2

TIGR04521

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

28-246

1.18e-50

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: 167.63 E-value: 1.18e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   28 QALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGgELKIDGQPVDIARRRPGTEMRSKVQMVFQNP------ 100
Cdd:TIGR04521  19 KALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLLKPTSG-TVTIDGRDITAKKKKKLKDLRKKVGLVFQFPehqlfe 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  101 --------YGslnPRqkvgdvlmepliiNTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNP 172
Cdd:TIGR04521  98 etvykdiaFG---PK-------------NLGLSEEEAEERVKEALELVGLDEEYLERSPFELSGGQMRRVAIAGVLAMEP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338  173 ALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:TIGR04521 162 EVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235

ArtP

COG4161

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

1-246

2.02e-50

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

Pssm-ID: 443326 [Multi-domain] Cd Length: 242 Bit Score: 165.96 E-value: 2.02e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGkgITRDYHVpgglfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:COG4161    1 MSIQLKN--INCFYGS----------HQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFDF 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARR---RPGTEMRSKVQMVFQNpYgSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGG 157
Cdd:COG4161   69 SQKpseKAIRLLRQKVGMVFQQ-Y-NLWPHLTVMENLIEAPCKVLGLSKEQAREKAMKLLARLRLT-DKADRFPLHLSGG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 158 QRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGT 237
Cdd:COG4161  146 QQQRVAIARALMMEPQVLLFDEPTAALDPEITAQVVEIIRELSQT-GITQVIVTHEVEFARKVASQVVYMEKGRIIEQGD 224


                 ....*....
gi 739227338 238 rEELFADPK 246
Cdd:COG4161  225 -ASHFTQPQ 232

ABC_PotA_N

cd03300

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

28-246

4.05e-50

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: 165.10 E-value: 4.05e-50

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-DI-ARRRPgtemrskVQMVFQNpYgSLN 105
Cdd:cd03300   14 VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDItNLpPHKRP-------VNTVFQN-Y-ALF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03300   85 PHLTVFENIAFGLRLK-KLPKAEIKERVAEALDLVQLE-GYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEPLGALD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:cd03300  163 LKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPA 223

FetA

COG4619

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

30-231

1.28e-49

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

Pssm-ID: 443661 [Multi-domain] Cd Length: 209 Bit Score: 163.06 E-value: 1.28e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarRRPGTEMRSKVQMVFQNPY---GSlnp 106
Cdd:COG4619   16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLS---AMPPPEWRRQVAYVPQEPAlwgGT--- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 rqkVGDVLMEPLIINTKIPaseRRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:COG4619   90 ---VRDNLPFPFQLRERKF---DRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSALDP 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:COG4619  164 ENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGR 208

PhnC

COG3638

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

27-241

4.67e-49

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

Pssm-ID: 442855 [Multi-domain] Cd Length: 249 Bit Score: 162.53 E-value: 4.67e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNPYgsLNP 106
Cdd:COG3638   16 TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRLRRRIGMIFQQFN--LVP 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGD-VLM-----EPLI--INTKIPASERrERAEAMLVKVGLGPEHFNRyPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:COG3638   94 RLSVLTnVLAgrlgrTSTWrsLLGLFPPEDR-ERALEALERVGLADKAYQR-ADQLSGGQQQRVAIARALVQEPKLILAD 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:COG3638  172 EPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVVFDGPPAEL 234

MalK

COG3839

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

21-256

5.68e-49

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

Pssm-ID: 443050 [Multi-domain] Cd Length: 352 Bit Score: 165.63 E-value: 5.68e-49

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-DIARRRPGtemrskVQMVFQN 99
Cdd:COG3839   13 YGG---VEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVtDLPPKDRN------IAMVFQS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PygSLNPRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:COG3839   84 Y--ALYPHMTVYENIAFPLKLR-KVPKAEIDRRVREAAELLGLED-LLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 180 PVSALD--LSVQAQVlnLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHpytrqLFAA 256
Cdd:COG3839  160 PLSNLDakLRVEMRA--EIKRLHRRLGTTTIYVTHDQVEAMTLADRIAVMNDGRIQQVGTPEELYDRPAN-----LFVA 231

ABC_Pro_Gly_Betaine

cd03294

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

29-262

2.12e-48

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: 161.66 E-value: 2.12e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPaSGGELKIDGQPVDIARRRPGTEMRSK-VQMVFQNpYGsLNP 106
Cdd:cd03294   39 GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCInRLIEP-TSGKVLIDGQDIAAMSRKELRELRRKkISMVFQS-FA-LLP 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGP-EHfnRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03294  116 HRTVLENVAFGLEVQ-GVPRAEREERAAEALELVGLEGwEH--KYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALD 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATPITDV 262
Cdd:cd03294  193 PLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGVDRAKV 269

ABC_OpuCA_Osmoprotection

cd03295

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

21-256

4.52e-48

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: 160.16 E-value: 4.52e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARmvQALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGgELKIDGQPVdiaRRRPGTEMRSKVQMVFQN 99
Cdd:cd03295   10 YGGGK--KAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMInRLIEPTSG-EIFIDGEDI---REQDPVELRRKIGYVIQQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PygSLNPRQKVGD--VLMEPLIintKIPASERRERAEAMLVKVGLGPEHF-NRYPHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:cd03295   84 I--GLFPHMTVEEniALVPKLL---KWPKEKIRERADELLALVGLDPAEFaDRYPHELSGGQQQRVGVARALAADPPLLL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 177 LDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAA 256
Cdd:cd03295  159 MDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPANDFVAEFVGA 238

phnK

PRK11701

phosphonate C-P lyase system protein PhnK; Provisional

8-253

6.05e-48

phosphonate C-P lyase system protein PhnK; Provisional

Pssm-ID: 183280 [Multi-domain] Cd Length: 258 Bit Score: 160.09 E-value: 6.05e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYhvpgglfgGARmvQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKI---DGQPVDI---- 80
Cdd:PRK11701  10 RGLTKLY--------GPR--KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYrmrDGQLRDLyals 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 -ARRRpgTEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQR 159
Cdd:PRK11701  80 eAERR--RLLRTEWGFVHQHPRDGLRMQVSAGGNIGERLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFSGGMQ 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 160 QRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTRE 239
Cdd:PRK11701 158 QRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESGLTD 237

                        250
                 ....*....|....
gi 739227338 240 ELFADPKHPYTRQL 253
Cdd:PRK11701 238 QVLDDPQHPYTQLL 251

artP

PRK11124

arginine transporter ATP-binding subunit; Provisional

28-246

8.67e-48

arginine transporter ATP-binding subunit; Provisional

Pssm-ID: 182980 [Multi-domain] Cd Length: 242 Bit Score: 159.41 E-value: 8.67e-48

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARR---RPGTEMRSKVQMVFQNpYgSL 104
Cdd:PRK11124  16 QALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFDFSKTpsdKAIRELRRNVGMVFQQ-Y-NL 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 NPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:PRK11124  94 WPHLTVQQNLIEAPCRVLGLSKDQALARAEKLLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAAL 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 185 DLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREElFADPK 246
Cdd:PRK11124 173 DPEITAQIVSIIRELAET-GITQVIVTHEVEVARKTASRVVYMENGHIVEQGDASC-FTQPQ 232

HisP

COG4598

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

30-252

1.53e-47

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

Pssm-ID: 443652 [Multi-domain] Cd Length: 259 Bit Score: 159.20 E-value: 1.53e-47

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPG----------TEMRSKVQMVFQ- 98
Cdd:COG4598   24 LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRDGelvpadrrqlQRIRTRLGMVFQs 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  99 -NPYGSLNPRQKVgdvlMEPLIINTKIPASERRERAEAMLVKVGLGPEHfNRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:COG4598  104 fNLWSHMTVLENV----IEAPVHVLGRPKAEAIERAEALLAKVGLADKR-DAYPAHLSGGQQQRAAIARALAMEPEVMLF 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ 252
Cdd:COG4598  179 DEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVFGNPKSERLRQ 252

3a0106s01

TIGR00968

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

28-249

3.85e-46

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

Pssm-ID: 130041 [Multi-domain] Cd Length: 237 Bit Score: 154.96 E-value: 3.85e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPgteMRSKVQMVFQNpYgSLNPR 107
Cdd:TIGR00968  14 QALDDVNLEVPTGSLVALLGPSGSGKSTLLRIIAGLEQPDSGRIRLNGQ--DATRVHA---RDRKIGFVFQH-Y-ALFKH 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  108 QKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:TIGR00968  87 LTVRDNIAFGLEIR-KHPKAKIKARVEELLELVQL--EGLgDRYPNQLSGGQRQRVALARALAVEPQVLLLDEPFGALDA 163

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338  187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPY 249
Cdd:TIGR00968 164 KVRKELRSWLRKLHDEVHVTTVFVTHDQEEAMEVADRIVVMSNGKIEQIGSPDEVYDHPANPF 226

OpuBA

COG1125

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

29-254

8.26e-46

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

Pssm-ID: 440742 [Multi-domain] Cd Length: 306 Bit Score: 156.02 E-value: 8.26e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPaSGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQNpyGSLNPR 107
Cdd:COG1125   17 AVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMInRLIEP-TSGRILIDGEDI---RDLDPVELRRRIGYVIQQ--IGLFPH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGD-VLMEPLIIntKIPASERRERAEAMLVKVGLGPEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:COG1125   91 MTVAEnIATVPRLL--GWDKERIRARVDELLELVGLDPEEYrDRYPHELSGGQQQRVGVARALAADPPILLMDEPFGALD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLF 254
Cdd:COG1125  169 PITREQLQDELLRLQRELGKTIVFVTHDIDEALKLGDRIAVMREGRIVQYDTPEEILANPANDFVADFV 237

ThiQ

COG3840

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

33-253

9.36e-46

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

Pssm-ID: 443051 [Multi-domain] Cd Length: 232 Bit Score: 153.76 E-value: 9.36e-46

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGtemRSKVQMVFQ--NPYGSLNPRQKV 110
Cdd:COG3840   18 FDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQ--DLTALPPA---ERPVSMLFQenNLFPHLTVAQNI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 111 GdvlmepLIINTKI-PASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQ 189
Cdd:COG3840   93 G------LGLRPGLkLTAEQRAQVEQALERVGLA-GLLDRLPGQLSGGQRQRVALARCLVRKRPILLLDEPFSALDPALR 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338 190 AQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQL 253
Cdd:COG3840  166 QEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGPTAALLDGEPPPALAAY 229

ABC_PhnC_transporter

cd03256

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

27-241

7.42e-45

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: 151.57 E-value: 7.42e-45

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASgGELKIDGQPVDIARRRPGTEMRSKVQMVFQNPygSLN 105
Cdd:cd03256   14 KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNgLVEPTS-GSVLIDGTDINKLKGKALRQLRRQIGMIFQQF--NLI 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGD-VLMEPLIINTKIPA------SERRERAEAMLVKVGLGPEHFNRYPHMfSGGQRQRIAIARALMLNPALLVLD 178
Cdd:cd03256   91 ERLSVLEnVLSGRLGRRSTWRSlfglfpKEEKQRALAALERVGLLDKAYQRADQL-SGGQQQRVAIARALMQQPKLILAD 169

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:cd03256  170 EPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGPPAEL 232

CP_lyasePhnK

TIGR02323

phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...

28-256

7.89e-45

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: 151.91 E-value: 7.89e-45

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKI---DGQPVDI-----ARRRpgTEMRSKVQMVFQN 99
Cdd:TIGR02323  17 KGCRDVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELELyqlseAERR--RLMRTEWGFVHQN 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  100 PYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:TIGR02323  95 PRDGLRMRVSAGANIGERLMAIGARHYGNIRATAQDWLEEVEIDPTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDE 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  180 PVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAA 256
Cdd:TIGR02323 175 PTGGLDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAQRLLVMQQGRVVESGLTDQVLDDPQHPYTQLLVSS 251

cbiO

PRK13635

energy-coupling factor ABC transporter ATP-binding protein;

28-243

1.02e-44

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184195 [Multi-domain] Cd Length: 279 Bit Score: 152.48 E-value: 1.02e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDPASGgELKIDGQPVDIArrrpgT--EMRSKVQMVFQNPygsl 104
Cdd:PRK13635  21 YALKDVSFSVYEGEWVAIVGHNGSGKSTLAKlLNGLLLPEAG-TITVGGMVLSEE-----TvwDVRRQVGMVFQNP---- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 nPRQKVG-----DVL--MEpliiNTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:PRK13635  91 -DNQFVGatvqdDVAfgLE----NIGVPREEMVERVDQALRQVGM-EDFLNREPHRLSGGQKQRVAIAGVLALQPDIIIL 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK13635 165 DEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEGTPEEIFK 229

FepC

COG1120

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

30-242

1.58e-44

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: 151.35 E-value: 1.58e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQNPygSLNPRQK 109
Cdd:COG1120   17 LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDL---ASLSRRELARRIAYVPQEP--PAPFGLT 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGD-VLM--EPLIINTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:COG1120   92 VRElVALgrYPHLGLFGRPSAEDREAVEEALERTGL--EHLaDRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLD 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELF 242
Cdd:COG1120  170 LAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVL 226

glnQ

PRK09493

glutamine ABC transporter ATP-binding protein GlnQ;

27-252

2.04e-44

glutamine ABC transporter ATP-binding protein GlnQ;

Pssm-ID: 181906 [Multi-domain] Cd Length: 240 Bit Score: 150.63 E-value: 2.04e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiARRRPGTEMRSKVQMVFQNPYgsLNP 106
Cdd:PRK09493  14 TQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVN-DPKVDERLIRQEAGMVFQQFY--LFP 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 R-QKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK09493  91 HlTALENVMFGPLRVR-GASKEEAEKQARELLAKVGLA-ERAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALD 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 186 LSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ 252
Cdd:PRK09493 169 PELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234

ABC_PstB_phosphate_transporter

cd03260

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

28-241

2.33e-44

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: 150.02 E-value: 2.33e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASG----GELKIDGQPVDIARRRPgTEMRSKVQMVFQNPyg 102
Cdd:cd03260   14 HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNrLNDLIPGapdeGEVLLDGKDIYDLDVDV-LELRRRVGMVFQKP-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 slNP-RQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNR-YPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03260   91 --NPfPGSIYDNVAYGLRLHGIKLKEELDERVEEALRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEPEVLLLDEP 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:cd03260  169 TSALDPISTAKIEELIAELKK--EYTIVIVTHNMQQAARVADRTAFLLNGRLVEFGPTEQI 227

YbbA

COG4181

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

22-240

4.64e-44

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: 149.51 E-value: 4.64e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVD------IARRRPGtemrsKVQM 95
Cdd:COG4181   20 TGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFaldedaRARLRAR-----HVGF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  96 VFQN----PygSLNPRQKVgdvlMEPLIINtkiPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLN 171
Cdd:COG4181   95 VFQSfqllP--TLTALENV----MLPLELA---GRRDARARARALLERVGLG-HRLDHYPAQLSGGEQQRVALARAFATE 164

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 172 PALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREE 240
Cdd:COG4181  165 PAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVEDTAATA 232

SapD

COG4170

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

26-258

6.58e-44

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

Pssm-ID: 443330 [Multi-domain] Cd Length: 331 Bit Score: 151.98 E-value: 6.58e-44

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  26 MVQALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDP---ASGGELKIDGQpvDI------ARRRPgteMRSKVQM 95
Cdd:COG4170   19 RVKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDnwhVTADRFRWNGI--DLlklsprERRKI---IGREIAM 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  96 VFQNPYGSLNPRQKVGDVLMEpliintKIPASE-----------RRERAEAMLVKVGLgPEH---FNRYPHMFSGGQRQR 161
Cdd:COG4170   94 IFQEPSSCLDPSAKIGDQLIE------AIPSWTfkgkwwqrfkwRKKRAIELLHRVGI-KDHkdiMNSYPHELTEGECQK 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 162 IAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:COG4170  167 VMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQI 246

                        250
                 ....*....|....*..
gi 739227338 242 FADPKHPYTRQLFAATP 258
Cdd:COG4170  247 LKSPHHPYTKALLRSMP 263

cbiO

PRK13639

cobalt transporter ATP-binding subunit; Provisional

28-246

1.00e-43

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184199 [Multi-domain] Cd Length: 275 Bit Score: 149.84 E-value: 1.00e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgTEMRSKVQMVFQNPYGSLNPR 107
Cdd:PRK13639  16 EALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSL-LEVRKTVGIVFQNPDDQLFAP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:PRK13639  95 TVEEDVAFGPL--NLGLSKEEVEKRVKEALKAVGM--EGFeNKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDP 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 187 SVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:PRK13639 171 MGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIE 229

potA

TIGR01187

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

45-275

3.81e-43

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: 149.57 E-value: 3.81e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   45 IVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPgtEMRSkVQMVFQNpYgSLNPRQKVGDVLMEPLIINtKI 124
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDG--EDVTNVPP--HLRH-INMVFQS-Y-ALFPHMTVEENVAFGLKMR-KV 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  125 PASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFE 204
Cdd:TIGR01187  73 PRAEIKPRVLEALRLVQLE-EFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLRDQMQLELKTIQEQLG 151

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338  205 LTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHpytrqLFAATPITDVDAIRARVERRKAA 275
Cdd:TIGR01187 152 ITFVFVTHDQEEAMTMSDRIAIMRKGKIAQIGTPEEIYEEPAN-----LFVARFIGEINVFEATVIERKSE 217

ABC_ModC_molybdenum_transporter

cd03297

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

33-236

6.53e-43

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: 145.90 E-value: 6.53e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVErGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRR---PGTemRSKVQMVFQN----PYgsLN 105
Cdd:cd03297   17 IDFDLN-EEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKinlPPQ--QRKIGLVFQQyalfPH--LN 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLmepliinTKIPASERRERAEAMLVKVGLGPEhFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03297   92 VRENLAFGL-------KRKRNREDRISVDELLDLLGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03297  164 RALRLQLLPELKQIKKNLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214

ABC_tran

pfam00005

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

30-180

6.84e-43

Pssm-ID: 394964 [Multi-domain] Cd Length: 150 Bit Score: 143.56 E-value: 6.84e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgteMRSKVQMVFQNPygSLNPRQK 109
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKS---LRKEIGYVFQDP--QLFPRLT 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338  110 VGDVLMEPLIInTKIPASERRERAEAMLVKVGLGP---EHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:pfam00005  76 VRENLRLGLLL-KGLSKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEP 148

PRK10619

histidine ABC transporter ATP-binding protein HisP;

28-257

8.51e-43

histidine ABC transporter ATP-binding protein HisP;

Pssm-ID: 182592 [Multi-domain] Cd Length: 257 Bit Score: 147.04 E-value: 8.51e-43

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGT----------EMRSKVQMVF 97
Cdd:PRK10619  19 EVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQlkvadknqlrLLRTRLTMVF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  98 QnpYGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:PRK10619  99 Q--HFNLWSHMTVLENVMEAPIQVLGLSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLF 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAAT 257
Cdd:PRK10619 177 DEPTSALDPELVGEVLRIMQQLAEEGK-TMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLKGS 255

ABC_phnC

TIGR02315

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

27-244

1.16e-42

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: 145.90 E-value: 1.16e-42

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPaSGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNpYgSLN 105
Cdd:TIGR02315  15 KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCInRLVEP-SSGSILLEGTDITKLRGKKLRKLRRRIGMIFQH-Y-NLI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  106 PRQKV-GDVLMEPLIINTKIPA------SERRERAEAMLVKVGLGPEHFNRYPHMfSGGQRQRIAIARALMLNPALLVLD 178
Cdd:TIGR02315  92 ERLTVlENVLHGRLGYKPTWRSllgrfsEEDKERALSALERVGLADKAYQRADQL-SGGQQQRVAIARALAQQPDLILAD 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338  179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGAPSELDDE 236

ZnuC

COG1121

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

29-242

2.56e-42

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

Pssm-ID: 440738 [Multi-domain] Cd Length: 245 Bit Score: 145.23 E-value: 2.56e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVDIARRRPGtemrskvqmvfqnpY----GS 103
Cdd:COG1121   21 VLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILgLLPPTSG-TVRLFGKPPRRARRRIG--------------YvpqrAE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 LNPRQ--KVGDVLMEPLIINT---KIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:COG1121   86 VDWDFpiTVRDVVLMGRYGRRglfRRPSRADREAVDEALERVGL--EDLaDRPIGELSGGQQQRVLLARALAQDPDLLLL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGeAVEQGTREELF 242
Cdd:COG1121  164 DEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVL 226

ABCC_MRP_Like

cd03228

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

23-231

3.95e-42

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: 142.52 E-value: 3.95e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPV-DIARRrpgtEMRSKVQMVFQNP 100
Cdd:cd03228   11 PGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLrLYDPTSG-EILIDGVDLrDLDLE----SLRKNIAYVPQDP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 Y---GSLnprqkvgdvlmepliintkipaserreraeamlvkvglgpeHFNryphMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:cd03228   86 FlfsGTI-----------------------------------------REN----ILSGGQRQRIAIARALLRDPPILIL 120

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVISKGE 231
Cdd:cd03228  121 DEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171

ABC_ModC_like

cd03299

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

30-246

5.52e-42

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: 144.02 E-value: 5.52e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPgtEMRsKVQMVFQNPYgsLNPRQK 109
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNG--KDITNLPP--EKR-DISYVPQNYA--LFPHMT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLmEPLIINTKIPASERRERAEAMLVKvgLGPEH-FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSV 188
Cdd:cd03299   88 VYKNI-AYGLKKRKVDKKEIERKVLEIAEM--LGIDHlLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRT 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 189 QAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:cd03299  165 KEKLREELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPK 222

nikD

PRK10418

nickel transporter ATP-binding protein NikD; Provisional

31-256

7.22e-42

nickel transporter ATP-binding protein NikD; Provisional

Pssm-ID: 236688 [Multi-domain] Cd Length: 254 Bit Score: 144.46 E-value: 7.22e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  31 KGIDFAVERGKTLAIVGESGSGKS-TLARIIALIDP---ASGGELKIDGQPVDIARRRpGTemrsKVQMVFQNPYGSLNP 106
Cdd:PRK10418  20 HGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVAPCALR-GR----KIATIMQNPRSAFNP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIInTKIPASERRERAeaMLVKVGLGPEH--FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:PRK10418  95 LHTMHTHARETCLA-LGKPADDATLTA--ALEAVGLENAArvLKLYPFEMSGGMLQRMMIALALLCEAPFIIADEPTTDL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 185 DLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAA 256
Cdd:PRK10418 172 DVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLVSA 243

cbiO

PRK13636

cobalt transporter ATP-binding subunit; Provisional

14-244

7.66e-42

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184196 [Multi-domain] Cd Length: 283 Bit Score: 145.38 E-value: 7.66e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  14 YHVPGGlfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgTEMRSKV 93
Cdd:PRK13636  13 YNYSDG-------THALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIDYSRKGL-MKLRESV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  94 QMVFQNPYGSLNPRQKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLgpEHFNRYP-HMFSGGQRQRIAIARALMLNP 172
Cdd:PRK13636  85 GMVFQDPDNQLFSASVYQDVSFGAV--NLKLPEDEVRKRVDNALKRTGI--EHLKDKPtHCLSFGQKKRVAIAGVLVMEP 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 173 ALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13636 161 KVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232

FtsE

COG2884

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

27-240

9.37e-42

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

Pssm-ID: 442130 [Multi-domain] Cd Length: 223 Bit Score: 142.88 E-value: 9.37e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNpyGSLNP 106
Cdd:COG2884   15 REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYLRRRIGVVFQD--FRLLP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:COG2884   93 DRTVYENVALPLRV-TGKSRKEIRRRVREVLDLVGLS-DKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTGNLDP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 187 SVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:COG2884  171 ETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEARGV 223

SunT

COG2274

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

29-243

9.68e-42

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: 152.30 E-value: 9.68e-42

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPV-DIARRrpgtEMRSKVQMVFQNPY---GS 103
Cdd:COG2274  490 VLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLgLYEPTSG-RILIDGIDLrQIDPA----SLRRQIGVVLQDVFlfsGT 564

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 L--NprqkvgdvlmeplIINTKIPASErrERAEAMLVKVGLGpEHFNRYPH-----------MFSGGQRQRIAIARALML 170
Cdd:COG2274  565 IreN-------------ITLGDPDATD--EEIIEAARLAGLH-DFIEALPMgydtvvgeggsNLSGGQRQRLAIARALLR 628

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFA 243
Cdd:COG2274  629 NPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDGTHEELLA 698

ModC

COG4148

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

33-272

2.02e-41

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: 146.01 E-value: 2.02e-41

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQP-VDIARR--RPgTEMRSkVQMVFQNPygSLNPRQK 109
Cdd:COG4148   18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGifLP-PHRRR-IGYVFQEA--RLFPHLS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLMEPLiinTKIPASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQ 189
Cdd:COG4148   94 VRGNLLYGR---KRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARK 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 190 AQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPkhpytrQLFAATPITDVDAI-RAR 268
Cdd:COG4148  170 AEILPYLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRP------DLLPLAGGEEAGSVlEAT 243


                 ....
gi 739227338 269 VERR 272
Cdd:COG4148  244 VAAH 247

ABC_DR_subfamily_A

cd03230

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

28-231

1.23e-40

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: 138.68 E-value: 1.23e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarRRPGTEMRSKVQMVFQNP--YGSLN 105
Cdd:cd03230   14 TALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDI----KKEPEEVKRRIGYLPEEPslYENLT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRqkvgdvlmepliintkipaserreraeamlvkvglgpEHFnryphMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03230   90 VR-------------------------------------ENL-----KLSGGMKQRLALAQALLHDPELLILDEPTSGLD 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 739227338 186 LSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03230  128 PESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGR 172

ABC_CysA_sulfate_importer

cd03296

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

1-249

1.37e-40

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: 140.55 E-value: 1.37e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGkgITRDyhvpgglFGGARmvqALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDI 80
Cdd:cd03296    1 MSIEVRN--VSKR-------FGDFV---ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGE--DA 66

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRRPgteMRSKVQMVFQN--PYGSLNPRQKVGDVL-MEPliINTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSG 156
Cdd:cd03296   67 TDVPV---QERNVGFVFQHyaLFRHMTVFDNVAFGLrVKP--RSERPPEAEIRAKVHELLKLVQL--DWLaDRYPAQLSG 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 157 GQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGeAVEQ- 235
Cdd:cd03296  140 GQRQRVALARALAVEPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKG-RIEQv 218

                        250
                 ....*....|....
gi 739227338 236 GTREELFADPKHPY 249
Cdd:cd03296  219 GTPDEVYDHPASPF 232

ABC_ATPase

cd00267

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

28-231

1.38e-40

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: 137.76 E-value: 1.38e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQnpygslnpr 107
Cdd:cd00267   13 TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDI---AKLPLEELRRRIGYVPQ--------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 qkvgdvlmepliintkipaserreraeamlvkvglgpehfnryphmFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:cd00267   81 ----------------------------------------------LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPA 114

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 739227338 188 VQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd00267  115 SRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157

LolD_lipo_ex

TIGR02211

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

23-230

2.64e-40

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: 139.41 E-value: 2.64e-40

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSK-VQMVFQnpY 101
Cdd:TIGR02211  14 GKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKLRNKkLGFIYQ--F 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  102 GSLNPRQKVGDVLMEPLIINTKIPAsERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:TIGR02211  92 HHLLPDFTALENVAMPLLIGKKSVK-EAKERAYEMLEKVGLE-HRINHRPSELSGGERQRVAIARALVNQPSLVLADEPT 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 739227338  182 SALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIaDDVMVISKG 230
Cdd:TIGR02211 170 GNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKL-DRVLEMKDG 217

NatA

COG4555

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

27-241

1.53e-39

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

Pssm-ID: 443618 [Multi-domain] Cd Length: 243 Bit Score: 138.07 E-value: 1.53e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVDIARRRPgtemRSKVQMVFQNPYgsLN 105
Cdd:COG4555   14 VPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAgLLKPDSG-SILIDGEDVRKEPREA----RRQIGVLPDERG--LY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:COG4555   87 DRLTVRENIRYFAELY-GLFDEELKKRIEELIELLGLE-EFLDRRVGELSTGMKKKVALARALVHDPKVLLLDEPTNGLD 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 186 LSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:COG4555  165 VMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQGSLDEL 219

MdlB

COG1132

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

28-256

2.93e-39

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

Pssm-ID: 440747 [Multi-domain] Cd Length: 579 Bit Score: 144.15 E-value: 2.93e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPaSGGELKIDGQPV-DIARRrpgtEMRSKVQMVFQNPY---G 102
Cdd:COG1132  354 PVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLrFYDP-TSGRILIDGVDIrDLTLE----SLRRQIGVVPQDTFlfsG 428

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SL--NprqkvgdvlmeplIINTKIPASErrERAEAMLVKVGLgpEHF-NRYPH-----------MFSGGQRQRIAIARAL 168
Cdd:COG1132  429 TIreN-------------IRYGRPDATD--EEVEEAAKAAQA--HEFiEALPDgydtvvgergvNLSGGQRQRIAIARAL 491

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 169 MLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFAdpKHP 248
Cdd:COG1132  492 LKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIR-NADRILVLDDGRIVEQGTHEELLA--RGG 566


                 ....*...
gi 739227338 249 YTRQLFAA 256
Cdd:COG1132  567 LYARLYRL 574

PRK10851

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

28-245

7.56e-39

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;

Pssm-ID: 182778 [Multi-domain] Cd Length: 353 Bit Score: 139.06 E-value: 7.56e-39

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI--ARRRpgtemrsKVQMVFQNpYgSLN 105
Cdd:PRK10851  16 QVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRlhARDR-------KVGFVFQH-Y-ALF 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLiinTKIPaseRRERAEAMLVK---------VGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALL 175
Cdd:PRK10851  87 RHMTVFDNIAFGL---TVLP---RRERPNAAAIKakvtqllemVQL--AHLaDRYPAQLSGGQKQRVALARALAVEPQIL 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEaVEQ-GTREELFADP 245
Cdd:PRK10851 159 LLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGN-IEQaGTPDQVWREP 228

potA

PRK09452

spermidine/putrescine ABC transporter ATP-binding protein PotA;

