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Conserved domains on  [gi|504695722|ref|WP_014882824|]
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MULTISPECIES: iron efflux ABC transporter ATP-binding subunit FetA [Enterobacter]

Protein Classification

iron ABC transporter ATP-binding protein FetA( domain architecture ID 11484628)

iron ABC transporter ATP-binding protein FetA is part of the ABC transporter complex FetAB, which may be involved in iron export and enhances resistance to H(2)O(2)-mediated oxidative stress, and is probably responsible for energy coupling to the transport system

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-221 1.37e-158

putative ABC transporter ATP-binding protein YbbL; Provisional


:

Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 437.61  E-value: 1.37e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYR 80
Cdd:PRK10247   1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFDSTVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK10247  81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 161 LDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQPHGGKMQEAN 221
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEAR 221
 
Name Accession Description Interval E-value
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-221 1.37e-158

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 437.61  E-value: 1.37e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYR 80
Cdd:PRK10247   1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFDSTVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK10247  81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 161 LDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQPHGGKMQEAN 221
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEAR 221
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
8-213 7.76e-110

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 313.68  E-value: 7.76e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSV 87
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDSTVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSA 167
Cdd:COG4619   81 QEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 168 LDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQPH 213
Cdd:COG4619  161 LDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 8-211 8.51e-57

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: 179.61  E-value: 8.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVG--YRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA----Y 79
Cdd:cd03255    1 IELKNLSktYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVSYSVQTPSLFDS-TVYDNLLFPWQI--RHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELPLLLagVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDP 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03255  160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELR 214
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 23-166 7.14e-42

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: 138.93  E-value: 7.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLF-DSTVYDNL 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  102 LFPWQIRH--KTPDPERFSADLARFNLPP---DTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:pfam00005  81 RLGLLLKGlsKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 10-210 1.20e-36

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: 129.09  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   10 IEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGkdISTLSPEAY---RQQVS 84
Cdd:TIGR04520   3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweiRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   85 YSVQTPslfD-----STVYDNLLF--------PWQIRHKTPDPerfsadLARFNLPpDTLTKSVSELSGGEKQRVSLIRN 151
Cdd:TIGR04520  81 MVFQNP---DnqfvgATVEDDVAFglenlgvpREEMRKRVDEA------LKLVGME-DFRDREPHLLSGGQKQRVAIAGV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722  152 LQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVM 209
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-210 1.56e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.16  E-value: 1.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  14 GYrtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDistlspeayrqQVSYSVQTPSLF 93
Cdd:NF040873   1 GY--GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DS---TVYDNL-------LFPWQiRHKTPDPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:NF040873  68 DSlplTVRDLVamgrwarRGLWR-RLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 164 ITSALDDANKRNVNEIIHRYVREQnIAVLWVTHDANEITHADDVLTL 210
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-169 1.01e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 66.69  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  16 RTGGTTILNNVSFSLLPGE-FRLItGPSGCGKSTLLKIIASLLTPTSG--KIF---FEGKDISTlspeayRQQVSYSVQT 89
Cdd:NF033858 275 RFGDFTAVDHVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGeaWLFgqpVDAGDIAT------RRRVGYMSQA 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 PSLF-DSTVYDNL-----LFpwqirHKTPD--PERFSADLARFNLPP--DTLTksvSELSGGEKQRVSL----IRNlqfl 155
Cdd:NF033858 348 FSLYgELTVRQNLelharLF-----HLPAAeiAARVAEMLERFDLADvaDALP---DSLPLGIRQRLSLavavIHK---- 415

                        170
                 ....*....|....
gi 504695722 156 PKVLLLDEITSALD 169
Cdd:NF033858 416 PELLILDEPTSGVD 429
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-201 4.96e-11

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: 58.92  E-value: 4.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    32 PGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFegkdistLSPEAYRQQvsysvqtpslfdstvydnllfpwqirhkt 111
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEE----------------------------- 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   112 pdperfsadlARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYV-----RE 186
Cdd:smart00382  45 ----------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkSE 114

                          170
                   ....*....|....*
gi 504695722   187 QNIAVLWVTHDANEI 201
Cdd:smart00382 115 KNLTVILTTNDEKDL 129
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-169 8.36e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.05  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGefR---LItGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlspEAYRQQV 83
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAG--CmvgLI-GPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 S----YSVQT------PSLfdsTVYDNL-----LF-------PWQIRHKTPdperfSADLARFnlppdtLTKSVSELSGG 141
Cdd:NF033858  75 CpriaYMPQGlgknlyPTL---SVFENLdffgrLFgqdaaerRRRIDELLR-----ATGLAPF------ADRPAGKLSGG 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504695722 142 EKQRVS----LIRNlqflPKVLLLDEITSALD 169
Cdd:NF033858 141 MKQKLGlccaLIHD----PDLLILDEPTTGVD 168
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-209 2.37e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.56  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIaSLLTPT---SGKIFFEG-----KDIS--------------TLSPEAyr 80
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL-SGVYPHgsyEGEILFDGevcrfKDIRdsealgiviihqelALIPYL-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 qqvsysvqtpslfdsTVYDNL----------LFPWQIRHKtpdpeRFSADLARFNL--PPDTLtksVSELSGGEKQRVSL 148
Cdd:NF040905  94 ---------------SIAENIflgnerakrgVIDWNETNR-----RARELLAKVGLdeSPDTL---VTDIGVGKQQLVEI 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITHADDVLT 209
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLL-LELKAQGITSIIISHKLNEIRRVADSIT 210
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
116-203 4.08e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 37.79  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 116 RFSAD--LARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLW 193
Cdd:NF000106 122 RARADelLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200

                         90
                 ....*....|..
gi 504695722 194 VTH--DANEITH 203
Cdd:NF000106 201 TQYmeEAEQLAH 212
 
Name Accession Description Interval E-value
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 1-221 1.37e-158

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 437.61  E-value: 1.37e-158
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYR 80
Cdd:PRK10247   1 MQENSPLLQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFDSTVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK10247  81 QQVSYCAQTPTLFGDTVYDNLIFPWQIRNQQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 161 LDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQPHGGKMQEAN 221
Cdd:PRK10247 161 LDEITSALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVITLQPHAGEMQEAR 221
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
8-213 7.76e-110

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 313.68  E-value: 7.76e-110
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSV 87
Cdd:COG4619    1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRRQVAYVP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDSTVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSA 167
Cdd:COG4619   81 QEPALWGGTVRDNLPFPFQLRERKFDRERALELLERLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSA 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 168 LDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQPH 213
Cdd:COG4619  161 LDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERvADRVLTLEAG 207
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
5-211 9.59e-58

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 182.17  E-value: 9.59e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVG--YRTGG--TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE--- 77
Cdd:COG1136    2 SPLLELRNLTksYGTGEgeVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERela 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  78 AYR-QQVSYSVQTPSLFDS-TVYDNLLFPWQIRHKTP--DPERFSADLARFNLpPDTLTKSVSELSGGEKQRVS----LI 149
Cdd:COG1136   82 RLRrRHIGFVFQFFNLLPElTALENVALPLLLAGVSRkeRRERARELLERVGL-GDRLDHRPSQLSGGQQQRVAiaraLV 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 150 RNlqflPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:COG1136  161 NR----PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLR 218
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 8-211 8.51e-57

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: 179.61  E-value: 8.51e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVG--YRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA----Y 79
Cdd:cd03255    1 IELKNLSktYGGGGEKvqALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKElaafR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVSYSVQTPSLFDS-TVYDNLLFPWQI--RHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:cd03255   81 RRHIGFVFQSFNLLPDlTALENVELPLLLagVPKKERRERAEELLERVGL-GDRLNHYPSELSGGQQQRVAIARALANDP 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03255  160 KIILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELR 214
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 1-219 5.37e-52

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 168.34  E-value: 5.37e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVG--YRT--GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP 76
Cdd:COG1116    1 MSAAAPALELRGVSkrFPTggGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  77 EayrqqVSYSVQTPSLFD-STVYDNLLFPWQIRHKTPDPERFSAD--LARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQ 153
Cdd:COG1116   81 D-----RGVVFQEPALLPwLTVLDNVALGLELRGVPKAERRERARelLELVGL-AGFEDAYPHQLSGGMRQRVAIARALA 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLQPHGGKMQE 219
Cdd:COG1116  155 NDPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDVDEaVFLADRVVVLSARPGRIVE 221
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 7-217 1.21e-51

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: 167.53  E-value: 1.21e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYS 86
Cdd:COG1120    1 MLEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELARRIAYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSL-FDSTVYDNLL---FPWQIRHKTPDPE-RFSAD--LARFNLppDTL-TKSVSELSGGEKQRVSLIRNL--QflP 156
Cdd:COG1120   81 PQEPPApFGLTVRELVAlgrYPHLGLFGRPSAEdREAVEeaLERTGL--EHLaDRPVDELSGGERQRVLIARALaqE--P 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGKM 217
Cdd:COG1120  157 PLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLaARYADRLVLL--KDGRI 216
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 10-201 1.33e-51

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: 166.91  E-value: 1.33e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY---RQQVSYS 86
Cdd:cd03261    3 LRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELyrlRRRMGML 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLLFPwqIRHKTPDPERFSADLARFNLP----PDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:cd03261   83 FQSGALFDSlTVFENVAFP--LREHTRLSEEEIREIVLEKLEavglRGAEDLYPAELSGGMKKRVALARALALDPELLLY 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 162 DEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEI 201
Cdd:cd03261  161 DEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTA 200
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 2-219 2.26e-51

ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440740 [Multi-domain]  Cd Length: 514  Bit Score: 173.55  E-value: 2.26e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   2 KDNSAVLTIEDVGYR-----TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP 76
Cdd:COG1123  255 AAAEPLLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSR 334

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  77 E---AYRQQVSYSVQTP--SLF-DSTVYDNLLFPWQIRHKTPDPERfsAD-----LARFNLPPDTLTKSVSELSGGEKQR 145
Cdd:COG1123  335 RslrELRRRVQMVFQDPysSLNpRMTVGDIIAEPLRLHGLLSRAER--RErvaelLERVGLPPDLADRYPHELSGGQRQR 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 146 VSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD---ANEIthADDVLTLqpHGGKMQE 219
Cdd:COG1123  413 VAIARALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDlavVRYI--ADRVAVM--YDGRIVE 485
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 7-219 4.67e-51

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: 164.99  E-value: 4.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVG--YRTGG--TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE---AY 79
Cdd:cd03257    1 LLEVKNLSvsFPTGGgsVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRlrkIR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVS------YSVQTPSLfdsTVYDNLLFPWQIRHKTPDPERFSA----DLARFNLPPDTLTKSVSELSGGEKQRVSLI 149
Cdd:cd03257   81 RKEIQmvfqdpMSSLNPRM---TIGEQIAEPLRIHGKLSKKEARKEavllLLVGVGLPEEVLNRYPHELSGGQRQRVAIA 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695722 150 RNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD---ANEIthADDVLTLqpHGGKMQE 219
Cdd:cd03257  158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDlgvVAKI--ADRVAVM--YAGKIVE 226
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 8-217 1.45e-50

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: 164.04  E-value: 1.45e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYS 86
Cdd:COG1122    1 IELENLSFSyPGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLRELRRKVGLV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPS--LFDSTVYDNLLFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:COG1122   81 FQNPDdqLFAPTVEEDVAFGPENLGLPREeiRERVEEALELVGL-EHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLD 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 163 EITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEIT-HADDVLTLqpHGGKM 217
Cdd:COG1122  160 EPTAGLDPRGRRELLELLKRL-NKEGKTVIIVTHDLDLVAeLADRVIVL--DDGRI 212
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 3-219 1.54e-50

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: 164.00  E-value: 1.54e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE---AY 79
Cdd:COG1127    1 MSEPMIEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKelyEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVSYSVQTPSLFDS-TVYDNLLFPwqIRHKTPDPERFSADLARFNLP----PDTLTKSVSELSGGEKQRVSLIRNLQF 154
Cdd:COG1127   81 RRRIGMLFQGGALFDSlTVFENVAFP--LREHTDLSEAEIRELVLEKLElvglPGAADKMPSELSGGMRKRVALARALAL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 155 LPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEI-THADDVLTLqpHGGKMQE 219
Cdd:COG1127  159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAfAIADRVAVL--ADGKIIA 222
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 10-216 5.25e-50

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: 161.87  E-value: 5.25e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVGYR--TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSV 87
Cdd:cd03225    2 LKNLSFSypDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRRKVGLVF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPS--LFDSTVYDNLLFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVS----LIRNlqflPKVL 159
Cdd:cd03225   82 QNPDdqFFGPTVEEEVAFGLENLGLPEEeiEERVEEALELVGL-EGLRDRSPFTLSGGQKQRVAiagvLAMD----PDIL 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI-THADDVLTLqpHGGK 216
Cdd:cd03225  157 LLDEPTAGLDPAGRRELLELLKK-LKAEGKTIIIVTHDLDLLlELADRVIVL--EDGK 211
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 9-208 3.60e-49

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: 157.79  E-value: 3.60e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   9 TIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYsvq 88
Cdd:cd00267    1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELRRRIGY--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 tpslfdstvydnllfpwqirhktpdperfsadlarfnlppdtltksVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:cd00267   78 ----------------------------------------------VPQLSGGQRQRVALARALLLNPDLLLLDEPTSGL 111

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 169 DDANKRNVNEIIHRYvREQNIAVLWVTHDANEITHADDVL 208
Cdd:cd00267  112 DPASRERLLELLREL-AEEGRTVIIVTHDPELAELAADRV 150
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 8-216 3.78e-49

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


Pssm-ID: 213226 [Multi-domain]  Cd Length: 213  Bit Score: 159.61  E-value: 3.78e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSYSV 87
Cdd:cd03259    1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE--RRNIGMVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFPWQIRhKTPDPE---RFSADLARFNLPPDtLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:cd03259   79 QDYALFPHlTVAENIAFGLKLR-GVPKAEiraRVRELLELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDE 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504695722 164 ITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGK 216
Cdd:cd03259  157 PLSALDAKLREELREELKELQRELGITTIYVTHDQEEaLALADRIAVM--NEGR 208
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 8-219 7.40e-49

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: 159.17  E-value: 7.40e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVG--YRTGG--TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPeayrqQV 83
Cdd:cd03293    1 LEVRNVSktYGGGGgaVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP-----DR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSVQTPSLFD-STVYDNLLFPWQIRHKTPDP--ERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:cd03293   76 GYVFQQDALLPwLTVLDNVALGLELQGVPKAEarERAEELLELVGL-SGFENAYPHQLSGGMRQRVALARALAVDPDVLL 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 161 LDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLQPHGGKMQE 219
Cdd:cd03293  155 LDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEaVFLADRVVVLSARPGRIVA 214
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
8-217 4.23e-48

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 157.92  E-value: 4.23e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGE-FRLItGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYS 86
Cdd:COG1131    1 IEVRGLTKRYGDKTALDGVSLTVEPGEiFGLL-GPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVAR-DPAEVRRRIGYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLLFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:COG1131   79 PQEPALYPDlTVRENLRFFARLYGLPRKeaRERIDELLELFGL-TDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 164 ITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKM 217
Cdd:COG1131  158 PTSGLDPEARRELWELLREL-AAEGKTVLLSTHYLEEAERlCDRVAII--DKGRI 209
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 8-210 1.18e-47

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: 154.46  E-value: 1.18e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:cd03228    1 IEFKNVsfSYPGRPKPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLDLESLRKNIAY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNLLfpwqirhktpdperfsadlarfnlppdtltksvselSGGEKQRVS----LIRNlqflPKVLLL 161
Cdd:cd03228   81 VPQDPFLFSGTIRENIL------------------------------------SGGQRQRIAiaraLLRD----PPILIL 120

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504695722 162 DEITSALDDANKRNVNEIIHRyvREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:cd03228  121 DEATSALDPETEALILEALRA--LAKGKTVIVIAHRLSTIRDADRIIVL 167
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 3-220 2.05e-47

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: 163.78  E-value: 2.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQ 81
Cdd:COG4988  332 AGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWRR 411

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSVQTPSLFDSTVYDNLLFPwqirHKTPDPERF-----SADLARF--NLP--PDTLtksVSE----LSGGEKQRVSL 148
Cdd:COG4988  412 QIAWVPQNPYLFAGTIRENLRLG----RPDASDEELeaaleAAGLDEFvaALPdgLDTP---LGEggrgLSGGQAQRLAL 484

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 149 IRnlQFL--PKVLLLDEITSALDDANKRNVNEIIHRYVREQniAVLWVTHDANEITHADDVLTLqpHGGKMQEA 220
Cdd:COG4988  485 AR--ALLrdAPLLLLDEPTAHLDAETEAEILQALRRLAKGR--TVILITHRLALLAQADRILVL--DDGRIVEQ 552
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 8-219 2.47e-47

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: 156.12  E-value: 2.47e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIED--VGYRTG--GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQV 83
Cdd:COG1124    2 LEVRNlsVSYGQGgrRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRKAFRRRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSVQTPslFDS-----TVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKV 158
Cdd:COG1124   82 QMVFQDP--YASlhprhTVDRILAEPLRIHGLPDREERIAELLEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPEL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 159 LLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQphGGKMQE 219
Cdd:COG1124  160 LLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHlCDRVAVMQ--NGRIVE 219
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 8-219 4.76e-47

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: 164.62  E-value: 4.76e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:COG2274  474 IELENVsfRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQIDPASLRRQIGV 553

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNLLFpwqiRHKTPDPERF-----SADLARF--NLPP--DTLtksVSE----LSGGEKQRV----SL 148
Cdd:COG2274  554 VLQDVFLFSGTIRENITL----GDPDATDEEIieaarLAGLHDFieALPMgyDTV---VGEggsnLSGGQRQRLaiarAL 626

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 149 IRNlqflPKVLLLDEITSALDDANKRNVNEIIHRyvREQNIAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:COG2274  627 LRN----PRILILDEATSALDAETEAIILENLRR--LLKGRTVIIIAHRLSTIRLADRIIVLD--KGRIVE 689
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 4-200 6.40e-47

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 157.95  E-value: 6.40e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   4 NSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFrlIT--GPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQ 81
Cdd:COG3842    2 AMPALELENVSKRYGDVTALDDVSLSIEPGEF--VAllGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPPE--KR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSVQTPSLFDS-TVYDNLLFPWQIRHKTPDPERFSAD--LARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKV 158
Cdd:COG3842   78 NVGMVFQDYALFPHlTVAENVAFGLRMRGVPKAEIRARVAelLELVGL-EGLADRYPHQLSGGQQQRVALARALAPEPRV 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504695722 159 LLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE 200
Cdd:COG3842  157 LLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEE 198
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 6-213 8.67e-47

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: 153.40  E-value: 8.67e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSY 85
Cdd:COG4133    1 MMLEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRD-AREDYRRRLAY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS-TVYDNLLFpWQ-IRHKTPDPERFSADLARFNLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:COG4133   80 LGHADGLKPElTVRENLRF-WAaLYGLRADREAIDEALEAVGLAG-LADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504695722 164 ITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEIThADDVLTLQPH 213
Cdd:COG4133  158 PFTALDAAGVALLAELIAAH-LARGGAVLLTTHQPLELA-AARVLDLGDF 205
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 9-217 1.62e-46

ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related proteins; ABC transporters, involved in the uptake of siderophores, heme, and vitamin B12, are widely conserved in bacteria and archaea. Only very few species lack representatives of the siderophore family transporters. The E. coli BtuCD protein is an ABC transporter mediating vitamin B12 uptake. The two ATP-binding cassettes (BtuD) are in close contact with each other, as are the two membrane-spanning subunits (BtuC); this arrangement is distinct from that observed for the E. coli lipid flippase MsbA. The BtuC subunits provide 20 transmembrane helices grouped around a translocation pathway that is closed to the cytoplasm by a gate region, whereas the dimer arrangement of the BtuD subunits resembles the ATP-bound form of the Rad50 DNA repair enzyme. A prominent cytoplasmic loop of BtuC forms the contact region with the ATP-binding cassette and represent a conserved motif among the ABC transporters.