28-272

1.10e-38

spermidine/putrescine ABC transporter ATP-binding protein PotA;

Pssm-ID: 236523 [Multi-domain] Cd Length: 375 Bit Score: 139.31 E-value: 1.10e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVD--IARRRPgtemrskVQMVFQNpYgSLN 105
Cdd:PRK09452  28 EVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDIThvPAENRH-------VNTVFQS-Y-ALF 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGD-----VLMEpliintKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:PRK09452  99 PHMTVFEnvafgLRMQ------KTPAAEITPRVMEALRMVQL--EEFaQRKPHQLSGGQQQRVAIARAVVNKPKVLLLDE 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 180 PVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ------L 253
Cdd:PRK09452 171 SLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARfigeinI 250

                        250       260
                 ....*....|....*....|.
gi 739227338 254 FAATPITDVDA--IRARVERR 272
Cdd:PRK09452 251 FDATVIERLDEqrVRANVEGR 271

ABC_Metallic_Cations

cd03235

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

29-230

1.21e-38

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: 134.58 E-value: 1.21e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVdiarrrpgTEMRSKVQMVFQNPYGSLNPR 107
Cdd:cd03235   14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILgLLKPTSG-SIRVFGKPL--------EKERKRIGYVPQRRSIDRDFP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPL---IINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:cd03235   85 ISVRDVVLMGLyghKGLFRRLSKADKAKVDEALERVGLS-ELADRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGV 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 739227338 185 DLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKG 230
Cdd:cd03235  164 DPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRT 208

ABC_Iron-Siderophores_B12_Hemin

cd03214

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

28-236

1.47e-38

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: 133.33 E-value: 1.47e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarRRPGTEMRSKVQMVFQnpygslnpr 107
Cdd:cd03214   13 TVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLA---SLSPKELARKIAYVPQ--------- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 qkvgdvlmepliintkipaserreraeaMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03214   81 ----------------------------ALELLGL--AHLaDRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDI 130

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03214  131 AHQIELLELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180

cbiO

PRK13632

cobalt transporter ATP-binding subunit; Provisional

28-244

1.82e-38

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237452 [Multi-domain] Cd Length: 271 Bit Score: 135.89 E-value: 1.82e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarRRPGTEMRSKVQMVFQNPygslnPR 107
Cdd:PRK13632  23 NALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITIS---KENLKEIRKKIGIIFQNP-----DN 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGdVLMEPLII----NTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSA 183
Cdd:PRK13632  95 QFIG-ATVEDDIAfgleNKKVPPKKMKDIIDDLAKKVGME-DYLDKEPQNLSGGQKQRVAIASVLALNPEIIIFDESTSM 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 184 LDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVrYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13632 173 LDPKGKREIKKIMVDLRKTRKKTLISITHDMDEA-ILADKVIVFSEGKLIAQGKPKEILNN 232

cbiO

PRK13646

energy-coupling factor transporter ATPase;

28-258

2.51e-38

energy-coupling factor transporter ATPase;

Pssm-ID: 184205 [Multi-domain] Cd Length: 286 Bit Score: 136.06 E-value: 2.51e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASG----GELKIDGQPVDIARRrpgtEMRSKVQMVFQNPYG 102
Cdd:PRK13646  21 QAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNInALLKPTTGtvtvDDITITHKTKDKYIR----PVRKRIGMVFQFPES 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK13646  97 QLFEDTVEREIIFGPK--NFKMNLDEVKNYAHRLLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTA 174

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKhpYTRQLFAATP 258
Cdd:PRK13646 175 GLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK--KLADWHIGLP 248

PstB

COG1117

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

28-251

2.81e-38

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

Pssm-ID: 440734 [Multi-domain] Cd Length: 258 Bit Score: 135.16 E-value: 2.81e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLA----RIIALIDPAS-GGELKIDGQpvDI-ARRRPGTEMRSKVQMVFQNPy 101
Cdd:COG1117   25 QALKDINLDIPENKVTALIGPSGCGKSTLLrclnRMNDLIPGARvEGEILLDGE--DIyDPDVDVVELRRRVGMVFQKP- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 gslNPRQK-VGD-VLMePLIINTKIPASERRERAEAMLVKVGLGPE---HFNRYPHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:COG1117  102 ---NPFPKsIYDnVAY-GLRLHGIKSKSELDEIVEESLRKAALWDEvkdRLKKSALGLSGGQQQRLCIARALAVEPEVLL 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 177 LDEPVSALD-LSVqAQVLNLLRDLQEEFelTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTR 251
Cdd:COG1117  178 MDEPTSALDpIST-AKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTE 250

LivG

COG0411

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

21-246

4.32e-38

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: 134.40 E-value: 4.32e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPgtEMRSKVQMV--FQ 98
Cdd:COG0411   14 FGG---LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGR--DITGLPP--HRIARLGIArtFQ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  99 NP--YGSLNPRQKV--------GDVLMEPLIINTKIPASER--RERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIAR 166
Cdd:COG0411   87 NPrlFPELTVLENVlvaaharlGRGLLAALLRLPRARREEReaRERAEELLERVGLA-DRADEPAGNLSYGQQRRLEIAR 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:COG0411  166 ALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGTPAEVRADPR 245

modC_ABC

TIGR02142

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

33-249

5.80e-38

molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding cassette (ABC) protein of the three subunit molybdate ABC transporter. The three proteins of this complex are homologous to proteins of the sulfate ABC transporter. Molybdenum may be used in nitrogenases of nitrogen-fixing bacteria and in molybdopterin cofactors. In some cases, molybdate may be transported by a sulfate transporter rather than by a specific molybdate transporter. [Transport and binding proteins, Anions]

Pssm-ID: 131197 [Multi-domain] Cd Length: 354 Bit Score: 136.78 E-value: 5.80e-38

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEM-RSKVQMVFQNpyGSLNPRQKVG 111
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIFLPPeKRRIGYVFQE--ARLFPHLSVR 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  112 DVLMEPLiinTKIPASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQ 191
Cdd:TIGR02142  94 GNLRYGM---KRARPSERRISFERVIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYE 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338  192 VLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPY 249
Cdd:TIGR02142 170 ILPYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPW 227

ABC_Carb_Monos_I

cd03216

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

21-233

7.97e-38

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: 131.01 E-value: 7.97e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARrrPGTEMRSKVQMVFQnp 100
Cdd:cd03216   10 FGG---VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFAS--PRDARRAGIAMVYQ-- 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ygslnprqkvgdvlmepliintkipaserreraeamlvkvglgpehfnryphmFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03216   83 -----------------------------------------------------LSVGERQMVEIARALARNARLLILDEP 109

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAV 233
Cdd:cd03216  110 TAALTPAEVERLFKVIRRLRAQ-GVAVIFISHRLDEVFEIADRVTVLRDGRVV 161

PRK13633

energy-coupling factor transporter ATPase;

29-244

8.62e-38

energy-coupling factor transporter ATPase;

Pssm-ID: 237453 [Multi-domain] Cd Length: 280 Bit Score: 134.44 E-value: 8.62e-38

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPaSGGELKIDGqpVDIARRRPGTEMRSKVQMVFQNPYGSLNPR 107
Cdd:PRK13633  25 ALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMnALLIP-SEGKVYVDG--LDTSDEENLWDIRNKAGMVFQNPDNQIVAT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLgpEHFNRY-PHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:PRK13633 102 IVEEDVAFGPE--NLGIPPEEIRERVDESLKKVGM--YEYRRHaPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDL-SVVRyiADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13633 178 SGRREVVNTIKELNKKYGITIILITHYMeEAVE--ADRIIVMDSGKVVMEGTPKEIFKE 234

thiQ

PRK10771

thiamine ABC transporter ATP-binding protein ThiQ;

34-241

1.96e-37

thiamine ABC transporter ATP-binding protein ThiQ;

Pssm-ID: 182716 [Multi-domain] Cd Length: 232 Bit Score: 132.01 E-value: 1.96e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  34 DFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIAR----RRPgtemrskVQMVFQ--NPYGSLNPR 107
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQ--DHTTtppsRRP-------VSMLFQenNLFSHLTVA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLIINtkipaSERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:PRK10771  90 QNIGLGLNPGLKLN-----AAQREKLHAIARQMGIE-DLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPA 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 188 VQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:PRK10771 164 LRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGPTDEL 217

CydD

COG4988

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

28-243

6.84e-37

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: 137.58 E-value: 6.84e-37

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVdiaRRRPGTEMRSKVQMVFQNPY---GS 103
Cdd:COG4988  351 PALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLgFLPPYSG-SILINGVDL---SDLDPASWRRQIAWVPQNPYlfaGT 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 L--NprqkvgdVLMepliinTKIPASErrERAEAMLVKVGLGpEHFNRYPH-----------MFSGGQRQRIAIARALML 170
Cdd:COG4988  427 IreN-------LRL------GRPDASD--EELEAALEAAGLD-EFVAALPDgldtplgeggrGLSGGQAQRLALARALLR 490

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFA 243
Cdd:COG4988  491 DAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLA-QADRILVLDDGRIVEQGTHEELLA 560

cbiO

PRK13648

cobalt transporter ATP-binding subunit; Provisional

29-244

1.01e-36

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184207 [Multi-domain] Cd Length: 269 Bit Score: 131.41 E-value: 1.01e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPygslnPRQ 108
Cdd:PRK13648  24 TLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE---KLRKHIGIVFQNP-----DNQ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEPLII---NTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13648  96 FVGSIVKYDVAFgleNHAVPYDEMHRRVSEALKQVDM-LERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLD 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13648 175 PDARQNLLDLVRKVKSEHNITIISITHDLSEAME-ADHVIVMNKGTVYKEGTPTEIFDH 232

ABC_MalK_N

cd03301

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

27-235

1.15e-36

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: 129.68 E-value: 1.15e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGtemRSKVQMVFQNpYgSLNP 106
Cdd:cd03301   13 VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGR--DVTDLPPK---DRDIAMVFQN-Y-ALYP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINtKIPASERRERAE--AMLVKVGlgpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:cd03301   86 HMTVYDNIAFGLKLR-KVPKDEIDERVRevAELLQIE---HLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEPLSNL 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739227338 185 DLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGeAVEQ 235
Cdd:cd03301  162 DAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDG-QIQQ 211

cbiO

PRK13634

cobalt transporter ATP-binding subunit; Provisional

29-245

1.51e-36

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237454 [Multi-domain] Cd Length: 290 Bit Score: 131.68 E-value: 1.51e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDPASGgELKIdGQPVDIARRRPGT--EMRSKVQMVFQNPYGSLN 105
Cdd:PRK13634  22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQhLNGLLQPTSG-TVTI-GERVITAGKKNKKlkPLRKKVGIVFQFPEHQLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13634 100 EETVEKDICFGP--MNFGVSEEDAKQKAREMIELVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK13634 178 PKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237

cbiO

PRK13637

energy-coupling factor transporter ATPase;

1-242

1.88e-36

energy-coupling factor transporter ATPase;

Pssm-ID: 237455 [Multi-domain] Cd Length: 287 Bit Score: 131.32 E-value: 1.88e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGkgITRDYhVPGGLFGGarmvQALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGgELKIDGqpVD 79
Cdd:PRK13637   1 MSIKIEN--LTHIY-MEGTPFEK----KALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLnGLLKPTSG-KIIIDG--VD 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  80 IARRRPG-TEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLGPEHF-NRYPHMFSGG 157
Cdd:PRK13637  71 ITDKKVKlSDIRKKVGLVFQYPEYQLFEETIEKDIAFGP--INLGLSEEEIENRVKRAMNIVGLDYEDYkDKSPFELSGG 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 158 QRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGT 237
Cdd:PRK13637 149 QKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGT 228


                 ....*
gi 739227338 238 REELF 242
Cdd:PRK13637 229 PREVF 233

ABC_Mj1267_LivG_branched

cd03219

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

21-246

2.59e-36

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: 129.48 E-value: 2.59e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNP 100
Cdd:cd03219   10 FGG---LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGE--DITGLPPHEIARLGIGRTFQIP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 --YGSLNPRQ--KVGDVLMEPLIINTKIPASER---RERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPA 173
Cdd:cd03219   85 rlFPELTVLEnvMVAAQARTGSGLLLARARREEreaRERAEELLERVGLA-DLADRPAGELSYGQQRRLEIARALATDPK 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 174 LLVLDEPVSALDLSVQAQVLNLLRDLQeEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:cd03219  164 LLLLDEPAAGLNPEETEELAELIRELR-ERGITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235

fbpC

PRK11432

ferric ABC transporter ATP-binding protein;

21-246

4.97e-36

ferric ABC transporter ATP-binding protein;

Pssm-ID: 183133 [Multi-domain] Cd Length: 351 Bit Score: 131.77 E-value: 4.97e-36

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMVQALkgiDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRrpGTEMRSkVQMVFQNp 100
Cdd:PRK11432  16 FGSNTVIDNL---NLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGE--DVTHR--SIQQRD-ICMVFQS- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YgSLNPRQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGL-GPEhfNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:PRK11432  87 Y-ALFPHMSLGENVGYGLKM-LGVPKEERKQRVKEALELVDLaGFE--DRYVDQISGGQQQRVALARALILKPKVLLFDE 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 180 PVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:PRK11432 163 PLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPA 229

ABCC_Glucan_exporter_like

cd03254

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...

21-243

1.17e-35

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: 127.34 E-value: 1.17e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQNP 100
Cdd:cd03254   10 FSYDEKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDI---RDISRKSLRSMIGVVLQDT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YgsLNPrqkvgDVLMEPLIINTKIPASERRERAEAMLvkvglGPEHF-----NRYPHM-------FSGGQRQRIAIARAL 168
Cdd:cd03254   87 F--LFS-----GTIMENIRLGRPNATDEEVIEAAKEA-----GAHDFimklpNGYDTVlgenggnLSQGERQLLAIARAM 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 169 MLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:cd03254  155 LRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEGTHDELLA 226

cbiO

PRK13640

energy-coupling factor transporter ATPase;

29-245

1.29e-35

energy-coupling factor transporter ATPase;

Pssm-ID: 184200 [Multi-domain] Cd Length: 282 Bit Score: 128.76 E-value: 1.29e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARII---ALIDPASGGELKIDGQPVDiarRRPGTEMRSKVQMVFQNPygsln 105
Cdd:PRK13640  22 ALNDISFSIPRGSWTALIGHNGSGKSTISKLInglLLPDDNPNSKITVDGITLT---AKTVWDIREKVGIVFQNP----- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLII---NTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK13640  94 DNQFVGATVGDDVAFgleNRAVPRPEMIKIVRDVLADVGM-LDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEAN-MADQVLVLDDGKLLAQGSPVEIFSKV 234

ABC_DrrA

cd03265

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

21-241

1.47e-35

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: 127.10 E-value: 1.47e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARmvqALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiaRRRPgTEMRSKVQMVFQNP 100
Cdd:cd03265   10 YGDFE---AVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDV---VREP-REVRRRIGIVFQDL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ygslnprqKVGDVLM--EPLIINTKI---PASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALL 175
Cdd:cd03265   83 --------SVDDELTgwENLYIHARLygvPGAERRERIDELLDFVGLL-EAADRLVKTYSGGMRRRLEIARSLVHRPEVL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:cd03265  154 FLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEGTPEEL 219

CydC

COG4987

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

29-255

1.91e-35

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

Pssm-ID: 444011 [Multi-domain] Cd Length: 569 Bit Score: 133.35 E-value: 1.91e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVdiaRRRPGTEMRSKVQMVFQNPY---GSL 104
Cdd:COG4987  350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLrFLDPQSG-SITLGGVDL---RDLDEDDLRRRIAVVPQRPHlfdTTL 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 -------NPRqkvgdvlmepliintkipASErrERAEAMLVKVGLGPeHFNRYPH-----------MFSGGQRQRIAIAR 166
Cdd:COG4987  426 renlrlaRPD------------------ATD--EELWAALERVGLGD-WLAALPDgldtwlgeggrRLSGGERRRLALAR 484

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFelTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFADpk 246
Cdd:COG4987  485 ALLRDAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLER-MDRILVLEDGRIVEQGTHEELLAQ-- 559


                 ....*....
gi 739227338 247 HPYTRQLFA 255
Cdd:COG4987  560 NGRYRQLYQ 568

MglA

COG1129

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

21-241

2.81e-35

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 132.06 E-value: 2.81e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIarRRPGTEMRSKVQMVFQNP 100
Cdd:COG1129   14 FGG---VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRF--RSPRDAQAAGIAIIHQEL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ygSLNPRQKV------GDVLMEPLIINTKipasERRERAEAMLVKVGLgpeHFNryPHM----FSGGQRQRIAIARALML 170
Cdd:COG1129   89 --NLVPNLSVaeniflGREPRRGGLIDWR----AMRRRARELLARLGL---DID--PDTpvgdLSVAQQQLVEIARALSR 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:COG1129  158 DARVLILDEPTASLTEREVERLFRIIRRLKAQ-GVAIIYISHRLDEVFEIADRVTVLRDGRLVGTGPVAEL 227

ABC_ThiQ_thiamine_transporter

cd03298

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

34-236

3.53e-35

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

Pssm-ID: 213265 [Multi-domain] Cd Length: 211 Bit Score: 125.68 E-value: 3.53e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  34 DFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIA--RRRPgtemrskVQMVFQ--NPYGSLNPRQK 109
Cdd:cd03298   18 DLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAppADRP-------VSMLFQenNLFAHLTVEQN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLMEPLIINtkipaSERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQ 189
Cdd:cd03298   91 VGLGLSPGLKLT-----AEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALR 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 739227338 190 AQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03298  165 AEMLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211

ABCC_ATM1_transporter

cd03253

ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...

28-243

3.95e-35

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: 126.19 E-value: 3.95e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGgELKIDGQPVdiaRRRPGTEMRSKVQMVFQNP------ 100
Cdd:cd03253   15 PVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLfRFYDVSSG-SILIDGQDI---REVTLDSLRRAIGVVPQDTvlfndt 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ------YGSLNP----------RQKVGDVLME-PLIINTKIpaSERreraeamlvkvGLgpehfnryphMFSGGQRQRIA 163
Cdd:cd03253   91 igynirYGRPDAtdeevieaakAAQIHDKIMRfPDGYDTIV--GER-----------GL----------KLSGGEKQRVA 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 164 IARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVrYIADDVMVISKGEAVEQGTREELFA 243
Cdd:cd03253  148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTI-VNADKIIVLKDGRIVERGTHEELLA 224

YnjD

COG4136

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

30-213

4.70e-35

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

Pssm-ID: 443311 [Multi-domain] Cd Length: 211 Bit Score: 125.29 E-value: 4.70e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKST-LARIIALIDPA--SGGELKIDGQPVD---IARRRPGtemrskvqMVFQNPYgs 103
Cdd:COG4136   17 LAPLSLTVAPGEILTLMGPSGSGKSTlLAAIAGTLSPAfsASGEVLLNGRRLTalpAEQRRIG--------ILFQDDL-- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 LNPRQKVGDVLmePLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSA 183
Cdd:COG4136   87 LFPHLSVGENL--AFALPPTIGRAQRRARVEQALEEAGLA-GFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSK 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 739227338 184 LDLSVQAQVLNLLRDLQEEFELTYVFVSHD 213
Cdd:COG4136  164 LDAALRAQFREFVFEQIRQRGIPALLVTHD 193

PRK10070

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

29-262

6.73e-35

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

Pssm-ID: 182221 [Multi-domain] Cd Length: 400 Bit Score: 129.77 E-value: 6.73e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPGT---EMRSKVQMVFQNpyGSLN 105
Cdd:PRK10070  43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDG--VDIAKISDAElreVRRKKIAMVFQS--FALM 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK10070 119 PHMTVLDNTAFGMEL-AGINAEERREKALDALRQVGL-ENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALD 196

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATPITDV 262
Cdd:PRK10070 197 PLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGVDISQV 273

cbiO

PRK13631

cobalt transporter ATP-binding subunit; Provisional

27-262

6.95e-35

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237451 [Multi-domain] Cd Length: 320 Bit Score: 128.04 E-value: 6.95e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLA-RIIALIDPASG----GELKIdGQPVDIARRRPGT---------EMRSK 92
Cdd:PRK13631  39 LVALNNISYTFEKNKIYFIIGNSGSGKSTLVtHFNGLIKSKYGtiqvGDIYI-GDKKNNHELITNPyskkiknfkELRRR 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  93 VQMVFQNPYGSLNPRQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNP 172
Cdd:PRK13631 118 VSMVFQFPEYQLFKDTIEKDIMFGP--VALGVKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQP 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 173 ALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPkHPYTRQ 252
Cdd:PRK13631 196 EILIFDEPTAGLDPKGEHEMMQLILDAKANNK-TVFVITHTMEHVLEVADEVIVMDKGKILKTGTPYEIFTDQ-HIINST 273

                        250
                 ....*....|
gi 739227338 253 LFAATPITDV 262
Cdd:PRK13631 274 SIQVPRVIQV 283

cbiO

PRK13652

cobalt transporter ATP-binding subunit; Provisional

27-245

7.13e-35

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 172200 [Multi-domain] Cd Length: 277 Bit Score: 126.84 E-value: 7.13e-35

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPYGSLNP 106
Cdd:PRK13652  17 KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIR---EVRKFVGLVFQNPDDQIFS 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:PRK13652  94 PTVEQDIAFGP--INLGLDEETVAHRVSSALHMLGL-EELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK13652 171 QGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229

thiQ

TIGR01277

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

34-236

1.46e-34

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: 124.20 E-value: 1.46e-34

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   34 DFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQpvDIARRRPgteMRSKVQMVFQ--NPYGSLNPRQKV 110
Cdd:TIGR01277  18 DLNVADGEIVAIMGPSGAGKSTLLNLIAgFIEPASG-SIKVNDQ--SHTGLAP---YQRPVSMLFQenNLFAHLTVRQNI 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  111 GDVLMEPLIINtkipaSERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQA 190
Cdd:TIGR01277  92 GLGLHPGLKLN-----AEQQEKVVDAAQQVGIA-DYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLLRE 165

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 739227338  191 QVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:TIGR01277 166 EMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKIKVVS 211

ABC_MTABC3_MDL1_MDL2

cd03249

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...

27-243

1.55e-34

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: 124.96 E-value: 1.55e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTlarIIALI----DPASGgELKIDGQPVDiarrrpgtemrskvqmvfqnpyg 102
Cdd:cd03249   16 VPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLerfyDPTSG-EILLDGVDIR----------------------- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNP---RQKVGDVLMEPLIINTKI----------PASERRERA----EAMLVKVGLgPEHFN----RYPHMFSGGQRQR 161
Cdd:cd03249   69 DLNLrwlRSQIGLVSQEPVLFDGTIaenirygkpdATDEEVEEAakkaNIHDFIMSL-PDGYDtlvgERGSQLSGGQKQR 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 162 IAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFelTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREEL 241
Cdd:cd03249  148 IAIARALLRNPKILLLDEATSALDAESEKLVQEALDRAMKGR--TTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGTHDEL 224


                 ..
gi 739227338 242 FA 243
Cdd:cd03249  225 MA 226

cbiO

PRK13650

energy-coupling factor transporter ATPase;

30-243

1.59e-34

energy-coupling factor transporter ATPase;

Pssm-ID: 184209 [Multi-domain] Cd Length: 279 Bit Score: 126.00 E-value: 1.59e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRrpgTEMRSKVQMVFQNPygslnPRQK 109
Cdd:PRK13650  23 LNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENV---WDIRHKIGMVFQNP-----DNQF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLMEPLII---NTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13650  95 VGATVEDDVAFgleNKGIPHEEMKERVNEALELVGM--QDFkEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLD 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK13650 173 PEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQVESTSTPRELFS 229

TauB

COG4525

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

22-230

2.01e-34

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

Pssm-ID: 443596 [Multi-domain] Cd Length: 262 Bit Score: 124.97 E-value: 2.01e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarRRPGTEmRSkvqMVFQNpy 101
Cdd:COG4525   15 GGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV----TGPGAD-RG---VVFQK-- 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 GSLNPRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:COG4525   85 DALLPWLNVLDNVAFGLRLR-GVPKAERRARAEELLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPF 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 739227338 182 SALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKG 230
Cdd:COG4525  163 GALDALTREQMQELLLDVWQRTGKGVFLITHSVEEALFLATRLVVMSPG 211

cbiO

PRK13641

energy-coupling factor transporter ATPase;

28-246

2.25e-34

energy-coupling factor transporter ATPase;

Pssm-ID: 237456 [Multi-domain] Cd Length: 287 Bit Score: 125.71 E-value: 2.25e-34

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDPASGgELKIDGQPVDIARRRPG-TEMRSKVQMVFQNPYGSLN 105
Cdd:PRK13641  21 KGLDNISFELEEGSFVALVGHTGSGKSTLMQhFNALLKPSSG-TITIAGYHITPETGNKNlKKLRKKVSLVFQFPEAQLF 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13641 100 ENTVLKDVEFGPK--NFGFSEDEAKEKALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLD 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 186 LSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:PRK13641 178 PEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237

ABC_cobalt_CbiO_domain2

cd03226

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

21-233

1.12e-33

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: 121.60 E-value: 1.12e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVDIARRRpgtemrSKVQMVFQN 99
Cdd:cd03226    7 FSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAgLIKESSG-SILLNGKPIKAKERR------KSIGYVMQD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PYgslnpRQKVGDVLMEPLIINTKiPASERRERAEAMLVKVGLGPEHfNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:cd03226   80 VD-----YQLFTDSVREELLLGLK-ELDAGNEQAETVLKDLDLYALK-ERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 180 PVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAV 233
Cdd:cd03226  153 PTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEFLAKVCDRVLLLANGAIV 205

ssuB

PRK11247

aliphatic sulfonates transport ATP-binding subunit; Provisional

8-231

4.82e-33

aliphatic sulfonates transport ATP-binding subunit; Provisional

Pssm-ID: 183055 [Multi-domain] Cd Length: 257 Bit Score: 121.32 E-value: 4.82e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYhvpgglfgGARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELkidgqpvdIARRRPGT 87
Cdd:PRK11247  16 NAVSKRY--------GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL--------LAGTAPLA 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  88 EMRSKVQMVFQNpyGSLNPRQKVGDvlmepliiNTKIPASER-RERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIAR 166
Cdd:PRK11247  78 EAREDTRLMFQD--ARLLPWKKVID--------NVGLGLKGQwRDAALQALAAVGLA-DRANEWPAALSGGQKQRVALAR 146

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:PRK11247 147 ALIHRPGLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEAVAMADRVLLIEEGK 211

PRK15093

peptide ABC transporter ATP-binding protein SapD;

27-258

8.22e-33

peptide ABC transporter ATP-binding protein SapD;

Pssm-ID: 185049 [Multi-domain] Cd Length: 330 Bit Score: 122.60 E-value: 8.22e-33

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDP----ASGGELKIDGqpVDIARRRPGTEMR---SKVQMVFQN 99
Cdd:PRK15093  20 VKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTKdnwrVTADRMRFDD--IDLLRLSPRERRKlvgHNVSMIFQE 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PYGSLNPRQKVGDVLMEpliintKIPASE-----------RRERAEAMLVKVGLgPEH---FNRYPHMFSGGQRQRIAIA 165
Cdd:PRK15093  98 PQSCLDPSERVGRQLMQ------NIPGWTykgrwwqrfgwRKRRAIELLHRVGI-KDHkdaMRSFPYELTEGECQKVMIA 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 166 RALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK15093 171 IALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSKELVTTP 250

                        250
                 ....*....|...
gi 739227338 246 KHPYTRQLFAATP 258
Cdd:PRK15093 251 HHPYTQALIRAIP 263

ugpC

PRK11650

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

27-245

2.55e-32

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

Pssm-ID: 236947 [Multi-domain] Cd Length: 356 Bit Score: 121.87 E-value: 2.55e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV--------DIArrrpgtemrskvqMVFQ 98
Cdd:PRK11650  17 TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVnelepadrDIA-------------MVFQ 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  99 NpYgSLNPRQKVGDVlMEPLIINTKIPASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK11650  84 N-Y-ALYPHMSVREN-MAYGLKIRGMPKAEIEERVAEAARILELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVFLFD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEaVEQ-GTREELFADP 245
Cdd:PRK11650 160 EPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDQVEAMTLADRVVVMNGGV-AEQiGTPVEVYEKP 226

PRK14247

phosphate ABC transporter ATP-binding protein; Provisional

27-252

4.01e-32

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172735 [Multi-domain] Cd Length: 250 Bit Score: 118.86 E-value: 4.01e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALID----PASGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQ--N 99
Cdd:PRK14247  16 VEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFnRLIElypeARVSGEVYLDGQDI---FKMDVIELRRRVQMVFQipN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PYGSLNPRQKVGDVLMEPLIINTKipaSERRERAEAMLVKVGLGPEHFNRY---PHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:PRK14247  93 PIPNLSIFENVALGLKLNRLVKSK---KELQERVRWALEKAQLWDEVKDRLdapAGKLSGGQQQRLCIARALAFQPEVLL 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 177 LDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ 252
Cdd:PRK14247 170 ADEPTANLDPENTAKIESLFLELKK--DMTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEK 243

met_CoM_red_A2

TIGR03269

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

26-244

4.16e-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: 123.76 E-value: 4.16e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   26 MVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGEL--KIDGQPVDIARRRPGTEMRSKVQMVFQNPYGS 103
Cdd:TIGR03269 296 VVKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVnvRVGDEWVDMTKPGPDGRGRAKRYIGILHQEYD 375

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  104 LNPRQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLGPEH----FNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:TIGR03269 376 LYPHRTVLDNLTEA--IGLELPDELARMKAVITLKMVGFDEEKaeeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDE 453

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338  180 PVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:TIGR03269 454 PTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGDPEEIVEE 518

ntrCD

TIGR01184

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

30-247

4.82e-32

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: 117.95 E-value: 4.82e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarrRPGTEMrskvQMVFQNpYgSLNPRQK 109
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQIT----EPGPDR----MVVFQN-Y-SLLPWLT 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  110 VGD-VLMEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSV 188
Cdd:TIGR01184  71 VREnIALAVDRVLPDLSKSERRAIVEEHIALVGLT-EAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALT 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  189 QAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGT-----------REELFADPKH 247
Cdd:TIGR01184 150 RGNLQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQilevpfprprdRLEVVEDPSY 219

ABC_drug_resistance_like

cd03264

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

28-236

8.78e-32

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: 116.91 E-value: 8.78e-32

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTlAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarRRPGTEMRSKVQMVFQNPygSLNPR 107
Cdd:cd03264   14 RALDGVSLTLGPGMY-GLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDV----LKQPQKLRRRIGYLPQEF--GVYPN 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLmEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:cd03264   87 FTVREFL-DYIAWLKGIPSKEVKARVDEVLELVNLG-DRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGLDPE 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 739227338 188 VQAQVLNLLRDLQEefELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03264  165 ERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211

YhaQ

COG4152

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

21-268

1.25e-31

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

Pssm-ID: 443322 [Multi-domain] Cd Length: 298 Bit Score: 118.67 E-value: 1.25e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRR-----PgtEMRskvqm 95
Cdd:COG4152   11 FGD---KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPEDRRrigylP--EER----- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  96 vfqnpygSLNPRQKVGDVL--------MepliintkiPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARA 167
Cdd:COG4152   81 -------GLYPKMKVGEQLvylarlkgL---------SKAEAKRRADEWLERLGLG-DRANKKVEELSKGNQQKVQLIAA 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 168 LMLNPALLVLDEPVSALDlSVQAQVL-NLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELfadpK 246
Cdd:COG4152  144 LLHDPELLILDEPFSGLD-PVNVELLkDVIRELAAK-GTTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVDEI----R 217

                        250       260
                 ....*....|....*....|..
gi 739227338 247 HPYTRQLFAATPITDVDAIRAR 268
Cdd:COG4152  218 RQFGRNTLRLEADGDAGWLRAL 239

ABC_FtsE

cd03292

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

26-231

1.34e-31

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: 116.35 E-value: 1.34e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  26 MVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNpyGSLN 105
Cdd:cd03292   13 GTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLRRKIGVVFQD--FRLL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGPEHfNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03292   91 PDRNVYENVAFALEV-TGVPPREIRKRVPAALELVGLSHKH-RALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLD 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 739227338 186 LSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03292  169 PDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGK 213

ABC_TM1139_LivF_branched

cd03224

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

27-244

2.20e-31

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: 115.99 E-value: 2.20e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNPygSLNP 106
Cdd:cd03224   13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGR--DITGLPPHERARAGIGYVPEGR--RIFP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGlgpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03224   89 ELTVEENLLLGAYARRRAKRKARLERVYELFPRLK---ERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAP 165

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 187 SVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:cd03224  166 KIVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGTAAELLAD 222

ModF

COG1119

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

30-244

2.60e-31

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: 116.72 E-value: 2.60e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGGELKIDGqpvdiaRRRPGT---EMRSK---VQMVFQNPYg 102
Cdd:COG1119   19 LDDISWTVKPGEHWAILGPNGAGKSTLLSLItGDLPPTYGNDVRLFG------ERRGGEdvwELRKRiglVSPALQLRF- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 slNPRQKVGDVLMEPL---IINTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:COG1119   92 --PRDETVLDVVLSGFfdsIGLYREPTDEQRERARELLELLGL--AHLaDRPFGTLSQGEQRRVLIARALVKDPELLILD 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLS-VVRYIaDDVMVISKGEAVEQGTREELFAD 244
Cdd:COG1119  168 EPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAAGPKEEVLTS 233

ABC_putative_ATPase

cd03269

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

27-236

2.67e-31

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: 115.46 E-value: 2.67e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIA-RRRPG--TEMRskvqmvfqnpygS 103
Cdd:cd03269   13 VTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAaRNRIGylPEER------------G 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 LNPRQKVGDVLMepLIINTK-IPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:cd03269   81 LYPKMKVIDQLV--YLAQLKgLKKEEARRRIDEWLERLELS-EYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEPFS 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03269  158 GLDPVNVELLKDVIRELARA-GKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210

CcmA

COG4133

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

30-213

2.77e-31

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: 115.27 E-value: 2.77e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRrpgtEMRSKVQMVFQNP--YGSLNPR 107
Cdd:COG4133   18 FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDARE----DYRRRLAYLGHADglKPELTVR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 qkvgdvlmEPLIINTKI-PASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:COG4133   94 --------ENLRFWAALyGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTALDA 164

                        170       180
                 ....*....|....*....|....*..
gi 739227338 187 SVQAQVLNLLRDLQEEfELTYVFVSHD 213
Cdd:COG4133  165 AGVALLAELIAAHLAR-GGAVLLTTHQ 190

PhnT

TIGR03258

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

23-259

3.15e-31

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: 118.94 E-value: 3.15e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG--GELKIDGQpvDIARRRPgteMRSKVQMVFQNP 100
Cdd:TIGR03258  16 GANTV--LDDLSLEIEAGELLALIGKSGCGKTTLLRAIAGFVKAAGltGRIAIADR--DLTHAPP---HKRGLALLFQNY 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  101 ygSLNPRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:TIGR03258  89 --ALFPHLKVEDNVAFGLRAQ-KMPKADIAERVADALKLVGLG-DAAAHLPAQLSGGMQQRIAIARAIAIEPDVLLLDEP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  181 VSALDLSVQAQVLNLLRDLQEEF-ELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATPI 259
Cdd:TIGR03258 165 LSALDANIRANMREEIAALHEELpELTILCVTHDQDDALTLADKAGIMKDGRLAAHGEPQALYDAPADGFAAEFLGAANI 244

PRK10584

putative ABC transporter ATP-binding protein YbbA; Provisional

23-213

3.30e-31

putative ABC transporter ATP-binding protein YbbA; Provisional

Pssm-ID: 182569 [Multi-domain] Cd Length: 228 Bit Score: 116.03 E-value: 3.30e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSK-VQMVFQN-- 99
Cdd:PRK10584  19 GEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKhVGFVFQSfm 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 --PygSLNPRQkvgdvlmepliiNTKIPA-----SER--RERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALML 170
Cdd:PRK10584  99 liP--TLNALE------------NVELPAllrgeSSRqsRNGAKALLEQLGLG-KRLDHLPAQLSGGEQQRVALARAFNG 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHD 213
Cdd:PRK10584 164 RPDVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHD 206

cbiO

PRK13647

cobalt transporter ATP-binding subunit; Provisional

28-277

4.58e-31

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 237457 [Multi-domain] Cd Length: 274 Bit Score: 116.76 E-value: 4.58e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPYGSLNPR 107
Cdd:PRK13647  19 KALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEK---WVRSKVGLVFQDPDDQVFSS 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPliINTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:PRK13647  96 TVWDDVAFGP--VNMGLDKDEVERRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPR 172

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 188 VQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELF-------ADPKHPYTRQLFAATPIT 260
Cdd:PRK13647 173 GQETLMEILDRLHNQGK-TVIVATHDVDLAAEWADQVIVLKEGRVLAEGDKSLLTdediveqAGLRLPLVAQIFEDLPEL 251

                        250
                 ....*....|....*...
gi 739227338 261 DVDAIRARV-ERRKAARQ 277
Cdd:PRK13647 252 GQSKLPLTVkEAVQIIRK 269

PhnL

COG4778

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...

20-230

5.26e-31

Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion transport and metabolism];

Pssm-ID: 443809 [Multi-domain] Cd Length: 229 Bit Score: 115.22 E-value: 5.26e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  20 LFGGARMVqALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKI--DGQPVDIARRRPgTEM----RSKV 93
Cdd:COG4778   18 LQGGKRLP-VLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhDGGWVDLAQASP-REIlalrRRTI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  94 QMVFQnpygSLN--PRQKVGDVLMEPLIINTkIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLN 171
Cdd:COG4778   96 GYVSQ----FLRviPRVSALDVVAEPLLERG-VDREEARARARELLARLNLPERLWDLPPATFSGGEQQRVNIARGFIAD 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 172 PALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKG 230
Cdd:COG4778  171 PPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228

3a01208

TIGR00958

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

27-245

5.46e-31

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

Pssm-ID: 273363 [Multi-domain] Cd Length: 711 Bit Score: 121.75 E-value: 5.46e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiaRRRPGTEMRSKVQMVFQNPygslnp 106
Cdd:TIGR00958 494 VPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPL---VQYDHHYLHRQVALVGQEP------ 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  107 rqkvgdVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHF-NRYPHMF-----------SGGQRQRIAIARALMLNPAL 174
Cdd:TIGR00958 565 ------VLFSGSVRENIAYGLTDTPDEEIMAAAKAANAHDFiMEFPNGYdtevgekgsqlSGGQKQRIAIARALVRKPRV 638

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338  175 LVLDEPVSALDlsvqAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFADP 245
Cdd:TIGR00958 639 LILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTVER-ADQILVLKKGSVVEMGTHKQLMEDQ 704

lolD

PRK11629

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

30-218

8.63e-31

lipoprotein-releasing ABC transporter ATP-binding protein LolD;

Pssm-ID: 183244 [Multi-domain] Cd Length: 233 Bit Score: 114.91 E-value: 8.63e-31

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKvQMVFQNPYGSLNPR-Q 108
Cdd:PRK11629  25 LHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQ-KLGFIYQFHHLLPDfT 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMePLIINTKIPAsERRERAEAMLVKVGLGPEHFNRyPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSV 188
Cdd:PRK11629 104 ALENVAM-PLLIGKKKPA-EINSRALEMLAAVGLEHRANHR-PSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180

                        170       180       190
                 ....*....|....*....|....*....|
gi 739227338 189 QAQVLNLLRDLQEEFELTYVFVSHDLSVVR 218
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHDLQLAK 210

PRK14267

phosphate ABC transporter ATP-binding protein; Provisional

11-252

1.34e-30

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184596 [Multi-domain] Cd Length: 253 Bit Score: 114.94 E-value: 1.34e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  11 TRDYHVpgglFGGARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLAR----IIALIDPAS-GGELKIDGQPVDIARRRP 85
Cdd:PRK14267   7 TVNLRV----YYGSNHV--IKGVDLKIPQNGVFALMGPSGCGKSTLLRtfnrLLELNEEARvEGEVRLFGRNIYSPDVDP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  86 gTEMRSKVQMVFQ--NPYGSLNPRQKVGDVLMEPLIINTKipaSERRERAEAMLVKVGLGPEHFNR---YPHMFSGGQRQ 160
Cdd:PRK14267  81 -IEVRREVGMVFQypNPFPHLTIYDNVAIGVKLNGLVKSK---KELDERVEWALKKAALWDEVKDRlndYPSNLSGGQRQ 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 161 RIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFelTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:PRK14267 157 RLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRK 234

                        250
                 ....*....|..
gi 739227338 241 LFADPKHPYTRQ 252
Cdd:PRK14267 235 VFENPEHELTEK 246

potG

PRK11607

putrescine ABC transporter ATP-binding subunit PotG;

29-273

2.20e-30

putrescine ABC transporter ATP-binding subunit PotG;

Pssm-ID: 183226 [Multi-domain] Cd Length: 377 Bit Score: 117.24 E-value: 2.20e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPgteMRSKVQMVFQNpYgSLNPRQ 108
Cdd:PRK11607  34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGV--DLSHVPP---YQRPINMMFQS-Y-ALFPHM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEPLIiNTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSV 188
Cdd:PRK11607 107 TVEQNIAFGLK-QDKLPKAEIASRVNEMLGLVHM-QEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKL 184

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 189 QAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFadpKHPYTRqlFAATPITDVDAIRAR 268
Cdd:PRK11607 185 RDRMQLEVVDILERVGVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIY---EHPTTR--YSAEFIGSVNVFEGV 259


                 ....*
gi 739227338 269 VERRK 273
Cdd:PRK11607 260 LKERQ 264

tauB

PRK11248

taurine ABC transporter ATP-binding subunit;

29-230

2.51e-30

taurine ABC transporter ATP-binding subunit;

Pssm-ID: 183056 [Multi-domain] Cd Length: 255 Bit Score: 114.41 E-value: 2.51e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarrRPGTEMrskvQMVFQNPygSLNPRQ 108
Cdd:PRK11248  16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE----GPGAER----GVVFQNE--GLLPWR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEPLIInTKIPASERRERAEAMLVKVGL-GPEHfnRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:PRK11248  86 NVQDNVAFGLQL-AGVEKMQRLEIAHQMLKKVGLeGAEK--RYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAF 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 739227338 188 VQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKG 230
Cdd:PRK11248 163 TREQMQTLLLKLWQETGKQVLLITHDIEEAVFMATELVLLSPG 205

cbiO

PRK13642

energy-coupling factor transporter ATPase;

27-243

3.55e-30

energy-coupling factor transporter ATPase;

Pssm-ID: 184202 [Multi-domain] Cd Length: 277 Bit Score: 114.42 E-value: 3.55e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRrpgTEMRSKVQMVFQNPygslnP 106
Cdd:PRK13642  20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENV---WNLRRKIGMVFQNP-----D 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLII---NTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSA 183
Cdd:PRK13642  92 NQFVGATVEDDVAFgmeNQGIPREEMIKRVDEALLAVNM-LDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSM 170

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 184 LDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK13642 171 LDPTGRQEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELFA 229

ABCC_MsbA

cd03251

ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...

29-244

4.09e-30

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: 113.09 E-value: 4.09e-30

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGqpVDIaRRRPGTEMRSKVQMVFQNPYgslnpr 107
Cdd:cd03251   17 VLRDISLDIPAGETVALVGPSGSGKSTLVNLIPrFYDVDSG-RILIDG--HDV-RDYTLASLRRQIGLVSQDVF------ 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 qKVGDVLMEPLIINTKIPASERRERAeamlVKVGLGPEHFNRYPHMF-----------SGGQRQRIAIARALMLNPALLV 176
Cdd:cd03251   87 -LFNDTVAENIAYGRPGATREEVEEA----ARAANAHEFIMELPEGYdtvigergvklSGGQRQRIAIARALLKDPPILI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 177 LDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFAD 244
Cdd:cd03251  162 LDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIEN-ADRIVVLEDGKIVERGTHEELLAQ 226

PRK14246

phosphate ABC transporter ATP-binding protein; Provisional

30-252

1.26e-29

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172734 [Multi-domain] Cd Length: 257 Bit Score: 112.45 E-value: 1.26e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIAR---RRPGTEMRSKVQMVFQNPygSLNP 106
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKdifQIDAIKLRKEVGMVFQQP--NPFP 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRY---PHMFSGGQRQRIAIARALMLNPALLVLDEPVSA 183
Cdd:PRK14246 104 HLSIYDNIAYPLKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLnspASQLSGGQQQRLTIARALALKPKVLLMDEPTSM 183

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 184 LDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQ 252
Cdd:PRK14246 184 IDIVNSQAIEKLITELKN--EIAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKNELTEK 250

PRK10535

macrolide ABC transporter ATP-binding protein/permease MacB;

1-255

1.31e-29

macrolide ABC transporter ATP-binding protein/permease MacB;

Pssm-ID: 182528 [Multi-domain] Cd Length: 648 Bit Score: 117.52 E-value: 1.31e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHvpgglfGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-- 78
Cdd:PRK10535   1 MTALLELKDIRRSYP------SGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVat 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  79 ----DIARRRpgtemRSKVQMVFQNPY--GSLNPRQKVgdvlmEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPH 152
Cdd:PRK10535  75 ldadALAQLR-----REHFGFIFQRYHllSHLTAAQNV-----EVPAVYAGLERKQRLLRAQELLQRLGLE-DRVEYQPS 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 153 MFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYiADDVMVISKGEA 232
Cdd:PRK10535 144 QLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGH-TVIIVTHDPQVAAQ-AERVIEIRDGEI 221

                        250       260       270
                 ....*....|....*....|....*....|.
gi 739227338 233 V--------EQGTREELFADPKHPYTRQLFA 255
Cdd:PRK10535 222 VrnppaqekVNVAGGTEPVVNTASGWRQFVS 252

PRK11176

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

29-243

1.50e-29

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

Pssm-ID: 183016 [Multi-domain] Cd Length: 582 Bit Score: 117.04 E-value: 1.50e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIaRRRPGTEMRSKVQMVFQNPYgslnprq 108
Cdd:PRK11176 358 ALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDG--HDL-RDYTLASLRNQVALVSQNVH------- 427

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 kvgdvLMEPLIINTKIPASER---RERAEAMlVKVGLGPEHFNRYPH-----------MFSGGQRQRIAIARALMLNPAL 174
Cdd:PRK11176 428 -----LFNDTIANNIAYARTEqysREQIEEA-ARMAYAMDFINKMDNgldtvigengvLLSGGQRQRIAIARALLRDSPI 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 175 LVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK11176 502 LILDEATSALDTESERAIQAALDELQK--NRTSLVIAHRLSTIEK-ADEILVVEDGEIVERGTHAELLA 567

ABCC_Protease_Secretion

cd03246

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...

30-232

1.88e-29

ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of the protease secretion system PrtD, a 60-kDa integral membrane protein sharing 37% identity with HlyB, the ABC component of the alpha-hemolysin secretion pathway, in the C-terminal domain. They export degradative enzymes by using a type I protein secretion system and lack an N-terminal signal peptide, but contain a C-terminal secretion signal. The Type I secretion apparatus is made up of three components, an ABC transporter, a membrane fusion protein (MFP), and an outer membrane protein (OMP). For the HlyA transporter complex, HlyB (ABC transporter) and HlyD (MFP) reside in the inner membrane of E. coli. The OMP component is TolC, which is thought to interact with the MFP to form a continuous channel across the periplasm from the cytoplasm to the exterior. HlyB belongs to the family of ABC transporters, which are ubiquitous, ATP-dependent transmembrane pumps or channels. The spectrum of transport substrates ranges from inorganic ions, nutrients such as amino acids, sugars, or peptides, hydrophobic drugs, to large polypeptides, such as HlyA.

Pssm-ID: 213213 [Multi-domain] Cd Length: 173 Bit Score: 109.61 E-value: 1.88e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarrrpgtemrskvqmvfqNPYGSLNPRQK 109
Cdd:cd03246   18 LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADI--------------------SQWDPNELGDH 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLMEPLIINTKIpaserrerAEAMLvkvglgpehfnryphmfSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQ 189
Cdd:cd03246   78 VGYLPQDDELFSGSI--------AENIL-----------------SGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGE 132

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 739227338 190 AQVLNLLRDLQEEfELTYVFVSHDLSVVRyIADDVMVISKGEA 232
Cdd:cd03246  133 RALNQAIAALKAA-GATRIVIAHRPETLA-SADRILVLEDGRV 173

ABC_BcrA_bacitracin_resist

cd03268

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

28-236

3.94e-29

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

Pssm-ID: 213235 [Multi-domain] Cd Length: 208 Bit Score: 109.61 E-value: 3.94e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarrrPGTEMRSKVQMVFQNP--YGSLN 105
Cdd:cd03268   14 RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQ-----KNIEALRRIGALIEAPgfYPNLT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRqkvgdvlmEPLIINTKIPASeRRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03268   89 AR--------ENLRLLARLLGI-RKKRIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDEPTNGLD 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739227338 186 LSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03268  159 PDGIKELRELILSLRDQ-GITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208

ABCC_Hemolysin

cd03252

ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...

29-243

8.18e-29

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: 109.88 E-value: 8.18e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPgTEMRSKVQMVFQ-NPYGSLNPR 107
Cdd:cd03252   17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDG--HDLALADP-AWLRRQVGVVLQeNVLFNRSIR 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGdvLMEPLIINTKIPASERRERAEAMLVKVGLGpehfnrYPHM-------FSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03252   94 DNIA--LADPGMSMERVIEAAKLAGAHDFISELPEG------YDTIvgeqgagLSGGQRQRIAIARALIHNPRILIFDEA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:cd03252  166 TSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGSHDELLA 225

cbiO

PRK13644

energy-coupling factor transporter ATPase;

29-245

1.12e-28

energy-coupling factor transporter ATPase;

Pssm-ID: 106587 [Multi-domain] Cd Length: 274 Bit Score: 110.46 E-value: 1.12e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLA-RIIALIDPASGgelKIDGQPVDIARRRPGTEMRSKVQMVFQNPygslnPR 107
Cdd:PRK13644  17 ALENINLVIKKGEYIGIIGKNGSGKSTLAlHLNGLLRPQKG---KVLVSGIDTGDFSKLQGIRKLVGIVFQNP-----ET 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLII---NTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:PRK13644  89 QFVGRTVEEDLAFgpeNLCLPPIEIRKRVDRALAEIGLE-KYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSML 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 185 DLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVrYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK13644 168 DPDSGIAVLERIKKLHEKGK-TIVYITHNLEEL-HDADRIIVMDRGKIVLEGEPENVLSDV 226

PRK14271

phosphate ABC transporter ATP-binding protein; Provisional

44-267

2.90e-28

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 172759 [Multi-domain] Cd Length: 276 Bit Score: 109.42 E-value: 2.90e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  44 AIVGESGSGKSTLARIIALI-DPASG----GELKIDGQpvDIARRRPGTEMRSKVQMVFQNPygslNP-RQKVGDVLMEP 117
Cdd:PRK14271  51 SLMGPTGSGKTTFLRTLNRMnDKVSGyrysGDVLLGGR--SIFNYRDVLEFRRRVGMLFQRP----NPfPMSIMDNVLAG 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 118 LIINTKIPASERRERAEAMLVKVGLG---PEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLN 194
Cdd:PRK14271 125 VRAHKLVPRKEFRGVAQARLTEVGLWdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEKIEE 204

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 195 LLRDLQEefELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAATPITDVDAIRA 267
Cdd:PRK14271 205 FIRSLAD--RLTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLSGDVKDAKRG 275

MsbA_rel

TIGR02204

ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...

29-243

5.04e-28

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

Pssm-ID: 131259 [Multi-domain] Cd Length: 576 Bit Score: 112.87 E-value: 5.04e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVDIARRRpgtEMRSKVQMVFQNP---YGSL 104
Cdd:TIGR02204 355 ALDGLNLTVRPGETVALVGPSGAGKSTLFQLLLrFYDPQSG-RILLDGVDLRQLDPA---ELRARMALVPQDPvlfAASV 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  105 --NPRQKVGDVLMEPLIintkipASERRERAEAMLVKVglgPEHFNRY----PHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:TIGR02204 431 meNIRYGRPDATDEEVE------AAARAAHAHEFISAL---PEGYDTYlgerGVTLSGGQRQRIAIARAILKDAPILLLD 501

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338  179 EPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR02204 502 EATSALDAESEQLVQQALETLMK--GRTTLIIAHRLATVLK-ADRIVVMDQGRIVAQGTHAELIA 563

NHLM_micro_ABC1

TIGR03796

NHLM bacteriocin system ABC transporter, peptidase/ATP-binding protein; This protein describes ...

21-251

5.14e-28

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

Pssm-ID: 274788 [Multi-domain] Cd Length: 710 Bit Score: 113.11 E-value: 5.14e-28

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   21 FGGARMVQAL-KGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPaSGGELKIDGQPV-DIARRRpgteMRSKVQMVF 97
Cdd:TIGR03796 485 FGYSPLEPPLiENFSLTLQPGQRVALVGGSGSGKSTIAKLVAgLYQP-WSGEILFDGIPReEIPREV----LANSVAMVD 559

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   98 QNPY---GSlnprqkVGDVLMeplIINTKIPASERRERA------EAMLVKVGlgpehfnRYPHM-------FSGGQRQR 161
Cdd:TIGR03796 560 QDIFlfeGT------VRDNLT---LWDPTIPDADLVRACkdaaihDVITSRPG-------GYDAElaegganLSGGQRQR 623

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  162 IAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRdlqeEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREEL 241
Cdd:TIGR03796 624 LEIARALVRNPSILILDEATSALDPETEKIIDDNLR----RRGCTCIIVAHRLSTIRD-CDEIIVLERGKVVQRGTHEEL 698

                         250
                  ....*....|
gi 739227338  242 FADPKhPYTR 251
Cdd:TIGR03796 699 WAVGG-AYAR 707

SufC

COG0396

Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...

30-239

6.81e-28

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

Pssm-ID: 440165 [Multi-domain] Cd Length: 245 Bit Score: 107.46 E-value: 6.81e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALID--PASGGELKIDGQpvDIarrrpgTEM----RSK--VQMVFQNPy 101
Cdd:COG0396   16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGHPkyEVTSGSILLDGE--DI------LELspdeRARagIFLAFQYP- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 gslnPR---QKVGDVLMEPL--IINTKIPASERRERAEAMLVKVGLGPEHFNRYPHM-FSGGQRQRIAIARALMLNPALL 175
Cdd:COG0396   87 ----VEipgVSVSNFLRTALnaRRGEELSAREFLKLLKEKMKELGLDEDFLDRYVNEgFSGGEKKRNEILQMLLLEPKLA 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 176 VLDEPVSALD---LSVQAQVLNLLRDlqEEFelTYVFVSHDLSVVRYI-ADDVMVISKGEAVEQGTRE 239
Cdd:COG0396  163 ILDETDSGLDidaLRIVAEGVNKLRS--PDR--GILIITHYQRILDYIkPDFVHVLVDGRIVKSGGKE 226

PRK13657

glucan ABC transporter ATP-binding protein/ permease;

21-243

8.53e-28

glucan ABC transporter ATP-binding protein/ permease;

Pssm-ID: 184214 [Multi-domain] Cd Length: 588 Bit Score: 111.98 E-value: 8.53e-28

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARmvQALKGIDFAVERGKTLAIVGESGSGKSTLariIALI----DPASGgELKIDGQPV-DIARRrpgtemrskvqm 95
Cdd:PRK13657 344 YDNSR--QGVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLqrvfDPQSG-RILIDGTDIrTVTRA------------ 405

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  96 vfqnpygSLnpRQKVGDVLMEPLIINTKIP-----------------ASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQ 158
Cdd:PRK13657 406 -------SL--RRNIAVVFQDAGLFNRSIEdnirvgrpdatdeemraAAERAQAHDFIERKPDGYDTVVGERGRQLSGGE 476

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 159 RQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVfVSHDLSVVRYiADDVMVISKGEAVEQGTR 238
Cdd:PRK13657 477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMKG-RTTFI-IAHRLSTVRN-ADRILVFDNGRVVESGSF 553


                 ....*
gi 739227338 239 EELFA 243
Cdd:PRK13657 554 DELVA 558

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

1-241

1.39e-27

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 110.89 E-value: 1.39e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDyhvpgglFGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:COG3845    2 MPPALELRGITKR-------FGG---VVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRI 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 arRRPGTEMRSKVQMVFQNPygSLNPRQKVGD--VL-MEPLiINTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGG 157
Cdd:COG3845   72 --RSPRDAIALGIGMVHQHF--MLVPNLTVAEniVLgLEPT-KGGRLDRKAARARIRELSERYGL-DVDPDAKVEDLSVG 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 158 QRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG- 236
Cdd:COG3845  146 EQQRVEILKALYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVd 224


                 ....*....
gi 739227338 237 ----TREEL 241
Cdd:COG3845  225 taetSEEEL 233

ABC_subfamily_A

cd03263

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

23-241

1.52e-27

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: 106.05 E-value: 1.52e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRpgTEMRSKVQMVFQNP-- 100
Cdd:cd03263   11 KKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGY--SIRTDR--KAARQSLGYCPQFDal 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YGSLNPRQKVgdVLMEPLiinTKIPASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03263   87 FDELTVREHL--RFYARL---KGLPKSEIKEEVELLLRVLGLTD-KANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:cd03263  161 TSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIGSPQEL 219

MsbA_lipidA

TIGR02203

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...

23-243

2.35e-27

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: 110.58 E-value: 2.35e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQnpyg 102
Cdd:TIGR02203 341 PGRDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLADYTLA---SLRRQVALVSQ---- 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  103 slnprqkvgDVLMEPLIINTKIPASER----RERAEAMLVKVGLgPEHFNRYPHMF-----------SGGQRQRIAIARA 167
Cdd:TIGR02203 414 ---------DVVLFNDTIANNIAYGRTeqadRAEIERALAAAYA-QDFVDKLPLGLdtpigengvllSGGQRQRLAIARA 483

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338  168 LMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR02203 484 LLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERGTHNELLA 556

urea_trans_UrtE

TIGR03410

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

28-241

3.17e-27

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 274567 [Multi-domain] Cd Length: 230 Bit Score: 105.30 E-value: 3.17e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKV------QMVFqnpy 101
Cdd:TIGR03410  14 HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGE--DITKLPPHERARAGIayvpqgREIF---- 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  102 gslnPRQKVGDVLMepliinTKIPASERRERAeamlvkvgLGPEHFNRYPHMF----------SGGQRQRIAIARALMLN 171
Cdd:TIGR03410  88 ----PRLTVEENLL------TGLAALPRRSRK--------IPDEIYELFPVLKemlgrrggdlSGGQQQQLAIARALVTR 149

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  172 PALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:TIGR03410 150 PKLLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASGAGDEL 219

hmuV

PRK13548

hemin importer ATP-binding subunit; Provisional

30-240

3.70e-27

hemin importer ATP-binding subunit; Provisional

Pssm-ID: 237422 [Multi-domain] Cd Length: 258 Bit Score: 106.01 E-value: 3.70e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV------DIARRRpgTEMRSKVQMVFqnPYgs 103
Cdd:PRK13548  18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLadwspaELARRR--AVLPQHSSLSF--PF-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 lnprqKVGDVLMEPLIINTKIPASERRERAEAMLvKVGLgpEHF-NRYPHMFSGGQRQRIAIARALM------LNPALLV 176
Cdd:PRK13548  92 -----TVEEVVAMGRAPHGLSRAEDDALVAAALA-QVDL--AHLaGRDYPQLSGGEQQRVQLARVLAqlwepdGPPRWLL 163

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 177 LDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSV-VRYiADDVMVISKGEAVEQGTREE 240
Cdd:PRK13548 164 LDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLaARY-ADRIVLLHQGRLVADGTPAE 227

cbiO

PRK13643

energy-coupling factor transporter ATPase;

28-244

4.24e-27

energy-coupling factor transporter ATPase;

Pssm-ID: 184203 [Multi-domain] Cd Length: 288 Bit Score: 106.74 E-value: 4.24e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNPYGSLNP 106
Cdd:PRK13643  20 RALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLnGLLQPTEGKVTVGDIVVSSTSKQKEIKPVRKKVGVVFQFPESQLFE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:PRK13643 100 ETVLKDVAFGPQ--NFGIPKEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 187 SVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13643 178 KARIEMMQLFESIHQSGQ-TVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234

ATM1

COG5265

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...