Pssm-ID: 213181 [Multi-domain]  Cd Length: 180  Bit Score: 151.82  E-value: 1.62e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   9 TIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQ 88
Cdd:cd03214    1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARKIAYVPQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 TPSLFDstvydnllfpwqirhktpdperfSADLARfnlppdtltKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:cd03214   81 ALELLG-----------------------LAHLAD---------RPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL 128

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504695722 169 DDANKRNVNEIIHRYVREQNIAVLWVTHDAN-EITHADDVLTLqpHGGKM 217
Cdd:cd03214  129 DIAHQIELLELLRRLARERGKTVVMVLHDLNlAARYADRVILL--KDGRI 176
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
7-219 3.70e-45

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 149.82  E-value: 3.70e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---YRQQ 82
Cdd:COG2884    1 MIRFENVSKRyPGGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREipyLRRR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 VSYSVQTPSL-FDSTVYDNLLFPWQIRHKTPDP--ERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:COG2884   81 IGVVFQDFRLlPDRTVYENVALPLRVTGKSRKEirRRVREVLDLVGL-SDKAKALPHELSGGEQQRVAIARALVNRPELL 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADD-VLTLqpHGGKMQE 219
Cdd:COG2884  160 LADEPTGNLDPETSWEIMELLEE-INRRGTTVLIATHDLELVDRMPKrVLEL--EDGRLVR 217
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 8-219 9.01e-45

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: 148.87  E-value: 9.01e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLL-----TPTSGKIFFEGKDISTLS--PEAYR 80
Cdd:cd03260    1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLNdlipgAPDEGEVLLDGKDIYDLDvdVLELR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFDSTVYDNLLFPWQIRHKTPDPERFSAD---LARFNLPPDTLTK-SVSELSGGEKQRVSLIRNLQFLP 156
Cdd:cd03260   81 RRVGMVFQKPNPFPGSIYDNVAYGLRLHGIKLKEELDERVeeaLRKAALWDEVKDRlHALGLSGGQQQRLCLARALANEP 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREqnIAVLWVTHDANEITH-ADDVLTLqpHGGKMQE 219
Cdd:cd03260  161 EVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARvADRTAFL--LNGRLVE 220
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 8-211 3.91e-44

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: 145.44  E-value: 3.91e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:cd03246    1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDPNELGDHVGY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNLlfpwqirhktpdperfsadlarfnlppdtltksvseLSGGEKQRVSLIRNLQFLPKVLLLDEIT 165
Cdd:cd03246   81 LPQDDELFSGSIAENI------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 504695722 166 SALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03246  125 SHLDVEGERALNQAIAA-LKAAGATRIVIAHRPETLASADRILVLE 169
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 8-211 4.07e-44

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: 145.79  E-value: 4.07e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLS--PEAYRQQVSY 85
Cdd:cd03229    1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEdeLPPLRRRIGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS-TVYDNLLFPwqirhktpdperfsadlarfnlppdtltksvseLSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:cd03229   81 VFQDFALFPHlTVLENIALG---------------------------------LSGGQQQRVALARALAMDPDVLLLDEP 127

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 165 TSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQ 211
Cdd:cd03229  128 TSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARlADRVVVLR 175
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 8-219 8.27e-44

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: 146.61  E-value: 8.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPeaYRQQVSYSV 87
Cdd:cd03300    1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPP--HKRPVNTVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:cd03300   79 QNYALFPHlTVFENIAFGLRLKKLPKAeiKERVAEALDLVQL-EGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDEP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 165 TSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGKMQE 219
Cdd:cd03300  158 LGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEaLTMSDRIAVM--NKGKIQQ 211
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 3-210 1.75e-43

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 146.39  E-value: 1.75e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDistlsPEAYRQQ 82
Cdd:COG1121    2 MMMPAIELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKP-----PRRARRR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 VSYSVQTPSL---FDSTVYDNLL------FPWQIRHKTPDPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNL- 152
Cdd:COG1121   77 IGYVPQRAEVdwdFPITVRDVVLmgrygrRGLFRRPSRADREAVDEALERVGLE-DLADRPIGELSGGQQQRVLLARALa 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 153 -QflPKVLLLDEITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEI-THADDVLTL 210
Cdd:COG1121  156 qD--PDLLLLDEPFAGVDAATEEALYELLREL-RREGKTILVVTHDLGAVrEYFDRVLLL 212
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 6-218 2.26e-43

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 148.68  E-value: 2.26e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSY 85
Cdd:COG3839    2 ASLELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPK--DRNIAM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS-TVYDNLLFPWQIRhKTPDPERfsaD------LARFNLpPDTLTKSVSELSGGEKQRVSL----IRNlqf 154
Cdd:COG3839   80 VFQSYALYPHmTVYENIAFPLKLR-KVPKAEI---DrrvreaAELLGL-EDLLDRKPKQLSGGQRQRVALgralVRE--- 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 155 lPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGKMQ 218
Cdd:COG3839  152 -PKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEaMTLADRIAVM--NDGRIQ 213
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 5-210 5.95e-43

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: 151.84  E-value: 5.95e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQ 82
Cdd:COG4987  331 GPSLELEDVsfRYPGAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLRRR 410

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 VSYSVQTPSLFDSTVYDNLLF--PwqirhkTPDPERFSADLARFNL------PPDTLTKSVSE----LSGGEKQRVSLIR 150
Cdd:COG4987  411 IAVVPQRPHLFDTTLRENLRLarP------DATDEELWAALERVGLgdwlaaLPDGLDTWLGEggrrLSGGERRRLALAR 484

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 151 NLqfL--PKVLLLDEITSALDDANKRNVNEIIHRYVREQniAVLWVTHDANEITHADDVLTL 210
Cdd:COG4987  485 AL--LrdAPILLLDEPTEGLDAATEQALLADLLEALAGR--TVLLITHRLAGLERMDRILVL 542
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 5-219 1.88e-42

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: 149.67  E-value: 1.88e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIED--VGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPT---SGKIFFEGKDISTLSPEAY 79
Cdd:COG1123    2 TPLLEVRDlsVRYPGGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVSYSVQTP--SLFDSTVYDNLLFPWQIRHKTPD--PERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFL 155
Cdd:COG1123   82 GRRIGMVFQDPmtQLNPVTVGDQIAEALENLGLSRAeaRARVLELLEAVGLE-RRLDRYPHQLSGGQRQRVAIAMALALD 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 156 PKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEI-THADDVLTLqpHGGKMQE 219
Cdd:COG1123  161 PDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVaEIADRVVVM--DDGRIVE 223
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 8-197 3.34e-42

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: 142.58  E-value: 3.34e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSYS 86
Cdd:cd03219    1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPhEIARLGIGRT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLLFPWQIRHKTPDPERFSAD------------LARFNLPP--DTLtksVSELSGGEKQRVSLIRN 151
Cdd:cd03219   81 FQIPRLFPElTVLENVMVAAQARTGSGLLLARARReereareraeelLERVGLADlaDRP---AGELSYGQQRRLEIARA 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 504695722 152 LQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHD 197
Cdd:cd03219  158 LATDPKLLLLDEPAAGLNPEETEELAELI-RELRERGITVLLVEHD 202
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 23-166 7.14e-42

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: 138.93  E-value: 7.14e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLF-DSTVYDNL 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTDDERKSLRKEIGYVFQDPQLFpRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  102 LFPWQIRH--KTPDPERFSADLARFNLPP---DTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:pfam00005  81 RLGLLLKGlsKREKDARAEEALEKLGLGDladRPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 8-210 4.75e-41

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 138.77  E-value: 4.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP---TSGKIFFEGKDISTLSPEayRQQVS 84
Cdd:COG4136    2 LSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRLTALPAE--QRRIG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLFDS-TVYDNLLFpwQIRHKTPDPER--------FSADLA-RFNLPPDTltksvseLSGGEKQRVSLIRNLQF 154
Cdd:COG4136   80 ILFQDDLLFPHlSVGENLAF--ALPPTIGRAQRrarveqalEEAGLAgFADRDPAT-------LSGGQRARVALLRALLA 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 155 LPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:COG4136  151 EPRALLLDEPFSKLDAALRAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 8-217 5.31e-41

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: 137.53  E-value: 5.31e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYSV 87
Cdd:cd03230    1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKK-EPEEVKRRIGYLP 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLlfpwqirhktpdperfsadlarfnlppdtltksvsELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:cd03230   80 EEPSLYENlTVRENL-----------------------------------KLSGGMKQRLALAQALLHDPELLILDEPTS 124

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504695722 167 ALDDANKRNVNEIIHRYVREqNIAVLWVTHDANEI-THADDVLTLqpHGGKM 217
Cdd:cd03230  125 GLDPESRREFWELLRELKKE-GKTILLSSHILEEAeRLCDRVAIL--NNGRI 173
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 23-201 1.67e-40

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: 138.24  E-value: 1.67e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSYSVQTPSLF-DSTVYDNL 101
Cdd:cd03299   15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE--KRDISYVPQNYALFpHMTVYKNI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 LFpwQIRHKTPDP---ERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNE 178
Cdd:cd03299   93 AY--GLKKRKVDKkeiERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLRE 170

                        170       180
                 ....*....|....*....|...
gi 504695722 179 IIHRYVREQNIAVLWVTHDANEI 201
Cdd:cd03299  171 ELKKIRKEFGVTVLHVTHDFEEA 193
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 8-219 2.82e-40

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: 137.00  E-value: 2.82e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPeaYRQQVSYSV 87
Cdd:cd03301    1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPP--KDRDIAMVF 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLF-DSTVYDNLLFPWQIRHKTPDP--ERFSaDLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:cd03301   79 QNYALYpHMTVYDNIAFGLKLRKVPKDEidERVR-EVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 165 TSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGKMQE 219
Cdd:cd03301  158 LSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEaMTMADRIAVM--NDGQIQQ 211
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
8-216 5.02e-40

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 137.55  E-value: 5.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA-------YR 80
Cdd:COG4559    2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWElarrravLP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSvqtpslFDSTVYDNLLF---PWQiRHKTPDPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNL----- 152
Cdd:COG4559   82 QHSSLA------FPFTVEEVVALgraPHG-SSAAQDRQIVREALALVGLA-HLAGRSYQTLSGGEQQRVQLARVLaqlwe 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 153 --QFLPKVLLLDEITSALDDANKRNVNEIIHRYVReQNIAVLWVTHDANeIT--HADDVLTLqpHGGK 216
Cdd:COG4559  154 pvDGGPRWLFLDEPTSALDLAHQHAVLRLARQLAR-RGGGVVAVLHDLN-LAaqYADRILLL--HQGR 217
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 8-208 6.96e-40

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 139.51  E-value: 6.96e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIST-LSPeayRQ-QVSY 85
Cdd:COG1118    3 IEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTnLPP---RErRVGF 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLF-DSTVYDNLLFPwqIRHKTPDPERFSAD----LARFNLP------PdtltksvSELSGGEKQRVSLIRNLQF 154
Cdd:COG1118   80 VFQHYALFpHMTVAENIAFG--LRVRPPSKAEIRARveelLELVQLEgladryP-------SQLSGGQRQRVALARALAV 150

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 155 LPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD---ANEIthADDVL 208
Cdd:COG1118  151 EPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDqeeALEL--ADRVV 205
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 6-218 8.42e-40

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 137.21  E-value: 8.42e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA------- 78
Cdd:PRK13548   1 AMLEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAElarrrav 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 YRQQVSYSvqtpslFDSTVYDNL---LFPWQiRHKTPDPERFSADLARFNLppDTL-TKSVSELSGGEKQRVSLIRNLQF 154
Cdd:PRK13548  81 LPQHSSLS------FPFTVEEVVamgRAPHG-LSRAEDDALVAAALAQVDL--AHLaGRDYPQLSGGEQQRVQLARVLAQ 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 155 L------PKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQ 218
Cdd:PRK13548 152 LwepdgpPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARyADRIVLL--HQGRLV 220
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 7-196 1.42e-39

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: 135.79  E-value: 1.42e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDV----GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---Y 79
Cdd:cd03258    1 MIELKNVskvfGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKElrkA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVSYSVQTPSLFDS-TVYDNLLFPWQIRH--KTPDPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:cd03258   81 RRRIGMIFQHFNLLSSrTVFENVALPLEIAGvpKAEIEERVLELLELVGLE-DKADAYPAQLSGGQKQRVGIARALANNP 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTH 196
Cdd:cd03258  160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITH 199
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 8-219 3.89e-39

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: 134.77  E-value: 3.89e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSYSV 87
Cdd:cd03296    3 IEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQ--ERNVGFVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFPWQIRHKTPDP------ERFSADLARFNLppDTLTKSV-SELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:cd03296   81 QHYALFRHmTVFDNVAFGLRVKPRSERPpeaeirAKVHELLKLVQL--DWLADRYpAQLSGGQRQRVALARALAVEPKVL 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGKMQE 219
Cdd:cd03296  159 LLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEaLEVADRVVVM--NKGRIEQ 217
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 10-210 1.02e-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: 133.04  E-value: 1.02e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDistlsPEAYRQQVSYSVQT 89
Cdd:cd03235    2 VEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKP-----LEKERKRIGYVPQR 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 PSL---FDSTVYDNLL------FPWQIRHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:cd03235   77 RSIdrdFPISVRDVVLmglyghKGLFRRLSKADKAKVDEALERVGL-SELADRQIGELSGGQQQRVLLARALVQDPDLLL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504695722 161 LDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEIT-HADDVLTL 210
Cdd:cd03235  156 LDEPFAGVDPKTQEDIYELL-RELRREGMTILVVTHDLGLVLeYFDRVLLL 205
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 7-219 1.25e-38

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: 133.83  E-value: 1.25e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYS 86
Cdd:COG4555    1 MIEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRK-EPREARRQIGVL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLLFPWQIRHKTPD--PERFSADLARFNLPPDtLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:COG4555   80 PDERGLYDRlTVRENIRYFAELYGLFDEelKKRIEELIELLGLEEF-LDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 164 ITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQE 219
Cdd:COG4555  159 PTNGLDVMARRLLREILRAL-KKEGKTVLFSSHIMQEVEAlCDRVVIL--HKGKVVA 212
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 5-218 5.66e-38

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: 138.34  E-value: 5.66e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQ 82
Cdd:COG4618  328 KGRLSVENLTVVPPGSKrpILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQWDREELGRH 407

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 VSYSVQTPSLFDSTVYDNllfpwqI-RHKTPDPERF--SADLA-------RFNLPPDTLtksVSE----LSGGEKQRVSL 148
Cdd:COG4618  408 IGYLPQDVELFDGTIAEN------IaRFGDADPEKVvaAAKLAgvhemilRLPDGYDTR---IGEggarLSGGQRQRIGL 478

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITHADDVLTLQphGGKMQ 218
Cdd:COG4618  479 ARALYGDPRLVVLDEPNSNLDDEGEAALAAAI-RALKARGATVVVITHRPSLLAAVDKLLVLR--DGRVQ 545
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 8-200 9.10e-38

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: 131.27  E-value: 9.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYS 86
Cdd:cd03295    1 IEFENVTKRyGGGKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRRKIGYV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNL-----LFPW---QIRhktpdpERFSADLARFNLPPDTLT-KSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:cd03295   81 IQQIGLFPHmTVEENIalvpkLLKWpkeKIR------ERADELLALVGLDPAEFAdRYPHELSGGQQQRVGVARALAADP 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE 200
Cdd:cd03295  155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDE 198
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
8-219 6.53e-37

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 135.68  E-value: 6.53e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYS 86
Cdd:COG1132  340 IEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRRQIGVV 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDSTVYDNLLFPwqiRHKTPDPE-RFSADLARF-----NLP--PDTLtksVSE----LSGGEKQRVS----LIR 150
Cdd:COG1132  420 PQDTFLFSGTIRENIRYG---RPDATDEEvEEAAKAAQAhefieALPdgYDTV---VGErgvnLSGGQRQRIAiaraLLK 493

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 151 NlqflPKVLLLDEITSALDdankrNVNE-IIHRYVRE--QNIAVLWVTHDANEITHADDVLTLqpHGGKMQE 219
Cdd:COG1132  494 D----PPILILDEATSALD-----TETEaLIQEALERlmKGRTTIVIAHRLSTIRNADRILVL--DDGRIVE 554
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 18-197 1.12e-36

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: 128.45  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---YRQQVSYSVQTPSLFD 94
Cdd:cd03256   12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKAlrqLRRQIGMIFQQFNLIE 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 -STVYDNLLF-------PWQI---RHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:cd03256   92 rLSVLENVLSgrlgrrsTWRSlfgLFPKEEKQRALAALERVGL-LDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504695722 164 ITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:cd03256  171 PVASLDPASSRQVMDLLKRINREEGITVIVSLHQ 204
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 10-210 1.20e-36

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: 129.09  E-value: 1.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   10 IEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGkdISTLSPEAY---RQQVS 84
Cdd:TIGR04520   3 VENVSFSYPESEkpALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDG--LDTLDEENLweiRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   85 YSVQTPslfD-----STVYDNLLF--------PWQIRHKTPDPerfsadLARFNLPpDTLTKSVSELSGGEKQRVSLIRN 151
Cdd:TIGR04520  81 MVFQNP---DnqfvgATVEDDVAFglenlgvpREEMRKRVDEA------LKLVGME-DFRDREPHLLSGGQKQRVAIAGV 150

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722  152 LQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:TIGR04520 151 LAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVM 209
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 22-219 1.22e-36

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: 128.43  E-value: 1.22e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDNL 101
Cdd:cd03249   18 ILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDLNLRWLRSQIGLVSQEPVLFDGTIAENI 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 LFPwqiRHKTPDPERFSAdlARF--------NLPP--DTLTKSV-SELSGGEKQRVS----LIRNlqflPKVLLLDEITS 166
Cdd:cd03249   98 RYG---KPDATDEEVEEA--AKKanihdfimSLPDgyDTLVGERgSQLSGGQKQRIAiaraLLRN----PKILLLDEATS 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504695722 167 ALDDANKRNVNEIIHRYVReqNIAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:cd03249  169 ALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRNADLIAVLQ--NGQVVE 217
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
6-207 1.34e-36