28-243

5.19e-27

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];

Pssm-ID: 444078 [Multi-domain] Cd Length: 605 Bit Score: 109.91 E-value: 5.19e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPaSGGELKIDGQpvDIARrrpgtemrskvqmVFQnpyGSLnp 106
Cdd:COG5265  372 PILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFrFYDV-TSGRILIDGQ--DIRD-------------VTQ---ASL-- 430

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINTKI--------P-ASERRERAEAMLVKVglgpEHF-NRYPHMF-----------SGGQRQRIAIA 165
Cdd:COG5265  431 RAAIGIVPQDTVLFNDTIayniaygrPdASEEEVEAAARAAQI----HDFiESLPDGYdtrvgerglklSGGEKQRVAIA 506

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 166 RALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:COG5265  507 RTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEAGRIVERGTHAELLA 581

ABCC_TAP

cd03248

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...

27-231

6.02e-27

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: 104.48 E-value: 6.02e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPY---GS 103
Cdd:cd03248   27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHK---YLHSKVSLVGQEPVlfaRS 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 L--NPRQKVGDVLMEpliintKIPASERRERAEAMLVKVGLGP-EHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03248  104 LqdNIAYGLQSCSFE------CVKEAAQKAHAHSFISELASGYdTEVGEKGSQLSGGQKQRVAIARALIRNPQVLILDEA 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGE 231
Cdd:cd03248  178 TSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTVER-ADQILVLDGGR 225

CP_lyasePhnL

TIGR02324

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL protein of C-P ...

23-225

6.61e-27

phosphonate C-P lyase system protein PhnL; Members of this family are the PhnL 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 C-P lysase complex. This protein (PhnL) and the adjacent-encoded PhnK (TIGR02323) resemble transporter ATP-binding proteins but are suggested, based on mutatgenesis studies, to be part of this C-P lyase complex rather than part of a transporter per se.

Pssm-ID: 131377 [Multi-domain] Cd Length: 224 Bit Score: 104.40 E-value: 6.61e-27

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGGEL-KIDGQPVDIARRRPgTEM----RSKVQMV 96
Cdd:TIGR02324  17 GGVRLPVLKNVSLTVNAGECVALSGPSGAGKSTLLKSLyANYLPDSGRILvRHEGAWVDLAQASP-REVlevrRKTIGYV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   97 FQnpYGSLNPRQKVGDVLMEPLIINtKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:TIGR02324  96 SQ--FLRVIPRVSALEVVAEPLLER-GVPREAARARARELLARLNIPERLWHLPPATFSGGEQQRVNIARGFIADYPILL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 739227338  177 LDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVM 225
Cdd:TIGR02324 173 LDEPTASLDAANRQVVVELIAEAKAR-GAALIGIFHDEEVRELVADRVM 220

ABCC_cytochrome_bd

cd03247

ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...

28-236

7.48e-27

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: 102.78 E-value: 7.48e-27

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIArrrpGTEMRSKVQMVFQNPY---GSL 104
Cdd:cd03247   16 QVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDL----EKALSSLISVLNQRPYlfdTTL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 npRQKVGdvlmepliintkipaseRReraeamlvkvglgpehfnryphmFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:cd03247   92 --RNNLG-----------------RR-----------------------FSGGERQRLALARILLQDAPIVLLDEPTVGL 129

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739227338 185 DLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQG 236
Cdd:cd03247  130 DPITERQLLSLIFEVLK--DKTLIWITHHLTGIEH-MDKILFLENGKIIMQG 178

PRK11831

phospholipid ABC transporter ATP-binding protein MlaF;

33-252

1.52e-26

phospholipid ABC transporter ATP-binding protein MlaF;

Pssm-ID: 236997 [Multi-domain] Cd Length: 269 Bit Score: 104.46 E-value: 1.52e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNpyGSLNPRQKVGD 112
Cdd:PRK11831  26 ISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQS--GALFTDMNVFD 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 113 VLMEPLIINTKIPASERRERAEAMLVKVGL-GPEHFnrYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQ 191
Cdd:PRK11831 104 NVAYPLREHTQLPAPLLHSTVMMKLEAVGLrGAAKL--MPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGV 181

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 192 VLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKhPYTRQ 252
Cdd:PRK11831 182 LVKLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHGSAQALQANPD-PRVRQ 241

cbiO

PRK13645

energy-coupling factor transporter ATPase;

28-244

2.01e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184204 [Multi-domain] Cd Length: 289 Bit Score: 104.70 E-value: 2.01e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASG----GELKIdgqPVDIARRRPGTEMRSKVQMVFQNPYG 102
Cdd:PRK13645  25 KALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTnGLIISETGqtivGDYAI---PANLKKIKEVKRLRKEIGLVFQFPEY 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK13645 102 QLFQETIEKDIAFGP--VNLGENKQEAYKKVPELLKLVQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTG 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13645 180 GLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFSN 241

LivF

COG0410

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

27-246

2.09e-26

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: 103.14 E-value: 2.09e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV------DIAR------------------ 82
Cdd:COG0410   16 IHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDItglpphRIARlgigyvpegrrifpsltv 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  83 ----------RRPGTEMRSKVQMVFQnpygsLNPRQKvgdvlmepliintkipasERRERAEAMLvkvglgpehfnryph 152
Cdd:COG0410   96 eenlllgayaRRDRAEVRADLERVYE-----LFPRLK------------------ERRRQRAGTL--------------- 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 153 mfSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEA 232
Cdd:COG0410  138 --SGGEQQMLAIGRALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRI 214

                        250
                 ....*....|....
gi 739227338 233 VEQGTREELFADPK 246
Cdd:COG0410  215 VLEGTAAELLADPE 228

cbiO

PRK13649

energy-coupling factor transporter ATPase;

29-244

2.92e-26

energy-coupling factor transporter ATPase;

Pssm-ID: 184208 [Multi-domain] Cd Length: 280 Bit Score: 104.06 E-value: 2.92e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-DIARRRPGTEMRSKVQMVFQNPYGSLNPR 107
Cdd:PRK13649  22 ALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItSTSKNKDIKQIRKKVGLVFQFPESQLFEE 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLMEPLiiNTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:PRK13649 102 TVLKDVAFGPQ--NFGVSQEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPK 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 188 VQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13649 180 GRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQD 235

type_I_sec_HlyB

TIGR01846

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...

30-243

1.03e-25

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

Pssm-ID: 273831 [Multi-domain] Cd Length: 694 Bit Score: 106.37 E-value: 1.03e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPGTEmrskvqmvfqnpygslnpRQK 109
Cdd:TIGR01846 473 LSNLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDG--VDLAIADPAWL------------------RRQ 532

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  110 VGDVLMEPLIINTKI---------PASERRERAEAMLVkvglGPEHF-NRYPHMF-----------SGGQRQRIAIARAL 168
Cdd:TIGR01846 533 MGVVLQENVLFSRSIrdnialcnpGAPFEHVIHAAKLA----GAHDFiSELPQGYntevgekganlSGGQRQRIAIARAL 608

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338  169 MLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR01846 609 VGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRA-CDRIIVLEKGQIAESGRHEELLA 680

PRK10908

cell division ATP-binding protein FtsE;

15-230

1.08e-25

cell division ATP-binding protein FtsE;

Pssm-ID: 182829 [Multi-domain] Cd Length: 222 Bit Score: 101.10 E-value: 1.08e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  15 HVPGGLFGGArmvQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQ 94
Cdd:PRK10908   6 HVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFLRRQIG 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  95 MVFQNPYGSLNprQKVGDVLMEPLIInTKIPASERRERAEAMLVKVGLGPEHFNrYPHMFSGGQRQRIAIARALMLNPAL 174
Cdd:PRK10908  83 MIFQDHHLLMD--RTVYDNVAIPLII-AGASGDDIRRRVSAALDKVGLLDKAKN-FPIQLSGGEQQRVGIARAVVNKPAV 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 175 LVLDEPVSALDLSVQAQVLNLLrdlqEEFE---LTYVFVSHDLSVVRYIADDVMVISKG 230
Cdd:PRK10908 159 LLADEPTGNLDDALSEGILRLF----EEFNrvgVTVLMATHDIGLISRRSYRMLTLSDG 213

ArpD

COG4618

ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...

22-243

1.20e-25

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: 105.60 E-value: 1.20e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRR----------------P 85
Cdd:COG4618  342 GSKRPI--LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREelgrhigylpqdvelfD 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  86 GTemrskvqmVFQN--PYGSLNPRqkvgdvlmepliintKIPASERRERAEAMLVK--------VGLGPehfnrypHMFS 155
Cdd:COG4618  420 GT--------IAENiaRFGDADPE---------------KVVAAAKLAGVHEMILRlpdgydtrIGEGG-------ARLS 469

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 156 GGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRyIADDVMVISKGEAVEQ 235
Cdd:COG4618  470 GGQRQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKAR-GATVVVITHRPSLLA-AVDKLLVLRDGRVQAF 547


                 ....*...
gi 739227338 236 GTREELFA 243
Cdd:COG4618  548 GPRDEVLA 555

type_I_sec_LssB

TIGR03375

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

29-243

2.17e-25

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: 105.33 E-value: 2.17e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPgTEMRSKVQMVFQNP---YGSLn 105
Cdd:TIGR03375 480 ALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDG--VDIRQIDP-ADLRRNIGYVPQDPrlfYGTL- 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  106 pRQKVgdVLMEPLiintkipASERRERAEAMLVKVG-LGPEHFNRYPHM-------FSGGQRQRIAIARALMLNPALLVL 177
Cdd:TIGR03375 556 -RDNI--ALGAPY-------ADDEEILRAAELAGVTeFVRRHPDGLDMQigergrsLSGGQRQAVALARALLRDPPILLL 625

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338  178 DEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR03375 626 DEPTSAMDNRSEERFKDRLKRWLA--GKTLVLVTHRTSLLD-LVDRIIVMDNGRIVADGPKDQVLE 688

ABC_Carb_Monos_II

cd03215

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

29-231

4.69e-25

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: 98.27 E-value: 4.69e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPvdIARRRPGTEMRSKVQMVfqnpygslnP-- 106
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKP--VTRRSPRDAIRAGIAYV---------Ped 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIINTKIPaserreraeamlvkvglgpehfnrypHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03215   84 RKREGLVLDLSVAENIALS--------------------------SLLSGGNQQKVVLARWLARDPRVLILDEPTRGVDV 137

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 739227338 187 SVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03215  138 GAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGR 181

YddA

COG4178

ABC-type uncharacterized transport system, permease and ATPase components [General function ...

30-219

9.10e-25

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

Pssm-ID: 443337 [Multi-domain] Cd Length: 571 Bit Score: 103.35 E-value: 9.10e-25

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELkidgqpvdiarRRPGTEmrskvQMVF--QNPY---GSL 104
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRI-----------ARPAGA-----RVLFlpQRPYlplGTL 442

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 npRqkvgDVLMEPliintKIPASERRERAEAMLVKVGLGpeHF-------NRYPHMFSGGQRQRIAIARALMLNPALLVL 177
Cdd:COG4178  443 --R----EALLYP-----ATAEAFSDAELREALEAVGLG--HLaerldeeADWDQVLSLGEQQRLAFARLLLHKPDWLFL 509

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 739227338 178 DEPVSALDLSVQAQVLNLLRdlQEEFELTYVFVSHDLSVVRY 219
Cdd:COG4178  510 DEATSALDEENEAALYQLLR--EELPGTTVISVGHRSTLAAF 549

PRK13549

xylose transporter ATP-binding subunit; Provisional

1-238

5.87e-24

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 100.77 E-value: 5.87e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDyhvpgglFGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPAS--GGELKIDGQPV 78
Cdd:PRK13549   2 MEYLLEMKNITKT-------FGG---VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGVYPHGtyEGEIIFEGEEL 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  79 dIARRRPGTEmRSKVQMVFQNPygSLNPRQKVGD--VLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHmFSG 156
Cdd:PRK13549  72 -QASNIRDTE-RAGIAIIHQEL--ALVKELSVLEniFLGNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGN-LGL 146

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 157 GQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVeqG 236
Cdd:PRK13549 147 GQQQLVEIAKALNKQARLLILDEPTASLTESETAVLLDIIRDLKAH-GIACIYISHKLNEVKAISDTICVIRDGRHI--G 223


                 ..
gi 739227338 237 TR 238
Cdd:PRK13549 224 TR 225

ABCC_MRP_domain2

cd03244

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...

29-237

7.22e-24

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

Pssm-ID: 213211 [Multi-domain] Cd Length: 221 Bit Score: 96.02 E-value: 7.22e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLA----RIIalidPASGGELKIDGqpVDIARRRPgTEMRSKVQMVFQNPY--- 101
Cdd:cd03244   19 VLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLV----ELSSGSILIDG--VDISKIGL-HDLRSRISIIPQDPVlfs 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 GS----LNPRQKVGDvlmepliintkipasERRERAeamLVKVGLGpEHFNRYPHM-----------FSGGQRQRIAIAR 166
Cdd:cd03244   92 GTirsnLDPFGEYSD---------------EELWQA---LERVGLK-EFVESLPGGldtvveeggenLSVGQRQLLCLAR 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRdlqEEF-ELTYVFVSHDL-SVVRYiaDDVMVISKGEAVEQGT 237
Cdd:cd03244  153 ALLRKSKILVLDEATASVDPETDALIQKTIR---EAFkDCTVLTIAHRLdTIIDS--DRILVLDKGRVVEFDS 220

cbiO

PRK13638

energy-coupling factor ABC transporter ATP-binding protein;

28-243

8.23e-24

energy-coupling factor ABC transporter ATP-binding protein;

Pssm-ID: 184198 [Multi-domain] Cd Length: 271 Bit Score: 97.39 E-value: 8.23e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTL-ARIIALIDPASGGELkIDGQPVDIARRRPgTEMRSKVQMVFQNPYGSLNP 106
Cdd:PRK13638  15 PVLKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLLRPQKGAVL-WQGKPLDYSKRGL-LALRQQVATVFQDPEQQIFY 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEplIINTKIPASERRERAEAMLVKVGlgPEHFNRYP-HMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13638  93 TDIDSDIAFS--LRNLGVPEAEITRRVDEALTLVD--AQHFRHQPiQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLD 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 186 LSVQAQVLNLLRDLQEEFELTyVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK13638 169 PAGRTQMIAIIRRIVAQGNHV-IISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFA 225

ABCC_bacteriocin_exporters

cd03245

ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...

29-236

9.12e-24

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: 95.73 E-value: 9.12e-24

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPgTEMRSKVQMVFQNP---YGSLN 105
Cdd:cd03245   19 ALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDG--TDIRQLDP-ADLRRNIGYVPQDVtlfYGTLR 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLmepliintkipASERRERAEAMLVKVGlgpEHFNRYPHMF-----------SGGQRQRIAIARALMLNPAL 174
Cdd:cd03245   96 DNITLGAPL-----------ADDERILRAAELAGVT---DFVNKHPNGLdlqigergrglSGGQRQAVALARALLNDPPI 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 175 LVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVISKGEAVEQG 236
Cdd:cd03245  162 LLLDEPTSAMDMNSEERLKERLRQLLG--DKTLIIITHRPSLLD-LVDRIIVMDSGRIVADG 220

bacteriocin_ABC

TIGR01193

ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...

29-243

1.15e-23

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: 100.20 E-value: 1.15e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-DIARrrpgTEMRSKVQMVFQNPY---GSL 104
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkDIDR----HTLRQFINYLPQEPYifsGSI 564

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  105 nprqkvgdvlMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHM--------FSGGQRQRIAIARALMLNPALLV 176
Cdd:TIGR01193 565 ----------LENLLLGAKENVSQDEIWAACEIAEIKDDIENMPLGYQTelseegssISGGQKQRIALARALLTDSKVLI 634

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  177 LDEPVSALDLSVQAQVLNLLRDLQEEfelTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR01193 635 LDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQ-SDKIIVLDHGKIIEQGSHDELLD 697

COG4586

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

3-243

1.45e-23

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

Pssm-ID: 443643 [Multi-domain] Cd Length: 323 Bit Score: 97.47 E-value: 1.45e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   3 IVVKGkgITRDYHVP---GGLFGGA--------RMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPaSGGE 70
Cdd:COG4586    2 IEVEN--LSKTYRVYekePGLKGALkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTgILVP-TSGE 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  71 LKIDGqpVDIARRRPgtEMRSKVQMVFqnpyGslnprQKVG---DV-LMEPLIINTKI---PASERRERAEaMLVKVgLG 143
Cdd:COG4586   79 VRVLG--YVPFKRRK--EFARRIGVVF----G-----QRSQlwwDLpAIDSFRLLKAIyriPDAEYKKRLD-ELVEL-LD 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 144 PEHFNRYP-HMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIAD 222
Cdd:COG4586  144 LGELLDTPvRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCD 223

                        250       260
                 ....*....|....*....|.
gi 739227338 223 DVMVISKGEAVEQGTREELFA 243
Cdd:COG4586  224 RVIVIDHGRIIYDGSLEELKE 244

PRK14258

phosphate ABC transporter ATP-binding protein; Provisional

30-252

1.53e-23

phosphate ABC transporter ATP-binding protein; Provisional

Pssm-ID: 184593 [Multi-domain] Cd Length: 261 Bit Score: 96.26 E-value: 1.53e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGgELKIDGQ----PVDIARRRPG-TEMRSKVQMVFQNPygSL 104
Cdd:PRK14258  23 LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELES-EVRVEGRveffNQNIYERRVNlNRLRRQVSMVHPKP--NL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 NPRQKVGDVLMEPLIINTKiPASERRERAEAMLVKVGLGPEHFNRYPHM---FSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:PRK14258 100 FPMSVYDNVAYGVKIVGWR-PKLEIDDIVESALKDADLWDEIKHKIHKSaldLSGGQQQRLCIARALAVKPKVLLMDEPC 178

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 182 SALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEA-----VEQGTREELFADPKHPYTRQ 252
Cdd:PRK14258 179 FGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNENrigqlVEFGLTKKIFNSPHDSRTRE 254

PRK11000

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

31-246

1.81e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;

Pssm-ID: 182893 [Multi-domain] Cd Length: 369 Bit Score: 98.18 E-value: 1.81e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  31 KGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV-DIARRRPGtemrskVQMVFQNpYgSLNPRQK 109
Cdd:PRK11000  20 KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMnDVPPAERG------VGMVFQS-Y-ALYPHLS 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLMEPLIInTKIPASERRERAEAMLVKVGLGpeHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSV 188
Cdd:PRK11000  92 VAENMSFGLKL-AGAKKEEINQRVNQVAEVLQLA--HLlDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEPLSNLDAAL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 189 QAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:PRK11000 169 RVQMRIEISRLHKRLGRTMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPA 226

ABC_NatA_like

cd03267

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...

25-236

3.01e-23

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: 95.09 E-value: 3.01e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  25 RMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQpVDIARRRpgtEMRSKVQMVFqnpyGS 103
Cdd:cd03267   32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSgLLQPTSG-EVRVAGL-VPWKRRK---KFLRRIGVVF----GQ 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 LNprQKVGDV-LMEPLIINTKI---PASERRERAEAMLVKVGLGPEhFNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:cd03267  103 KT--QLWWDLpVIDSFYLLAAIydlPPARFKKRLDELSELLDLEEL-LDTPVRQLSLGQRMRAEIAAALLHEPEILFLDE 179

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 180 PVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03267  180 PTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236

modC

PRK11144

molybdenum ABC transporter ATP-binding protein ModC;

44-245

3.19e-23

molybdenum ABC transporter ATP-binding protein ModC;

Pssm-ID: 182993 [Multi-domain] Cd Length: 352 Bit Score: 97.25 E-value: 3.19e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  44 AIVGESGSGKSTLARIIA-LIDPASGgELKIDGQP-VDIARR--RPgTEMRsKVQMVFQNpyGSLNPRQKV-GDVL--Me 116
Cdd:PRK11144  28 AIFGRSGAGKTSLINAISgLTRPQKG-RIVLNGRVlFDAEKGicLP-PEKR-RIGYVFQD--ARLFPHYKVrGNLRygM- 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 117 pliintkipASERRERAEAmLVKVgLGPEH-FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNL 195
Cdd:PRK11144 102 ---------AKSMVAQFDK-IVAL-LGIEPlLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPY 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 739227338 196 LRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK11144 171 LERLAREINIPILYVSHSLDEILRLADRVVVLEQGKVKAFGPLEEVWASS 220

ABCG_EPDR

cd03213

Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...

14-236

3.38e-23

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: 93.77 E-value: 3.38e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  14 YHVPGGLFGGARmvQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA--LIDPASGGELKIDGQPVDIarrrpgTEMRS 91
Cdd:cd03213   11 VTVKSSPSKSGK--QLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAgrRTGLGVSGEVLINGRPLDK------RSFRK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  92 KVQMVFQNpygslnprqkvgDVLMEPLIIntkipaserrerAEAMLVKVGL-GpehfnryphmFSGGQRQRIAIARALML 170
Cdd:cd03213   83 IIGYVPQD------------DILHPTLTV------------RETLMFAAKLrG----------LSGGERKRVSIALELVS 128

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRY-IADDVMVISKGEAVEQG 236
Cdd:cd03213  129 NPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHQPSSEIFeLFDKLLLLSQGRVIYFG 194

TagH

COG1134

ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...

1-240

5.03e-23

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

Pssm-ID: 440749 [Multi-domain] Cd Length: 245 Bit Score: 94.38 E-value: 5.03e-23

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYHVPGGLFG------------GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG 68
Cdd:COG1134    1 MSSMIEVENVSKSYRLYHEPSRslkelllrrrrtRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  69 GELKIDGQ---PVDIArrrpgtemrskvqmvfqnpyGSLNP----RQkvgdvlmepliiNTKIPAS---ERRERAEAMLV 138
Cdd:COG1134   81 GRVEVNGRvsaLLELG--------------------AGFHPeltgRE------------NIYLNGRllgLSRKEIDEKFD 128

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 139 KV----GLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDL 214
Cdd:COG1134  129 EIvefaELG-DFIDQPVKTYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIRELRESGR-TVIFVSHSM 206

                        250       260
                 ....*....|....*....|....*.
gi 739227338 215 SVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:COG1134  207 GAVRRLCDRAIWLEKGRLVMDGDPEE 232

NHLM_micro_ABC2

TIGR03797

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...

28-243

6.78e-23

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

Pssm-ID: 274789 [Multi-domain] Cd Length: 686 Bit Score: 98.10 E-value: 6.78e-23

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALID-PASGGELkIDGQP---VDIARrrpgteMRSKVQMVFQNpyGS 103
Cdd:TIGR03797 467 LILDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFEtPESGSVF-YDGQDlagLDVQA------VRRQLGVVLQN--GR 537

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  104 LNPrqkvgDVLMEPLIINTKIPASERRERAEamlvKVGLGpEHFNRYPhM------------FSGGQRQRIAIARALMLN 171
Cdd:TIGR03797 538 LMS-----GSIFENIAGGAPLTLDEAWEAAR----MAGLA-EDIRAMP-MgmhtvisegggtLSGGQRQRLLIARALVRK 606

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338  172 PALLVLDEPVSALDLSVQAQVLNLLRDLQeefeLTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR03797 607 PRILLFDEATSALDNRTQAIVSESLERLK----VTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQGTYDELMA 673

livG

PRK11300

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

21-245

1.11e-22

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

Pssm-ID: 183080 [Multi-domain] Cd Length: 255 Bit Score: 93.90 E-value: 1.11e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarRRPGTEM-RSKVQMVFQN 99
Cdd:PRK11300  15 FGG---LLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIE---GLPGHQIaRMGVVRTFQH 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 P--YGSLN--------PRQKVGDVLMEPLIintKIPASERRERaEAM------LVKVGLGpEHFNRYPHMFSGGQRQRIA 163
Cdd:PRK11300  89 VrlFREMTvienllvaQHQQLKTGLFSGLL---KTPAFRRAES-EALdraatwLERVGLL-EHANRQAGNLAYGQQRRLE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 164 IARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK11300 164 IARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGTPEEIRN 243


                 ..
gi 739227338 244 DP 245
Cdd:PRK11300 244 NP 245

PRK13651

cobalt transporter ATP-binding subunit; Provisional

28-246

1.36e-22

cobalt transporter ATP-binding subunit; Provisional

Pssm-ID: 184210 [Multi-domain] Cd Length: 305 Bit Score: 94.77 E-value: 1.36e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTL-ARIIALIDPASG---------------GELKIDGQPVDIARRRPG----- 86
Cdd:PRK13651  21 KALDNVSVEINQGEFIAIIGQTGSGKTTFiEHLNALLLPDTGtiewifkdeknkkktKEKEKVLEKLVIQKTRFKkikki 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  87 TEMRSKVQMVFQNPYGSLNPRQKVGDVLMEPliINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIAR 166
Cdd:PRK13651 101 KEIRRRVGVVFQFAEYQLFEQTIEKDIIFGP--VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPFELSGGQKRRVALAG 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGK-TIILVTHDLDNVLEWTKRTIFFKDGKIIKDGDTYDILSDNK 257

type_I_sec_PrtD

TIGR01842

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...

30-243

1.44e-22

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: 97.03 E-value: 1.44e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPGTemrskvqmvFQNPYGSLnPRqk 109
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDG--ADLKQWDRET---------FGKHIGYL-PQ-- 399

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  110 vgDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEH--FNRYPHMF-----------SGGQRQRIAIARALMLNPALLV 176
Cdd:TIGR01842 400 --DVELFPGTVAENIARFGENADPEKIIEAAKLAGVHelILRLPDGYdtvigpggatlSGGQRQRIALARALYGDPKLVV 477

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  177 LDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR01842 478 LDEPNSNLDEEGEQALANAIKALKAR-GITVVVITHRPSLLG-CVDKILVLQDGRIARFGERDEVLA 542

ABC_KpsT_Wzt

cd03220

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...

8-236

1.49e-22

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.

Pssm-ID: 213187 [Multi-domain] Cd Length: 224 Bit Score: 92.60 E-value: 1.49e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYHVPGGLFGGARM------------VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDG 75
Cdd:cd03220    4 ENVSKSYPTYKGGSSSLKKlgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRG 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  76 Q---PVDIArrrpgtemrskvqmvfqnpyGSLNPRQKVGD-VLMEPLIINtkIPASERRERAEAMLVKVGLGpEHFNRYP 151
Cdd:cd03220   84 RvssLLGLG--------------------GGFNPELTGREnIYLNGRLLG--LSRKEIDEKIDEIIEFSELG-DFIDLPV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 152 HMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03220  141 KTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGK 219


                 ....*
gi 739227338 232 AVEQG 236
Cdd:cd03220  220 IRFDG 224

CydC

TIGR02868

thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...

29-214

2.18e-22

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

Pssm-ID: 274331 [Multi-domain] Cd Length: 530 Bit Score: 96.28 E-value: 2.18e-22

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIArrrPGTEMRSKVQMVFQNPYgslnprq 108
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSL---DQDEVRRRVSVCAQDAH------- 419

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  109 kvgdVLMEPLIINTKIPASE-RRERAEAMLVKVGLGpEHFNRYPH-----------MFSGGQRQRIAIARALMLNPALLV 176
Cdd:TIGR02868 420 ----LFDTTVRENLRLARPDaTDEELWAALERVGLA-DWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILL 494

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 739227338  177 LDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDL 214
Cdd:TIGR02868 495 LDEPTEHLDAETADELLEDLLAALS--GRTVVLITHHL 530

ycf16

CHL00131

sulfate ABC transporter protein; Validated

30-239

2.89e-22

sulfate ABC transporter protein; Validated

Pssm-ID: 214372 [Multi-domain] Cd Length: 252 Bit Score: 92.78 E-value: 2.89e-22

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALiDPA---SGGELKIDGQpvDIARRRPgtEMRSK--VQMVFQNPYG-- 102
Cdd:CHL00131  23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAG-HPAykiLEGDILFKGE--SILDLEP--EERAHlgIFLAFQYPIEip 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 ----------SLNPRQK-VGDVLMEPL----IINTKIPaserreraeamlvKVGLGPEHFNRYPHM-FSGGQRQRIAIAR 166
Cdd:CHL00131  98 gvsnadflrlAYNSKRKfQGLPELDPLefleIINEKLK-------------LVGMDPSFLSRNVNEgFSGGEKKRNEILQ 164

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 167 ALMLNPALLVLDEPVSALD---LSVQAQVLNLLRDLQEefelTYVFVSHDLSVVRYIADD-VMVISKGEAVEQGTRE 239
Cdd:CHL00131 165 MALLDSELAILDETDSGLDidaLKIIAEGINKLMTSEN----SIILITHYQRLLDYIKPDyVHVMQNGKIIKTGDAE 237

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

21-241

1.64e-21

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 93.58 E-value: 1.64e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiARRRPGTEMRSKVQMVFQNP 100
Cdd:PRK15439  21 YSG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC--ARLTPAKAHQLGIYLVPQEP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YgsLNPRQKVGDVlmepliINTKIPASERR-ERAEAMLVKVGLgpeHFNryPHMFSG----GQRQRIAIARALMLNPALL 175
Cdd:PRK15439  96 L--LFPNLSVKEN------ILFGLPKRQASmQKMKQLLAALGC---QLD--LDSSAGslevADRQIVEILRGLMRDSRIL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:PRK15439 163 ILDEPTASLTPAETERLFSRIRELLAQ-GVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL 227

PRK10575

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

40-241

1.65e-21

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

Pssm-ID: 182561 [Multi-domain] Cd Length: 265 Bit Score: 91.00 E-value: 1.65e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  40 GKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiarrrpgtEMRSKVqmvFQNPYGSLnPRQ--KVGDVLMEP 117
Cdd:PRK10575  37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLE--------SWSSKA---FARKVAYL-PQQlpAAEGMTVRE 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 118 LIINTKIP--------ASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQ 189
Cdd:PRK10575 105 LVAIGRYPwhgalgrfGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQ 183

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739227338 190 AQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:PRK10575 184 VDVLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQGTPAEL 235

sufC

TIGR01978

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...