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 133.61  E-value: 1.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVS 84
Cdd:COG1129    3 PLLEMRGISKSFGGVKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPrDAQAAGIA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLFDS-TVYDNLLFPWQIRHK-TPDP----ERFSADLARFNL--PPDTLtksVSELSGGEKQRVSLIRNLQFLP 156
Cdd:COG1129   83 IIHQELNLVPNlSVAENIFLGREPRRGgLIDWramrRRARELLARLGLdiDPDTP---VGDLSVAQQQLVEIARALSRDA 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI-THADDV 207
Cdd:COG1129  160 RVLILDEPTASLTEREVERLFRIIRR-LKAQGVAIIYISHRLDEVfEIADRV 210
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 11-200 1.02e-35

ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This family comprises the glycine betaine/L-proline ATP binding subunit in bacteria and its equivalents in archaea. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporters is the obligatory coupling of ATP hydrolysis to substrate translocation. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 126.99  E-value: 1.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  11 EDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQ----QVSYS 86
Cdd:cd03294   28 EEILKKTGQTVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRElrrkKISMV 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLF-DSTVYDNLLFPWQIRHkTPDPERFSAD---LARFNLPPDtLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:cd03294  108 FQSFALLpHRTVLENVAFGLEVQG-VPRAEREERAaeaLELVGLEGW-EHKYPDELSGGMQQRVGLARALAVDPDILLMD 185

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 163 EITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE 200
Cdd:cd03294  186 EAFSALDPLIRREMQDELLRLQAELQKTIVFITHDLDE 223
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 5-210 1.30e-35

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: 131.64  E-value: 1.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    5 SAVLTIEDVGYRTGGTT-ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQV 83
Cdd:TIGR02857 319 ASSLEFSGVSVAYPGRRpALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRDQI 398

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   84 SYSVQTPSLFDSTVYDNllfpwqIRHKTPDPERFS-------ADLARF--NLPPDTLTK---SVSELSGGEKQRVSLIRN 151
Cdd:TIGR02857 399 AWVPQHPFLFAGTIAEN------IRLARPDASDAEirealerAGLDEFvaALPQGLDTPigeGGAGLSGGQAQRLALARA 472

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722  152 LQFLPKVLLLDEITSALDDANKRNVNEIIHRYVreQNIAVLWVTHDANEITHADDVLTL 210
Cdd:TIGR02857 473 FLRDAPLLLLDEPTAHLDAETEAEVLEALRALA--QGRTVLLVTHRLALAALADRIVVL 529
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 15-201 2.88e-35

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: 124.15  E-value: 2.88e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  15 YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYSVQTPSLFD 94
Cdd:cd03263   10 YKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT-DRKAARQSLGYCPQFDALFD 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 S-TVYDNLLFPWQIRHKTPDPERFSADLAR--FNLPPDtLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDA 171
Cdd:cd03263   89 ElTVREHLRFYARLKGLPKSEIKEEVELLLrvLGLTDK-ANKRARTLSGGMKRKLSLAIALIGGPSVLLLDEPTSGLDPA 167

                        170       180       190
                 ....*....|....*....|....*....|
gi 504695722 172 NKRNVNEIIHRYVREQniAVLWVTHDANEI 201
Cdd:cd03263  168 SRRAIWDLILEVRKGR--SIILTTHSMDEA 195
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 27-210 5.30e-35

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: 123.56  E-value: 5.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  27 SFSL-----LPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEG-------KDIStLSPEayRQQVSYSVQTPSLFD 94
Cdd:cd03297   12 DFTLkidfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKIN-LPPQ--QRKIGLVFQQYALFP 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 S-TVYDNLLFpwQIRHKTPDPERFSAD--LARFNLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDda 171
Cdd:cd03297   89 HlNVRENLAF--GLKRKRNREDRISVDelLDLLGLDH-LLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALD-- 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 172 nkRNVNEIIHRYVREQ----NIAVLWVTHDANEI-THADDVLTL 210
Cdd:cd03297  164 --RALRLQLLPELKQIkknlNIPVIFVTHDLSEAeYLADRIVVM 205
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
1-200 3.04e-34

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 125.44  E-value: 3.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayR 80
Cdd:PRK09452   8 PSSLSPLVELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE--N 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFDS-TVYDNLLFPWQIRhKTPDPE---RFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:PRK09452  86 RHVNTVFQSYALFPHmTVFENVAFGLRMQ-KTPAAEitpRVMEALRMVQL-EEFAQRKPHQLSGGQQQRVAIARAVVNKP 163

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE 200
Cdd:PRK09452 164 KVLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEE 207
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 23-217 6.01e-34

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: 120.77  E-value: 6.01e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDNLL 102
Cdd:cd03245   20 LDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPADLRRNIGYVPQDVTLFYGTLRDNIT 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 103 FpwqiRHKTPDPERF--SADLA---RF-NLPPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:cd03245  100 L----GAPLADDERIlrAAELAgvtDFvNKHPNGLDLQIGErgrgLSGGQRQAVALARALLNDPPILLLDEPTSAMDMNS 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 173 KRNVNEIIHRYVREQNIAVlwVTHDANEITHADDVLTLQphGGKM 217
Cdd:cd03245  176 EERLKERLRQLLGDKTLII--ITHRPSLLDLVDRIIVMD--SGRI 216
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 11-211 6.21e-34

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: 121.18  E-value: 6.21e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  11 EDV--GYRTGGTtILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQ 88
Cdd:cd03253    4 ENVtfAYDPGRP-VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVTLDSLRRAIGVVPQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 TPSLFDSTVYDNllfpwqIRHKTPD--PERF-----SADLARF--NLPPDTLTKsVSE----LSGGEKQRVSLIRNLQFL 155
Cdd:cd03253   83 DTVLFNDTIGYN------IRYGRPDatDEEVieaakAAQIHDKimRFPDGYDTI-VGErglkLSGGEKQRVAIARAILKN 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 156 PKVLLLDEITSALDDANKRNVNEIIHRYVReqNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03253  156 PPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVNADKIIVLK 209
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 9-197 6.35e-34

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: 120.44  E-value: 6.35e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   9 TIEDVGYRTG-GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIstlSPEAYRQQVSYSV 87
Cdd:cd03226    1 RIENISFSYKkGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRKSIGYVM 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPS--LFDSTVYDNLLFPWQIRHKtpDPERFSADLARFNL-------PPDtltksvseLSGGEKQRV----SLIRNlqf 154
Cdd:cd03226   78 QDVDyqLFTDSVREELLLGLKELDA--GNEQAETVLKDLDLyalkerhPLS--------LSGGQKQRLaiaaALLSG--- 144

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504695722 155 lPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHD 197
Cdd:cd03226  145 -KDLLIFDEPTSGLDYKNMERVGELI-RELAAQGKAVIVITHD 185
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 8-210 7.04e-34

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: 119.07  E-value: 7.04e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVsys 86
Cdd:cd03216    1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPrDARRAGI--- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 vqtpslfdSTVYdnllfpwqirhktpdperfsadlarfnlppdtltksvsELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:cd03216   78 --------AMVY--------------------------------------QLSVGERQMVEIARALARNARLLILDEPTA 111

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 167 ALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI-THADDVLTL 210
Cdd:cd03216  112 ALTPAEVERLFKVIRR-LRAQGVAVIFISHRLDEVfEIADRVTVL 155
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 15-222 7.42e-34

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: 121.05  E-value: 7.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  15 YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFD 94
Cdd:cd03252   10 YKPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALADPAWLRRQVGVVLQENVLFN 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 STVYDNLLF--PWQIRHKTPDPERFSADLARFNLPPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:cd03252   90 RSIRDNIALadPGMSMERVIEAAKLAGAHDFISELPEGYDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSAL 169

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504695722 169 DDANKRNVNEIIHRYVreQNIAVLWVTHDANEITHADDVLTLQphGGKMQEANR 222
Cdd:cd03252  170 DYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVME--KGRIVEQGS 219
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 8-216 9.32e-34

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: 120.33  E-value: 9.32e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY--RQQVSY 85
Cdd:cd03262    1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTDDKKNINelRQKVGM 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS-TVYDNLLFPWQIRHKTPDPErfsAD------LARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKV 158
Cdd:cd03262   81 VFQQFNLFPHlTVLENITLAPIKVKGMSKAE---AEeralelLEKVGL-ADKADAYPAQLSGGQQQRVAIARALAMNPKV 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 159 LLLDEITSALDDANKRNVNEIIHRYVREqNIAVLWVTHD---ANEIthADDVLTLqpHGGK 216
Cdd:cd03262  157 MLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEmgfAREV--ADRVIFM--DDGR 212
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 8-199 2.17e-33

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: 119.46  E-value: 2.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDV--GYrtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA-YRQQVS 84
Cdd:cd03224    1 LEVENLnaGY--GKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHErARAGIG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLFDS-TVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:cd03224   79 YVPEGRRIFPElTVEENLLLGAYARRRAKRKARLERVYELFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDE 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504695722 164 ITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDAN 199
Cdd:cd03224  159 PSEGLAPKIVEEIFEAIRE-LRDEGVTILLVEQNAR 193
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
6-219 2.66e-33

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 120.35  E-value: 2.66e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGG----TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIStlSPEAYRQ 81
Cdd:COG4525    2 SMLTVRHVSVRYPGggqpQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVT--GPGADRG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVsysVQTPSLFD-STVYDNLLFPWQIRhKTPDPERFS-AD--LARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPK 157
Cdd:COG4525   80 VV---FQKDALLPwLNVLDNVAFGLRLR-GVPKAERRArAEelLALVGLA-DFARRRIWQLSGGMRQRVGIARALAADPR 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695722 158 VLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLQPHGGKMQE 219
Cdd:COG4525  155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITHSVEEaLFLATRLVVMSPGPGRIVE 217
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 1-218 3.51e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 120.48  E-value: 3.51e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA 78
Cdd:PRK13632   1 IKNKSVMIKVENVsfSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 YRQQVSYSVQTP--SLFDSTVYDNLLFpwQIRHKTPDPERFSA---DLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQ 153
Cdd:PRK13632  81 IRKKIGIIFQNPdnQFIGATVEDDIAF--GLENKKVPPKKMKDiidDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLA 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQphGGKMQ 218
Cdd:PRK13632 159 LNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFS--EGKLI 221
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
7-220 1.62e-32

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 118.96  E-value: 1.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdisTLSPEAY---RQ 81
Cdd:PRK13635   5 IIRVEHISFRYPDAAtyALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVwdvRR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSVQTP--SLFDSTVYDNLLFPWQiRHKTPDPE---RFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:PRK13635  82 QVGMVFQNPdnQFVGATVQDDVAFGLE-NIGVPREEmveRVDQALRQVGME-DFLNREPHRLSGGQKQRVAIAGVLALQP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQpHGGKMQEA 220
Cdd:PRK13635 160 DIIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMN-KGEILEEG 222
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
8-208 1.70e-32

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 117.55  E-value: 1.70e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTIlnNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPeaYRQQVSYSV 87
Cdd:COG3840    2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPP--AERPVSMLF 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNL---LFPwQIRHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNL-QFLPkVLLLD 162
Cdd:COG3840   78 QENNLFPHlTVAQNIglgLRP-GLKLTAEQRAQVEQALERVGL-AGLLDRLPGQLSGGQRQRVALARCLvRKRP-ILLLD 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504695722 163 EITSALDDANKRN----VNEIihryVREQNIAVLWVTHDANEITH-ADDVL 208
Cdd:COG3840  155 EPFSALDPALRQEmldlVDEL----CRERGLTVLMVTHDPEDAARiADRVL 201
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 21-197 2.35e-32

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 117.88  E-value: 2.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLsPEAYR-QQVSYSVQTPSL---FDST 96
Cdd:COG1101   20 RALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKL-PEYKRaKYIGRVFQDPMMgtaPSMT 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLL--------FPWQIRHKTPDPERFSADLARFNLP-PDTLTKSVSELSGGEKQRVSL----IRNlqflPKVLLLDE 163
Cdd:COG1101   99 IEENLAlayrrgkrRGLRRGLTKKRRELFRELLATLGLGlENRLDTKVGLLSGGQRQALSLlmatLTK----PKLLLLDE 174

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504695722 164 ITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:COG1101  175 HTAALDPKTAALVLELTEKIVEENNLTTLMVTHN 208
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 7-219 2.67e-32

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 117.02  E-value: 2.67e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDI--STLSPEAYRQQVS 84
Cdd:COG1126    1 MIEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLtdSKKDINKLRRKVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLFDS-TVYDNL-LFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:COG1126   81 MVFQQFNLFPHlTVLENVtLAPIKVKKMSKAeaEERAMELLERVGL-ADKADAYPAQLSGGQQQRVAIARALAMEPKVML 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 161 LDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHD---ANEIthADDVLTLqpHGGKMQE 219
Cdd:COG1126  160 FDEPTSALDPELVGEVLDVM-RDLAKEGMTMVVVTHEmgfAREV--ADRVVFM--DGGRIVE 216
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
18-223 3.51e-32

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 116.51  E-value: 3.51e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---YRQQVSYSVQTPSLF- 93
Cdd:PRK10908  13 GGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREvpfLRRQIGMIFQDHHLLm 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DSTVYDNLLFPWQIRHKTPDP--ERFSADLARFNLppdtLTKSVS---ELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:PRK10908  93 DRTVYDNVAIPLIIAGASGDDirRRVSAALDKVGL----LDKAKNfpiQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722 169 DDAnkrnVNEIIHRYVREQN---IAVLWVTHDANEITHAD-DVLTLQPhgGKMQEANRG 223
Cdd:PRK10908 169 DDA----LSEGILRLFEEFNrvgVTVLMATHDIGLISRRSyRMLTLSD--GHLHGGVGG 221
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 8-197 6.54e-32

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: 121.31  E-value: 6.54e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    8 LTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYS 86
Cdd:TIGR02868 335 LELRDLSAGyPGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRRRVSVC 414

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   87 VQTPSLFDSTVYDNLLfpwqIRHKTPDPERFSADLARFNL------PPDTLTKSVSE----LSGGEKQRVSLIRNLQFLP 156
Cdd:TIGR02868 415 AQDAHLFDTTVRENLR----LARPDATDEELWAALERVGLadwlraLPDGLDTVLGEggarLSGGERQRLALARALLADA 490

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 504695722  157 KVLLLDEITSALDDANKRNVNEIIHRYVREQniAVLWVTHD 197
Cdd:TIGR02868 491 PILLLDEPTEHLDAETADELLEDLLAALSGR--TVVLITHH 529
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 7-208 1.97e-31

ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid transport and metabolism, Inorganic ion transport and metabolism];


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 116.69  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIED--VGYRTGGTTI--LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP---TSGKIFFEGKDISTLSPEAY 79
Cdd:COG0444    1 LLEVRNlkVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKLSEKEL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQ----QVSYSVQTPslFDS-----TVYDNLLFPWQIRHKTPDPERFSA-----DLARFNLPPDTLTKSVSELSGGEKQR 145
Cdd:COG0444   81 RKirgrEIQMIFQDP--MTSlnpvmTVGDQIAEPLRIHGGLSKAEARERaiellERVGLPDPERRLDRYPHELSGGMRQR 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 146 VSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD---ANEIthADDVL 208
Cdd:COG0444  159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDlgvVAEI--ADRVA 222
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
8-214 2.58e-31

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 117.11  E-value: 2.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSpeAYRQQVSYSV 87
Cdd:PRK10851   3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLH--ARDRKVGFVF 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFPWQI--RHKTPDPERFSADLARFnLPPDTLT----KSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK10851  81 QHYALFRHmTVFDNIAFGLTVlpRRERPNAAAIKAKVTQL-LEMVQLAhladRYPAQLSGGQKQRVALARALAVEPQILL 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 161 LDEITSALDdankRNVNEIIHRYVR----EQNIAVLWVTHDANEITHADDVLTLQPHG 214
Cdd:PRK10851 160 LDEPFGALD----AQVRKELRRWLRqlheELKFTSVFVTHDQEEAMEVADRVVVMSQG 213
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
8-219 3.46e-31

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 116.72  E-value: 3.46e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVG--YRTGGTTI--LNNVSFSLLPGE-FRLItGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE---AY 79
Cdd:COG1135    2 IELENLSktFPTKGGPVtaLDDVSLTIEKGEiFGII-GYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelrAA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RQQVSYSVQTPSLFDS-TVYDNLLFPWQIrHKTPDPERFS--ADLARF--------NLPpdtltksvSELSGGEKQRVSL 148
Cdd:COG1135   81 RRKIGMIFQHFNLLSSrTVAENVALPLEI-AGVPKAEIRKrvAELLELvglsdkadAYP--------SQLSGGQKQRVGI 151

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDAN---EIthADDVLTLQphGGKMQE 219
Cdd:COG1135  152 ARALANNPKVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDvvrRI--CDRVAVLE--NGRIVE 221
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 23-200 3.79e-31

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: 114.10  E-value: 3.79e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVsysVQTPSLFD-STVYDNL 101
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPD--RMVV---FQNYSLLPwLTVRENI 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  102 -LFPWQIRHKTPDPERfsADLARFNLPPDTLT----KSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNV 176
Cdd:TIGR01184  76 aLAVDRVLPDLSKSER--RAIVEEHIALVGLTeaadKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNL 153

                         170       180
                  ....*....|....*....|....
gi 504695722  177 NEIIHRYVREQNIAVLWVTHDANE 200
Cdd:TIGR01184 154 QEELMQIWEEHRVTVLMVTHDVDE 177
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 5-213 4.12e-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: 113.68  E-value: 4.12e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVG-----YRTGGTTI--LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFF----EGKDIST 73
Cdd:COG4778    2 TTLLEVENLSktftlHLQGGKRLpvLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVrhdgGWVDLAQ 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  74 LSP----EAYRQQVSYSVQ-------TPSLfdSTVYDNLLfpwqiRHKTPDPE---RFSADLARFNLPPDTLTKSVSELS 139
Cdd:COG4778   82 ASPreilALRRRTIGYVSQflrviprVSAL--DVVAEPLL-----ERGVDREEaraRARELLARLNLPERLWDLPPATFS 154

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 140 GGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEITH-ADDVLTLQPH 213
Cdd:COG4778  155 GGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEEVREAvADRVVDVTPF 228
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 3-223 4.26e-31

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: 113.68  E-value: 4.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYR----TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA 78
Cdd:COG4181    4 SSAPIIELRGLTKTvgtgAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 Y----RQQVSYSVQT----PSLfdsTVYDNLLFPWQIRHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIR 150
Cdd:COG4181   84 RarlrARHVGFVFQSfqllPTL---TALENVMLPLELAGRRDARARARALLERVGL-GHRLDHYPAQLSGGEQQRVALAR 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695722 151 NLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQphGGKMQEANRG 223
Cdd:COG4181  160 AFATEPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLR--AGRLVEDTAA 230
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 6-219 5.91e-31

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 114.52  E-value: 5.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    6 AVLTIEDVG--YRTGG-------TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP 76
Cdd:TIGR02769   1 SLLEVRDVThtYRTGGlfgakqrAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   77 E---AYRQQVSYSVQ-TPSLFD--STVYDNLLFPwqIRH-----KTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQR 145
Cdd:TIGR02769  81 KqrrAFRRDVQLVFQdSPSAVNprMTVRQIIGEP--LRHltsldESEQKARIAELLDMVGLRSEDADKLPRQLSGGQLQR 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722  146 VSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQE 219
Cdd:TIGR02769 159 INIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSfCQRVAVM--DKGQIVE 231
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 18-198 7.26e-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: 112.89  E-value: 7.26e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---YRQQVSYSVQTPSLF- 93
Cdd:cd03292   12 NGTAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAipyLRRKIGVVFQDFRLLp 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DSTVYDNLLFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDA 171
Cdd:cd03292   92 DRNVYENVAFALEVTGVPPReiRKRVPAALELVGL-SHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPD 170

                        170       180
                 ....*....|....*....|....*..
gi 504695722 172 NKRNVNEIIHRyVREQNIAVLWVTHDA 198
Cdd:cd03292  171 TTWEIMNLLKK-INKAGTTVVVATHAK 196
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 8-210 1.39e-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: 112.71  E-value: 1.39e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:cd03251    1 VEFKNVTFRYPGDGppVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQIGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNllfpwqIRHKTPDPER----FSADLA---RF--NLpPDTLTKSVSE----LSGGEKQRVSLIRNL 152
Cdd:cd03251   81 VSQDVFLFNDTVAEN------IAYGRPGATReeveEAARAAnahEFimEL-PEGYDTVIGErgvkLSGGQRQRIAIARAL 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 153 QFLPKVLLLDEITSALDDANKRNVNEIIHRYVreQNIAVLWVTHDANEITHADDVLTL 210
Cdd:cd03251  154 LKDPPILILDEATSALDTESERLVQAALERLM--KNRTTFVIAHRLSTIENADRIVVL 209
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 25-211 1.97e-30

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: 114.81  E-value: 1.97e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  25 NVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGK---DIST---LSPEayRQQVSYSVQTPSLFDS-TV 97
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEvlqDSARgifLPPH--RRRIGYVFQEARLFPHlSV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLLFPWQIRHKTPDPERFSADLARFNLPPdTLTKSVSELSGGEKQRVSLIRNLqfL--PKVLLLDEITSALDDANKRn 175
Cdd:COG4148   95 RGNLLYGRKRAPRAERRISFDEVVELLGIGH-LLDRRPATLSGGERQRVAIGRAL--LssPRLLLMDEPLAALDLARKA- 170

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 176 vnEIIH---RYVREQNIAVLWVTHDANEITH-ADDVLTLQ 211
Cdd:COG4148  171 --EILPyleRLRDELDIPILYVSHSLDEVARlADHVVLLE 208
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
20-197 6.64e-30

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 110.68  E-value: 6.64e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  20 TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA----YRQQVSYSVQTPSLF-D 94
Cdd:PRK11629  22 TDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAkaelRNQKLGFIYQFHHLLpD 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 STVYDNLLFPWQIRHKTPDP--ERFSADLARFNLPPDTLTKSvSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:PRK11629 102 FTALENVAMPLLIGKKKPAEinSRALEMLAAVGLEHRANHRP-SELSGGERQRVAIARALVNNPRLVLADEPTGNLDARN 180

                        170       180
                 ....*....|....*....|....*
gi 504695722 173 KRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK11629 181 ADSIFQLLGELNRLQGTAFLVVTHD 205
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
3-220 7.48e-30

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 113.28  E-value: 7.48e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQ 82
Cdd:PRK11432   2 TQKNFVVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTHRSIQ--QRD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 VSYSVQTPSLFDS-TVYDNLLFPWQIRhKTPDPERFS--------ADLARFNlppdtlTKSVSELSGGEKQRVSLIRNLQ 153
Cdd:PRK11432  80 ICMVFQSYALFPHmSLGENVGYGLKML-GVPKEERKQrvkealelVDLAGFE------DRYVDQISGGQQQRVALARALI 152

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 154 FLPKVLLLDEITSALdDAN-KRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGK-MQEA 220
Cdd:PRK11432 153 LKPKVLLFDEPLSNL-DANlRRSMREKIRELQQQFNITSLYVTHDQSEaFAVSDTVIVM--NKGKiMQIG 219
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 20-217 7.61e-30

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: 110.64  E-value: 7.61e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  20 TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYD 99
Cdd:cd03248   27 TLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYLHSKVSLVGQEPVLFARSLQD 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 100 NLLFPWQ---IRHKTPDPERFSAD--LARFNLPPDTLT-KSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANK 173
Cdd:cd03248  107 NIAYGLQscsFECVKEAAQKAHAHsfISELASGYDTEVgEKGSQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESE 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 174 RNVNEIIhrYVREQNIAVLWVTHDANEITHADDVLTLQphGGKM 217
Cdd:cd03248  187 QQVQQAL--YDWPERRTVLVIAHRLSTVERADQILVLD--GGRI 226
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 7-204 1.30e-29

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 109.19  E-value: 1.30e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSpeaYRQQVSY- 85
Cdd:PRK13539   2 MLEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPD---VAEACHYl 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 ---SVQTPSLfdsTVYDNLLFpWQiRHKTPDPERFSADLARFNLPPDTLTKSvSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:PRK13539  79 ghrNAMKPAL---TVAENLEF-WA-AFLGGEELDIAAALEAVGLAPLAHLPF-GYLSAGQKRRVALARLLVSNRPIWILD 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504695722 163 EITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEITHA 204
Cdd:PRK13539 153 EPTAALDAAAVALFAELIRAH-LAQGGIVIAATHIPLGLPGA 193
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 5-204 1.93e-29

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


Pssm-ID: 440736 [Multi-domain]  Cd Length: 250  Bit Score: 109.79  E-value: 1.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSG---KIF---FEGKDISTLspea 78
Cdd:COG1119    1 DPLLELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGndvRLFgerRGGEDVWEL---- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 yRQQ---VSYSVQTPSLFDSTVYDNLL---FPWQIRHKTPDPE-RFSAD--LARFNLpPDTLTKSVSELSGGEKQRV--- 146
Cdd:COG1119   77 -RKRiglVSPALQLRFPRDETVLDVVLsgfFDSIGLYREPTDEqRERARelLELLGL-AHLADRPFGTLSQGEQRRVlia 154

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 504695722 147 -SLIRNlqflPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEI----THA 204
Cdd:COG1119  155 rALVKD----PELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEEIppgiTHV 213
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 8-201 3.09e-29

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: 109.17  E-value: 3.09e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLsPEAYRQQ--VSY 85
Cdd:cd03218    1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKL-PMHKRARlgIGY 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLF-DSTVYDNLLFPWQIRHKTPDPERFSAD--LARFNLppDTLTKSV-SELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:cd03218   80 LPQEASIFrKLTVEENILAVLEIRGLSKKEREEKLEelLEEFHI--THLRKSKaSSLSGGERRRVEIARALATNPKFLLL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 162 DEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI 201
Cdd:cd03218  158 DEPFAGVDPIAVQDIQKIIKI-LKDRGIGVLITDHNVRET 196
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 23-169 5.12e-29

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 110.59  E-value: 5.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---YRQQVSYSVQTPslFDS---- 95
Cdd:COG4608   34 VDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRElrpLRRRMQMVFQDP--YASlnpr 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 -TVYDNLLFPWQIRHKTPDPERfsAD-----LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALD 169
Cdd:COG4608  112 mTVGDIIAEPLRIHGLASKAER--RErvaelLELVGLRPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALD 189
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 7-169 8.28e-29

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 112.47  E-value: 8.28e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEfRL-ITGPSGCGKSTLLKIIASLLTPTSGKIFFeGKDIstlspeayrqQVSY 85
Cdd:COG0488  315 VLELEGLSKSYGDKTLLDDLSLRIDRGD-RIgLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV----------KIGY 382

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS--TVYDNLlfpWQIRHKtpDPERFSAD-LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:COG0488  383 FDQHQEELDPdkTVLDEL---RDGAPG--GTEQEVRGyLGRFLFSGDDAFKPVGVLSGGEKARLALAKLLLSPPNVLLLD 457


                 ....*..
gi 504695722 163 EITSALD 169
Cdd:COG0488  458 EPTNHLD 464
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
8-219 1.18e-28

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 108.25  E-value: 1.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIStlSPEAYRQQVsysV 87
Cdd:PRK11248   2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVE--GPGAERGVV---F 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFD-STVYDNLLFPWQIRhKTPDPERFSA--------DLARFNlppdtlTKSVSELSGGEKQRVSLIRNLQFLPKV 158
Cdd:PRK11248  77 QNEGLLPwRNVQDNVAFGLQLA-GVEKMQRLEIahqmlkkvGLEGAE------KRYIWQLSGGQRQRVGIARALAANPQL 149

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 159 LLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLQPHGGKMQE 219
Cdd:PRK11248 150 LLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDIEEaVFMATELVLLSPGPGRVVE 211
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 8-211 1.23e-28

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: 106.98  E-value: 1.23e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIStlspEAYRQQVSYSV 87
Cdd:cd03269    1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLD----IAARNRIGYLP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLF-DSTVYDNLLFPWQIRHKTPDPERFSAD--LARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:cd03269   77 EERGLYpKMKVIDQLVYLAQLKGLKKEEARRRIDewLERLEL-SEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDEP 155

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 165 TSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITH-ADDVLTLQ 211
Cdd:cd03269  156 FSGLDPVNVELLKDVI-RELARAGKTVILSTHQMELVEElCDRVLLLN 202
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 1-196 1.28e-28

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 107.82  E-value: 1.28e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEfrlIT---GPSGCGKSTLLKIIASL--LTP---TSGKIFFEGKDI- 71
Cdd:COG1117    5 ASTLEPKIEVRNLNVYYGDKQALKDINLDIPENK---VTaliGPSGCGKSTLLRCLNRMndLIPgarVEGEILLDGEDIy 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  72 -STLSPEAYRQQVSYSVQTPSLFDSTVYDNLLFPWQIRHKTPDPErfsAD------LARFNLPP---DTLTKSVSELSGG 141
Cdd:COG1117   82 dPDVDVVELRRRVGMVFQKPNPFPKSIYDNVAYGLRLHGIKSKSE---LDeiveesLRKAALWDevkDRLKKSALGLSGG 158

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 142 EKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHryvrE--QNIAVLWVTH 196
Cdd:COG1117  159 QQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELIL----ElkKDYTIVIVTH 211
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 3-215 1.31e-28

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 112.21  E-value: 1.31e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYRT-GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFF-EGKDISTLSpeayr 80
Cdd:COG4178  358 SEDGALALEDLTLRTpDGRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP----- 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 qqvsysvQTPSLFDSTVYDNLLFPwQIRHKTPDpERFSADLARFNLPPdtLTKSVSE-------LSGGEKQRVSLIRNLQ 153
Cdd:COG4178  433 -------QRPYLPLGTLREALLYP-ATAEAFSD-AELREALEAVGLGH--LAERLDEeadwdqvLSLGEQQRLAFARLLL 501

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRyvREQNIAVLWVTHDANEITHADDVLTLQPHGG 215
Cdd:COG4178  502 HKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGHRSTLAAFHDRVLELTGDGS 561
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
14-210 1.56e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 106.16  E-value: 1.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  14 GYrtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDistlspeayrqQVSYSVQTPSLF 93
Cdd:NF040873   1 GY--GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGGA-----------RVAYVPQRSEVP 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DS---TVYDNL-------LFPWQiRHKTPDPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:NF040873  68 DSlplTVRDLVamgrwarRGLWR-RLTRDDRAAVDDALERVGLA-DLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDE 145

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 164 ITSALDDANKRNVNEIIHRYVREQnIAVLWVTHDANEITHADDVLTL 210
Cdd:NF040873 146 PTTGLDAESRERIIALLAEEHARG-ATVVVVTHDLELVRRADPCVLL 191
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 8-210 1.76e-28

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 105.47  E-value: 1.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSpEAYRQQVSY 85
Cdd:cd03247    1 LSINNVsfSYPEQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLE-KALSSLISV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNLlfpwqirhktpdPERFsadlarfnlppdtltksvselSGGEKQRVSLIRNLQFLPKVLLLDEIT 165
Cdd:cd03247   80 LNQRPYLFDTTLRNNL------------GRRF---------------------SGGERQRLALARILLQDAPIVLLDEPT 126

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 166 SALDDANKRNVNEIIHRYVREQNIavLWVTHDANEITHADDVLTL 210
Cdd:cd03247  127 VGLDPITERQLLSLIFEVLKDKTL--IWITHHLTGIEHMDKILFL 169
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 15-196 7.74e-28

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 107.58  E-value: 7.74e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  15 YRTGGTTI--LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE---AYRQQVSYSVQT 89
Cdd:PRK11153  11 FPQGGRTIhaLNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKelrKARRQIGMIFQH 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 PSLFDS-TVYDNLLFPWQIRHKTPD--PERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:PRK11153  91 FNLLSSrTVFDNVALPLELAGTPKAeiKARVTELLELVGL-SDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATS 169

                        170       180       190
                 ....*....|....*....|....*....|
gi 504695722 167 ALDDANKRNVNEIIHRYVREQNIAVLWVTH 196
Cdd:PRK11153 170 ALDPATTRSILELLKDINRELGLTIVLITH 199
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 5-192 9.12e-28

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: 105.06  E-value: 9.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIED--VGYrtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY-RQ 81
Cdd:COG0410    1 MPMLEVENlhAGY--GGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDITGLPPHRIaRL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSVQTPSLFDS-TVYDNLLFPWQIRhktPDPERFSADLAR-FNLPP---DTLTKSVSELSGGEKQRVS----LIRNl 152
Cdd:COG0410   79 GIGYVPEGRRIFPSlTVEENLLLGAYAR---RDRAEVRADLERvYELFPrlkERRRQRAGTLSGGEQQMLAigraLMSR- 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504695722 153 qflPKVLLLDEITSALddANK--RNVNEIIHRyVREQNIAVL 192
Cdd:COG0410  155 ---PKLLLLDEPSLGL--APLivEEIFEIIRR-LNREGVTIL 190
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 8-215 9.54e-28

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: 103.39  E-value: 9.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTG-GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFF-EGKDISTLSpeayrqqvsy 85
Cdd:cd03223    1 IELENLSLATPdGRVLLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP---------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 svQTPSLFDSTVYDNLLFPWQirhktpdperfsadlarfnlppdtltksvSELSGGEKQRVSLIRNLQFLPKVLLLDEIT 165
Cdd:cd03223   71 --QRPYLPLGTLREQLIYPWD-----------------------------DVLSGGEQQRLAFARLLLHKPKFVFLDEAT 119

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504695722 166 SALDDANKRNvneiIHRYVREQNIAVLWVTHDANEITHADDVLTLQPHGG 215
Cdd:cd03223  120 SALDEESEDR----LYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 16-211 1.35e-27

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: 107.51  E-value: 1.35e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   16 RTGGTTIlnNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKI------FFEGKDISTLSPEayRQQVSYSVQT 89
Cdd:TIGR02142   8 RLGDFSL--DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIvlngrtLFDSRKGIFLPPE--KRRIGYVFQE 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   90 PSLFDS-TVYDNLLFpwQIRHKTPDPERFSAD--LARFNLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:TIGR02142  84 ARLFPHlSVRGNLRY--GMKRARPSERRISFErvIELLGIGH-LLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLA 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 504695722  167 ALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQ 211
Cdd:TIGR02142 161 ALDDPRKYEILPYLERLHAEFGIPILYVSHSLQEVLRlADRVVVLE 206
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 10-214 1.38e-27

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: 104.37  E-value: 1.38e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYSVQT 89
Cdd:cd03265    3 VENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVR-EPREVRRRIGIVFQD 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 PSLFDS-TVYDNLL-------FPWQIRHktpdpERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:cd03265   82 LSVDDElTGWENLYiharlygVPGAERR-----ERIDELLDFVGL-LEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFL 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504695722 162 DEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQPHG 214
Cdd:cd03265  156 DEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHG 208
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 10-219 1.58e-27

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: 104.61  E-value: 1.58e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDV--GYRtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSV 87
Cdd:cd03254    5 FENVnfSYD-EKKPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRSMIGVVL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDSTVYDNllfpwqIRHKTPDPER----FSADLARFNLPPDTLTK----SVSE----LSGGEKQRVSLIRNLQFL 155
Cdd:cd03254   84 QDTFLFSGTIMEN------IRLGRPNATDeeviEAAKEAGAHDFIMKLPNgydtVLGEnggnLSQGERQLLAIARAMLRD 157

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 156 PKVLLLDEITSALDDANKRNVNEIIHRYVreQNIAVLWVTHDANEITHADDVLTLqpHGGKMQE 219
Cdd:cd03254  158 PKILILDEATSNIDTETEKLIQEALEKLM--KGRTSIIIAHRLSTIKNADKILVL--DDGKIIE 217
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 1-210 3.30e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 104.83  E-value: 3.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTT--ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA 78
Cdd:PRK13648   1 MEDKNSIIVFKNVSFQYQSDAsfTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEK 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 YRQQVSYSVQTP--SLFDSTV-YD------NLLFPWQIRHktpdpERFSADLARFNLppdtLTKSVSE---LSGGEKQRV 146
Cdd:PRK13648  81 LRKHIGIVFQNPdnQFVGSIVkYDvafgleNHAVPYDEMH-----RRVSEALKQVDM----LERADYEpnaLSGGQKQRV 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 147 SLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:PRK13648 152 AIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVM 215
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 8-169 3.53e-27

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: 103.04  E-value: 3.53e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLItGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYSV 87
Cdd:cd03264    1 LQLENLTKRYGKKRALDGVSLTLGPGMYGLL-GPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLK-QPQKLRRRIGYLP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFPWQIR--HKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:cd03264   79 QEFGVYPNfTVREFLDYIAWLKgiPSKEVKARVDEVLELVNL-GDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDEP 157


                 ....*
gi 504695722 165 TSALD 169
Cdd:cd03264  158 TAGLD 162
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
8-200 4.72e-27

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 103.94  E-value: 4.72e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIE--DVGYrtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:PRK11231   3 LRTEnlTVGY--GTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLARRLAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQ---TPSlfDSTVYDNLLF---PWQI---RHKTPDPERFSADLARFNLppDTLT-KSVSELSGGEKQRVSLIRNLQFL 155
Cdd:PRK11231  81 LPQhhlTPE--GITVRELVAYgrsPWLSlwgRLSAEDNARVNQAMEQTRI--NHLAdRRLTDLSGGQRQRAFLAMVLAQD 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 156 PKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANE 200
Cdd:PRK11231 157 TPVVLLDEPTTYLDINHQVELMRLM-RELNTQGKTVVTVLHDLNQ 200
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 17-210 8.92e-27