30-239

2.04e-21

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

Pssm-ID: 273907 [Multi-domain] Cd Length: 243 Bit Score: 90.01 E-value: 2.04e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALiDPA---SGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNP------ 100
Cdd:TIGR01978  16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAG-HPSyevTSGTILFKGQ--DLLELEPDERARAGLFLAFQYPeeipgv 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  101 ------YGSLNPRQKVGDvlmepliiNTKIPASERRERAEAMLVKVGLGPEHFNRYPHM-FSGGQRQRIAIARALMLNPA 173
Cdd:TIGR01978  93 snleflRSALNARRSARG--------EEPLDLLDFEKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQMALLEPK 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  174 LLVLDEPVSALD---LSVQAQVLNLLRDLQEEFeltyVFVSHDLSVVRYIADD-VMVISKGEAVEQGTRE 239
Cdd:TIGR01978 165 LAILDEIDSGLDidaLKIVAEGINRLREPDRSF----LIITHYQRLLNYIKPDyVHVLLDGRIVKSGDVE 230

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

8-239

2.71e-21

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: 92.97 E-value: 2.71e-21

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    8 KGITRDyhvpgglFGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG--GELKIDGQPVdIARRRP 85
Cdd:TIGR02633   5 KGIVKT-------FGG---VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPHGTwdGEIYWSGSPL-KASNIR 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   86 GTEmRSKVQMVFQNPygSLNPRQKVgdvlMEPLIINTKIPASERR-------ERAEAMLVKVGLGPEHFNRYPHMFSGGQ 158
Cdd:TIGR02633  74 DTE-RAGIVIIHQEL--TLVPELSV----AENIFLGNEITLPGGRmaynamyLRAKNLLRELQLDADNVTRPVGDYGGGQ 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  159 RQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVeqGTR 238
Cdd:TIGR02633 147 QQLVEIAKALNKQARLLILDEPSSSLTEKETEILLDIIRDLKAH-GVACVYISHKLNEVKAVCDTICVIRDGQHV--ATK 223


                  .
gi 739227338  239 E 239
Cdd:TIGR02633 224 D 224

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

30-234

3.29e-21

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.82 E-value: 3.29e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIdGQPVDIArrrpgtemrskvqmVF-QNpYGSLNPRQ 108
Cdd:COG0488  331 LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETVKIG--------------YFdQH-QEELDPDK 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEpliINTKIPASERRERAEAMLvkvgLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLsv 188
Cdd:COG0488  395 TVLDELRD---GAPGGTEQEVRGYLGRFL----FSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLDEPTNHLDI-- 465

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 739227338 189 qaQVLNLLRDLQEEFELTYVFVSHDlsvvRY----IADDVMVISKGEAVE 234
Cdd:COG0488  466 --ETLEALEEALDDFPGTVLLVSHD----RYfldrVATRILEFEDGGVRE 509

PRK10247

putative ABC transporter ATP-binding protein YbbL; Provisional

30-240

3.41e-21

putative ABC transporter ATP-binding protein YbbL; Provisional

Pssm-ID: 182331 [Multi-domain] Cd Length: 225 Bit Score: 89.00 E-value: 3.41e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQpvDIARRRPGTeMRSKVQMVFQNP--YGslnp 106
Cdd:PRK10247  23 LNNISFSLRAGEFKLITGPSGCGKSTLLKIVAsLISPTSG-TLLFEGE--DISTLKPEI-YRQQVSYCAQTPtlFG---- 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 rQKVGDVLMEPLIINTKIPaseRRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:PRK10247  95 -DTVYDNLIFPWQIRNQQP---DPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDE 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREE 240
Cdd:PRK10247 171 SNKHNVNEIIHRYVREQNIAVLWVTHDKDEINH-ADKVITLQPHAGEMQEARYE 223

Uup

COG0488

ATPase components of ABC transporters with duplicated ATPase domains [General function ...

30-224

5.46e-21

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

Pssm-ID: 440254 [Multi-domain] Cd Length: 520 Bit Score: 92.05 E-value: 5.46e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELkidgqpvdiaRRRPGTemrsKVQMVFQNPYgsLNPRQK 109
Cdd:COG0488   14 LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEV----------SIPKGL----RIGYLPQEPP--LDDDLT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLME---PLI--------INTKIPASERRE--------------------RAEAMLVKVGLGPEHFNRYPHMFSGGQ 158
Cdd:COG0488   78 VLDTVLDgdaELRaleaeleeLEAKLAEPDEDLerlaelqeefealggweaeaRAEEILSGLGFPEEDLDRPVSELSGGW 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 159 RQRIAIARALMLNPALLVLDEPVSALDL-SVQaqvlnLLRDLQEEFELTYVFVSHDlsvvRYIADDV 224
Cdd:COG0488  158 RRRVALARALLSEPDLLLLDEPTNHLDLeSIE-----WLEEFLKNYPGTVLVVSHD----RYFLDRV 215

fecE

PRK11231

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

21-242

6.52e-21

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

Pssm-ID: 183044 [Multi-domain] Cd Length: 255 Bit Score: 88.92 E-value: 6.52e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMVQALkgiDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPV------DIARR-------RPG 86
Cdd:PRK11231  12 YGTKRILNDL---SLSLPTGKITALIGPNGCGKSTLLKCFArLLTPQSG-TVFLGDKPIsmlssrQLARRlallpqhHLT 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  87 TEMRSKVQMVF--QNPYGSL------NPRQKVgDVLMEpliiNTKIpaSERRERAEAMLvkvglgpehfnryphmfSGGQ 158
Cdd:PRK11231  88 PEGITVRELVAygRSPWLSLwgrlsaEDNARV-NQAME----QTRI--NHLADRRLTDL-----------------SGGQ 143

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 159 RQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLS-VVRYiADDVMVISKGEAVEQGT 237
Cdd:PRK11231 144 RQRAFLAMVLAQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQGK-TVVTVLHDLNqASRY-CDHLVVLANGHVMAQGT 221


                 ....*
gi 739227338 238 REELF 242
Cdd:PRK11231 222 PEEVM 226

ABCD_peroxisomal_ALDP

cd03223

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...

30-212

7.18e-21

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: 86.82 E-value: 7.18e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKidgqpvdiarrRPGtemRSKVQMVFQNPY---GSLnp 106
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIG-----------MPE---GEDLLFLPQRPYlplGTL-- 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 rqkvgdvlMEPLIintkipaserreraeamlvkvglgpehfnrYP--HMFSGGQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:cd03223   81 --------REQLI------------------------------YPwdDVLSGGEQQRLAFARLLLHKPKFVFLDEATSAL 122

                        170       180
                 ....*....|....*....|....*...
gi 739227338 185 DLSVQAQVLNLLRDLqeefELTYVFVSH 212
Cdd:cd03223  123 DEESEDRLYQLLKEL----GITVISVGH 146

PhnK

COG1101

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

22-214

7.50e-21

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

Pssm-ID: 440718 [Multi-domain] Cd Length: 264 Bit Score: 88.99 E-value: 7.50e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRpgTEMRSK-VQMVFQNP 100
Cdd:COG1101   14 GTVNEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGK--DVTKLP--EYKRAKyIGRVFQDP 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 Y----GSL----------NPRQKVGdvlmepLIINTKipaSERRERAEAMLVKVGLGPEHfnrypHM------FSGGQRQ 160
Cdd:COG1101   90 MmgtaPSMtieenlalayRRGKRRG------LRRGLT---KKRRELFRELLATLGLGLEN-----RLdtkvglLSGGQRQ 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 739227338 161 RIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDL 214
Cdd:COG1101  156 ALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNM 209

PRK11160

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

28-253

8.15e-21

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

Pssm-ID: 236865 [Multi-domain] Cd Length: 574 Bit Score: 91.81 E-value: 8.15e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLariIALI----DPASGgELKIDGQPVDiarRRPGTEMRSKVQMVFQNPY-- 101
Cdd:PRK11160 354 PVLKGLSLQIKAGEKVALLGRTGCGKSTL---LQLLtrawDPQQG-EILLNGQPIA---DYSEAALRQAISVVSQRVHlf 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 -GSLNprqkvgdvlmEPLIInTKIPASErrERAEAMLVKVGL-----GPEHFN-------RyphMFSGGQRQRIAIARAL 168
Cdd:PRK11160 427 sATLR----------DNLLL-AAPNASD--EALIEVLQQVGLeklleDDKGLNawlgeggR---QLSGGEQRRLGIARAL 490

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 169 MLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYIaDDVMVISKGEAVEQGTREELFAdpKHP 248
Cdd:PRK11160 491 LHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGLEQF-DRICVMDNGQIIEQGTHQELLA--QQG 565


                 ....*
gi 739227338 249 YTRQL 253
Cdd:PRK11160 566 RYYQL 570

ABC_NatA_sodium_exporter

cd03266

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

24-236

1.50e-20

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: 87.42 E-value: 1.50e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  24 ARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDG-----QPVDiARRRPGtemrskvqmVFQ 98
Cdd:cd03266   15 KKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGfdvvkEPAE-ARRRLG---------FVS 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  99 NPYGsLNPRQKVgdvlMEPLIINTKIPASERRErAEAMLVKVG--LGPEHF-NRYPHMFSGGQRQRIAIARALMLNPALL 175
Cdd:cd03266   85 DSTG-LYDRLTA----RENLEYFAGLYGLKGDE-LTARLEELAdrLGMEELlDRRVGGFSTGMRQKVAIARALVHDPPVL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03266  159 LLDEPTTGLDVMATRALREFIRQLRALGK-CILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218

ABCC_NFT1

cd03369

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...

23-237

1.67e-20

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

Pssm-ID: 213269 [Multi-domain] Cd Length: 207 Bit Score: 87.08 E-value: 1.67e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIALIDPASgGELKIDGQpvDIArRRPGTEMRSKVQMVFQNPy 101
Cdd:cd03369   17 APDLPPVLKNVSFKVKAGEKIGIVGRTGAGKSTLILaLFRFLEAEE-GKIEIDGI--DIS-TIPLEDLRSSLTIIPQDP- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 gslnprqkvgdVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHfnryphmFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:cd03369   92 -----------TLFSGTIRSNLDPFDEYSDEEIYGALRVSEGGLN-------LSQGQRQLLCLARALLKRPRVLVLDEAT 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 182 SALDLSVQAQVLNLLRdlqEEF-ELTYVFVSHDL-SVVRYiaDDVMVISKGEAVEQGT 237
Cdd:cd03369  154 ASIDYATDALIQKTIR---EEFtNSTILTIAHRLrTIIDY--DKILVMDAGEVKEYDH 206

AztA

NF040873

zinc ABC transporter ATP-binding protein AztA;

29-218

2.38e-20

zinc ABC transporter ATP-binding protein AztA;

Pssm-ID: 468810 [Multi-domain] Cd Length: 191 Bit Score: 86.13 E-value: 2.38e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDG--------QPVDIARRRPGTeMRSKVQMVFQNP 100
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGgarvayvpQRSEVPDSLPLT-VRDLVAMGRWAR 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YGSLNPrqkvgdvlmepliintkiPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:NF040873  86 RGLWRR------------------LTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEP 146

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVR 218
Cdd:NF040873 147 TTGLDAESRERIIALLAEEHAR-GATVVVVTHDLELVR 183

MglA

COG1129

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

29-241

2.46e-20

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

Pssm-ID: 440745 [Multi-domain] Cd Length: 497 Bit Score: 90.08 E-value: 2.46e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIarRRPGTEMRSKVQMVFQNpygslnpRQ 108
Cdd:COG1129  267 VVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRI--RSPRDAIRAGIAYVPED-------RK 337

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEPLIINTKIPA----------SERRER--AEAMLVKVGLgpehfnRYPHM------FSGGQRQRIAIARALML 170
Cdd:COG1129  338 GEGLVLDLSIRENITLASldrlsrggllDRRRERalAEEYIKRLRI------KTPSPeqpvgnLSGGNQQKVVLAKWLAT 411

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:COG1129  412 DPKVLILDEPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGELDREEA 481

PRK09984

phosphonate ABC transporter ATP-binding protein;

28-241

3.18e-20

phosphonate ABC transporter ATP-binding protein;

Pssm-ID: 182182 [Multi-domain] Cd Length: 262 Bit Score: 87.38 E-value: 3.18e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LI--DPASGGELKIDGQPVDIARRRPGTEMRSKVQM--VFQNpYG 102
Cdd:PRK09984  18 QALHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSgLItgDKSAGSHIELLGRTVQREGRLARDIRKSRANTgyIFQQ-FN 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEPLiinTKIP---------ASERRERAEAMLVKVGLGpeHF-NRYPHMFSGGQRQRIAIARALMLNP 172
Cdd:PRK09984  97 LVNRLSVLENVLIGAL---GSTPfwrtcfswfTREQKQRALQALTRVGMV--HFaHQRVSTLSGGQQQRVAIARALMQQA 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 173 ALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:PRK09984 172 KVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDGSSQQF 240

PRK14239

phosphate transporter ATP-binding protein; Provisional

28-250

3.65e-20

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184585 [Multi-domain] Cd Length: 252 Bit Score: 87.14 E-value: 3.65e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIAL---IDP--ASGGELKIDGQpvDIARRRPGT-EMRSKVQMVFQNPy 101
Cdd:PRK14239  19 KALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRmndLNPevTITGSIVYNGH--NIYSPRTDTvDLRKEIGMVFQQP- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 gslNP-RQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYpH----MFSGGQRQRIAIARALMLNPALLV 176
Cdd:PRK14239  96 ---NPfPMSIYENVVYGLRLKGIKDKQVLDEAVEKSLKGASIWDEVKDRL-HdsalGLSGGQQQRVCIARVLATSPKIIL 171

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 739227338 177 LDEPVSALDLSVQAQVLNLLRDLQEEFelTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPKHPYT 250
Cdd:PRK14239 172 LDEPTSALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKET 243

PRK10790

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

30-243

3.90e-20

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

Pssm-ID: 182733 [Multi-domain] Cd Length: 592 Bit Score: 89.78 E-value: 3.90e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgteMRSKVQMVFQNPYgslnprqk 109
Cdd:PRK10790 357 LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSV---LRQGVAMVQQDPV-------- 425

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 vgdVLMEPLIINTKIPASERRERAEAMLVKVGLGP--------------EHFNRyphmFSGGQRQRIAIARALMLNPALL 175
Cdd:PRK10790 426 ---VLADTFLANVTLGRDISEEQVWQALETVQLAElarslpdglytplgEQGNN----LSVGQKQLLALARVLVQTPQIL 498

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVrYIADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK10790 499 ILDEATANIDSGTEQAIQQALAAVRE--HTTLVVIAHRLSTI-VEADTILVLHRGQAVEQGTHQQLLA 563

ABCG_White

cd03234

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...

27-236

5.40e-20

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: 85.79 E-value: 5.40e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA---LIDPASGGELKIDGQPVDIArrrpgtEMRSKVQMVFQNPYgs 103
Cdd:cd03234   20 ARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISgrvEGGGTTSGQILFNGQPRKPD------QFQKCVAYVRQDDI-- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 LNPRQKVGDVL--MEPLIINTKIPASERRERAEAMLVK-VGLGPEHFNRYPHMfSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03234   92 LLPGLTVRETLtyTAILRLPRKSSDAIRKKRVEDVLLRdLALTRIGGNLVKGI-SGGERRRVSIAVQLLWDPKVLILDEP 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:cd03234  171 TSGLDSFTALNLVSTLSQLARRNRIVILTIHQPRSDLFRLFDRILLLSSGEIVYSG 226

PRK10789

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

29-245

5.46e-20

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

Pssm-ID: 182732 [Multi-domain] Cd Length: 569 Bit Score: 89.39 E-value: 5.46e-20

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRrpgTEMRSKVQMVFQNPYgslnprq 108
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQL---DSWRSRLAVVSQTPF------- 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEPLIINTKIPASERRERAeAMLVKVGlgpEHFNRYPH-----------MFSGGQRQRIAIARALMLNPALLVL 177
Cdd:PRK10789 400 LFSDTVANNIALGRPDATQQEIEHV-ARLASVH---DDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILIL 475

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK10789 476 DDALSAVDGRTEHQILHNLRQWGE--GRTVIISAHRLSALTE-ASEILVMQHGHIAQRGNHDQLAQQS 540

CydD

TIGR02857

thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...

29-227

9.02e-20

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: 88.50 E-value: 9.02e-20

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRrpgTEMRSKVQMVFQNPY---GSL- 104
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADA---DSWRDQIAWVPQHPFlfaGTIa 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  105 -NPR--QKVGDVLMepliintkipASERRERAEAMLVKVGLGPEH---FNRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:TIGR02857 414 eNIRlaRPDASDAE----------IREALERAGLDEFVAALPQGLdtpIGEGGAGLSGGQAQRLALARAFLRDAPLLLLD 483

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 739227338  179 EPVSALDLSVQAQVLNLLRDLQEefELTYVFVSHDLSVVRyIADDVMVI 227
Cdd:TIGR02857 484 EPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAA-LADRIVVL 529

GguA

NF040905

sugar ABC transporter ATP-binding protein;

8-234

1.08e-19

sugar ABC transporter ATP-binding protein;

Pssm-ID: 468840 [Multi-domain] Cd Length: 500 Bit Score: 88.31 E-value: 1.08e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   8 KGITRDYhvPGglfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPAS--GGELKIDGQPV---DIAr 82
Cdd:NF040905   5 RGITKTF--PG--------VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGVYPHGsyEGEILFDGEVCrfkDIR- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  83 rrpGTEMRSKV---QMVFQNPYGSL-------NPRQKVGdvlmeplIINTkipaSERRERAEAMLVKVGLGPEHFNRYPH 152
Cdd:NF040905  74 ---DSEALGIViihQELALIPYLSIaeniflgNERAKRG-------VIDW----NETNRRARELLAKVGLDESPDTLVTD 139

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 153 MFSGGQrQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEA 232
Cdd:NF040905 140 IGVGKQ-QLVEIAKALSKDVKLLILDEPTAALNEEDSAALLDLLLELKAQ-GITSIIISHKLNEIRRVADSITVLRDGRT 217


                 ..
gi 739227338 233 VE 234
Cdd:NF040905 218 IE 219

3a01204

TIGR00955

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

30-248

2.76e-19

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

Pssm-ID: 273361 [Multi-domain] Cd Length: 617 Bit Score: 87.41 E-value: 2.76e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPAS---GGELKIDGQPVDiarrrpGTEMRSKVQMVFQNP--YGSL 104
Cdd:TIGR00955  41 LKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPID------AKEMRAISAYVQQDDlfIPTL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  105 NPRQKVgdVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNR-----YPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:TIGR00955 115 TVREHL--MFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTRigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDE 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  180 PVSALDLSVQAQVLNLLRDL------------QEEFELTYVFvshdlsvvryiaDDVMVISKGEAVEQGTREEL---FAD 244
Cdd:TIGR00955 193 PTSGLDSFMAYSVVQVLKGLaqkgktiictihQPSSELFELF------------DKIILMAEGRVAYLGSPDQAvpfFSD 260


                  ....
gi 739227338  245 PKHP 248
Cdd:TIGR00955 261 LGHP 264

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

5-236

3.21e-19

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 87.15 E-value: 3.21e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   5 VKGKGITRDyhvpgglFGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRR 84
Cdd:PRK09700   6 ISMAGIGKS-------FGP---VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHK 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  85 PGTEMrsKVQMVFQ------------NPYGSLNPRQKVGDVLMepliintkIPASERRERAEAMLVKVGLGPEhFNRYPH 152
Cdd:PRK09700  76 LAAQL--GIGIIYQelsvideltvleNLYIGRHLTKKVCGVNI--------IDWREMRVRAAMMLLRVGLKVD-LDEKVA 144

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 153 MFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEA 232
Cdd:PRK09700 145 NLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGT-AIVYISHKLAEIRRICDRYTVMKDGSS 223


                 ....
gi 739227338 233 VEQG 236
Cdd:PRK09700 224 VCSG 227

PRK11174

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

28-245

3.46e-19

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

Pssm-ID: 236870 [Multi-domain] Cd Length: 588 Bit Score: 87.21 E-value: 3.46e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLarIIALIdpasG-----GELKIDGQPVdiaRRRPGTEMRSKVQMVFQNP-- 100
Cdd:PRK11174 364 TLAGPLNFTLPAGQRIALVGPSGAGKTSL--LNALL----GflpyqGSLKINGIEL---RELDPESWRKHLSWVGQNPql 434

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 -YGSLnpRQKV--GDVLMEPLIINTKIpaserrERAEAMlvkvglgpEHFNRYPH-----------MFSGGQRQRIAIAR 166
Cdd:PRK11174 435 pHGTL--RDNVllGNPDASDEQLQQAL------ENAWVS--------EFLPLLPQgldtpigdqaaGLSVGQAQRLALAR 498

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRdlQEEFELTYVFVSHDLSVVRYIaDDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK11174 499 ALLQPCQLLLLDEPTASLDAHSEQLVMQALN--AASRRQTTLMVTHQLEDLAQW-DQIWVMQDGQIVQQGDYAELSQAG 574

ABCF_EF-3

cd03221

ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...

30-231

9.13e-19

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: 80.57 E-value: 9.13e-19

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIAlidpasgGELKIDgqpvdiarrrPGTEMRSKVqmvfqnpygslnprqk 109
Cdd:cd03221   16 LKDISLTINPGDRIGLVGRNGAGKSTLLKLIA-------GELEPD----------EGIVTWGST---------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 vgdvlmepliintkipaserreraeamlVKVGlgpeHFNRyphmFSGGQRQRIAIARALMLNPALLVLDEPVSALDL-SV 188
Cdd:cd03221   63 ----------------------------VKIG----YFEQ----LSGGEKMRLALAKLLLENPNLLLLDEPTNHLDLeSI 106

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 739227338 189 QAqvlnlLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:cd03221  107 EA-----LEEALKEYPGTVILVSHDRYFLDQVATKIIELEDGK 144

PRK15056

manganese/iron ABC transporter ATP-binding protein;

29-242

1.21e-18

manganese/iron ABC transporter ATP-binding protein;

Pssm-ID: 185016 [Multi-domain] Cd Length: 272 Bit Score: 83.39 E-value: 1.21e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtemrSKVQMVFQNPYGSLNPRQ 108
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTRQALQK------NLVAYVPQSEEVDWSFPV 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 KVGDVLMEPLIINT---KIPASERRERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK15056  96 LVEDVVMMGRYGHMgwlRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLARAIAQQGQVILLDEPFTGVD 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 186 LSVQAQVLNLLRDLQEEFElTYVFVSHDL-SVVRYIADDVMVisKGEAVEQGTREELF 242
Cdd:PRK15056 175 VKTEARIISLLRELRDEGK-TMLVSTHNLgSVTEFCDYTVMV--KGTVLASGPTETTF 229

ABC_YhbG

cd03218

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

28-246

1.29e-18

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: 82.21 E-value: 1.29e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQ-----PVDiARRRPGTEMRSKVQMVFQnpyg 102
Cdd:cd03218   14 KVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQditklPMH-KRARLGIGYLPQEASIFR---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEpliinTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:cd03218   89 KLTVEENILAVLEI-----RGLSKKEREEKLEELLEEFHI--THLrKSKASSLSGGERRRVEIARALATNPKFLLLDEPF 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 182 SALD-LSVQaQVLNLLRDLQeEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADPK 246
Cdd:cd03218  162 AGVDpIAVQ-DIQKIIKILK-DRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANEL 225

PRK10253

iron-enterobactin ABC transporter ATP-binding protein;

31-241

1.48e-18

iron-enterobactin ABC transporter ATP-binding protein;

Pssm-ID: 182336 [Multi-domain] Cd Length: 265 Bit Score: 82.73 E-value: 1.48e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  31 KGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVdiaRRRPGTEMRSKVQMVFQNpygSLNPrqk 109
Cdd:PRK10253  24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSrLMTPAHG-HVWLDGEHI---QHYASKEVARRIGLLAQN---ATTP--- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 vGDVLMEPLIINTKIPASE-----RRERAEAMLVKV-GLGPEHF-NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK10253  94 -GDITVQELVARGRYPHQPlftrwRKEDEEAVTKAMqATGITHLaDQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTT 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:PRK10253 173 WLDISHQIDLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231

PRK14243

phosphate transporter ATP-binding protein; Provisional

29-252

4.91e-18

phosphate transporter ATP-binding protein; Provisional

Pssm-ID: 184588 [Multi-domain] Cd Length: 264 Bit Score: 81.37 E-value: 4.91e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA----LIDPA-SGGELKIDGQPVDIARRRPgTEMRSKVQMVFQNPYGS 103
Cdd:PRK14243  25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNrlndLIPGFrVEGKVTFHGKNLYAPDVDP-VEVRRRIGMVFQKPNPF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 104 lnPRQKVGDVLMEPLIINTKIPASERRERA--EAML---VKvglgpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK14243 104 --PKSIYDNIAYGARINGYKGDMDELVERSlrQAALwdeVK-----DKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMD 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFelTYVFVSHDLSVVRYIADDVMVIS---------KGEAVEQGTREELFADPKHPY 249
Cdd:PRK14243 177 EPCSALDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAFFNveltegggrYGYLVEFDRTEKIFNSPQQQA 254


                 ...
gi 739227338 250 TRQ 252
Cdd:PRK14243 255 TRD 257

CeuD

COG4604

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

30-241

7.63e-18

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

Pssm-ID: 443654 [Multi-domain] Cd Length: 252 Bit Score: 80.51 E-value: 7.63e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV------DIARR------RPGTEMRSKV-QMV 96
Cdd:COG4604   17 LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVattpsrELAKRlailrqENHINSRLTVrELV 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  97 ----FqnPY--GSLNPrqkvgdvlmepliintkipasERRERAEAMLVKVGLGP-EHfnRYPHMFSGGQRQRIAIARALM 169
Cdd:COG4604   97 afgrF--PYskGRLTA---------------------EDREIIDEAIAYLDLEDlAD--RYLDELSGGQRQRAFIAMVLA 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 170 LNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVV-RYiADDVMVISKGEAVEQGTREEL 241
Cdd:COG4604  152 QDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFAsCY-ADHIVAMKDGRVVAQGTPEEI 223

ABC_FeS_Assembly

cd03217

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...

30-239

8.91e-18

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

Pssm-ID: 213184 [Multi-domain] Cd Length: 200 Bit Score: 79.49 E-value: 8.91e-18

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALiDPA---SGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNPYgslnp 106
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMG-HPKyevTEGEILFKGE--DITDLPPEERARLGIFLAFQYPP----- 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 rqkvgdvlmepliintKIPAserreraeamlVKVglgpEHFNRYPHM-FSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:cd03217   88 ----------------EIPG-----------VKN----ADFLRYVNEgFSGGEKKRNEILQLLLLEPDLAILDEPDSGLD 136

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 186 ---LSVQAQVLNLLRDLQEefelTYVFVSHDLSVVRYI-ADDVMVISKGEAVEQGTRE 239
Cdd:cd03217  137 idaLRLVAEVINKLREEGK----SVLIITHYQRLLDYIkPDRVHVLYDGRIVKSGDKE 190

PTZ00265

multidrug resistance protein (mdr1); Provisional

27-245

1.01e-17

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 83.15 E-value: 1.01e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGGELKIDGQPV-DIARRRpgteMRSKVQMVFQNP---- 100
Cdd:PTZ00265  398 VEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIErLYDPTEGDIIINDSHNLkDINLKW----WRSKIGVVSQDPllfs 473

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  101 -------------------------------YGSLNPRQKVGDVLMEPL--IINTK--------------IPASERRERA 133
Cdd:PTZ00265  474 nsiknnikyslyslkdlealsnyynedgndsQENKNKRNSCRAKCAGDLndMSNTTdsneliemrknyqtIKDSEVVDVS 553

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  134 EAMLVK--VGLGPEHFNRY----PHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTY 207
Cdd:PTZ00265  554 KKVLIHdfVSALPDKYETLvgsnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRIT 633

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 739227338  208 VFVSHDLSVVRYiADDVMVISKGEAVEQGTREELFADP 245
Cdd:PTZ00265  634 IIIAHRLSTIRY-ANTIFVLSNRERGSTVDVDIIGEDP 670

anch_rpt_ABC

TIGR03771

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...