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: 101.47  E-value: 8.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  17 TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP--TSGKIFFEGKDistLSPEAYRQQVSYSVQTPSLFD 94
Cdd:cd03213   19 KSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRP---LDKRSFRKIIGYVPQDDILHP 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 S-TVYDNLlfpwqirhktpdpeRFSADLarfnlppdtltksvSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANK 173
Cdd:cd03213   96 TlTVRETL--------------MFAAKL--------------RGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSA 147

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 174 RNVNEIIHRYvREQNIAVLWVTHDA-NEITHADDVLTL 210
Cdd:cd03213  148 LQVMSLLRRL-ADTGRTIICSIHQPsSEIFELFDKLLL 184
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 8-215 9.29e-27

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 105.69  E-value: 9.29e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSV 87
Cdd:PRK09536   4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAASRRVASVP 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSL-FDSTVYdnllfpwQIRH--KTPDPERFS----------------ADLARFnlppdtLTKSVSELSGGEKQRVSL 148
Cdd:PRK09536  84 QDTSLsFEFDVR-------QVVEmgRTPHRSRFDtwtetdraaveramerTGVAQF------ADRPVTSLSGGERQRVLL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVrEQNIAVLWVTHDANEITHADDVLTLQPHGG 215
Cdd:PRK09536 151 ARALAQATPVLLLDEPTASLDINHQVRTLELVRRLV-DDGKTAVAAIHDLDLAARYCDELVLLADGR 216
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 22-219 1.03e-26

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 107.12  E-value: 1.03e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDNL 101
Cdd:TIGR00958 496 VLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYLHRQVALVGQEPVLFSGSVRENI 575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  102 LFPWQirhKTPDPERFSADLARF------NLPPDTLT---KSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:TIGR00958 576 AYGLT---DTPDEEIMAAAKAANahdfimEFPNGYDTevgEKGSQLSGGQKQRIAIARALVRKPRVLILDEATSALDAEC 652

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 504695722  173 KRNVNEIIHRYVReqniAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:TIGR00958 653 EQLLQESRSRASR----TVLLIAHRLSTVERADQILVLK--KGSVVE 693
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 22-211 1.20e-26

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: 101.39  E-value: 1.20e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrqqVSYSVQTPSLFDSTVYDNL 101
Cdd:cd03250   20 TLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPGS-------------IAYVSQEPWIQNGTIRENI 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 LFpwqirHKTPDPERF---------SADLArfNLPPDTLT----KSVSeLSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:cd03250   87 LF-----GKPFDEERYekvikacalEPDLE--ILPDGDLTeigeKGIN-LSGGQKQRISLARAVYSDADIYLLDDPLSAV 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 169 DDankrNV-NEIIHRYVRE---QNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03250  159 DA----HVgRHIFENCILGlllNNKTRILVTHQLQLLPHADQIVVLD 201
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 10-197 1.28e-26

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 106.30  E-value: 1.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVGYRTGGTTILNNVSFSLLPGEfRL-ITGPSGCGKSTLLKIIASLLTPTSGKIFFE-GKDISTLSpeayrqqvsysv 87
Cdd:COG0488    1 LENLSKSFGGRPLLDDVSLSINPGD-RIgLVGRNGAGKSTLLKILAGELEPDSGEVSIPkGLRIGYLP------------ 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLL--FP--WQIRHK-----------TPDPERFSADLARF-------------------NLPPDTLT 132
Cdd:COG0488   68 QEPPLDDDlTVLDTVLdgDAelRALEAEleeleaklaepDEDLERLAELQEEFealggweaearaeeilsglGFPEEDLD 147

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 133 KSVSELSGGEKQRVSLIRNLqfL--PKVLLLDEITSALDdankrnvNEIIH---RYVREQNIAVLWVTHD 197
Cdd:COG0488  148 RPVSELSGGWRRRVALARAL--LsePDLLLLDEPTNHLD-------LESIEwleEFLKNYPGTVLVVSHD 208
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
8-197 1.49e-26

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 102.84  E-value: 1.49e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVG--YRTGGT-------TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE- 77
Cdd:PRK10419   4 LNVSGLShhYAHGGLsgkhqhqTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRAq 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  78 --AYRQQVSYSVQ-TPSLFD--STVYDNLLFPwqIRH-----KTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVS 147
Cdd:PRK10419  84 rkAFRRDIQMVFQdSISAVNprKTVREIIREP--LRHllsldKAERLARASEMLRAVDLDDSVLDKRPPQLSGGQLQRVC 161

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504695722 148 LIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK10419 162 LARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
 23-217 1.70e-26

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 102.23  E-value: 1.70e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLtPTSGKIFFEGKDISTLSPEAYRQQVSY-SVQTPSLFDSTVYDNL 101
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMAGLL-PGQGEILLNGRPLSDWSAAELARHRAYlSQQQSPPFAMPVFQYL 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 -LFpwqIRHKTPDPERFS--ADLA-RFNLpPDTLTKSVSELSGGEKQRVSLIRN-LQFLP------KVLLLDEITSALDD 170
Cdd:COG4138   91 aLH---QPAGASSEAVEQllAQLAeALGL-EDKLSRPLTQLSGGEWQRVRLAAVlLQVWPtinpegQLLLLDEPMNSLDV 166

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 171 ANKRNVNEIIhRYVREQNIAVLWVTHDANE-ITHADDVLTLqpHGGKM 217
Cdd:COG4138  167 AQQAALDRLL-RELCQQGITVVMSSHDLNHtLRHADRVWLL--KQGKL 211
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 8-215 1.92e-26

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: 106.36  E-value: 1.92e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    8 LTIEDVGYRTG-GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYS 86
Cdd:TIGR01193 474 IVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFINYL 553

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   87 VQTPSLFDSTVYDNLLFpwQIRHKTPDPERFSA--------DLARFNLPPDT-LTKSVSELSGGEKQRVSLIRNLQFLPK 157
Cdd:TIGR01193 554 PQEPYIFSGSILENLLL--GAKENVSQDEIWAAceiaeikdDIENMPLGYQTeLSEEGSSISGGQKQRIALARALLTDSK 631

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722  158 VLLLDEITSALDDANKRnvnEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQpHGG 215
Cdd:TIGR01193 632 VLILDESTSNLDTITEK---KIVNNLLNLQDKTIIFVAHRLSVAKQSDKIIVLD-HGK 685
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 33-206 3.44e-26

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: 100.65  E-value: 3.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  33 GEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSYSVQTPSLFDS-TVYDNL---LFPwQIR 108
Cdd:cd03298   24 GEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPA--DRPVSMLFQENNLFAHlTVEQNVglgLSP-GLK 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 109 HKTPDPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQN 188
Cdd:cd03298  101 LTAEDRQAIEVALARVGLA-GLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLHAETK 179

                        170
                 ....*....|....*...
gi 504695722 189 IAVLWVTHDANEITHADD 206
Cdd:cd03298  180 MTVLMVTHQPEDAKRLAQ 197
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 8-204 4.10e-26

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: 100.13  E-value: 4.10e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEaYRQQVSYSV 87
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDE-PHENILYLG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   88 QTPSL-FDSTVYDNLLFpWQIRHKTPDPERFSAdLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:TIGR01189  80 HLPGLkPELSALENLHF-WAAIHGGAQRTIEDA-LAAVGLT-GFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTT 156

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 504695722  167 ALDDANKRNVNEIIHRYVREQNIAVLwVTHDANEITHA 204
Cdd:TIGR01189 157 ALDKAGVALLAGLLRAHLARGGIVLL-TTHQDLGLVEA 193
cbiO PRK13641
energy-coupling factor transporter ATPase;
23-214 4.46e-26

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 102.21  E-value: 4.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDI----STLSPEAYRQQVSYSVQTP--SLFDST 96
Cdd:PRK13641  23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHItpetGNKNLKKLRKKVSLVFQFPeaQLFENT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLLFPWQIRHKTPDPERFSAD--LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKR 174
Cdd:PRK13641 103 VLKDVEFGPKNFGFSEDEAKEKALkwLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRK 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504695722 175 NVNEIIHRYVREQNIAVLwVTHDANEIT-HADDVLTLQpHG 214
Cdd:PRK13641 183 EMMQLFKDYQKAGHTVIL-VTHNMDDVAeYADDVLVLE-HG 221
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 10-210 8.53e-26

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: 99.88  E-value: 8.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVG--YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSV 87
Cdd:cd03244    5 FKNVSlrYRPNLPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLALFRLVELSSGSILIDGVDISKIGLHDLRSRISIIP 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDSTVYDNLlfpwQIRHKTPDPERFSAdLARFNL------PPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPK 157
Cdd:cd03244   85 QDPVLFSGTIRSNL----DPFGEYSDEELWQA-LERVGLkefvesLPGGLDTVVEEggenLSVGQRQLLCLARALLRKSK 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 158 VLLLDEITSALDDANkrnvNEIIHRYVREQ--NIAVLWVTHDANEITHADDVLTL 210
Cdd:cd03244  160 ILVLDEATASVDPET----DALIQKTIREAfkDCTVLTIAHRLDTIIDSDRILVL 210
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
12-209 1.53e-25

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 99.40  E-value: 1.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  12 DVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGkdISTLSPEA----YRQQVSYSV 87
Cdd:PRK09493   6 NVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDG--LKVNDPKVderlIRQEAGMVF 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLF-PWQIR-HKTPDPERFSADL-------ARFNLPPdtltksvSELSGGEKQRVSLIRNLQFLPK 157
Cdd:PRK09493  84 QQFYLFPHlTALENVMFgPLRVRgASKEEAEKQARELlakvglaERAHHYP-------SELSGGQQQRVAIARALAVKPK 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504695722 158 VLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHdanEITHADDVLT 209
Cdd:PRK09493 157 LMLFDEPTSALDPELRHEVLKVM-QDLAEEGMTMVIVTH---EIGFAEKVAS 204
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
 8-196 1.66e-25

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: 99.64  E-value: 1.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIAS--LLTPTSGKIFFEGKDISTLSP-EAYRQQVS 84
Cdd:TIGR01978   1 LKIKDLHVSVEDKEILKGVNLTVKKGEIHAIMGPNGSGKSTLSKTIAGhpSYEVTSGTILFKGQDLLELEPdERARAGLF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   85 YSVQTP--------SLFDSTVYDNLLfpwQIRHKTPDP-----ERFSADLARFNLPPDTLTKSVSE-LSGGEKQRVSLIR 150
Cdd:TIGR01978  81 LAFQYPeeipgvsnLEFLRSALNARR---SARGEEPLDlldfeKLLKEKLALLDMDEEFLNRSVNEgFSGGEKKRNEILQ 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 504695722  151 NLQFLPKVLLLDEITSALD-DAnKRNVNEIIHRYvREQNIAVLWVTH 196
Cdd:TIGR01978 158 MALLEPKLAILDEIDSGLDiDA-LKIVAEGINRL-REPDRSFLIITH 202
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 9-199 2.24e-25

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 99.39  E-value: 2.24e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   9 TIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQ 88
Cdd:COG4604    3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKRLAILRQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 TPSlFDS--TVYDnLL----FPW-QIRHKTPDPERFSADLARFNLPP--DtltKSVSELSGGEKQRVslirnlqFLPKVL 159
Cdd:COG4604   83 ENH-INSrlTVRE-LVafgrFPYsKGRLTAEDREIIDEAIAYLDLEDlaD---RYLDELSGGQRQRA-------FIAMVL 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 160 -------LLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDAN 199
Cdd:COG4604  151 aqdtdyvLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDIN 197
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 11-211 2.32e-25

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: 103.36  E-value: 2.32e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  11 EDV--GYRtGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQ 88
Cdd:COG5265  361 ENVsfGYD-PERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLFRFYDVTSGRILIDGQDIRDVTQASLRAAIGIVPQ 439

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 TPSLFDSTVYDNllfpwqIRHKTPDPERF-------SADLARF--NLPP--DTLtksVSE----LSGGEKQRVSLIRNLQ 153
Cdd:COG5265  440 DTVLFNDTIAYN------IAYGRPDASEEeveaaarAAQIHDFieSLPDgyDTR---VGErglkLSGGEKQRVAIARTLL 510

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRYVREQniAVLWVTHDANEITHADDVLTLQ 211
Cdd:COG5265  511 KNPPILIFDEATSALDSRTERAIQAALREVARGR--TTLVIAHRLSTIVDADEILVLE 566
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
5-217 3.20e-25

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 99.48  E-value: 3.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVS 84
Cdd:PRK10575   9 DTTFALRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARKVA 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 Y-SVQTPSLFDSTVYDNLL---FPWQ---IRHKTPDPERFSADLARFNLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPK 157
Cdd:PRK10575  89 YlPQQLPAAEGMTVRELVAigrYPWHgalGRFGAADREKVEEAISLVGLKP-LAHRLVDSLSGGERQRAWIAMLVAQDSR 167

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 158 VLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDAN-EITHADDVLTLqpHGGKM 217
Cdd:PRK10575 168 CLLLDEPTSALDIAHQVDVLALVHRLSQERGLTVIAVLHDINmAARYCDYLVAL--RGGEM 226
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
19-200 3.56e-25

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 101.07  E-value: 3.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPeaYRQQVSYSVQTPSLFDS-TV 97
Cdd:PRK11607  31 GQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP--YQRPINMMFQSYALFPHmTV 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLLFpwqirhktpdperfsaDLARFNLPPDTLTKSVSE-----------------LSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK11607 109 EQNIAF----------------GLKQDKLPKAEIASRVNEmlglvhmqefakrkphqLSGGQRQRVALARSLAKRPKLLL 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 161 LDEITSALD----DANKRNVNEIIHRYvreqNIAVLWVTHDANE 200
Cdd:PRK11607 173 LDEPMGALDkklrDRMQLEVVDILERV----GVTCVMVTHDQEE 212
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 8-208 3.73e-25

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 98.98  E-value: 3.73e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIffegkdISTLSPEAYRQQvsysv 87
Cdd:PRK11247  13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL------LAGTAPLAEARE----- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDstvyDNLLFPWQirhKTPD-----------PERFSAdLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:PRK11247  82 DTRLMFQ----DARLLPWK---KVIDnvglglkgqwrDAALQA-LAAVGLA-DRANEWPAALSGGQKQRVALARALIHRP 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504695722 157 KVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVL 208
Cdd:PRK11247 153 GLLLLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEaVAMADRVL 205
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 5-196 6.92e-25

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 98.31  E-value: 6.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL--LTP---TSGKIFFEGKDIstLSPEA- 78
Cdd:PRK14239   3 EPILQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndLNPevtITGSIVYNGHNI--YSPRTd 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 ---YRQQVSYSVQTPSLFDSTVYDNLLFPWQIRhKTPDPERFSADLAR-------FNLPPDTLTKSVSELSGGEKQRVSL 148
Cdd:PRK14239  81 tvdLRKEIGMVFQQPNPFPMSIYENVVYGLRLK-GIKDKQVLDEAVEKslkgasiWDEVKDRLHDSALGLSGGQQQRVCI 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIhrYVREQNIAVLWVTH 196
Cdd:PRK14239 160 ARVLATSPKIILLDEPTSALDPISAGKIEETL--LGLKDDYTMLLVTR 205
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 2-205 8.96e-25

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 101.44  E-value: 8.96e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   2 KDNSAVLTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLkiiaSLLT----PTSGKIFFEGKDISTLS 75
Cdd:PRK11160 333 AADQVSLTLNNVsfTYPDQPQPVLKGLSLQIKAGEKVALLGRTGCGKSTLL----QLLTrawdPQQGEILLNGQPIADYS 408

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  76 PEAYRQQVSYSVQTPSLFDSTVYDNLLfpwqIRHKTPDPERFSADLARFNLppDTLTKSVS-----------ELSGGEKQ 144
Cdd:PRK11160 409 EAALRQAISVVSQRVHLFSATLRDNLL----LAAPNASDEALIEVLQQVGL--EKLLEDDKglnawlgeggrQLSGGEQR 482

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 145 RVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVreQNIAVLWVTHDANEITHAD 205
Cdd:PRK11160 483 RLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA--QNKTVLMITHRLTGLEQFD 541
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 8-196 1.07e-24

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: 96.44  E-value: 1.07e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIA--SLLTPTSGKIFFEGKDISTLSPEAyRQQVsy 85
Cdd:cd03217    1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMghPKYEVTEGEILFKGEDITDLPPEE-RARL-- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 svqtpSLFDStvydnllfpWQirhktpDPERFS----ADLARFnlppdtltksVSE-LSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:cd03217   78 -----GIFLA---------FQ------YPPEIPgvknADFLRY----------VNEgFSGGEKKRNEILQLLLLEPDLAI 127

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504695722 161 LDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTH 196
Cdd:cd03217  128 LDEPDSGLDIDALRLVAEVI-NKLREEGKSVLIITH 162
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
11-214 1.32e-24

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 101.19  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  11 EDVGYRTGGTT-ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQT 89
Cdd:PRK13657 338 DDVSFSYDNSRqGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVTRASLRRNIAVVFQD 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 PSLFDSTVYDNllfpwqIRHKTPD--PERFSADLAR-----FNL-PPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPK 157
Cdd:PRK13657 418 AGLFNRSIEDN------IRVGRPDatDEEMRAAAERaqahdFIErKPDGYDTVVGErgrqLSGGERQRLAIARALLKDPP 491

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 158 VLLLDEITSALDDANKRNVNEIIHRyVReQNIAVLWVTHDANEITHADDVLTLQpHG 214
Cdd:PRK13657 492 ILILDEATSALDVETEAKVKAALDE-LM-KGRTTFIIAHRLSTVRNADRILVFD-NG 545
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 5-206 1.70e-24

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 97.55  E-value: 1.70e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL--LTPT---SGKIFFEGKDI--STLSPE 77
Cdd:PRK14243   8 ETVLRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLndLIPGfrvEGKVTFHGKNLyaPDVDPV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  78 AYRQQVSYSVQTPSLFDSTVYDNLLFPWQIRHKTPD----PERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQ 153
Cdd:PRK14243  88 EVRRRIGMVFQKPNPFPKSIYDNIAYGARINGYKGDmdelVERSLRQAALWDEVKDKLKQSGLSLSGGQQQRLCIARAIA 167

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVlwVTHDANEITHADD 206
Cdd:PRK14243 168 VQPEVILMDEPCSALDPISTLRIEELMHELKEQYTIII--VTHNMQQAARVSD 218
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
15-221 1.84e-24

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 100.56  E-value: 1.84e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  15 YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFD 94
Cdd:PRK10789 323 YPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQLDSWRSRLAVVSQTPFLFS 402

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 STVYDNLLF------PWQIRHktpdperfSADLAR-----FNLPPDTLTKsVSE----LSGGEKQRVSLIRNLQFLPKVL 159
Cdd:PRK10789 403 DTVANNIALgrpdatQQEIEH--------VARLASvhddiLRLPQGYDTE-VGErgvmLSGGQKQRISIARALLLNAEIL 473

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 160 LLDEITSALDDankRNVNEIIH--RYVREQNiAVLWVTHDANEITHADDVLTLQpHGGKMQEAN 221
Cdd:PRK10789 474 ILDDALSAVDG---RTEHQILHnlRQWGEGR-TVIISAHRLSALTEASEILVMQ-HGHIAQRGN 532
MsbA_rel TIGR02204
ABC transporter, permease/ATP-binding protein; This protein is related to a Proteobacterial ...
 23-210 3.33e-24