35-241

1.21e-17

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

Pssm-ID: 163483 [Multi-domain] Cd Length: 223 Bit Score: 79.51 E-value: 1.21e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   35 FAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTeMRSKVQMVFQNP---YGS-LNPRQKv 110
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAGASPGKGWRHIGY-VPQRHEFAWDFPisvAHTvMSGRTG- 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  111 gdvLMEPLiintKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQA 190
Cdd:TIGR03771  79 ---HIGWL----RRPCVADFAAVRDALRRVGLT-ELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 739227338  191 QVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISkGEAVEQGTREEL 241
Cdd:TIGR03771 151 LLTELFIELAGA-GTAILMTTHDLAQAMATCDRVVLLN-GRVIADGTPQQL 199

met_CoM_red_A2

TIGR03269

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

21-243

1.47e-17

Pssm-ID: 132313 [Multi-domain] Cd Length: 520 Bit Score: 82.16 E-value: 1.47e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   21 FGGarmVQALKGIDFAVERGKTLAIVGESGSGKSTL--------------ARII---------ALIDPAS---------G 68
Cdd:TIGR03269  10 FDG---KEVLKNISFTIEEGEVLGILGRSGAGKSVLmhvlrgmdqyeptsGRIIyhvalcekcGYVERPSkvgepcpvcG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   69 GEL---KIDGQPVDIARRRpgtEMRSKVQMVFQNPYgSLNPRQKVGDVLMEPLIiNTKIPASERRERAEAMLVKVGLGpe 145
Cdd:TIGR03269  87 GTLepeEVDFWNLSDKLRR---RIRKRIAIMLQRTF-ALYGDDTVLDNVLEALE-EIGYEGKEAVGRAVDLIEMVQLS-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  146 hfNRYPHM---FSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIAD 222
Cdd:TIGR03269 160 --HRITHIardLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLSD 237

                         250       260
                  ....*....|....*....|.
gi 739227338  223 DVMVISKGEAVEQGTREELFA 243
Cdd:TIGR03269 238 KAIWLENGEIKEEGTPDEVVA 258

znuC

PRK09544

high-affinity zinc transporter ATPase; Reviewed

23-225

4.03e-17

high-affinity zinc transporter ATPase; Reviewed

Pssm-ID: 181939 [Multi-domain] Cd Length: 251 Bit Score: 78.62 E-value: 4.03e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASG-----GELKID--GQPVDIARRRPGTEMRskvq 94
Cdd:PRK09544  15 GQRRV--LSDVSLELKPGKILTLLGPNGAGKSTLVRVVlGLVAPDEGvikrnGKLRIGyvPQKLYLDTTLPLTVNR---- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  95 mvfqnpYGSLNPRQKVGDVLmepliintkiPASERRERAeamlvkvglgpeHFNRYP-HMFSGGQRQRIAIARALMLNPA 173
Cdd:PRK09544  89 ------FLRLRPGTKKEDIL----------PALKRVQAG------------HLIDAPmQKLSGGETQRVLLARALLNRPQ 140

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739227338 174 LLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVM 225
Cdd:PRK09544 141 LLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVMAKTDEVL 192

PRK13539

cytochrome c biogenesis protein CcmA; Provisional

23-197

7.52e-17

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 237421 [Multi-domain] Cd Length: 207 Bit Score: 76.84 E-value: 7.52e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPgtemrskvQMVFqnpyg 102
Cdd:PRK13539  13 GGRVL--FSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAE--------ACHY----- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 sLNPRQKVGDVLM--EPLIINTKIPASERRERAEAmLVKVGLGPEhFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:PRK13539  78 -LGHRNAMKPALTvaENLEFWAAFLGGEELDIAAA-LEAVGLAPL-AHLPFGYLSAGQKRRVALARLLVSNRPIWILDEP 154

                        170
                 ....*....|....*..
gi 739227338 181 VSALDLSVQAQVLNLLR 197
Cdd:PRK13539 155 TAALDAAAVALFAELIR 171

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

27-241

2.31e-16

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 78.41 E-value: 2.31e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEmrSKVQMVFQNPYgsLNP 106
Cdd:PRK11288  17 VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTAALA--AGVAIIYQELH--LVP 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMepL--------IINTKIPASERRERAEAMLVKVglGPEHFNRYphmFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK11288  93 EMTVAENLY--LgqlphkggIVNRRLLNYEAREQLEHLGVDI--DPDTPLKY---LSIGQRQMVEIAKALARNARVIAFD 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFELTyVFVSHDLSVVRYIADDVMVISKG------EAVEQGTREEL 241
Cdd:PRK11288 166 EPTSSLSAREIEQLFRVIRELRAEGRVI-LYVSHRMEEIFALCDAITVFKDGryvatfDDMAQVDRDQL 233

btuD

PRK09536

corrinoid ABC transporter ATPase; Reviewed

21-245

2.85e-16

corrinoid ABC transporter ATPase; Reviewed

Pssm-ID: 236554 [Multi-domain] Cd Length: 402 Bit Score: 77.96 E-value: 2.85e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMvqaLKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASGgELKIDGQPVDiarRRPGTEMRSKVQMVFQN 99
Cdd:PRK09536  13 FGDTTV---LDGVDLSVREGSLVGLVGPNGAGKTTLLRAInGTLTPTAG-TVLVAGDDVE---ALSARAASRRVASVPQD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 PYGSLN--PRQKVGdvlMEPLIINTKI-PASERRERA-EAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALL 175
Cdd:PRK09536  86 TSLSFEfdVRQVVE---MGRTPHRSRFdTWTETDRAAvERAMERTGVA-QFADRPVTSLSGGERQRVLLARALAQATPVL 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 176 VLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFADP 245
Cdd:PRK09536 162 LLDEPTASLDINHQVRTLELVRRLVDDGK-TAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230

PRK10895

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

21-244

6.40e-16

lipopolysaccharide ABC transporter ATP-binding protein; Provisional

Pssm-ID: 182817 [Multi-domain] Cd Length: 241 Bit Score: 75.32 E-value: 6.40e-16

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARMVQalkGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI----ARRRPGTEMRSKVQMV 96
Cdd:PRK10895  13 YKGRRVVE---DVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLlplhARARRGIGYLPQEASI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  97 FQnpygslnpRQKVGDVLMEPLIINTKIPASERRERAEAMLVKVGLgpEHF-NRYPHMFSGGQRQRIAIARALMLNPALL 175
Cdd:PRK10895  90 FR--------RLSVYDNLMAVLQIRDDLSAEQREDRANELMEEFHI--EHLrDSMGQSLSGGERRRVEIARALAANPKFI 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 176 VLDEPVSALD-LSVQ--AQVLNLLRDlqeeFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK10895 160 LLDEPFAGVDpISVIdiKRIIEHLRD----SGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQD 227

NupO

COG3845

ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...

23-241

1.29e-15

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

Pssm-ID: 443055 [Multi-domain] Cd Length: 504 Bit Score: 76.22 E-value: 1.29e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKVQMVfqnpyg 102
Cdd:COG3845  267 DDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGE--DITGLSPRERRRLGVAYI------ 338

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 slnP--RQKVGDV----LMEPLIINT--KIPASER--------RERAEAML----VKVGlGPEHFNRyphMFSGGQRQRI 162
Cdd:COG3845  339 ---PedRLGRGLVpdmsVAENLILGRyrRPPFSRGgfldrkaiRAFAEELIeefdVRTP-GPDTPAR---SLSGGNQQKV 411

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 163 AIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE-----AVEQGT 237
Cdd:COG3845  412 ILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDA-GAAVLLISEDLDEILALSDRIAVMYEGRivgevPAAEAT 490


                 ....
gi 739227338 238 REEL 241
Cdd:COG3845  491 REEI 494

ccmA

TIGR01189

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...

23-198

1.55e-15

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

Pssm-ID: 273491 [Multi-domain] Cd Length: 198 Bit Score: 73.16 E-value: 1.55e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEMRskvqmvfqnpYG 102
Cdd:TIGR01189  11 GERML--FEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENIL----------YL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  103 SLNPRQKVGDVLMEPLIINTKIPASERRErAEAMLVKVGL-GPEHfnRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:TIGR01189  79 GHLPGLKPELSALENLHFWAAIHGGAQRT-IEDALAAVGLtGFED--LPAAQLSAGQQRRLALARLWLSRRPLWILDEPT 155

                         170
                  ....*....|....*..
gi 739227338  182 SALDLSVQAQVLNLLRD 198
Cdd:TIGR01189 156 TALDKAGVALLAGLLRA 172

PLN03232

ABC transporter C family member; Provisional

30-258

1.70e-15

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 76.55 E-value: 1.70e-15

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARRRPgTEMRSKVQMVFQNPygslnprqk 109
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDD--CDVAKFGL-TDLRRVLSIIPQSP--------- 1319

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  110 vgdVLMEPLIINTKIPASERR--------ERAEAMLV----KVGLGPEHFNRYPHmFSGGQRQRIAIARALMLNPALLVL 177
Cdd:PLN03232 1320 ---VLFSGTVRFNIDPFSEHNdadlwealERAHIKDVidrnPFGLDAEVSEGGEN-FSVGQRQLLSLARALLRRSKILVL 1395

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  178 DEPVSALDLSVQAQVlnlLRDLQEEFE-LTYVFVSHDLSVVrYIADDVMVISKGEAVEQGTREELFADPKHPYTRQLFAA 256
Cdd:PLN03232 1396 DEATASVDVRTDSLI---QRTIREEFKsCTMLVIAHRLNTI-IDCDKILVLSSGQVLEYDSPQELLSRDTSAFFRMVHST 1471


                  ..
gi 739227338  257 TP 258
Cdd:PLN03232 1472 GP 1473

PRK13538

cytochrome c biogenesis heme-transporting ATPase CcmA;

32-185

2.07e-15

cytochrome c biogenesis heme-transporting ATPase CcmA;

Pssm-ID: 184125 [Multi-domain] Cd Length: 204 Bit Score: 72.91 E-value: 2.07e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  32 GIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPvdIARRRPgtEMRSkvQMVFqnpYGSLNprqKV 110
Cdd:PRK13538  19 GLSFTLNAGELVQIEGPNGAGKTSLLRILAgLARPDAG-EVLWQGEP--IRRQRD--EYHQ--DLLY---LGHQP---GI 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 111 GDVL--MEPLIINTKIPASERRERAEAMLVKVGL-GPEHFnryP-HMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13538  86 KTELtaLENLRFYQRLHGPGDDEALWEALAQVGLaGFEDV---PvRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161

ABCC_MRP_domain1

cd03250

ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...

29-231

3.39e-15

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: 72.50 E-value: 3.39e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLarIIALIdpasgGEL-KIDGQpvdiarrrpgTEMRSKVQMVFQNPYgslnpr 107
Cdd:cd03250   20 TLKDINLEVPKGELVAIVGPVGSGKSSL--LSALL-----GELeKLSGS----------VSVPGSIAYVSQEPW------ 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 qkvgdvlmeplIINTKIP------ASERRERAEAMLVKVGLGPEhFNRYPH-----------MFSGGQRQRIAIARALML 170
Cdd:cd03250   77 -----------IQNGTIRenilfgKPFDEERYEKVIKACALEPD-LEILPDgdlteigekgiNLSGGQKQRISLARAVYS 144

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLN--LLRDLQEefELTYVFVSHDLSVVRYiADDVMVISKGE 231
Cdd:cd03250  145 DADIYLLDDPLSAVDAHVGRHIFEncILGLLLN--NKTRILVTHQLQLLPH-ADQIVVLDNGR 204

ABC_CcmA_heme_exporter

cd03231

Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...

23-197

4.70e-15

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: 71.76 E-value: 4.70e-15

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARrrpGTEMRSKVQMVFQNPY- 101
Cdd:cd03231   11 DGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQR---DSIARGLLYLGHAPGIk 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 GSLNPRQKVgdvlmepliinTKIPASERRERAEAMLVKVGL-GPEHfnRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03231   86 TTLSVLENL-----------RFWHADHSDEQVEEALARVGLnGFED--RPVAQLSAGQQRRVALARLLLSGRPLWILDEP 152

                        170
                 ....*....|....*..
gi 739227338 181 VSALDLSVQAQVLNLLR 197
Cdd:cd03231  153 TTALDKAGVARFAEAMA 169

PRK10762

D-ribose transporter ATP binding protein; Provisional

30-243

1.03e-14

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 73.50 E-value: 1.03e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIA----------------RRRPGT--EMRS 91
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRspqdglangivyisedRKRDGLvlGMSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  92 KVQMV------FQNPYGSLN---PRQKVGDVLMeplIINTKIPASERReraeamlvkVGLgpehfnryphmFSGGQRQRI 162
Cdd:PRK10762 348 KENMSltalryFSRAGGSLKhadEQQAVSDFIR---LFNIKTPSMEQA---------IGL-----------LSGGNQQKV 404

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 163 AIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE-----AVEQGT 237
Cdd:PRK10762 405 AIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRisgefTREQAT 483


                 ....*.
gi 739227338 238 REELFA 243
Cdd:PRK10762 484 QEKLMA 489

PRK15439

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

33-231

1.13e-14

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional

Pssm-ID: 185336 [Multi-domain] Cd Length: 510 Bit Score: 73.55 E-value: 1.13e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNpygslnpRQKVGD 112
Cdd:PRK15439 282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGK--EINALSTAQRLARGLVYLPED-------RQSSGL 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 113 VLMEPLIINTKI-----------PASERR--ERAEAMLvkvGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:PRK15439 353 YLDAPLAWNVCAlthnrrgfwikPARENAvlERYRRAL---NIKFNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDE 429

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739227338 180 PVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:PRK15439 430 PTRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGE 480

ABC_RNaseL_inhibitor_domain2

cd03237

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

25-237

2.61e-14

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: 70.90 E-value: 2.61e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  25 RMVQALKGIDFAVE-----RGKTLAIVGESGSGKSTLARIIA-LIDPaSGGELKIDG-----QPVDIARRRPGTE---MR 90
Cdd:cd03237    5 TMKKTLGEFTLEVEggsisESEVIGILGPNGIGKTTFIKMLAgVLKP-DEGDIEIELdtvsyKPQYIKADYEGTVrdlLS 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  91 SKVQMVFQNPYGSLNprqkvgdvLMEPLIINtKIPASERREraeamlvkvglgpehfnryphmFSGGQRQRIAIARALML 170
Cdd:cd03237   84 SITKDFYTHPYFKTE--------IAKPLQIE-QILDREVPE----------------------LSGGELQRVAIAACLSK 132

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 171 NPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISkGEAVEQGT 237
Cdd:cd03237  133 DADIYLLDEPSAYLDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE-GEPSVNGV 198

LptB

COG1137

ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...

23-246

4.05e-14

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

Pssm-ID: 440752 [Multi-domain] Cd Length: 240 Bit Score: 70.06 E-value: 4.05e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarrrpgTEM----RSKVQM--- 95
Cdd:COG1137   14 GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDI--------THLpmhkRARLGIgyl 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  96 -----VFQNpygsLNprqkVGDVLMEPLIInTKIPASERRERAEAMLVKVGLgpEHFNRYPHM-FSGGQRQRIAIARALM 169
Cdd:COG1137   84 pqeasIFRK----LT----VEDNILAVLEL-RKLSKKEREERLEELLEEFGI--THLRKSKAYsLSGGERRRVEIARALA 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 170 LNPALLVLDEPVSALD-LSVqAQVLNLLRDLQEefeltyvfvsHDLSV------VRY---IADDVMVISKGEAVEQGTRE 239
Cdd:COG1137  153 TNPKFILLDEPFAGVDpIAV-ADIQKIIRHLKE----------RGIGVlitdhnVREtlgICDRAYIISEGKVLAEGTPE 221


                 ....*..
gi 739227338 240 ELFADPK 246
Cdd:COG1137  222 EILNNPL 228

PLN03211

ABC transporter G-25; Provisional

30-236

4.25e-14

ABC transporter G-25; Provisional

Pssm-ID: 215634 [Multi-domain] Cd Length: 659 Bit Score: 72.22 E-value: 4.25e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIAlidpasgGELKIDG--QPVDIARRRPGTEMRSKVQMVFQNP--YGSLN 105
Cdd:PLN03211  84 LNGVTGMASPGEILAVLGPSGSGKSTLLNALA-------GRIQGNNftGTILANNRKPTKQILKRTGFVTQDDilYPHLT 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVgdVLMEPLIINTKIPASERRERAEAMLVKVGLGP-EHF---NRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:PLN03211 157 VRETL--VFCSLLRLPKSLTKQEKILVAESVISELGLTKcENTiigNSFIRGISGGERKRVSIAHEMLINPSLLILDEPT 234

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 182 SALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQG 236
Cdd:PLN03211 235 SGLDATAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFG 289

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

30-243

8.12e-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: 71.52 E-value: 8.12e-14

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGqpVDIARrrPGT-EMRSKVQMVFQNPY---GSL- 104
Cdd:TIGR00957 1302 LRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDG--LNIAK--IGLhDLRFKITIIPQDPVlfsGSLr 1377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   105 ---NPRQKVGD--VLMEPLIINTK-----IPASERRERAEamlvkvglGPEHFnryphmfSGGQRQRIAIARALMLNPAL 174
Cdd:TIGR00957 1378 mnlDPFSQYSDeeVWWALELAHLKtfvsaLPDKLDHECAE--------GGENL-------SVGQRQLVCLARALLRKTKI 1442

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338   175 LVLDEPVSALDLSVQAQVLNLLRdlqEEFE-LTYVFVSHDL-SVVRYIAddVMVISKGEAVEQGTREELFA 243
Cdd:TIGR00957 1443 LVLDEATAAVDLETDNLIQSTIR---TQFEdCTVLTIAHRLnTIMDYTR--VIVLDKGEVAEFGAPSNLLQ 1508

ABCC_SUR1_N

cd03290

ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...

16-230

1.48e-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: 68.13 E-value: 1.48e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  16 VPGGLFGGARMVQALKGIDFAVERGKTLAIVGESGSGKSTLA-RIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQ 94
Cdd:cd03290    3 VTNGYFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  95 MVFQNPYgSLNPRQKVGDVLMEPLiintkipaseRRERAEAMLVKVGLGPEhFNRYPH-----------MFSGGQRQRIA 163
Cdd:cd03290   83 YAAQKPW-LLNATVEENITFGSPF----------NKQRYKAVTDACSLQPD-IDLLPFgdqteigergiNLSGGQRQRIC 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 164 IARALMLNPALLVLDEPVSALDLSV-----QAQVLNLLRDLQEefelTYVFVSHDLSVVRYiADDVMVISKG 230
Cdd:cd03290  151 VARALYQNTNIVFLDDPFSALDIHLsdhlmQEGILKFLQDDKR----TLVLVTHKLQYLPH-ADWIIAMKDG 217

PRK13549

xylose transporter ATP-binding subunit; Provisional

33-231

1.62e-13

xylose transporter ATP-binding subunit; Provisional

Pssm-ID: 184134 [Multi-domain] Cd Length: 506 Bit Score: 69.96 E-value: 1.62e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDP-ASGGELKIDGQPVDIarRRPGTEMRSKVQMVFQNpygslnpRQKVG 111
Cdd:PRK13549 281 VSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPgRWEGEIFIDGKPVKI--RNPQQAIAQGIAMVPED-------RKRDG 351

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 112 DVLMEPLIINTKIPASER-------RERAEAMLVKVGLGPEHFnRYPHMF------SGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK13549 352 IVPVMGVGKNITLAALDRftggsriDDAAELKTILESIQRLKV-KTASPElaiarlSGGNQQKAVLAKCLLLNPKILILD 430

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:PRK13549 431 EPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGK 482

xylG

TIGR02633

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...

33-231

1.76e-13

Pssm-ID: 131681 [Multi-domain] Cd Length: 500 Bit Score: 69.85 E-value: 1.76e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDP-ASGGELKIDGQPVDIarRRPGTEMRSKVQMVFQNpygslnpRQKVG 111
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGAYPgKFEGNVFINGKPVDI--RNPAQAIRAGIAMVPED-------RKRHG 349

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  112 DVLMEPLIINTKIPASER-----RERAEAMLVKVGLGPEHFN-RYPHMF------SGGQRQRIAIARALMLNPALLVLDE 179
Cdd:TIGR02633 350 IVPILGVGKNITLSVLKSfcfkmRIDAAAELQIIGSAIQRLKvKTASPFlpigrlSGGNQQKAVLAKMLLTNPRVLILDE 429

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 739227338  180 PVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:TIGR02633 430 PTRGVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGK 480

PTZ00265

multidrug resistance protein (mdr1); Provisional

27-243

1.77e-13

multidrug resistance protein (mdr1); Provisional

Pssm-ID: 240339 [Multi-domain] Cd Length: 1466 Bit Score: 70.44 E-value: 1.77e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIdpasgGELKIDGQpvdIARRRPGTEMRSKVQM----------- 95
Cdd:PTZ00265 1181 VPIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLMRF-----YDLKNDHH---IVFKNEHTNDMTNEQDyqgdeeqnvgm 1252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   96 -------------------VFQNP------------YGSLNPRQKVGDVLMEPLIINTKIPASERRERAEAMLVKV---- 140
Cdd:PTZ00265 1253 knvnefsltkeggsgedstVFKNSgkilldgvdicdYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEDATREDVkrac 1332

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  141 ------------------GLGPehfnrYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEE 202
Cdd:PTZ00265 1333 kfaaidefieslpnkydtNVGP-----YGKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDK 1407

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 739227338  203 FELTYVFVSHDLSVVRYiADDVMVISK----GEAVE-QGTREELFA 243
Cdd:PTZ00265 1408 ADKTIITIAHRIASIKR-SDKIVVFNNpdrtGSFVQaHGTHEELLS 1452

ABCC_SUR2

cd03288

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...

30-250

2.14e-13

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: 68.40 E-value: 2.14e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLA----RIIALIDpasgGELKIDGqpVDIARRrPGTEMRSKVQMVFQNPY---G 102
Cdd:cd03288   37 LKHVKAYIKPGQKVGICGRTGSGKSSLSlaffRMVDIFD----GKIVIDG--IDISKL-PLHTLRSRLSIILQDPIlfsG 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 S----LNPRQKVGD-VLMEPL-IINTKIPASERRERAEAMLVKVGlgpehfnrypHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:cd03288  110 SirfnLDPECKCTDdRLWEALeIAQLKNMVKSLPGGLDAVVTEGG----------ENFSVGQRQLFCLARAFVRKSSILI 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 177 LDEPVSALDLS----VQAQVLNLLRDlqeefeLTYVFVSHDLSVVrYIADDVMVISKGEAVEQGTREELFADPKHPYT 250
Cdd:cd03288  180 MDEATASIDMAteniLQKVVMTAFAD------RTVVTIAHRVSTI-LDADLVLVLSRGILVECDTPENLLAQEDGVFA 250

araG

PRK11288

L-arabinose ABC transporter ATP-binding protein AraG;

22-240

2.28e-13

L-arabinose ABC transporter ATP-binding protein AraG;

Pssm-ID: 183077 [Multi-domain] Cd Length: 501 Bit Score: 69.55 E-value: 2.28e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  22 GGARM-VQALKG------IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIarRRPGTEMRSKVq 94
Cdd:PRK11288 254 GEVRLrLDGLKGpglrepISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDI--RSPRDAIRAGI- 330

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  95 mvfqnpygSLNP--RQKVGDVLMEPLIINTKIPA-----------SERRERAEA------MLVKVglgPEHfnRYPHMF- 154
Cdd:PRK11288 331 --------MLCPedRKAEGIIPVHSVADNINISArrhhlragcliNNRWEAENAdrfirsLNIKT---PSR--EQLIMNl 397

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVE 234
Cdd:PRK11288 398 SGGNQQKAILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQ-GVAVLFVSSDLPEVLGVADRIVVMREGRIAG 476


                 ....*.
gi 739227338 235 QGTREE 240
Cdd:PRK11288 477 ELAREQ 482

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

37-237

3.15e-13

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: 69.43 E-value: 3.15e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  37 VERGKTLAIVGESGSGKSTLARIIAlidpasgGELKIDGQPVDIARR--------RPGTEMRskvqmvfqnpygslnprq 108
Cdd:COG1245  363 IREGEVLGIVGPNGIGKTTFAKILA-------GVLKPDEGEVDEDLKisykpqyiSPDYDGT------------------ 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 kVGDVLMEplIINTKIPASerreRAEAMLVKvGLGPEH-FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLS 187
Cdd:COG1245  418 -VEEFLRS--ANTDDFGSS----YYKTEIIK-PLGLEKlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVE 489

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 739227338 188 VQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISkGEAVEQGT 237
Cdd:COG1245  490 QRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGH 538

PRK03695

vitamin B12-transporter ATPase; Provisional

35-240

3.30e-13

vitamin B12-transporter ATPase; Provisional

Pssm-ID: 235150 [Multi-domain] Cd Length: 248 Bit Score: 67.65 E-value: 3.30e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  35 FAVERGKTLAIVGESGSGKST-LARIIALIDpaSGGELKIDGQPV------DIARRRP--GTEMRSKVQM-VFQnpYGSL 104
Cdd:PRK03695  17 AEVRAGEILHLVGPNGAGKSTlLARMAGLLP--GSGSIQFAGQPLeawsaaELARHRAylSQQQTPPFAMpVFQ--YLTL 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 NPRQKVgdvlmepliiNTKIPASERRERAEAmlvkVGLGPEhFNRYPHMFSGGQRQRIAIARALM-----LNPA--LLVL 177
Cdd:PRK03695  93 HQPDKT----------RTEAVASALNEVAEA----LGLDDK-LGRSVNQLSGGEWQRVRLAAVVLqvwpdINPAgqLLLL 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREE 240
Cdd:PRK03695 158 DEPMNSLDVAQQAALDRLLSELCQQ-GIAVVMSSHDLNHTLRHADRVWLLKQGKLLASGRRDE 219

Rli1

COG1245

Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...

36-227

3.82e-13

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: 69.04 E-value: 3.82e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  36 AVERGKTLAIVGESGSGKSTLARIIAlidpasgGELK-----IDGQPV--DIARRRPGTEMRS--------------KVQ 94
Cdd:COG1245   95 VPKKGKVTGILGPNGIGKSTALKILS-------GELKpnlgdYDEEPSwdEVLKRFRGTELQDyfkklangeikvahKPQ 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  95 MVfqnpygSLNPRQ---KVGDVLMEpliintkipASER---RERAEAmlvkvgLGPEHF-NRYPHMFSGGQRQRIAIARA 167
Cdd:COG1245  168 YV------DLIPKVfkgTVRELLEK---------VDERgklDELAEK------LGLENIlDRDISELSGGELQRVAIAAA 226

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 168 LMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFelTYVF-VSHDLSVVRYIADDVMVI 227
Cdd:COG1245  227 LLRDADFYFFDEPSSYLDIYQRLNVARLIRELAEEG--KYVLvVEHDLAILDYLADYVHIL 285

PRK13537

nodulation factor ABC transporter ATP-binding protein NodI;

32-243

5.54e-13

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237420 [Multi-domain] Cd Length: 306 Bit Score: 67.52 E-value: 5.54e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  32 GIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPvdIARRRPGTEMRSKVQMVFQNpygsLNPRQKVg 111
Cdd:PRK13537  25 GLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEP--VPSRARHARQRVGVVPQFDN----LDPDFTV- 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 112 dvlMEPLIINTK---IPASERRERAEAMLVKVGLGPEHFNRYPHMfSGGQRQRIAIARALMLNPALLVLDEPVSALDLSV 188
Cdd:PRK13537  98 ---RENLLVFGRyfgLSAAAARALVPPLLEFAKLENKADAKVGEL-SGGMKRRLTLARALVNDPDVLVLDEPTTGLDPQA 173

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 189 QAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFA 243
Cdd:PRK13537 174 RHLMWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVIEEGRKIAEGAPHALIE 227

MK0520

COG2401

ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...

30-234

6.94e-13

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

Pssm-ID: 441957 [Multi-domain] Cd Length: 222 Bit Score: 66.14 E-value: 6.94e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEmrskvqmvfqnpygSLNPRQK 109
Cdd:COG2401   46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDNQFGREASLID--------------AIGRKGD 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 VGDVLmepliintkipaserreraeAMLVKVGLG--PEHFNRYPHMfSGGQRQRIAIARALMLNPALLVLDEPVSALDlS 187
Cdd:COG2401  112 FKDAV--------------------ELLNAVGLSdaVLWLRRFKEL-STGQKFRFRLALLLAERPKLLVIDEFCSHLD-R 169

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 739227338 188 VQAQVLNL-LRDLQEEFELTYVFVSHDLSVVRYIADDVMVI-SKGEAVE 234
Cdd:COG2401  170 QTAKRVARnLQKLARRAGITLVVATHHYDVIDDLQPDLLIFvGYGGVPE 218

livF

PRK11614

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

27-244

7.91e-13

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

Pssm-ID: 183231 [Multi-domain] Cd Length: 237 Bit Score: 66.44 E-value: 7.91e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKVQMVfqnPYGS-LN 105
Cdd:PRK11614  18 IQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGK--DITDWQTAKIMREAVAIV---PEGRrVF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLMEPLIINTKIPASERRERAeamlvkVGLGPEHFNRYPH---MFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK11614  93 SRMTVEENLAMGGFFAERDQFQERIKWV------YELFPRLHERRIQragTMSGGEQQMLAIGRALMSQPRLLLLDEPSL 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK11614 167 GLAPIIIQQIFDTIEQLREQ-GMTIFLVEQNANQALKLADRGYVLENGHVVLEDTGDALLAN 227

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

39-237

9.21e-13

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 9.21e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  39 RGKTLAIVGESGSGKSTLARIIA-LIDPASG---GELKIDGQPVDIarrRPGTEMRskvqmvfqnpygslnprqkVGDVL 114
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLAgVLKPDEGevdPELKISYKPQYI---KPDYDGT-------------------VEDLL 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 115 MEpliINTKIPASERRERaeamLVKvGLGPEH-FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVL 193
Cdd:PRK13409 422 RS---ITDDLGSSYYKSE----IIK-PLQLERlLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 739227338 194 NLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISkGEAVEQGT 237
Cdd:PRK13409 494 KAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE-GEPGKHGH 536

PRK13409

ribosome biogenesis/translation initiation ATPase RLI;

36-227

1.04e-12

ribosome biogenesis/translation initiation ATPase RLI;

Pssm-ID: 184037 [Multi-domain] Cd Length: 590 Bit Score: 67.91 E-value: 1.04e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  36 AVERGKTLAIVGESGSGKSTLARIIAlidpasgGELK-----IDGQPV--DIARRRPGTEMRS--------KVQMVFQNP 100
Cdd:PRK13409  95 IPKEGKVTGILGPNGIGKTTAVKILS-------GELIpnlgdYEEEPSwdEVLKRFRGTELQNyfkklyngEIKVVHKPQ 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 YGSLNPRQ---KVGDVLMEpliintkipASERRERAEamLVKVgLGPEHF-NRYPHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:PRK13409 168 YVDLIPKVfkgKVRELLKK---------VDERGKLDE--VVER-LGLENIlDRDISELSGGELQRVAIAAALLRDADFYF 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739227338 177 LDEPVSALDLSVQAQVLNLLRDLQEEfelTYVF-VSHDLSVVRYIADDVMVI 227
Cdd:PRK13409 236 FDEPTSYLDIRQRLNVARLIRELAEG---KYVLvVEHDLAVLDYLADNVHIA 284

PRK13536

nodulation factor ABC transporter ATP-binding protein NodI;

32-276

1.04e-12

nodulation factor ABC transporter ATP-binding protein NodI;

Pssm-ID: 237419 [Multi-domain] Cd Length: 340 Bit Score: 67.16 E-value: 1.04e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  32 GIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDiARRRPGtemRSKVQMVFQnpYGSLNPRQKVG 111
Cdd:PRK13536  59 GLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVP-ARARLA---RARIGVVPQ--FDNLDLEFTVR 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 112 DVL--------MEPLIINTKIPASERRERAEAML-VKVGLgpehfnryphmFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK13536 133 ENLlvfgryfgMSTREIEAVIPSLLEFARLESKAdARVSD-----------LSGGMKRRLTLARALINDPQLLILDEPTT 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELF-------------ADPKH-- 247
Cdd:PRK13536 202 GLDPHARHLIWERLRSLLARGK-TILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHALIdehigcqvieiygGDPHEls 280

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 739227338 248 ----PYTRQ-------LFAATPitDVDAIRARVERRKAAR 276
Cdd:PRK13536 281 slvkPYARRievsgetLFCYAP--DPEQVRVQLRGRAGLR 318

ABCG_PDR_domain2

cd03232

Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...

28-199

2.53e-12

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: 64.19 E-value: 2.53e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIAL--IDPASGGELKIDGQPVDIA-RRRPGtemrskvqMVFQNPygSL 104
Cdd:cd03232   21 QLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGrkTAGVITGEILINGRPLDKNfQRSTG--------YVEQQD--VH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 NPRQKVgdvlMEPLIINTKIpaseRreraeamlvkvGLGPEhfnryphmfsggQRQRIAIARALMLNPALLVLDEPVSAL 184
Cdd:cd03232   91 SPNLTV----REALRFSALL----R-----------GLSVE------------QRKRLTIGVELAAKPSILFLDEPTSGL 139

                        170
                 ....*....|....*
gi 739227338 185 DLSVQAQVLNLLRDL 199
Cdd:cd03232  140 DSQAAYNIVRFLKKL 154

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

30-224

2.60e-12

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: 66.50 E-value: 2.60e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGElkidgqpvdiARRRPGTemrsKVQMVFQNPYgsLNPRQK 109
Cdd:TIGR03719  21 LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGE----------ARPQPGI----KVGYLPQEPQ--LDPTKT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  110 VGDVLMEPLiintkipaSERR---ERAEAMLVKVGLGPEHFN--------------------------------RYP--- 151
Cdd:TIGR03719  85 VRENVEEGV--------AEIKdalDRFNEISAKYAEPDADFDklaaeqaelqeiidaadawdldsqleiamdalRCPpwd 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  152 ---HMFSGGQRQRIAIARALMLNPALLVLDEPVSALDlsvqAQ-VLNLLRDLQeEFELTYVFVSHDlsvvRYIADDV 224
Cdd:TIGR03719 157 advTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AEsVAWLERHLQ-EYPGTVVAVTHD----RYFLDNV 224

PRK10762

D-ribose transporter ATP binding protein; Provisional

1-231

2.85e-12

D-ribose transporter ATP binding protein; Provisional

Pssm-ID: 236755 [Multi-domain] Cd Length: 501 Bit Score: 66.57 E-value: 2.85e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   1 MSIVVKGKGITRDYhvPGglfggarmVQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDI 80
Cdd:PRK10762   1 MQALLQLKGIDKAF--PG--------VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  81 ARRRPGTEmrSKVQMVFQnpygSLN--PRQKVGDVLM---EPLIINTKIPASERRERAEAMLVKVGLgPEHFNRYPHMFS 155
Cdd:PRK10762  71 NGPKSSQE--AGIGIIHQ----ELNliPQLTIAENIFlgrEFVNRFGRIDWKKMYAEADKLLARLNL-RFSSDKLVGELS 143

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 156 GGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:PRK10762 144 IGEQQMVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIRELKSQ-GRGIVYISHRLKEIFEICDDVTVFRDGQ 218

PLN03130

ABC transporter C family member; Provisional

30-244

2.96e-12

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 66.69 E-value: 2.96e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKS----TLARIIALidpaSGGELKIDGqpVDIARRrpG-TEMRSKVQMVFQNPY--- 101
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSsmlnALFRIVEL----ERGRILIDG--CDISKF--GlMDLRKVLGIIPQAPVlfs 1326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  102 GS----LNPRQKVGDV-LMEPLiintkipasER-------RERAEAMLVKVGLGPEHFnryphmfSGGQRQRIAIARALM 169
Cdd:PLN03130 1327 GTvrfnLDPFNEHNDAdLWESL---------ERahlkdviRRNSLGLDAEVSEAGENF-------SVGQRQLLSLARALL 1390

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  170 LNPALLVLDEPVSALDLSVQAQVLNLLRdlqEEFE-LTYVFVSHDLSVVryI-ADDVMVISKGEAVEQGTREELFAD 244
Cdd:PLN03130 1391 RRSKILVLDEATAAVDVRTDALIQKTIR---EEFKsCTMLIIAHRLNTI--IdCDRILVLDAGRVVEFDTPENLLSN 1462

hmuV

PRK13547

heme ABC transporter ATP-binding protein;

30-237

3.01e-12

heme ABC transporter ATP-binding protein;

Pssm-ID: 184132 [Multi-domain] Cd Length: 272 Bit Score: 65.23 E-value: 3.01e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG--------GELKIDGQPV------DIARRRPGTEMRSKVQM 95
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGGaprgarvtGDVTLNGEPLaaidapRLARLRAVLPQAAQPAF 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  96 VFQnpygslnprqkvgdvlMEPLIINTKIPASER--------RERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARA 167
Cdd:PRK13547  97 AFS----------------AREIVLLGRYPHARRagalthrdGEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARV 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 168 L---------MLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGT 237
Cdd:PRK13547 160 LaqlwpphdaAQPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGA 238

MRP_assoc_pro

TIGR00957

multi drug resistance-associated protein (MRP); This model describes multi drug ...

30-243

6.57e-12

Pssm-ID: 188098 [Multi-domain] Cd Length: 1522 Bit Score: 65.74 E-value: 6.57e-12

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    30 LKGIDFAVERGKTLAIVGESGSGKSTLarIIALIdpasgGEL-KIDGQpvdiarrrpgTEMRSKVQMVFQNPY---GSLN 105
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSL--LSALL-----AEMdKVEGH----------VHMKGSVAYVPQQAWiqnDSLR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   106 PRQKVGDVLMEP----------LIINTKI-PASERREraeamlvkvgLGPEHFNryphmFSGGQRQRIAIARALMLNPAL 174
Cdd:TIGR00957  717 ENILFGKALNEKyyqqvleacaLLPDLEIlPSGDRTE----------IGEKGVN-----LSGGQKQRVSLARAVYSNADI 781

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   175 LVLDEPVSALDLSVQAQVL-NLLRDLQEEFELTYVFVSHDLSVVRYIaDDVMVISKGEAVEQGTREELFA 243
Cdd:TIGR00957  782 YLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMGSYQELLQ 850

ABC_RNaseL_inhibitor_domain1

cd03236

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...

40-227

7.85e-12

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: 63.92 E-value: 7.85e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  40 GKTLAIVGESGSGKSTLARIIAlidpasgGEL-----KIDGQPV--DIARRRPGTEMRS--------KVQMVFQNPYGSL 104
Cdd:cd03236   26 GQVLGLVGPNGIGKSTALKILA-------GKLkpnlgKFDDPPDwdEILDEFRGSELQNyftkllegDVKVIVKPQYVDL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 105 NPRQ---KVGDVLMEpliintkipASERRERAEamLVKVgLGPEH-FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:cd03236   99 IPKAvkgKVGELLKK---------KDERGKLDE--LVDQ-LELRHvLDRNIDQLSGGELQRVAIAAALARDADFYFFDEP 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEFELTYVfVSHDLSVVRYIADDVMVI 227
Cdd:cd03236  167 SSYLDIKQRLNAARLIRELAEDDNYVLV-VEHDLAVLDYLSDYIHCL 212

PLN03130

ABC transporter C family member; Provisional

155-244

8.31e-12

ABC transporter C family member; Provisional

Pssm-ID: 215595 [Multi-domain] Cd Length: 1622 Bit Score: 65.53 E-value: 8.31e-12

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLN--LLRDLQEEfelTYVFVSHDLSVVRYIaDDVMVISKGEA 232
Cdd:PLN03130  742 SGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFDkcIKDELRGK---TRVLVTNQLHFLSQV-DRIILVHEGMI 817

                          90
                  ....*....|..
gi 739227338  233 VEQGTREELFAD 244
Cdd:PLN03130  818 KEEGTYEELSNN 829

sufC

PRK09580

cysteine desulfurase ATPase component; Reviewed

30-236

8.54e-12

cysteine desulfurase ATPase component; Reviewed

Pssm-ID: 181965 [Multi-domain] Cd Length: 248 Bit Score: 63.66 E-value: 8.54e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALID--PASGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNPY------ 101
Cdd:PRK09580  17 LRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGK--DLLELSPEDRAGEGIFMAFQYPVeipgvs 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 102 ------GSLNPRQKVGDvlMEPL-------IINTKIPASERRERAEAMLVKVGlgpehfnryphmFSGGQRQRIAIARAL 168
Cdd:PRK09580  95 nqfflqTALNAVRSYRG--QEPLdrfdfqdLMEEKIALLKMPEDLLTRSVNVG------------FSGGEKKRNDILQMA 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 169 MLNPALLVLDEPVSALD---LSVQAQVLNLLRDLQEEFeltyVFVSHDLSVVRYIADD-VMVISKGEAVEQG 236
Cdd:PRK09580 161 VLEPELCILDESDSGLDidaLKIVADGVNSLRDGKRSF----IIVTHYQRILDYIKPDyVHVLYQGRIVKSG 228

ABCC_CFTR1

cd03291

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...

30-241

1.56e-11

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.

Pssm-ID: 213258 [Multi-domain] Cd Length: 282 Bit Score: 63.34 E-value: 1.56e-11

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQ---PVDIARRRPGTemrSKVQMVFQNPYGSLNP 106
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGRisfSSQFSWIMPGT---IKENIIFGVSYDEYRY 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 RQKVGDVLMEPLIinTKIPASERRERAEAMLVkvglgpehfnryphmFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03291  130 KSVVKACQLEEDI--TKFPEKDNTVLGEGGIT---------------LSGGQRARISLARAVYKDADLYLLDSPFGYLDV 192

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 187 SVQAQVLN--LLRDLQEEfelTYVFVSHDLSVVRyIADDVMVISKGEAVEQGTREEL 241
Cdd:cd03291  193 FTEKEIFEscVCKLMANK---TRILVTSKMEHLK-KADKILILHEGSSYFYGTFSEL 245

PLN03232

ABC transporter C family member; Provisional

30-242

4.97e-11

ABC transporter C family member; Provisional

Pssm-ID: 215640 [Multi-domain] Cd Length: 1495 Bit Score: 63.07 E-value: 4.97e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLarIIALIdpasgGELK-IDGQPVDIarrrpgtemRSKVQMVFQNPYgslnprq 108
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSL--ISAML-----GELShAETSSVVI---------RGSVAYVPQVSW------- 689

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  109 KVGDVLMEPLIINTKIpASERRERA---EAMLVKVGLGPEH----FNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPV 181
Cdd:PLN03232  690 IFNATVRENILFGSDF-ESERYWRAidvTALQHDLDLLPGRdlteIGERGVNISGGQKQRVSMARAVYSNSDIYIFDDPL 768

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338  182 SALDLSVQAQVLNLLrdLQEEFE-LTYVFVSHDLSVVRYIaDDVMVISKGEAVEQGTREELF 242
Cdd:PLN03232  769 SALDAHVAHQVFDSC--MKDELKgKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827

3a01203

TIGR00954

Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...

35-219

5.38e-11

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: 62.84 E-value: 5.38e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   35 FAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDgqpvdiarrRPGtemrsKVQMVFQNPYGSLNPRQkvgDVL 114
Cdd:TIGR00954 473 FEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKP---------AKG-----KLFYVPQRPYMTLGTLR---DQI 535

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  115 MEPLIINTKIPASERRERAEAMLVKVGL--------GPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:TIGR00954 536 IYPDSSEDMKRRGLSDKDLEQILDNVQLthileregGWSAVQDWMDVLSGGEKQRIAMARLFYHKPQFAILDECTSAVSV 615

                         170       180       190
                  ....*....|....*....|....*....|...
gi 739227338  187 SVQAQVLNLLRdlqeEFELTYVFVSHDLSVVRY 219
Cdd:TIGR00954 616 DVEGYMYRLCR----EFGITLFSVSHRKSLWKY 644

ABCG_PDR_domain1

cd03233

First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...

30-236

1.54e-10

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: 59.20 E-value: 1.54e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG---GELKIDGQPVDIARRRPgtemRSKVQMVFQNpygslnp 106
Cdd:cd03233   23 LKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNVsveGDIHYNGIPYKEFAEKY----PGEIIYVSEE------- 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 rqkvgDVLMEPLIIntkipaserRERAEAMLVKVGlgpehfNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL 186
Cdd:cd03233   92 -----DVHFPTLTV---------RETLDFALRCKG------NEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDS 151

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739227338 187 SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRY-IADDVMVISKGEAVEQG 236
Cdd:cd03233  152 STALEILKCIRTMADVLKTTTFVSLYQASDEIYdLFDKVLVLYEGRQIYYG 202

PRK09700

D-allose ABC transporter ATP-binding protein AlsA;

31-243

1.61e-10

D-allose ABC transporter ATP-binding protein AlsA;

Pssm-ID: 182036 [Multi-domain] Cd Length: 510 Bit Score: 60.95 E-value: 1.61e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  31 KGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQpvDIARRRPGTEMRSKVQMVFQNP-----YGSLN 105
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGK--DISPRSPLDAVKKGMAYITESRrdngfFPNFS 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGdvlMEPLIINTK-------IPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK09700 358 IAQNMA---ISRSLKDGGykgamglFHEVDEQRTAENQRELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFD 434

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGE------AVEQGTREELFA 243
Cdd:PRK09700 435 EPTRGIDVGAKAEIYKVMRQLADDGK-VILMVSSELPEIITVCDRIAVFCEGRltqiltNRDDMSEEEIMA 504

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

34-244

1.69e-10

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 61.18 E-value: 1.69e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  34 DFAVERGKTLAIVGESGSGKSTLARIIAlidpasgGELkidgqpvdiarrrpgTEMRSKVQMVFQNPYG-SLNPRQKV-- 110
Cdd:PRK10938  23 SLTLNAGDSWAFVGANGSGKSALARALA-------GEL---------------PLLSGERQSQFSHITRlSFEQLQKLvs 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 111 -------GDVLMEPL---------IINTKIPASERRERAEAMLvkvGLGPEHFNRYPHMfSGGQRQRIAIARALMLNPAL 174
Cdd:PRK10938  81 dewqrnnTDMLSPGEddtgrttaeIIQDEVKDPARCEQLAQQF---GITALLDRRFKYL-STGETRKTLLCQALMSEPDL 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 175 LVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK10938 157 LILDEPFDGLDVASRQQLAELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225

PRK11147

ABC transporter ATPase component; Reviewed

34-221

1.81e-10

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 61.12 E-value: 1.81e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  34 DFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDgQPVDIARRRpgtemrskvqmvfQNPygslnPR------ 107
Cdd:PRK11147  23 ELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDLIVARLQ-------------QDP-----PRnvegtv 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 --------QKVGDVLMEPLIINTKIpASERRERAEAMLVKVGLGPEHFNRY----------------PHM----FSGGQR 159
Cdd:PRK11147  84 ydfvaegiEEQAEYLKRYHDISHLV-ETDPSEKNLNELAKLQEQLDHHNLWqlenrinevlaqlgldPDAalssLSGGWL 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 160 QRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDlqeeFELTYVFVSHDLSVVRYIA 221
Cdd:PRK11147 163 RKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLKT----FQGSIIFISHDRSFIRNMA 220

PLN03073

ABC transporter F family; Provisional

31-232

2.80e-10

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 60.64 E-value: 2.80e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  31 KGIDFAVERGKTLAIVGESGSGKSTLARIIAlidpasgGELkidgQPVDiarrrpGTEMRS-KVQM-VF-QNPYGSLnpr 107
Cdd:PLN03073 526 KNLNFGIDLDSRIAMVGPNGIGKSTILKLIS-------GEL----QPSS------GTVFRSaKVRMaVFsQHHVDGL--- 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 qkvgDVLMEPLIINTKIPASERRERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL- 186
Cdd:PLN03073 586 ----DLSSNPLLYMMRCFPGVPEQKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLd 661

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 739227338 187 SVQAQVLNLLRdlqeeFELTYVFVSHDLSVVRYIADDVMVISKGEA 232
Cdd:PLN03073 662 AVEALIQGLVL-----FQGGVLMVSHDEHLISGSVDELWVVSEGKV 702

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

30-241

3.15e-10

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: 60.69 E-value: 3.15e-10

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    30 LKGIDFAVERGKTLAIVGESGSGKSTLARII-ALIDPASG-----GELKIDGQPVDIArrrPGTemrSKVQMVFQNPYGS 103
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMImGELEPSEGkikhsGRISFSPQTSWIM---PGT---IKDNIIFGLSYDE 515

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   104 LNPRQKVGDVLMEPLIinTKIPaserrERAEAMLVKVGLgpehfnryphMFSGGQRQRIAIARALMLNPALLVLDEPVSA 183
Cdd:TIGR01271  516 YRYTSVIKACQLEEDI--ALFP-----EKDKTVLGEGGI----------TLSGGQRARISLARAVYKDADLYLLDSPFTH 578

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   184 LDLSVQAQVLN--LLRDLQEEfelTYVFVSHDLSVVRYiADDVMVISKGEAVEQGTREEL 241
Cdd:TIGR01271  579 LDVVTEKEIFEscLCKLMSNK---TRILVTSKLEHLKK-ADKILLLHEGVCYFYGTFSEL 634

PLN03073

ABC transporter F family; Provisional

40-186

4.93e-10

ABC transporter F family; Provisional

Pssm-ID: 215558 [Multi-domain] Cd Length: 718 Bit Score: 59.87 E-value: 4.93e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  40 GKTLAIVGESGSGKSTLARIIAL--ID--PASGGELKIDGQPV-------------DIARRRPgteMRSKVQMVFQNPyg 102
Cdd:PLN03073 203 GRHYGLVGRNGTGKTTFLRYMAMhaIDgiPKNCQILHVEQEVVgddttalqcvlntDIERTQL---LEEEAQLVAQQR-- 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMEPLIINTKIPASERRE----------------RAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIAR 166
Cdd:PLN03073 278 ELEFETETGKGKGANKDGVDKDAVSQRLEeiykrlelidaytaeaRAASILAGLSFTPEMQVKATKTFSGGWRMRIALAR 357

                        170       180
                 ....*....|....*....|
gi 739227338 167 ALMLNPALLVLDEPVSALDL 186
Cdd:PLN03073 358 ALFIEPDLLLLDEPTNHLDL 377

ABC_UvrA

cd03238

ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...

21-230

5.94e-10

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

Pssm-ID: 213205 [Multi-domain] Cd Length: 176 Bit Score: 56.95 E-value: 5.94e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  21 FGGARmVQALKGIDFAVERGKTLAIVGESGSGKSTLAR-IIAlidpASGGELKIDGQPVdiarrrpgtemrskvqmvfqn 99
Cdd:cd03238    3 VSGAN-VHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNeGLY----ASGKARLISFLPK--------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 100 pygslNPRQKVgdVLMEPLiintkipaserreraeAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNP--ALLVL 177
Cdd:cd03238   57 -----FSRNKL--IFIDQL----------------QFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPpgTLFIL 113

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 739227338 178 DEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYiADDVMVISKG 230
Cdd:cd03238  114 DEPSTGLHQQDINQLLEVIKGLIDL-GNTVILIEHNLDVLSS-ADWIIDFGPG 164

ABC_UvrA_I

cd03270

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...

23-237

9.74e-10

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: 57.27 E-value: 9.74e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARmVQALKGIDFAVERGKTLAIVGESGSGKSTLAriialIDP--ASGGELKIDGQPVdIARRRPGTEMRSKVQMV---- 96
Cdd:cd03270    5 GAR-EHNLKNVDVDIPRNKLVVITGVSGSGKSSLA-----FDTiyAEGQRRYVESLSA-YARQFLGQMDKPDVDSIegls 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  97 ----FQNPYGSLNPRQKVGDVlmepliinTKIPASER--------RERAEaMLVKVGLGPEHFNRYPHMFSGGQRQRIAI 164
Cdd:cd03270   78 paiaIDQKTTSRNPRSTVGTV--------TEIYDYLRllfarvgiRERLG-FLVDVGLGYLTLSRSAPTLSGGEAQRIRL 148

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 165 ARAL--MLNPALLVLDEPVSAL---DLSVQAQVLNLLRDLQEefelTYVFVSHDLSVVRyIADDVMVISKGEAVEQGT 237
Cdd:cd03270  149 ATQIgsGLTGVLYVLDEPSIGLhprDNDRLIETLKRLRDLGN----TVLVVEHDEDTIR-AADHVIDIGPGAGVHGGE 221

ABC_RNaseL_inhibitor

cd03222

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...

155-227

1.47e-09

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: 56.04 E-value: 1.47e-09

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 739227338 155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYIADDVMVI 227
Cdd:cd03222   73 SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTALVVEHDLAVLDYLSDRIHVF 145

PvdE

COG4615

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...

33-83

1.73e-09

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: 57.89 E-value: 1.73e-09

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARR 83
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNR 401

PRK10522

multidrug transporter membrane component/ATP-binding component; Provisional

29-179

3.56e-09

multidrug transporter membrane component/ATP-binding component; Provisional

Pssm-ID: 236707 [Multi-domain] Cd Length: 547 Bit Score: 56.90 E-value: 3.56e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASgGELKIDGQPVDIARRRpgtEMRSKVQMVFQnpygslnpr 107
Cdd:PRK10522 338 SVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTgLYQPQS-GEILLDGKPVTAEQPE---DYRKLFSAVFT--------- 404

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 108 qkvgDV-LMEPLIINTKIPASErrERAEAMLVKVGLGP----EHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:PRK10522 405 ----DFhLFDQLLGPEGKPANP--ALVEKWLERLKMAHklelEDGRISNLKLSKGQKKRLALLLALAEERDILLLDE 475

AAA

smart00382

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

39-231

4.36e-09

Pssm-ID: 214640 [Multi-domain] Cd Length: 148 Bit Score: 54.30 E-value: 4.36e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    39 RGKTLAIVGESGSGKSTLARIIA-LIDPASGGELKIDGQPVDIARRrpgtemrskvqmvfqnpygslnprqkvgdvlmep 117
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALArELGPPGGGVIYIDGEDILEEVL---------------------------------- 46

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   118 liintkipaserreraeamlvkVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLR 197
Cdd:smart00382  47 ----------------------DQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEE 104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 739227338   198 D-----LQEEFELTYVFVSHDLSV-----VRYIADDVMVISKGE 231
Cdd:smart00382 105 LrllllLKSEKNLTVILTTNDEKDlgpalLRRRFDRRIVLLLIL 148

PRK11147

ABC transporter ATPase component; Reviewed

30-213

4.86e-09

ABC transporter ATPase component; Reviewed

Pssm-ID: 236861 [Multi-domain] Cd Length: 635 Bit Score: 56.88 E-value: 4.86e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARI-IALIDPASGgelkidgqpvdiaRRRPGTemrsKVQMVFQNPY-GSLNPR 107
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLmLGQLQADSG-------------RIHCGT----KLEVAYFDQHrAELDPE 397

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 108 QKVGDVLmepliintkipASERREraeamlVKVGLGPEHFNRYPHMF--------------SGGQRQRIAIARaLMLNPA 173
Cdd:PRK11147 398 KTVMDNL-----------AEGKQE------VMVNGRPRHVLGYLQDFlfhpkramtpvkalSGGERNRLLLAR-LFLKPS 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 739227338 174 -LLVLDEPVSALDLsvqaQVLNLLRDLQEEFELTYVFVSHD 213
Cdd:PRK11147 460 nLLILDEPTNDLDV----ETLELLEELLDSYQGTVLLVSHD 496

PRK13543

heme ABC exporter ATP-binding protein CcmA;

33-186

6.64e-09

heme ABC exporter ATP-binding protein CcmA;

Pssm-ID: 184129 [Multi-domain] Cd Length: 214 Bit Score: 54.85 E-value: 6.64e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRrpgtemrsKVQMVFQNPYGSLNPRQKVgd 112
Cdd:PRK13543  30 LDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDR--------SRFMAYLGHLPGLKADLST-- 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 739227338 113 vlMEPLIINTKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARaLMLNPA-LLVLDEPVSALDL 186
Cdd:PRK13543 100 --LENLHFLCGLHGRRAKQMPGSALAIVGLA-GYEDTLVRQLSAGQKKRLALAR-LWLSPApLWLLDEPYANLDL 170

tagH

PRK13545

teichoic acids export protein ATP-binding subunit; Provisional

29-241

8.17e-09

teichoic acids export protein ATP-binding subunit; Provisional

Pssm-ID: 184130 [Multi-domain] Cd Length: 549 Bit Score: 56.05 E-value: 8.17e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIArrrPGTEMRSKVQMVFQNPYGSLN--- 105
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIA---ISSGLNGQLTGIENIELKGLMmgl 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 106 PRQKVGDVLmePLIIntkipaserrERAEamlvkVGlgpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13545 116 TKEKIKEII--PEII----------EFAD-----IG---KFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 186 LSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:PRK13545 176 QTFTKKCLDKMNEFKEQGK-TIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEV 230

PRK13540

cytochrome c biogenesis protein CcmA; Provisional

30-185

9.48e-09

cytochrome c biogenesis protein CcmA; Provisional

Pssm-ID: 184127 [Multi-domain] Cd Length: 200 Bit Score: 54.19 E-value: 9.48e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIA-LIDPASGgELKIDGQPVDIARrrpgteMRSKVQMVFQNPYGSLNPRQ 108
Cdd:PRK13540  17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAgLLNPEKG-EILFERQSIKKDL------CTYQKQLCFVGHRSGINPYL 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 109 kvgdVLMEPLIINTKIPASERRERAEAMLVKVGlgpeHFNRYP-HMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:PRK13540  90 ----TLRENCLYDIHFSPGAVGITELCRLFSLE----HLIDYPcGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALD 159

40850658_otr

NF000106

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

27-241

1.04e-08

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

Pssm-ID: 411078 [Multi-domain] Cd Length: 351 Bit Score: 55.51 E-value: 1.04e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGelkidgQPVDI----ARRRPGTEMRSKVQMVFQNPYG 102
Cdd:NF000106  26 VKAVDGVDLDVREGTVLGVLGP*GAA**RGALPAHV*GPDAGR------RPWRF*twcANRRALRRTIG*HRPVR*GRRE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVgdvlmepLIINTKIPASER--RERAEAMLVKVGLgPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEP 180
Cdd:NF000106 100 SFSGRENL-------YMIGR*LDLSRKdaRARADELLERFSL-TEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEP 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 181 VSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:NF000106 172 TTGLDPRTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDEL 231

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

33-185

1.22e-08

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 55.52 E-value: 1.22e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPV---DIA-RRRPGTEMRSkvqmvFqNPYGSLNPRQ 108
Cdd:NF033858 285 VSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVdagDIAtRRRVGYMSQA-----F-SLYGELTVRQ 358

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338 109 KVgdVLMEPLIintKIPASERRERAEAMLVKVGLGpEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALD 185
Cdd:NF033858 359 NL--ELHARLF---HLPAAEIAARVAEMLERFDLA-DVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVD 429

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

45-224

2.08e-08

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 54.74 E-value: 2.08e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  45 IVGESGSGKSTLARIIALIDPASGGElkidgqpvdiARRRPGTemrsKVQMVFQNPYgsLNPRQKVGDVLMEPLiintki 124
Cdd:PRK11819  38 VLGLNGAGKSTLLRIMAGVDKEFEGE----------ARPAPGI----KVGYLPQEPQ--LDPEKTVRENVEEGV------ 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 125 paSERRE---RAEAMLVKVGLGPEHFN--------------------------------RYPHM------FSGGQRQRIA 163
Cdd:PRK11819  96 --AEVKAaldRFNEIYAAYAEPDADFDalaaeqgelqeiidaadawdldsqleiamdalRCPPWdakvtkLSGGERRRVA 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 164 IARALMLNPALLVLDEPVSALDlsvqAQ-VLNLLRDLQeEFELTYVFVSHDlsvvRYIADDV 224
Cdd:PRK11819 174 LCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLH-DYPGTVVAVTHD----RYFLDNV 226

PTZ00243

ABC transporter; Provisional

30-241

2.73e-08

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 54.78 E-value: 2.73e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRpgtEMRSKVQMVFQNPY---GSLnp 106
Cdd:PTZ00243 1326 LRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLR---ELRRQFSMIPQDPVlfdGTV-- 1400

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  107 RQKVgDVLME--PLIINTKIPASERRER----AEAMLVKVGLGPEHfnryphmFSGGQRQRIAIARALM-LNPALLVLDE 179
Cdd:PTZ00243 1401 RQNV-DPFLEasSAEVWAALELVGLRERvaseSEGIDSRVLEGGSN-------YSVGQRQLMCMARALLkKGSGFILMDE 1472

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 739227338  180 PVS----ALDLSVQAQVLNLLRdlqeefELTYVFVSHDL-SVVRYiaDDVMVISKGEAVEQGTREEL 241
Cdd:PTZ00243 1473 ATAnidpALDRQIQATVMSAFS------AYTVITIAHRLhTVAQY--DKIIVMDHGAVAEMGSPREL 1531

ABC_UvrA_II

cd03271

ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...