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


Pssm-ID: 131259 [Multi-domain]  Cd Length: 576  Bit Score: 99.77  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDNll 102
Cdd:TIGR02204 356 LDGLNLTVRPGETVALVGPSGAGKSTLFQLLLRFYDPQSGRILLDGVDLRQLDPAELRARMALVPQDPVLFAASVMEN-- 433

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  103 fpwqIRHKTPDPE----RFSADLARFN-----LPP--DT-LTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDD 170
Cdd:TIGR02204 434 ----IRYGRPDATdeevEAAARAAHAHefisaLPEgyDTyLGERGVTLSGGQRQRIAIARAILKDAPILLLDEATSALDA 509

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 504695722  171 ANKRNVNEIIHRYVREQniAVLWVTHDANEITHADDVLTL 210
Cdd:TIGR02204 510 ESEQLVQQALETLMKGR--TTLIIAHRLATVLKADRIVVM 547
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 1-196 3.89e-24

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 96.25  E-value: 3.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIAS--LLTPTSGKIFFEGKDISTLSPEA 78
Cdd:CHL00131   1 MNKNKPILEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGhpAYKILEGDILFKGESILDLEPEE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 YRQQ-----VSYSVQTPSLFDStvyDNLLFPWQIRHKTP-----DPERF----SADLARFNLPPDTLTKSVSE-LSGGEK 143
Cdd:CHL00131  81 RAHLgiflaFQYPIEIPGVSNA---DFLRLAYNSKRKFQglpelDPLEFleiiNEKLKLVGMDPSFLSRNVNEgFSGGEK 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 144 QRVSLirnLQFL---PKVLLLDEITSALD-DAnKRNVNEIIHRYVREQNIAVLwVTH 196
Cdd:CHL00131 158 KRNEI---LQMAlldSELAILDETDSGLDiDA-LKIIAEGINKLMTSENSIIL-ITH 209
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 22-210 5.79e-24

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: 94.79  E-value: 5.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDNL 101
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTIPLEDLRSSLTIIPQDPTLFSGTIRSNL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 lfpwqirhktpDPE-RFSADLARFNLppdTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANkrnvNEII 180
Cdd:cd03369  103 -----------DPFdEYSDEEIYGAL---RVSEGGLNLSQGQRQLLCLARALLKRPRVLVLDEATASIDYAT----DALI 164

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504695722 181 HRYVRE--QNIAVLWVTHDANEITHADDVLTL 210
Cdd:cd03369  165 QKTIREefTNSTILTIAHRLRTIIDYDKILVM 196
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 22-206 1.34e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 95.10  E-value: 1.34e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTS-----GKIFFEGKDI--STLSPEAYRQQVSYSVQTPSLFD 94
Cdd:PRK14258  22 ILEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMNELESevrveGRVEFFNQNIyeRRVNLNRLRRQVSMVHPKPNLFP 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 STVYDNL-----LFPWQIRHKTPD-PERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:PRK14258 102 MSVYDNVaygvkIVGWRPKLEIDDiVESALKDADLWDEIKHKIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGL 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 169 DDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADD 206
Cdd:PRK14258 182 DPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSD 219
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 26-217 1.65e-23

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 94.23  E-value: 1.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  26 VSFSLLPGEFRLITGPSGCGKSTLLKIIASLLtPTSGKIFFEGKDISTLS-PEAYRQQVSYSVQTPSLFDSTVYDNLLFP 104
Cdd:PRK03695  15 LSAEVRAGEILHLVGPNGAGKSTLLARMAGLL-PGSGSIQFAGQPLEAWSaAELARHRAYLSQQQTPPFAMPVFQYLTLH 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 105 WQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRN-LQFLP------KVLLLDEITSALDDANKRNVN 177
Cdd:PRK03695  94 QPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPdinpagQLLLLDEPMNSLDVAQQAALD 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504695722 178 EIIHRYVReQNIAVLWVTHDANE-ITHADDVLTLqpHGGKM 217
Cdd:PRK03695 174 RLLSELCQ-QGIAVVMSSHDLNHtLRHADRVWLL--KQGKL 211
cbiO PRK13640
energy-coupling factor transporter ATPase;
1-210 2.17e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 94.87  E-value: 2.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNsaVLTIEDVG--YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTS---GKIFFEGKDISTLS 75
Cdd:PRK13640   1 MKDN--IVEFKHVSftYPDSKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDnpnSKITVDGITLTAKT 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  76 PEAYRQQVSYSVQTP--SLFDSTVYDNLLFPWQIRhKTPDPE--RFSAD-LARFNLPpDTLTKSVSELSGGEKQRVSLIR 150
Cdd:PRK13640  79 VWDIREKVGIVFQNPdnQFVGATVGDDVAFGLENR-AVPRPEmiKIVRDvLADVGML-DYIDSEPANLSGGQKQRVAIAG 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 151 NLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:PRK13640 157 ILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVL 216
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 19-211 2.92e-23

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 97.22  E-value: 2.92e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLtPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVY 98
Cdd:PRK11174 362 GKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRELDPESWRKHLSWVGQNPQLPHGTLR 440

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  99 DNLLFpwqiRHKTPDPERFSADLAR-----F-NLPPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:PRK11174 441 DNVLL----GNPDASDEQLQQALENawvseFlPLLPQGLDTPIGDqaagLSVGQAQRLALARALLQPCQLLLLDEPTASL 516

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504695722 169 DDANKRNVNEIIHRYVREQniAVLWVTHDANEITHADDVLTLQ 211
Cdd:PRK11174 517 DAHSEQLVMQALNAASRRQ--TTLMVTHQLEDLAQWDQIWVMQ 557
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
6-211 3.23e-23

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 95.87  E-value: 3.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSY 85
Cdd:PRK11000   2 ASVTLRNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPA--ERGVGM 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS-TVYDNLLFPWQIRhKTPDPERFSadlaRFNLPPDTLT------KSVSELSGGEKQRVSLIRNLQFLPKV 158
Cdd:PRK11000  80 VFQSYALYPHlSVAENMSFGLKLA-GAKKEEINQ----RVNQVAEVLQlahlldRKPKALSGGQRQRVAIGRTLVAEPSV 154

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504695722 159 LLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE-ITHADDVLTLQ 211
Cdd:PRK11000 155 FLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEaMTLADKIVVLD 208
cbiO PRK13637
energy-coupling factor transporter ATPase;
20-216 3.61e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 94.34  E-value: 3.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  20 TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIS--TLSPEAYRQQVSYSVQTP--SLFDS 95
Cdd:PRK13637  20 KKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITdkKVKLSDIRKKVGLVFQYPeyQLFEE 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 TVYDNLLFPWQIRHKTPDP--ERFSADLARFNLPPDTLT-KSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:PRK13637 100 TIEKDIAFGPINLGLSEEEieNRVKRAMNIVGLDYEDYKdKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKG 179

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 173 KRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLqpHGGK 216
Cdd:PRK13637 180 RDEILNKIKELHKEYNMTIILVSHSMEDVAKlADRIIVM--NKGK 222
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 18-207 3.75e-23

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 96.63  E-value: 3.75e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSYSVQTPSLFDS- 95
Cdd:COG3845   16 GGVVANDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKPVRIRSPrDAIALGIGMVHQHFMLVPNl 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 TVYDNLLFPWQIRHKT-PDPERFSADLAR------FNLPPDTLtksVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:COG3845   96 TVAENIVLGLEPTKGGrLDRKAARARIRElserygLDVDPDAK---VEDLSVGEQQRVEILKALYRGARILILDEPTAVL 172

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 169 DDANKRNVNEIIHRyVREQNIAVLWVTHDANEI-THADDV 207
Cdd:COG3845  173 TPQEADELFEILRR-LAAEGKSIIFITHKLREVmAIADRV 211
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 23-202 4.02e-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: 93.17  E-value: 4.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQ-QVSYSVQTPSLFDSTVYDNL 101
Cdd:cd03267   37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRiGVVFGQKTQLWWDLPVIDSF 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 LFPWQIRHKtpDPERFSADLARF----NLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVN 177
Cdd:cd03267  117 YLLAAIYDL--PPARFKKRLDELsellDLEE-LLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIR 193

                        170       180
                 ....*....|....*....|....*
gi 504695722 178 EIIHRYVREQNIAVLWVTHDANEIT 202
Cdd:cd03267  194 NFLKEYNRERGTTVLLTSHYMKDIE 218
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 6-217 4.41e-23

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: 91.72  E-value: 4.41e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVgyRTGGTtiLNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVS 84
Cdd:cd03215    3 PVLEVRGL--SVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPrDAIRAGIA 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YsV----QTPSLF-DSTVYDNLLFPWQirhktpdperfsadlarfnlppdtltksvseLSGGEKQRVSLIRNLQFLPKVL 159
Cdd:cd03215   79 Y-VpedrKREGLVlDLSVAENIALSSL-------------------------------LSGGNQQKVVLARWLARDPRVL 126

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKM 217
Cdd:cd03215  127 ILDEPTRGVDVGAKAEIYRLIREL-ADAGKAVLLISSELDELLGlCDRILVM--YEGRI 182
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 22-214 4.45e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 93.57  E-value: 4.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLL------TPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDS 95
Cdd:PRK14246  25 ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIeiydskIKVDGKVLYFGKDIFQIDAIKLRKEVGMVFQQPNPFPH 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 -TVYDNLLFPWQ---IRHKTPDPERFSADLARFNLPP---DTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:PRK14246 105 lSIYDNIAYPLKshgIKEKREIKKIVEECLRKVGLWKevyDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMI 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 504695722 169 DDANKRNVNEIIHRYVREqnIAVLWVTHDANEITHADDVLTLQPHG 214
Cdd:PRK14246 185 DIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNG 228
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
27-201 8.38e-23

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 91.95  E-value: 8.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  27 SFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDiSTLSPEAYRqQVSYSVQTPSLFDS-TVYDNL---L 102
Cdd:PRK10771  19 DLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRR-PVSMLFQENNLFSHlTVAQNIglgL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 103 FPwQIRhKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHR 182
Cdd:PRK10771  97 NP-GLK-LNAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQ 174

                        170       180
                 ....*....|....*....|..
gi 504695722 183 YVREQNIAVLWVTH---DANEI 201
Cdd:PRK10771 175 VCQERQLTLLMVSHsleDAARI 196
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 23-201 1.00e-22

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: 91.66  E-value: 1.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYSVQTPSLFDS-TVYDNL 101
Cdd:cd03266   21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVK-EPAEARRRLGFVSDSTGLYDRlTARENL 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 LFPWQI----RHKTPDPERFSADLARFNlppDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVN 177
Cdd:cd03266  100 EYFAGLyglkGDELTARLEELADRLGME---ELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176

                        170       180
                 ....*....|....*....|....
gi 504695722 178 EIIHRYvREQNIAVLWVTHDANEI 201
Cdd:cd03266  177 EFIRQL-RALGKCILFSTHIMQEV 199
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 8-217 1.62e-22

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: 90.74  E-value: 1.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEayRQQVSYSV 87
Cdd:cd03268    1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA--LRRIGALI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFP---WQIRHKtpdpeRFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:cd03268   79 EAPGFYPNlTARENLRLLarlLGIRKK-----RIDEVLDVVGLK-DSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 164 ITSALDDANKRNVNEIIHRYvREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKM 217
Cdd:cd03268  153 PTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKvADRIGII--NKGKL 204
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 23-197 1.71e-22

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: 94.75  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEfRL-ITGPSGCGKSTLLKIIASLLtPTSGKIFFEGKDISTLSPEAYRQ-----QVsysV-QTPslFDS 95
Cdd:COG4172  302 VDGVSLTLRRGE-TLgLVGESGSGKSTLGLALLRLI-PSEGEIRFDGQDLDGLSRRALRPlrrrmQV---VfQDP--FGS 374

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 -----TVYDNLLFPWQIRHKTPDP----ERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:COG4172  375 lsprmTVGQIIAEGLRVHGPGLSAaerrARVAEALEEVGLDPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504695722 167 ALDdankRNV-NEIIH---RYVREQNIAVLWVTHD 197
Cdd:COG4172  455 ALD----VSVqAQILDllrDLQREHGLAYLFISHD 485
cbiO PRK13650
energy-coupling factor transporter ATPase;
22-211 1.72e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 92.49  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTP--SLFDSTVYD 99
Cdd:PRK13650  22 TLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEENVWDIRHKIGMVFQNPdnQFVGATVED 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 100 NLLFPWQ---IRHKTPDpERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNV 176
Cdd:PRK13650 102 DVAFGLEnkgIPHEEMK-ERVNEALELVGMQ-DFKEREPARLSGGQKQRVAIAGAVAMRPKIIILDEATSMLDPEGRLEL 179

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 504695722 177 NEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:PRK13650 180 IKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMK 214
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 22-192 2.19e-22

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: 90.79  E-value: 2.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP---TSGKIFFEGKDistLSPEAYRQQVSYSVQTPSLFDS-TV 97
Cdd:cd03234   22 ILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQP---RKPDQFQKCVAYVRQDDILLPGlTV 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLLFPWQIR--HKTPDPER-FSADLARFNLPPDTLTKS--VSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:cd03234   99 RETLTYTAILRlpRKSSDAIRkKRVEDVLLRDLALTRIGGnlVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDSFT 178

                        170       180
                 ....*....|....*....|
gi 504695722 173 KRNVNEIIHRYVREQNIAVL 192
Cdd:cd03234  179 ALNLVSTLSQLARRNRIVIL 198
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 8-218 3.82e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 91.62  E-value: 3.82e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTT-----ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFE------GKDISTLSP 76
Cdd:PRK13634   3 ITFQKVEHRYQYKTpferrALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGervitaGKKNKKLKP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  77 eaYRQQVSYSVQTP--SLFDSTVYDNLLF-PWQIRHKTPDPERFSAD-LARFNLPPDTLTKSVSELSGGEKQRVSLIRNL 152
Cdd:PRK13634  83 --LRKKVGIVFQFPehQLFEETVEKDICFgPMNFGVSEEDAKQKAREmIELVGLPEELLARSPFELSGGQMRRVAIAGVL 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 153 QFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQ 218
Cdd:PRK13634 161 AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARyADQIVVM--HKGTVF 225
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 25-197 6.47e-22

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 93.38  E-value: 6.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  25 NVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP---EAYRQQVSYSVQTP-SLFD--STVY 98
Cdd:PRK10261 342 KVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPgklQALRRDIQFIFQDPyASLDprQTVG 421

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  99 DNLLFPWQIR---HKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRN 175
Cdd:PRK10261 422 DSIMEPLRVHgllPGKAAAARVAWLLERVGLLPEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVSIRGQ 501

                        170       180
                 ....*....|....*....|..
gi 504695722 176 VNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK10261 502 IINLLLDLQRDFGIAYLFISHD 523
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 7-217 8.59e-22

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 90.55  E-value: 8.59e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGE-FRLItGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIStlspEAYRQQVSY 85
Cdd:COG4152    1 MLELKGLTKRFGDKTAVDDVSFTVPKGEiFGLL-GPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD----PEDRRRIGY 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLF-DSTVYDNLLFPWQIRHKTPDPERFSAD--LARFNLPpDTLTKSVSELSGGEKQRV----SLIRNlqflPKV 158
Cdd:COG4152   76 LPEERGLYpKMKVGEQLVYLARLKGLSKAEAKRRADewLERLGLG-DRANKKVEELSKGNQQKVqliaALLHD----PEL 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 159 LLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEI-THADDVLTLqpHGGKM 217
Cdd:COG4152  151 LILDEPFSGLDPVNVELLKDVI-RELAAKGTTVIFSSHQMELVeELCDRIVII--NKGRK 207
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 23-208 9.53e-22

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 91.18  E-value: 9.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA---YRQQVSYSVQTPslFDS---- 95
Cdd:PRK11308  31 LDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAqklLRQKIQIVFQNP--YGSlnpr 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 -TVYDNLLFPWQIRHKTPDPERFS---ADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDA 171
Cdd:PRK11308 109 kKVGQILEEPLLINTSLSAAERREkalAMMAKVGLRPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVS 188

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 172 NKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVL 208
Cdd:PRK11308 189 VQAQVLNLMMDLQQELGLSYVFISHDLSVVEHiADEVM 226
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 19-207 1.40e-21

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 89.42  E-value: 1.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP--------EAYRQQVSYSVQTP 90
Cdd:PRK11264  15 GQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkgliRQLRQHVGFVFQNF 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  91 SLF-DSTVYDNLLFPWQIRHKTPDPE---RFSADLARFNLP--PDTLTKsvsELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:PRK11264  95 NLFpHRTVLENIIEGPVIVKGEPKEEataRARELLAKVGLAgkETSYPR---RLSGGQQQRVAIARALAMRPEVILFDEP 171

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 165 TSALDdanKRNVNEIIH--RYVREQNIAVLWVTHdanEITHADDV 207
Cdd:PRK11264 172 TSALD---PELVGEVLNtiRQLAQEKRTMVIVTH---EMSFARDV 210
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
10-163 1.61e-21

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 89.44  E-value: 1.61e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  10 IEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE---AYRQQVSYS 86
Cdd:PRK11831  10 MRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSrlyTVRKRMSML 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLF-DSTVYDNLLFPWQIRHKTPDPERFSADLARF---------NLPPdtltksvSELSGGEKQRVSLIRNLQFLP 156
Cdd:PRK11831  90 FQSGALFtDMNVFDNVAYPLREHTQLPAPLLHSTVMMKLeavglrgaaKLMP-------SELSGGMARRAALARAIALEP 162


                 ....*..
gi 504695722 157 KVLLLDE 163
Cdd:PRK11831 163 DLIMFDE 169
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
18-197 1.62e-21

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 88.92  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEG------KDISTLSPEAYRQQVSYSVQTPS 91
Cdd:COG4161   13 GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGhqfdfsQKPSEKAIRLLRQKVGMVFQQYN 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  92 LFDS-TVYDNLL-FPWQIRHKTPDPERFSAD--LARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSA 167
Cdd:COG4161   93 LWPHlTVMENLIeAPCKVLGLSKEQAREKAMklLARLRLT-DKADRFPLHLSGGQQQRVAIARALMMEPQVLLFDEPTAA 171

                        170       180       190
                 ....*....|....*....|....*....|
gi 504695722 168 LDDANKRNVNEIIhRYVREQNIAVLWVTHD 197
Cdd:COG4161  172 LDPEITAQVVEII-RELSQTGITQVIVTHE 200
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 1-197 2.27e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 89.52  E-value: 2.27e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNsaVLTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGK--DISTLSPE 77
Cdd:PRK13636   1 MEDY--ILKVEELNYNySDGTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKpiDYSRKGLM 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  78 AYRQQVSYSVQTP--SLFDSTVYDNLLFPwQIRHKTPDPE---RFSADLARFNLPPdTLTKSVSELSGGEKQRVSLIRNL 152
Cdd:PRK13636  79 KLRESVGMVFQDPdnQLFSASVYQDVSFG-AVNLKLPEDEvrkRVDNALKRTGIEH-LKDKPTHCLSFGQKKRVAIAGVL 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 153 QFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK13636 157 VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMQKELGLTIIIATHD 201
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 6-200 3.14e-21