23-222

4.11e-08

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

Pssm-ID: 213238 [Multi-domain] Cd Length: 261 Bit Score: 53.00 E-value: 4.11e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  23 GARmVQALKGIDFAVERGKTLAIVGESGSGKSTLarIIALIDPASGGELKIDGQPVDIARRRPGTEMRSKVQMVFQNPYG 102
Cdd:cd03271    5 GAR-ENNLKNIDVDIPLGVLTCVTGVSGSGKSSL--INDTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVIVIDQSPIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SlNPR-------------------------------------QKVGDVL-M---EPLIINTKIPASERRERAeamLVKVG 141
Cdd:cd03271   82 R-TPRsnpatytgvfdeirelfcevckgkrynretlevrykgKSIADVLdMtveEALEFFENIPKIARKLQT---LCDVG 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 142 LGPEHFNRYPHMFSGGQRQRIAIARALmLNPA----LLVLDEPVSALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVV 217
Cdd:cd03271  158 LGYIKLGQPATTLSGGEAQRIKLAKEL-SKRStgktLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVI 235


                 ....*...
gi 739227338 218 R---YIAD 222
Cdd:cd03271  236 KcadWIID 243

ABC_ABC_ChvD

TIGR03719

ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...

3-213

4.52e-08

Pssm-ID: 274744 [Multi-domain] Cd Length: 552 Bit Score: 53.79 E-value: 4.52e-08

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    3 IVVKGKGITRDYhvpgglfgGARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIdGQPVDIAr 82
Cdd:TIGR03719 321 KVIEAENLTKAF--------GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETVKLA- 388

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   83 rrpgtemrskvqMVFQNpYGSLNPRQKVGDVLMEPLII----NTKIPAserreRAeamlvKVGLgpehFN-------RYP 151
Cdd:TIGR03719 389 ------------YVDQS-RDALDPNKTVWEEISGGLDIiklgKREIPS-----RA-----YVGR----FNfkgsdqqKKV 441

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338  152 HMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLsvqaQVLNLLRDLQEEFELTYVFVSHD 213
Cdd:TIGR03719 442 GQLSGGERNRVHLAKTLKSGGNVLLLDEPTNDLDV----ETLRALEEALLNFAGCAVVISHD 499

PRK15064

ABC transporter ATP-binding protein; Provisional

30-243

5.34e-08

ABC transporter ATP-binding protein; Provisional

Pssm-ID: 237894 [Multi-domain] Cd Length: 530 Bit Score: 53.36 E-value: 5.34e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIAlidpasgGELKIDGQPVDIARRrpgtemrSKVQMVFQNPYGSLNprqk 109
Cdd:PRK15064 335 FKNLNLLLEAGERLAIIGENGVGKTTLLRTLV-------GELEPDSGTVKWSEN-------ANIGYYAQDHAYDFE---- 396

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 110 vGDV-LMEPLIINTKIPASERRERAeaMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDL-S 187
Cdd:PRK15064 397 -NDLtLFDWMSQWRQEGDDEQAVRG--TLGRLLFSQDDIKKSVKVLSGGEKGRMLFGKLMMQKPNVLVMDEPTNHMDMeS 473

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 188 VQAqvLNL-LrdlqEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVE-QGTREELFA 243
Cdd:PRK15064 474 IES--LNMaL----EKYEGTLIFVSHDREFVSSLATRIIEITPDGVVDfSGTYEEYLR 525

PRK10636

putative ABC transporter ATP-binding protein; Provisional

130-227

2.82e-07

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 51.32 E-value: 2.82e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 130 RERAEAMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVqaqVLNLLRDLQeEFELTYVF 209
Cdd:PRK10636 126 RSRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQALICRSDLLLLDEPTNHLDLDA---VIWLEKWLK-SYQGTLIL 201

                         90
                 ....*....|....*...
gi 739227338 210 VSHDLSVVRYIADDVMVI 227
Cdd:PRK10636 202 ISHDRDFLDPIVDKIIHI 219

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

44-237

3.00e-07

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: 51.55 E-value: 3.00e-07

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    44 AIVGESGSGKSTLARIIALIDPASGGELKIDGQPV----DIARRRPGteMRSKVQMVFQNPygslnprqkvgdVLMEPLI 119
Cdd:TIGR01257  960 AFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIetnlDAVRQSLG--MCPQHNILFHHL------------TVAEHIL 1025

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   120 INTKIPASERRE---RAEAMLVKVGLGPEHfNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLL 196
Cdd:TIGR01257 1026 FYAQLKGRSWEEaqlEMEAMLEDTGLHHKR-NEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLL 1104

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 739227338   197 rdLQEEFELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGT 237
Cdd:TIGR01257 1105 --LKYRSGRTIIMSTHHMDEADLLGDRIAIISQGRLYCSGT 1143

PRK13546

teichoic acids export ABC transporter ATP-binding subunit TagH;

29-244

3.63e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;

Pssm-ID: 184131 [Multi-domain] Cd Length: 264 Bit Score: 50.20 E-value: 3.63e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIA------RRRPGTEmRSKVQMVfqnpyg 102
Cdd:PRK13546  39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGEVSVIAisaglsGQLTGIE-NIEFKML------ 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 103 SLNPRQKVGDVLMePLIIntkipasERRERAEAMLVKVglgpehfnrypHMFSGGQRQRIAIARALMLNPALLVLDEPVS 182
Cdd:PRK13546 112 CMGFKRKEIKAMT-PKII-------EFSELGEFIYQPV-----------KKYSSGMRAKLGFSINITVNPDILVIDEALS 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 739227338 183 ALDLSVQAQVLNLLRDLQEEFElTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK13546 173 VGDQTFAQKCLDKIYEFKEQNK-TIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233

PRK10636

putative ABC transporter ATP-binding protein; Provisional

154-231

4.19e-07

putative ABC transporter ATP-binding protein; Provisional

Pssm-ID: 236729 [Multi-domain] Cd Length: 638 Bit Score: 50.94 E-value: 4.19e-07

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 739227338 154 FSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRDlqeeFELTYVFVSHDLSVVRYIADDVMVISKGE 231
Cdd:PRK10636 431 FSGGEKARLVLALIVWQRPNLLLLDEPTNHLDLDMRQALTEALID----FEGALVVVSHDRHLLRSTTDDLYLVHDGK 504

oligo_HPY

pfam08352

Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found ...

233-261

7.47e-07

Oligopeptide/dipeptide transporter, C-terminal region; This family features a region found towards the C-terminus of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid.

Pssm-ID: 400588 [Multi-domain] Cd Length: 65 Bit Score: 45.47 E-value: 7.47e-07

                          10        20
                  ....*....|....*....|....*....
gi 739227338  233 VEQGTREELFADPKHPYTRQLFAATPITD 261
Cdd:pfam08352   1 VEEGPTDDILENPLHPYTRALLNSVPRLD 29

PRK10938

putative molybdenum transport ATP-binding protein ModF; Provisional

30-212

2.20e-06

putative molybdenum transport ATP-binding protein ModF; Provisional

Pssm-ID: 182852 [Multi-domain] Cd Length: 490 Bit Score: 48.47 E-value: 2.20e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASG-------GELKIDGQPV-DIARR------------RPGTEM 89
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGDHPQGYsndltlfGRRRGSGETIwDIKKHigyvssslhldyRVSTSV 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  90 RSKVQMVFqnpYGSLNPRQKVGDvlmepliintkipaserRERAEAM--LVKVGLGPEHFNRYPHMFSGGQrQRIA-IAR 166
Cdd:PRK10938 356 RNVILSGF---FDSIGIYQAVSD-----------------RQQKLAQqwLDILGIDKRTADAPFHSLSWGQ-QRLAlIVR 414

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 739227338 167 ALMLNPALLVLDEPVSALDLSVQAQVLNLLRDLQEEFELTYVFVSH 212
Cdd:PRK10938 415 ALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSH 460

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

128-246

2.55e-06

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: 48.47 E-value: 2.55e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  128 ERRERAEaMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARAL--MLNPALLVLDEPVSAL---DLSVQAQVLNLLRDLQEe 202
Cdd:TIGR00630 464 EIRERLG-FLIDVGLDYLSLSRAAGTLSGGEAQRIRLATQIgsGLTGVLYVLDEPSIGLhqrDNRRLINTLKRLRDLGN- 541

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 739227338  203 felTYVFVSHDLSVVRyIADDVMVISK------GEAVEQGTREELFADPK 246
Cdd:TIGR00630 542 ---TLIVVEHDEDTIR-AADYVIDIGPgagehgGEVVASGTPEEILANPD 587

PRK11819

putative ABC transporter ATP-binding protein; Reviewed

2-213

3.19e-06

putative ABC transporter ATP-binding protein; Reviewed

Pssm-ID: 236992 [Multi-domain] Cd Length: 556 Bit Score: 48.19 E-value: 3.19e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   2 SIVVKGKGITRDYhvpgglfgGARMVqaLKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIdGQPVDIA 81
Cdd:PRK11819 322 DKVIEAENLSKSF--------GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKI-GETVKLA 390

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  82 rrrpgtemrskvqMVFQNpYGSLNPRQKVGDVLMEPL-II---NTKIPAserreRAeamLV------------KVGlgpe 145
Cdd:PRK11819 391 -------------YVDQS-RDALDPNKTVWEEISGGLdIIkvgNREIPS-----RA---YVgrfnfkggdqqkKVG---- 444

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 739227338 146 hfnryphMFSGGQRQRIAIARALMLNPALLVLDEPVSALDlsvqaqvLNLLRDLQE---EFELTYVFVSHD 213
Cdd:PRK11819 445 -------VLSGGERNRLHLAKTLKQGGNVLLLDEPTNDLD-------VETLRALEEallEFPGCAVVISHD 501

oligo_HPY

TIGR01727

oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model ...

231-259

4.07e-06

oligopeptide/dipeptide ABC transporter, ATP-binding protein, C-terminal domain; This model represents a domain found in the C-terminal regions of oligopeptide ABC transporter ATP binding proteins, immediately following the ATP-binding domain (pfam00005). All characterized members appear able to be involved in the transport of oligopeptides or dipeptides. Some are important for sporulation or antibiotic resistance. Some dipeptide transporters also act on the heme precursor delta-aminolevulinic acid. [Transport and binding proteins, Amino acids, peptides and amines]

Pssm-ID: 213647 [Multi-domain] Cd Length: 87 Bit Score: 44.28 E-value: 4.07e-06

                          10        20
                  ....*....|....*....|....*....
gi 739227338  231 EAVEQGTREELFADPKHPYTRQLFAATPI 259
Cdd:TIGR01727   1 KIVETGPAEEIFKNPLHPYTKALLSAIPT 29

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

29-232

5.53e-06

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 47.42 E-value: 5.53e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  29 ALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVD--------------IARRRPGTEMRSKVQ 94
Cdd:PRK10982 263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINnhnaneainhgfalVTEERRSTGIYAYLD 342

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  95 MVFQNPYGSLNP-RQKVGdvlmepLIINTKIpASERRERAEAMLVKVglgPEHFNRYPHMfSGGQRQRIAIARALMLNPA 173
Cdd:PRK10982 343 IGFNSLISNIRNyKNKVG------LLDNSRM-KSDTQWVIDSMRVKT---PGHRTQIGSL-SGGNQQKVIIGRWLLTQPE 411

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 739227338 174 LLVLDEPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEA 232
Cdd:PRK10982 412 ILMLDEPTRGIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469

rim_protein

TIGR01257

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...

36-241

8.38e-06

Pssm-ID: 130324 [Multi-domain] Cd Length: 2272 Bit Score: 47.32 E-value: 8.38e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    36 AVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVdiarrrpgtemRSKVQMVFQNpYGSLNPRQKVGDVLM 115
Cdd:TIGR01257 1961 GVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSI-----------LTNISDVHQN-MGYCPQFDAIDDLLT 2028

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   116 --EPLIINTK---IPASERRERAEAMLVKVGLGPeHFNRYPHMFSGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQA 190
Cdd:TIGR01257 2029 grEHLYLYARlrgVPAEEIEKVANWSIQSLGLSL-YADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARR 2107

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 739227338   191 QVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREEL 241
Cdd:TIGR01257 2108 MLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKGAFQCLGTIQHL 2157

3a01205

TIGR00956

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

28-199

1.20e-05

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

Pssm-ID: 273362 [Multi-domain] Cd Length: 1394 Bit Score: 46.64 E-value: 1.20e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIA------LIdpaSGGELKIDGQPVDIA-RRRPG----TEMRSKVQMV 96
Cdd:TIGR00956  777 VILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAervttgVI---TGGDRLVNGRPLDSSfQRSIGyvqqQDLHLPTSTV 853

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    97 FQNPYGSLNPRQ--------------KVGDVLmepliintkipasERRERAEAMLVKVGLGpehfnryphmFSGGQRQRI 162
Cdd:TIGR00956  854 RESLRFSAYLRQpksvsksekmeyveEVIKLL-------------EMESYADAVVGVPGEG----------LNVEQRKRL 910

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 739227338   163 AIARALMLNPALLV-LDEPVSALDLSVQAQVLNLLRDL 199
Cdd:TIGR00956  911 TIGVELVAKPKLLLfLDEPTSGLDSQTAWSICKLMRKL 948

ABC_Rad50

cd03240

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...

33-229

1.29e-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: 44.91 E-value: 1.29e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFavERGKTLaIVGESGSGKSTlarIIALIDPASGGEL---KIDGQPV-DIARRrpgTEMRSKVQMVFQNPYGslnprq 108
Cdd:cd03240   18 IEF--FSPLTL-IVGQNGAGKTT---IIEALKYALTGELppnSKGGAHDpKLIRE---GEVRAQVKLAFENANG------ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 109 kvgdvlmEPLIINTKIPASErreraEAMLVKVG----LGPEHFNRyphmFSGGQRQ------RIAIARALMLNPALLVLD 178
Cdd:cd03240   83 -------KKYTITRSLAILE-----NVIFCHQGesnwPLLDMRGR----CSGGEKVlasliiRLALAETFGSNCGILALD 146

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 739227338 179 EPVSALDL-SVQAQVLNLLRDLQEEFELTYVFVSHDLSVVRYiADDVMVISK 229
Cdd:cd03240  147 EPTTNLDEeNIEESLAEIIEERKSQKNFQLIVITHDEELVDA-ADHIYRVEK 197

CFTR_protein

TIGR01271

cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...

30-211

2.21e-05

Pssm-ID: 273530 [Multi-domain] Cd Length: 1490 Bit Score: 45.67 E-value: 2.21e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338    30 LKGIDFAVERGKTLAIVGESGSGKSTLarIIALIDPASG-GELKIDG---QPVDIARRRPGTEMRSKVQMVFQNPY-GSL 104
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTL--LSALLRLLSTeGEIQIDGvswNSVTLQTWRKAFGVIPQKVFIFSGTFrKNL 1312

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   105 NPRQKVGD-----VLMEpliINTKIPASERRERAEAMLVKVGlgpehfnrypHMFSGGQRQRIAIARALMLNPALLVLDE 179
Cdd:TIGR01271 1313 DPYEQWSDeeiwkVAEE---VGLKSVIEQFPDKLDFVLVDGG----------YVLSNGHKQLMCLARSILSKAKILLLDE 1379

                          170       180       190
                   ....*....|....*....|....*....|..
gi 739227338   180 PVSALDlSVQAQVLNllRDLQEEFELTYVFVS 211
Cdd:TIGR01271 1380 PSAHLD-PVTLQIIR--KTLKQSFSNCTVILS 1408

PRK10982

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

27-244

2.48e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional

Pssm-ID: 182880 [Multi-domain] Cd Length: 491 Bit Score: 45.11 E-value: 2.48e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIALIDPASGGELKIDGQPVDIARRRPGTEmrSKVQMVFQnpygSLNP 106
Cdd:PRK10982  11 VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKEALE--NGISMVHQ----ELNL 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 107 -RQK-------VGDVLMEPLIINTKipasERRERAEAMLVKVGLGPEHFNRYPHMfSGGQRQRIAIARALMLNPALLVLD 178
Cdd:PRK10982  85 vLQRsvmdnmwLGRYPTKGMFVDQD----KMYRDTKAIFDELDIDIDPRAKVATL-SVSQMQMIEIAKAFSYNAKIVIMD 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338 179 EPVSALDLSVQAQVLNLLRDLQEEfELTYVFVSHDLSVVRYIADDVMVISKGEAVEQGTREELFAD 244
Cdd:PRK10982 160 EPTSSLTEKEVNHLFTIIRKLKER-GCGIVYISHKMEEIFQLCDEITILRDGQWIATQPLAGLTMD 224

ABCC_CFTR2

cd03289

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...

30-214

3.01e-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: 44.46 E-value: 3.01e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  30 LKGIDFAVERGKTLAIVGESGSGKSTL-ARIIALIDpaSGGELKIDG---QPVDIARRRPGTEMRSKVQMVFQ------- 98
Cdd:cd03289   20 LENISFSISPGQRVGLLGRTGSGKSTLlSAFLRLLN--TEGDIQIDGvswNSVPLQKWRKAFGVIPQKVFIFSgtfrknl 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  99 NPYGSLNPRQ--KVGDVLMEPLIINtKIPAserreRAEAMLVKVGlgpehfnrypHMFSGGQRQRIAIARALMLNPALLV 176
Cdd:cd03289   98 DPYGKWSDEEiwKVAEEVGLKSVIE-QFPG-----QLDFVLVDGG----------CVLSHGHKQLMCLARSVLSKAKILL 161

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 739227338 177 LDEPVSALDlSVQAQVLNllRDLQEEF-ELTYVFVSHDL 214
Cdd:cd03289  162 LDEPSAHLD-PITYQVIR--KTLKQAFaDCTVILSEHRI 197

PLN03140

ABC transporter G family member; Provisional

27-198

8.77e-05

ABC transporter G family member; Provisional

Pssm-ID: 215599 [Multi-domain] Cd Length: 1470 Bit Score: 44.07 E-value: 8.77e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   27 VQALKGIDFAVERGKTLAIVGESGSGKSTLARIIA------LIDpasgGELKIDGQPvdiarrrpgtemrsKVQMVF--- 97
Cdd:PLN03140  893 LQLLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAgrktggYIE----GDIRISGFP--------------KKQETFari 954

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338   98 -----QNPYGSlnPRQKVgdvlMEPLIINT--KIPASERRERA-----EAM-LVK--------VGLgpehfnryPHM--F 154
Cdd:PLN03140  955 sgyceQNDIHS--PQVTV----RESLIYSAflRLPKEVSKEEKmmfvdEVMeLVEldnlkdaiVGL--------PGVtgL 1020

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 739227338  155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLNLLRD 198
Cdd:PLN03140 1021 STEQRKRLTIAVELVANPSIIFMDEPTSGLDARAAAIVMRTVRN 1064

ABC_Class2

cd03227

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...

39-214

9.15e-05

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.

Pssm-ID: 213194 [Multi-domain] Cd Length: 162 Bit Score: 41.96 E-value: 9.15e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  39 RGKTLAIVGESGSGKSTLARIIALIdpASGgelkidgqpvdiarrrpgtemrskvQMVFQNPYGSLNPRQKVGDVlmepl 118
Cdd:cd03227   20 EGSLTIITGPNGSGKSTILDAIGLA--LGG-------------------------AQSATRRRSGVKAGCIVAAV----- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 119 iintkipaserreRAEAMLVKVGLgpehfnryphmfSGGQRQRIAIARALML---NPA-LLVLDEPVSALDLSVQAQVLN 194
Cdd:cd03227   68 -------------SAELIFTRLQL------------SGGEKELSALALILALaslKPRpLYILDEIDRGLDPRDGQALAE 122

                        170       180
                 ....*....|....*....|
gi 739227338 195 LLRDLQEEFeLTYVFVSHDL 214
Cdd:cd03227  123 AILEHLVKG-AQVIVITHLP 141

COG3950

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

33-212

1.09e-04

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

Pssm-ID: 443150 [Multi-domain] Cd Length: 276 Bit Score: 42.68 E-value: 1.09e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  33 IDFAVERGKTLaIVGESGSGKSTLARIIAL--------IDPASGGELKI-DGQPVDIA---------RR------RPGTE 88
Cdd:COG3950   19 IDFDNPPRLTV-LVGENGSGKTTLLEAIALalsgllsrLDDVKFRKLLIrNGEFGDSAklilyygtsRLlldgplKKLER 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  89 MRSKVQMVFQNPYGSLNPRQKVGDVL---------------------MEPL--IINTKIPASE--RRERAEAMLVKVGLG 143
Cdd:COG3950   98 LKEEYFSRLDGYDSLLDEDSNLREFLewlreyledlenklsdeldekLEAVreALNKLLPDFKdiRIDRDPGRLVILDKN 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 144 PEHFNryPHMFSGGQRQRIAIA-----RALMLNPAL--------LVL-DEPvsalDLS--VQAQVlNLLRDLQEEF-ELT 206
Cdd:COG3950  178 GEELP--LNQLSDGERSLLALVgdlarRLAELNPALenplegegIVLiDEI----DLHlhPKWQR-RILPDLRKIFpNIQ 250


                 ....*.
gi 739227338 207 YVFVSH 212
Cdd:COG3950  251 FIVTTH 256

PTZ00243

ABC transporter; Provisional

155-278

1.62e-04

ABC transporter; Provisional

Pssm-ID: 240327 [Multi-domain] Cd Length: 1560 Bit Score: 43.23 E-value: 1.62e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  155 SGGQRQRIAIARALMLNPALLVLDEPVSALDLSVQAQVLnllrdlqEEFEL------TYVFVSHDLSVVRYiADDVMVIS 228
Cdd:PTZ00243  784 SGGQKARVSLARAVYANRDVYLLDDPLSALDAHVGERVV-------EECFLgalagkTRVLATHQVHVVPR-ADYVVALG 855

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 739227338  229 KGEAVEQGTREElfadpkhpytrqlFAATPITdvDAIRARVERRKAARQA 278
Cdd:PTZ00243  856 DGRVEFSGSSAD-------------FMRTSLY--ATLAAELKENKDSKEG 890

ABC2_perm_RbbA

NF033858

ribosome-associated ATPase/putative transporter RbbA;

27-180

1.74e-04

ribosome-associated ATPase/putative transporter RbbA;

Pssm-ID: 468210 [Multi-domain] Cd Length: 907 Bit Score: 42.80 E-value: 1.74e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  27 VQALKGIDFAVERGKTLAIVGESGSGKSTLariIALIdpaSG------GELKIDGQpvDIARRRpgteMRSKVQmvfqnp 100
Cdd:NF033858  14 TVALDDVSLDIPAGCMVGLIGPDGVGKSSL---LSLI---AGarkiqqGRVEVLGG--DMADAR----HRRAVC------ 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338 101 ygslnPR-----QKVGDVLMEPLIINTKI---------PASERRERAEAMLVKVGLGPehF-NRYPHMFSGGQRQRIAIA 165
Cdd:NF033858  76 -----PRiaympQGLGKNLYPTLSVFENLdffgrlfgqDAAERRRRIDELLRATGLAP--FaDRPAGKLSGGMKQKLGLC 148

                        170
                 ....*....|....*
gi 739227338 166 RALMLNPALLVLDEP 180
Cdd:NF033858 149 CALIHDPDLLILDEP 163

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

123-241

3.09e-04

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 41.92 E-value: 3.09e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  123 KIPASERRERAeamLVKVGLGPEHFNRYPHMFSGGQRQRIAIARALM---LNPALLVLDEPVSALDLSVQAQVLNLLRDL 199
Cdd:TIGR00630 802 AVPSISRKLQT---LCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRL 878

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 739227338  200 QEEFElTYVFVSHDLSVVRyIADDVMVISK------GEAVEQGTREEL 241
Cdd:TIGR00630 879 VDKGN-TVVVIEHNLDVIK-TADYIIDLGPeggdggGTVVASGTPEEV 924

PRK00635

excinuclease ABC subunit A; Provisional

135-243

7.70e-04

excinuclease ABC subunit A; Provisional

Pssm-ID: 234806 [Multi-domain] Cd Length: 1809 Bit Score: 40.97 E-value: 7.70e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 739227338  135 AMLVKVGLGPEHFNRYPHMFSGGQRQRIAIARAL--MLNPALLVLDEPVSAL---DLSVQAQVLNLLRDLQEefelTYVF 209
Cdd:PRK00635  458 SILIDLGLPYLTPERALATLSGGEQERTALAKHLgaELIGITYILDEPSIGLhpqDTHKLINVIKKLRDQGN----TVLL 533

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 739227338  210 VSHDLSVVRYiADDVMVISK------GEAVEQGTREELFA 243
Cdd:PRK00635  534 VEHDEQMISL-ADRIIDIGPgagifgGEVLFNGSPREFLA 572

ExeA

COG3267

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...

17-58

7.97e-04

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];

Pssm-ID: 442498 [Multi-domain] Cd Length: 261 Bit Score: 40.16 E-value: 7.97e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 739227338  17 PGGLFGGARMVQALKGIDFAVERGKTLA-IVGESGSGKSTLAR 58
Cdd:COG3267   19 PRFLFLSPSHREALARLEYALAQGGGFVvLTGEVGTGKTTLLR 61

COG3910

Predicted ATPase [General function prediction only];

27-69

1.74e-03

Predicted ATPase [General function prediction only];

Pssm-ID: 443116 [Multi-domain] Cd Length: 239 Bit Score: 38.98 E-value: 1.74e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 739227338  27 VQALKGIDFavERGKTLaIVGESGSGKSTLARIIAL---IDPASGG 69
Cdd:COG3910   27 VRNLEGLEF--HPPVTF-FVGENGSGKSTLLEAIAVaagFNPEGGS 69

NACHT

COG5635

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];

28-62

2.80e-03

Predicted NTPase, NACHT family domain [Signal transduction mechanisms];

Pssm-ID: 444362 [Multi-domain] Cd Length: 935 Bit Score: 39.02 E-value: 2.80e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 739227338  28 QALKGIDFAVERGKTLAIVGESGSGKSTLARIIAL 62
Cdd:COG5635  168 ESLKRLELLEAKKKRLLILGEPGSGKTTLLRYLAL 202

UvrA

COG0178

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

23-57

3.87e-03

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

Pssm-ID: 439948 [Multi-domain] Cd Length: 941 Bit Score: 38.47 E-value: 3.87e-03

                         10        20        30
                 ....*....|....*....|....*....|....*
gi 739227338  23 GARmVQALKGIDFAVERGKTLAIVGESGSGKSTLA 57
Cdd:COG0178   10 GAR-EHNLKNIDVDIPRNKLVVITGLSGSGKSSLA 43

RNA_helicase

pfam00910

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...

45-101

5.72e-03

RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding during viral RNA replication. Members of this family are found in a variety of single stranded RNA viruses.

Pssm-ID: 459992 Cd Length: 102 Bit Score: 35.66 E-value: 5.72e-03

                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 739227338   45 IVGESGSGKSTLARIIALIDPASGGELK---------------IDGQPV----DIARRRPGTEMRSKVQMVFQNPY 101
Cdd:pfam00910   3 LYGPPGCGKSTLAKYLARALLKKLGLPKdsvysrnpdddfwdgYTGQPVviidDFGQNPDGPDEAELIRLVSSTPY 78

AAA_29

pfam13555

P-loop containing region of AAA domain;

19-67

8.49e-03

P-loop containing region of AAA domain;

Pssm-ID: 433304 [Multi-domain] Cd Length: 61 Bit Score: 34.11 E-value: 8.49e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 739227338   19 GLFGGARMVQALKGIdfavergkTLaIVGESGSGKSTL--ArIIALIDPAS 67
Cdd:pfam13555  10 GTFDGHTIPIDPRGN--------TL-LTGPSGSGKSTLldA-IQTLLVPAK 50

uvra

TIGR00630

excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...

23-57

9.56e-03

Pssm-ID: 273184 [Multi-domain] Cd Length: 925 Bit Score: 37.30 E-value: 9.56e-03

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 739227338   23 GARmVQALKGIDFAVERGKTLAIVGESGSGKSTLA 57
Cdd:TIGR00630   6 GAR-EHNLKNIDVEIPRDKLVVITGLSGSGKSSLA 39

VirB11-like_ATPase

cd01130

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, ...

33-65

9.58e-03

Type IV secretory pathway component VirB11-like; Type IV secretory pathway component VirB11, and related ATPases. The homohexamer, VirB11 is one of eleven Vir (virulence) proteins, which are required for T-pilus biogenesis and virulence in the transfer of T-DNA from the bacterial Ti (tumor-inducing)-plasmid into plant cells. The pilus is a fibrous cell surface organelle, which mediates adhesion between bacteria during conjugative transfer or between bacteria and host eukaryotic cells during infection. VirB11-related ATPases include Sulfolobus acidocaldarius FlaI, which plays key roles in archaellum (archaeal flagellum) assembly and motility functions, and the pilus assembly proteins CpaF/TadA and TrbB. This alignment contains the C-terminal domain, which is the ATPase.

Pssm-ID: 410874 [Multi-domain] Cd Length: 177 Bit Score: 36.36 E-value: 9.58e-03

                         10        20        30
                 ....*....|....*....|....*....|....
gi 739227338  33 IDFAVERGKTLAIVGESGSGKSTLAR-IIALIDP 65
Cdd:cd01130    5 LRLAVRARKNILISGGTGSGKTTLLNaLLSFIPP 38

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