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 88.03  E-value: 3.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLS-PEAYRQQVS 84
Cdd:PRK10895   2 ATLTAKNLAKAYKGRRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPlHARARRGIG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLFDS-TVYDNLLFPWQIRH---KTPDPERFSADLARFNLP--PDTLTKSvseLSGGEKQRVSLIRNLQFLPKV 158
Cdd:PRK10895  82 YLPQEASIFRRlSVYDNLMAVLQIRDdlsAEQREDRANELMEEFHIEhlRDSMGQS---LSGGERRRVEIARALAANPKF 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504695722 159 LLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANE 200
Cdd:PRK10895 159 ILLDEPFAGVDPISVIDIKRII-EHLRDSGLGVLITDHNVRE 199
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
1-200 3.19e-21

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 88.89  E-value: 3.19e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYR 80
Cdd:PRK10253   1 MTESVARLRGEQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQ---TPSlfDSTVYDNLL---FPWQ---IRHKTPDPERFSADLaRFNLPPDTLTKSVSELSGGEKQRVSLIRN 151
Cdd:PRK10253  81 RRIGLLAQnatTPG--DITVQELVArgrYPHQplfTRWRKEDEEAVTKAM-QATGITHLADQSVDTLSGGQRQRAWIAMV 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504695722 152 LQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANE 200
Cdd:PRK10253 158 LAQETAIMLLDEPTTWLDISHQIDLLELLSELNREKGYTLAAVLHDLNQ 206
cbiO PRK13642
energy-coupling factor transporter ATPase;
23-220 3.78e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 88.61  E-value: 3.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTP--SLFDSTVYDN 100
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAENVWNLRRKIGMVFQNPdnQFVGATVEDD 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 101 LLFPWQiRHKTPDPE---RFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVN 177
Cdd:PRK13642 103 VAFGME-NQGIPREEmikRVDEALLAVNML-DFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQEIM 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 504695722 178 EIIHRYVREQNIAVLWVTHDANEITHADDVLTLQPhGGKMQEA 220
Cdd:PRK13642 181 RVIHEIKEKYQLTVLSITHDLDEAASSDRILVMKA-GEIIKEA 222
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 4-197 4.44e-21

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 88.12  E-value: 4.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   4 NSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY-RQQ 82
Cdd:PRK11300   2 SQPLLSVSGLMMRFGGLLAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIaRMG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 VSYSVQTPSLFDS-TVYDNLLFPwQIRH----------KTPD---PERFSADLARFNLPPDTLT----KSVSELSGGEKQ 144
Cdd:PRK11300  82 VVRTFQHVRLFREmTVIENLLVA-QHQQlktglfsgllKTPAfrrAESEALDRAATWLERVGLLehanRQAGNLAYGQQR 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 504695722 145 RVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK11300 161 RLEIARCMVTQPEILMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
cbiO PRK13646
energy-coupling factor transporter ATPase;
23-211 7.72e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 87.91  E-value: 7.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY----RQQVSYSVQTP--SLFDST 96
Cdd:PRK13646  23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKDKYirpvRKRIGMVFQFPesQLFEDT 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLLFpwqirhktpDPERFSAD-----------LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEIT 165
Cdd:PRK13646 103 VEREIIF---------GPKNFKMNldevknyahrlLMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPT 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 166 SALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEIT-HADDVLTLQ 211
Cdd:PRK13646 174 AGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVArYADEVIVMK 220
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 14-211 8.97e-21

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: 86.62  E-value: 8.97e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  14 GYRTGGTTI--LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY----RQQVSYSV 87
Cdd:cd03290    6 GYFSWGSGLatLSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATrsrnRYSVAYAA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDSTVYDNLLFpwqirhKTP-DPERFSADLARFNLPPDT----------LTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:cd03290   86 QKPWLLNATVEENITF------GSPfNKQRYKAVTDACSLQPDIdllpfgdqteIGERGINLSGGQRQRICVARALYQNT 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 157 KVLLLDEITSALD-DANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03290  160 NIVFLDDPFSALDiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMK 215
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
20-210 1.47e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 87.07  E-value: 1.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  20 TTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSpeayrqqvsysvqtpslfdstvyd 99
Cdd:PRK13633  23 KLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEE------------------------ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 100 NLlfpWQIRHKT------PDPERFSA----DLA----RFNLPPDTLTKSVSE-----------------LSGGEKQRVSL 148
Cdd:PRK13633  79 NL---WDIRNKAgmvfqnPDNQIVATiveeDVAfgpeNLGIPPEEIRERVDEslkkvgmyeyrrhaphlLSGGQKQRVAI 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:PRK13633 156 AGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVM 217
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 5-201 1.69e-20

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 88.95  E-value: 1.69e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVS 84
Cdd:PRK15439   9 PPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQLGI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSV-QTPSLFDS-TVYDNLLFPWQirhKTPDP-ERFSADLARFNLPPDtLTKSVSELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:PRK15439  89 YLVpQEPLLFPNlSVKENILFGLP---KRQASmQKMKQLLAALGCQLD-LDSSAGSLEVADRQIVEILRGLMRDSRILIL 164

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 162 DEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEI 201
Cdd:PRK15439 165 DEPTASLTPAETERLFSRI-RELLAQGVGIVFISHKLPEI 203
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
5-208 3.76e-20

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 88.24  E-value: 3.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDV--GYRTGGTTI--LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAY- 79
Cdd:PRK10535   2 TALLELKDIrrSYPSGEEQVevLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALa 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 ---RQQVSYSVQTPSLFDS-TVYDNLLFP--WQIRHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQ 153
Cdd:PRK10535  82 qlrREHFGFIFQRYHLLSHlTAAQNVEVPavYAGLERKQRLLRAQELLQRLGL-EDRVEYQPSQLSGGQQQRVSIARALM 160

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADDVL 208
Cdd:PRK10535 161 NGGQVILADEPTGALDSHSGEEVMAILHQ-LRDRGHTVIIVTHDPQVAAQAERVI 214
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
7-171 4.92e-20

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 84.09  E-value: 4.92e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLsPEAYRQQVSYS 86
Cdd:PRK13538   1 MLEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRQ-RDEYHQDLLYL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLLFPWQIRHKTPDPERFSAdLARFNL------PpdtltksVSELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:PRK13538  80 GHQPGIKTElTALENLRFYQRLHGPGDDEALWEA-LAQVGLagfedvP-------VRQLSAGQQRRVALARLWLTRAPLW 151

                        170
                 ....*....|..
gi 504695722 160 LLDEITSALDDA 171
Cdd:PRK13538 152 ILDEPFTAIDKQ 163
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 5-213 6.54e-20

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 84.78  E-value: 6.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrQQVS 84
Cdd:PRK09544   2 TSLVSLENVSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNGK-----------LRIG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLfDSTVydnllfPWQI-RHKTPDPERFSAD----LARFNlPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:PRK09544  71 YVPQKLYL-DTTL------PLTVnRFLRLRPGTKKEDilpaLKRVQ-AGHLIDAPMQKLSGGETQRVLLARALLNRPQLL 142

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEI-THADDVLTLQPH 213
Cdd:PRK09544 143 VLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLVmAKTDEVLCLNHH 197
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
4-219 1.64e-19

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 86.31  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   4 NSAVLTIEDV--GYRTGgTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQ 81
Cdd:PRK10790 337 QSGRIDIDNVsfAYRDD-NLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSHSVLRQ 415

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSVQTPSLFDSTVYDNLLFP--------WQIRHKTPdperfSADLARfnLPPDTLTKSVSE----LSGGEKQRVSLI 149
Cdd:PRK10790 416 GVAMVQQDPVVLADTFLANVTLGrdiseeqvWQALETVQ-----LAELAR--SLPDGLYTPLGEqgnnLSVGQKQLLALA 488

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 150 RNLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLwVTHDANEITHADDVLTLqpHGGKMQE 219
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQAL-AAVREHTTLVV-IAHRLSTIVEADTILVL--HRGQAVE 554
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
6-205 1.64e-19

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 85.28  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDV--GYrTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPeAYRqQV 83
Cdd:PRK11650   2 AGLKLQAVrkSY-DGKTQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEP-ADR-DI 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSVQTPSLFDS-TVYDNLLFPWQIRhKTPDPE--RFSADLAR-FNLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:PRK11650  79 AMVFQNYALYPHmSVRENMAYGLKIR-GMPKAEieERVAEAARiLELEP-LLDRKPRELSGGQRQRVAMGRAIVREPAVF 156

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 160 LLDEITSALdDANKRNVNEI-IHRYVREQNIAVLWVTHDANE-ITHAD 205
Cdd:PRK11650 157 LFDEPLSNL-DAKLRVQMRLeIQRLHRRLKTTSLYVTHDQVEaMTLAD 203
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 7-220 2.52e-19

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 85.49  E-value: 2.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDV---GYRtggttilnNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA----- 78
Cdd:PRK15439 268 VLTVEDLtgeGFR--------NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQrlarg 339

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 --Y----RQQVSYSVQTPSLFD--STVYDNLLFpWQirhktpDPERFSADLARF----NLPPDTLTKSVSELSGGEKQRV 146
Cdd:PRK15439 340 lvYlpedRQSSGLYLDAPLAWNvcALTHNRRGF-WI------KPARENAVLERYrralNIKFNHAEQAARTLSGGNQQKV 412

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 147 SLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQEA 220
Cdd:PRK15439 413 LIAKCLEASPQLLIVDEPTRGVDVSARNDIYQLI-RSIAAQNVAVLFISSDLEEIEQmADRVLVM--HQGEISGA 484
cbiO PRK13644
energy-coupling factor transporter ATPase;
7-211 2.98e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 83.50  E-value: 2.98e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVS 84
Cdd:PRK13644   1 MIRLENVSYSyPDGTPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFSKlQGIRKLVG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTP--SLFDSTVYDNLLF--------PWQIRhktpdpERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQF 154
Cdd:PRK13644  81 IVFQNPetQFVGRTVEEDLAFgpenlclpPIEIR------KRVDRALAEIGL-EKYRHRSPKTLSGGQGQCVALAGILTM 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 155 LPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADDVLTLQ 211
Cdd:PRK13644 154 EPECLIFDEVTSMLDPDSGIAVLERIKK-LHEKGKTIVYITHNLEELHDADRIIVMD 209
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 3-197 3.46e-19

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 83.05  E-value: 3.46e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGK-----DISTLSpE 77
Cdd:PRK11701   2 MDQPLLSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALS-E 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  78 AYRQQVS-----YSVQTPSlfdstvyDNL-------------LFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELS 139
Cdd:PRK11701  81 AERRRLLrtewgFVHQHPR-------DGLrmqvsaggnigerLMAVGARHYGDIRATAGDWLERVEIDAARIDDLPTTFS 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 140 GGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK11701 154 GGMQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHD 211
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 6-196 5.36e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 82.27  E-value: 5.36e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL--LTP---TSGKIFFEGKDISTLSPEAYR 80
Cdd:PRK14247   2 NKIEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLieLYPearVSGEVYLDGQDIFKMDVIELR 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFDS-TVYDNLLFPWQ----IRHKTPDPERFSADLARFNL---PPDTLTKSVSELSGGEKQRVSLIRNL 152
Cdd:PRK14247  82 RRVQMVFQIPNPIPNlSIFENVALGLKlnrlVKSKKELQERVRWALEKAQLwdeVKDRLDAPAGKLSGGQQQRLCIARAL 161

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 153 QFLPKVLLLDEITSALDDANKRNVNEIIHRYVREqnIAVLWVTH 196
Cdd:PRK14247 162 AFQPEVLLADEPTANLDPENTAKIESLFLELKKD--MTIVLVTH 203
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
8-218 6.52e-19

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 83.93  E-value: 6.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP----EAYRQQV 83
Cdd:PRK10070  29 LSKEQILEKTGLSLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDaelrEVRRKKI 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSVQTPSLFDS-TVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSV-SELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:PRK10070 109 AMVFQSFALMPHmTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYpDELSGGMRQRVGLARALAINPDILLM 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 162 DEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQPHGGKMQ 218
Cdd:PRK10070 189 DEAFSALDPLIRTEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQ 245
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
8-214 8.24e-19

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 84.07  E-value: 8.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE-AYRQQVSYS 86
Cdd:PRK09700   6 ISMAGIGKSFGPVHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKlAAQLGIGII 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLLFPwqiRHKTPD------------PERFSADLARFNLPPDtLTKSVSELSGGEKQRVSLIRNLQ 153
Cdd:PRK09700  86 YQELSVIDElTVLENLYIG---RHLTKKvcgvniidwremRVRAAMMLLRVGLKVD-LDEKVANLSISHKQMLEIAKTLM 161

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 154 FLPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADDVLTLQPHG 214
Cdd:PRK09700 162 LDAKVIIMDEPTSSLTNKEVDYLFLIMNQ-LRKEGTAIVYISHKLAEIRRICDRYTVMKDG 221
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
38-217 8.47e-19

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 83.39  E-value: 8.47e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  38 ITGPSGCGKSTLLKIIASLLTPTSGKIFFEG-------KDIStLSPEayRQQVSYSVQTPSLFDS-TVYDNLLFpwQIRH 109
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrvlfdaeKGIC-LPPE--KRRIGYVFQDARLFPHyKVRGNLRY--GMAK 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 110 KtpDPERFSADLARFNLPPdTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNI 189
Cdd:PRK11144 104 S--MVAQFDKIVALLGIEP-LLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINI 180

                        170       180
                 ....*....|....*....|....*....
gi 504695722 190 AVLWVTHDANEITH-ADDVLTLqpHGGKM 217
Cdd:PRK11144 181 PILYVSHSLDEILRlADRVVVL--EQGKV 207
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
6-169 1.36e-18

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 82.16  E-value: 1.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAyRQQVSY 85
Cdd:PRK13537   6 APIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHA-RQRVGV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLF-DSTVYDNLLF--------PWQIRHKTPDPERFsadlARFNLPPDTltkSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:PRK13537  85 VPQFDNLDpDFTVRENLLVfgryfglsAAAARALVPPLLEF----AKLENKADA---KVGELSGGMKRRLTLARALVNDP 157

                        170
                 ....*....|...
gi 504695722 157 KVLLLDEITSALD 169
Cdd:PRK13537 158 DVLVLDEPTTGLD 170
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 3-221 1.96e-18

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: 83.20  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIED--VGYRTGG--TTILNNVSFSLLPGEFRLITGPSGCGKS----TLLKIIASLLTPTSGKIFFEGKDISTL 74
Cdd:COG4172    2 MSMPLLSVEDlsVAFGQGGgtVEAVKGVSFDIAAGETLALVGESGSGKSvtalSILRLLPDPAAHPSGSILFDGQDLLGL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  75 SPEAYRQ----QVSYSVQTP--SLfdstvydNLLFPW--QI-----RHKT-------------------PDPERfsadla 122
Cdd:COG4172   82 SERELRRirgnRIAMIFQEPmtSL-------NPLHTIgkQIaevlrLHRGlsgaaararalellervgiPDPER------ 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 123 RFNLPPdtltksvSELSGGEKQRV----SLIRNlqflPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDA 198
Cdd:COG4172  149 RLDAYP-------HQLSGGQRQRVmiamALANE----PDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDL 217

                        250       260
                 ....*....|....*....|....
gi 504695722 199 NEITH-ADDVLTLQphGGKMQEAN 221
Cdd:COG4172  218 GVVRRfADRVAVMR--QGEIVEQG 239
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 8-214 2.00e-18

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 78.26  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEfRL-ITGPSGCGKSTLLKIIASLLTPTSGKIffegKDISTLSpeayrqqVSYs 86
Cdd:cd03221    1 IELENLSKTYGGKLLLKDISLTINPGD-RIgLVGRNGAGKSTLLKLIAGELEPDEGIV----TWGSTVK-------IGY- 67

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 vqtpslfdstvydnllfpwqirhktpdperfsadlarfnlppdtltksVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:cd03221   68 ------------------------------------------------FEQLSGGEKMRLALAKLLLENPNLLLLDEPTN 99

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504695722 167 ALDDANKrnvnEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQPHG 214
Cdd:cd03221  100 HLDLESI----EALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 24-210 2.02e-18

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 82.06  E-value: 2.02e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  24 NNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPE---AYRQQVSYSVQTP--SLFDS-TV 97
Cdd:PRK15079  38 DGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDewrAVRSDIQMIFQDPlaSLNPRmTI 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLLFPWQIRH----KTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANK 173
Cdd:PRK15079 118 GEIIAEPLRTYHpklsRQEVKDRVKAMMLKVGLLPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSALDVSIQ 197

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 174 RNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTL 210
Cdd:PRK15079 198 AQVVNLLQQLQREMGLSLIFIAHDLAVVKHiSDRVLVM 235
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
15-208 2.10e-18

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 83.14  E-value: 2.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  15 YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTllkiIASLLTP----TSGKIFFEGKDISTLSPEAYRQQVSYSVQTP 90
Cdd:PRK11176 351 YPGKEVPALRNINFKIPAGKTVALVGRSGSGKST----IANLLTRfydiDEGEILLDGHDLRDYTLASLRNQVALVSQNV 426

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  91 SLFDSTVYDNLLFPWQIRHKTPDPERfSADLAR----FNLPPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:PRK11176 427 HLFNDTIANNIAYARTEQYSREQIEE-AARMAYamdfINKMDNGLDTVIGEngvlLSGGQRQRIAIARALLRDSPILILD 505

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 163 EITSALDDANKRnvneIIHRYVRE--QNIAVLWVTHDANEITHADDVL 208
Cdd:PRK11176 506 EATSALDTESER----AIQAALDElqKNRTSLVIAHRLSTIEKADEIL 549
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 13-222 2.71e-18

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 80.00  E-value: 2.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  13 VGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIsTLSPEAyrqqvsysvqtpsl 92
Cdd:COG2401   36 VELRVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCVDVPDN-QFGREA-------------- 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  93 fdsTVYDNLLfpwqirhKTPDPERFSADLARFNL-PPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDA 171
Cdd:COG2401  101 ---SLIDAIG-------RKGDFKDAVELLNAVGLsDAVLWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 172 NKRNVNEIIHRYVREQNIAVLWVTHdaneitHADDVLTLQP-------HGGKMQEANR 222
Cdd:COG2401  171 TAKRVARNLQKLARRAGITLVVATH------HYDVIDDLQPdllifvgYGGVPEEKRR 222
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 21-210 3.80e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 81.05  E-value: 3.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKI----FFEGKDISTLSPEAY------------RQQVS 84
Cdd:PRK13631  40 VALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIqvgdIYIGDKKNNHELITNpyskkiknfkelRRRVS 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTP--SLFDSTVYDNLLF-PWQIR-HKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK13631 120 MVFQFPeyQLFKDTIEKDIMFgPVALGvKKSEAKKLAKFYLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILI 199

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504695722 161 LDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITH-ADDVLTL 210
Cdd:PRK13631 200 FDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEHVLEvADEVIVM 249
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 21-204 4.96e-18

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 78.76  E-value: 4.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLsPEAYRQQVSYSVQTPSlfDSTVYDN 100
Cdd:PRK13541  14 KNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNI-AKPYCTYIGHNLGLKL--EMTVFEN 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 101 LLFPWQIRHKTpdpERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEII 180
Cdd:PRK13541  91 LKFWSEIYNSA---ETLYAAIHYFKL-HDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166

                        170       180
                 ....*....|....*....|....
gi 504695722 181 HRYVREQNIaVLWVTHDANEITHA 204
Cdd:PRK13541 167 VMKANSGGI-VLLSSHLESSIKSA 189
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
1-219 6.53e-18

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 79.63  E-value: 6.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSavLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYR 80
Cdd:PRK10619   1 MSENK--LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKDGQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSL----------FD----STVYDNLL-FPWQIR--HKTPDPERFSADLARFNLPPDTLTKSVSELSGGEK 143
Cdd:PRK10619  79 LKVADKNQLRLLrtrltmvfqhFNlwshMTVLENVMeAPIQVLglSKQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQ 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 144 QRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLwVTHDANEITH-ADDVLTLqpHGGKMQE 219
Cdd:PRK10619 159 QRVSIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVV-VTHEMGFARHvSSHVIFL--HQGKIEE 232
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 7-210 7.35e-18

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: 81.41  E-value: 7.35e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLT--PTSGKIFFEGKDISTLS-PEAYRQQV 83
Cdd:TIGR02633   1 LLEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGVYPhgTWDGEIYWSGSPLKASNiRDTERAGI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   84 SYSVQTPSLF-DSTVYDNLLFPWQIRHK---TPDPE---RFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:TIGR02633  81 VIIHQELTLVpELSVAENIFLGNEITLPggrMAYNAmylRAKNLLRELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQA 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504695722  157 KVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:TIGR02633 161 RLLILDEPSSSLTEKETEILLDII-RDLKAHGVACVYISHKLNEVKAVCDTICV 213
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 23-202 9.82e-18

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 80.13  E-value: 9.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDistlsPeaYRQQVSYSVQTPSLF--------D 94
Cdd:COG4586   38 VDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYV-----P--FKRRKEFARRIGVVFgqrsqlwwD 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 STVYDNLLFPWQIrHKTPDpERFSADLARF----NLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDD 170
Cdd:COG4586  111 LPAIDSFRLLKAI-YRIPD-AEYKKRLDELvellDL-GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDV 187

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504695722 171 ANKRNVNEIIHRYVREQNIAVLWVTHDANEIT 202
Cdd:COG4586  188 VSKEAIREFLKEYNRERGTTILLTSHDMDDIE 219
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
7-214 1.13e-17

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 79.28  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGK--DISTLSPEAYRQQVS 84
Cdd:PRK13638   1 MLATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKplDYSKRGLLALRQQVA 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTP--SLFDSTVYDNLLFPW--------QIRHKTPDPERFsADLARFNLPPdtltksVSELSGGEKQRVSLIRNLQF 154
Cdd:PRK13638  81 TVFQDPeqQIFYTDIDSDIAFSLrnlgvpeaEITRRVDEALTL-VDAQHFRHQP------IQCLSHGQKKRVAIAGALVL 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 155 LPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLwVTHDANEITHADDVLTLQPHG 214
Cdd:PRK13638 154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVII-SSHDIDLIYEISDAVYVLRQG 212
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 18-199 1.63e-17

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 78.13  E-value: 1.63e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEG-----------KDISTLspeayRQQVSYS 86
Cdd:PRK11124  13 GAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGnhfdfsktpsdKAIREL-----RRNVGMV 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFDS-TVYDNLL-FPWQIRHKTPDPERFSAD--LARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:PRK11124  88 FQQYNLWPHlTVQQNLIeAPCRVLGLSKDQALARAEklLERLRLK-PYADRFPLHLSGGQQQRVAIARALMMEPQVLLFD 166

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504695722 163 EITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDAN 199
Cdd:PRK11124 167 EPTAALDPEITAQIVSIIRE-LAETGITQVIVTHEVE 202
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 7-210 1.87e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 78.58  E-value: 1.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDI--STLSPEAYRQQV 83
Cdd:PRK13639   1 ILETRDLKYSyPDGTEALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIkyDKKSLLEVRKTV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSVQTP--SLFDSTVYDNLLF-PWQIRHKTPDPERFSAD-LARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:PRK13639  81 GIVFQNPddQLFAPTVEEDVAFgPLNLGLSKEEVEKRVKEaLKAVGM-EGFENKPPHHLSGGQKKRVAIAGILAMKPEII 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI-THADDVLTL 210
Cdd:PRK13639 160 VLDEPTSGLDPMGASQIMKLLYD-LNKEGITIIISTHDVDLVpVYADKVYVM 210
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 23-197 1.90e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 78.97  E-value: 1.90e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKI--FFEGKDISTLSPEAYRQQVSYSVQTP---------- 90
Cdd:PRK13651  23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIewIFKDEKNKKKTKEKEKVLEKLVIQKTrfkkikkike 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  91 --------------SLFDSTVYDNLLF-PwqIRHKTPDPErfSADLAR-----FNLPPDTLTKSVSELSGGEKQRVSLIR 150
Cdd:PRK13651 103 irrrvgvvfqfaeyQLFEQTIEKDIIFgP--VSMGVSKEE--AKKRAAkyielVGLDESYLQRSPFELSGGQKRRVALAG 178

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 151 NLQFLPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHD 197
Cdd:PRK13651 179 ILAMEPDFLVFDEPTAGLDPQGVKEILEIFDN-LNKQGKTIILVTHD 224
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 8-171 2.10e-17

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: 77.15  E-value: 2.10e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEaYRQQVSYSV 87
Cdd:cd03231    1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDS-IARGLLYLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 QTPSLFDS-TVYDNLLFpWQIRHKTPDPERF--SADLARFNLPPdtltksVSELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:cd03231   80 HAPGIKTTlSVLENLRF-WHADHSDEQVEEAlaRVGLNGFEDRP------VAQLSAGQQRRVALARLLLSGRPLWILDEP 152


                 ....*..
gi 504695722 165 TSALDDA 171
Cdd:cd03231  153 TTALDKA 159
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 23-197 2.25e-17

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: 80.23  E-value: 2.25e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFF----EGKDISTLSPEA---YRQQVSYSVQTPSLF-D 94
Cdd:TIGR03269 300 VDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgdEWVDMTKPGPDGrgrAKRYIGILHQEYDLYpH 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   95 STVYDNLL------FPWQI-RHK---TPDPERFSADLARfnlppDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEI 164
Cdd:TIGR03269 380 RTVLDNLTeaigleLPDELaRMKaviTLKMVGFDEEKAE-----EILDKYPDELSEGERHRVALAQVLIKEPRIVILDEP 454

                         170       180       190
                  ....*....|....*....|....*....|...
gi 504695722  165 TSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:TIGR03269 455 TGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 21-219 3.07e-17

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 77.13  E-value: 3.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA----YRQQVSYSVQT----PSL 92
Cdd:PRK10584  24 SILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEAraklRAKHVGFVFQSfmliPTL 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  93 fdsTVYDNLLFPWQIRHKTpdpERFSADLARFNLPPDTLTKSV----SELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:PRK10584 104 ---NALENVELPALLRGES---SRQSRNGAKALLEQLGLGKRLdhlpAQLSGGEQQRVALARAFNGRPDVLFADEPTGNL 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 504695722 169 DDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:PRK10584 178 DRQTGDKIADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLV--NGQLQE 226
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 16-197 4.35e-17

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 79.36  E-value: 4.35e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  16 RTGGTTILNNVSFSLLPGEFRLITGPSGCGKST----LLKIIASlltptSGKIFFEGKDISTLSPEA---YRQQVSYSVQ 88
Cdd:PRK15134 295 TVDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLINS-----QGEIWFDGQPLHNLNRRQllpVRHRIQVVFQ 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 TP--SL-----FDSTVYDNLlfpwQIRHKTPDP----ERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPK 157
Cdd:PRK15134 370 DPnsSLnprlnVLQIIEEGL----RVHQPTLSAaqreQQVIAVMEEVGLDPETRHRYPAEFSGGQRQRIAIARALILKPS 445

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 158 VLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK15134 446 LIILDEPTSSLDKTVQAQILALLKSLQQKHQLAYLFISHD 485
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 22-196 4.57e-17

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 77.19  E-value: 4.57e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLpgefrlitGPSGCGKSTLLKIIASLL-----TPTSGKIFFEGKDIST--LSPEAYRQQVSYSVQTPSLFD 94
Cdd:PRK14267  27 IPQNGVFALM--------GPSGCGKSTLLRTFNRLLelneeARVEGEVRLFGRNIYSpdVDPIEVRREVGMVFQYPNPFP 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 S-TVYDNLLFPWQ----IRHKTPDPERFSADLARFNL---PPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:PRK14267  99 HlTIYDNVAIGVKlnglVKSKKELDERVEWALKKAALwdeVKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTA 178

                        170       180       190
                 ....*....|....*....|....*....|
gi 504695722 167 ALDDANKRNVNEIIHRYVREQNIAVlwVTH 196
Cdd:PRK14267 179 NIDPVGTAKIEELLFELKKEYTIVL--VTH 206
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-210 5.53e-17

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 77.17  E-value: 5.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPT--------SGKIFFEGKDISTLSPE--AYRQQVSYSVQTP 90
Cdd:PRK13547  15 AILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAIDAPrlARLRAVLPQAAQP 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  91 SlFDSTVYDNLL---FPWQIRHKTP---DPERFSADLARFNLPPdTLTKSVSELSGGEKQRVSLIRNLQFL--------- 155
Cdd:PRK13547  95 A-FAFSAREIVLlgrYPHARRAGALthrDGEIAWQALALAGATA-LVGRDVTTLSGGELARVQFARVLAQLwpphdaaqp 172

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 156 PKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDAN-EITHADDVLTL 210
Cdd:PRK13547 173 PRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNlAARHADRIAML 228
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 7-197 5.92e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 77.08  E-value: 5.92e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYR-TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:PRK13647   4 IIEVEDLHFRyKDGTKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRSKVGL 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTP--SLFDSTVYDNLLFPWQIRHKTPDP--ERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:PRK13647  84 VFQDPddQVFSSTVWDDVAFGPVNMGLDKDEveRRVEEALKAVRM-WDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVL 162

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504695722 162 DEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHD 197
Cdd:PRK13647 163 DEPMAYLDPRGQETLMEILDR-LHNQGKTVIVATHD 197
cbiO PRK13649
energy-coupling factor transporter ATPase;
8-211 5.97e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 77.48  E-value: 5.97e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYR-TGGTTI----LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP----EA 78
Cdd:PRK13649   3 INLQNVSYTyQAGTPFegraLFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnkdiKQ 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 YRQQVSYSVQTP--SLFDSTVYDNLLF-PWQIRHKTPDPERFSAD-LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQF 154
Cdd:PRK13649  83 IRKKVGLVFQFPesQLFEETVLKDVAFgPQNFGVSQEEAEALAREkLALVGISESLFEKNPFELSGGQMRRVAIAGILAM 162

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 155 LPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEIT-HADDVLTLQ 211
Cdd:PRK13649 163 EPKILVLDEPTAGLDPKGRKELMTLFKK-LHQSGMTIVLVTHLMDDVAnYADFVYVLE 219
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 7-196 7.33e-17

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 76.75  E-value: 7.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL--LTPTSGKIFFEGKDISTLSPEAYRQQ-- 82
Cdd:PRK09580   1 MLSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGRedYEVTGGTVEFKGKDLLELSPEDRAGEgi 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 ---VSYSVQTP----SLFDSTVYDNLLfpwQIRHKTP----DPERFSAD-LARFNLPPDTLTKSVSE-LSGGEKQRVSLI 149
Cdd:PRK09580  81 fmaFQYPVEIPgvsnQFFLQTALNAVR---SYRGQEPldrfDFQDLMEEkIALLKMPEDLLTRSVNVgFSGGEKKRNDIL 157

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 150 RNLQFLPKVLLLDEITSALD-DANKRNVNEIihRYVREQNIAVLWVTH 196
Cdd:PRK09580 158 QMAVLEPELCILDESDSGLDiDALKIVADGV--NSLRDGKRSFIIVTH 203
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 17-197 7.87e-17

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 77.15  E-value: 7.87e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  17 TGGTTILNNVSFsLLPGEFRL-ITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTP--SLF 93
Cdd:PRK13652  14 SGSKEALNNINF-IAPRNSRIaVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKFVGLVFQNPddQIF 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DSTVYDNLLF-PWQIRHKTPDPE-RFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDA 171
Cdd:PRK13652  93 SPTVEQDIAFgPINLGLDEETVAhRVSSALHMLGLE-ELRDRVPHHLSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQ 171

                        170       180
                 ....*....|....*....|....*.
gi 504695722 172 NKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK13652 172 GVKELIDFLNDLPETYGMTVIFSTHQ 197
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 23-221 1.02e-16

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: 76.29  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFR-----LITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIStlspeaYRQQvsysvQTPSLFDSTV 97
Cdd:cd03237   10 LGEFTLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVS------YKPQ-----YIKADYEGTV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLlfpwqiRHKTPD---PERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKR 174
Cdd:cd03237   79 RDLL------SSITKDfytHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRL 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 504695722 175 NVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQPHGGKMQEAN 221
Cdd:cd03237  153 MASKVIRRFAENNEKTAFVVEHDIIMIDYlADRLIVFEGEPSVNGVAN 200
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 21-219 1.19e-16

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 75.89  E-value: 1.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEfRL-ITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdISTLspeayrqqvsYSVQT---PSLfdsT 96
Cdd:COG1134   40 WALKDVSFEVERGE-SVgIIGRNGAGKSTLLKLIAGILEPTSGRVEVNGR-VSAL----------LELGAgfhPEL---T 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLLF--------PWQIRHKTPDPERFsADLARF-NLPpdtltksVSELSGGEKQRV--SLIRNLQflPKVLLLDEIT 165
Cdd:COG1134  105 GRENIYLngrllglsRKEIDEKFDEIVEF-AELGDFiDQP-------VKTYSSGMRARLafAVATAVD--PDILLVDEVL 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 166 SALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI-THADDVLTLqpHGGKMQE 219
Cdd:COG1134  175 AVGDAAFQKKCLARIRE-LRESGRTVIFVSHSMGAVrRLCDRAIWL--EKGRLVM 226
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
18-219 1.43e-16

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 77.18  E-value: 1.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAyRQQVSYSVQTPSL-FDST 96
Cdd:PRK13536  52 GDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLA-RARIGVVPQFDNLdLEFT 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLL-FPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRN 175
Cdd:PRK13536 131 VRENLLvFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILDEPTTGLDPHARHL 210

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 504695722 176 VNEIIhRYVREQNIAVLWVTHDANEITHADDVLTLQPHGGKMQE 219
Cdd:PRK13536 211 IWERL-RSLLARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAE 253
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 22-205 1.75e-16

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 74.60  E-value: 1.75e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSY----SVQTPSLfdsTV 97
Cdd:PRK13540  16 LLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKK-DLCTYQKQLCFvghrSGINPYL---TL 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLLFPWqirHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVN 177
Cdd:PRK13540  92 RENCLYDI---HFSPGAVGITELCRLFSL-EHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167

                        170       180
                 ....*....|....*....|....*...
gi 504695722 178 EIIHRYvREQNIAVLWVTHDANEITHAD 205
Cdd:PRK13540 168 TKIQEH-RAKGGAVLLTSHQDLPLNKAD 194
PLN03232 PLN03232
ABC transporter C family member; Provisional
 5-211 1.91e-16

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 77.71  E-value: 1.91e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    5 SAVLTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQ 82
Cdd:PLN03232 1232 RGSIKFEDVhlRYRPGLPPVLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   83 VSYSVQTPSLFDSTVYDNLlfpwqirhkTPDPERFSAD----LARFNLP------PDTLTKSVSE----LSGGEKQRVSL 148
Cdd:PLN03232 1312 LSIIPQSPVLFSGTVRFNI---------DPFSEHNDADlweaLERAHIKdvidrnPFGLDAEVSEggenFSVGQRQLLSL 1382

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504695722  149 IRNLQFLPKVLLLDEITSALDdankRNVNEIIHRYVREQ--NIAVLWVTHDANEITHADDVLTLQ 211
Cdd:PLN03232 1383 ARALLRRSKILVLDEATASVD----VRTDSLIQRTIREEfkSCTMLVIAHRLNTIIDCDKILVLS 1443
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
7-217 2.83e-16

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 76.60  E-value: 2.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGgttiLNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSY 85
Cdd:COG1129  256 VLEVEGLSVGGV----VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPrDAIRAGIAY 331

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 sV----QTPSLF-DSTVYDNLLFPWQ--------IRHKTpdpERFSAD--LARFNLPPDTLTKSVSELSGGEKQRVSLIR 150
Cdd:COG1129  332 -VpedrKGEGLVlDLSIRENITLASLdrlsrgglLDRRR---ERALAEeyIKRLRIKTPSPEQPVGNLSGGNQQKVVLAK 407

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 151 NLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVrEQNIAVLWVTHDANEITH-ADDVLTLqpHGGKM 217
Cdd:COG1129  408 WLATDPKVLILDEPTRGIDVGAKAEIYRLIRELA-AEGKAVIVISSELPELLGlSDRILVM--REGRI 472
PLN03130 PLN03130
ABC transporter C family member; Provisional
 5-219 3.42e-16

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 77.09  E-value: 3.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    5 SAVLTIEDV--GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQ 82
Cdd:PLN03130 1235 SGSIKFEDVvlRYRPELPPVLHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFGLMDLRKV 1314

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   83 VSYSVQTPSLFDSTVYDNLlfpwqirhktpDP--ERFSAD----LARFNLP------PDTLTKSVSE----LSGGEKQRV 146
Cdd:PLN03130 1315 LGIIPQAPVLFSGTVRFNL-----------DPfnEHNDADlwesLERAHLKdvirrnSLGLDAEVSEagenFSVGQRQLL 1383

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722  147 SLIRNLQFLPKVLLLDEITSALD---DAnkrnvneIIHRYVREQ--NIAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:PLN03130 1384 SLARALLRRSKILVLDEATAAVDvrtDA-------LIQKTIREEfkSCTMLIIAHRLNTIIDCDRILVLD--AGRVVE 1452
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 23-186 4.17e-16

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 76.20  E-value: 4.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSY--------------SV 87
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPqDGLANGIVYisedrkrdglvlgmSV 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  88 -QTPSLfdsTVYDNLLFPW-QIRHKTpdpERFSAD--LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:PRK10762 348 kENMSL---TALRYFSRAGgSLKHAD---EQQAVSdfIRLFNIKTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDE 421

                        170       180
                 ....*....|....*....|...
gi 504695722 164 ITSALDDANKRNVNEIIHRYVRE 186
Cdd:PRK10762 422 PTRGVDVGAKKEIYQLINQFKAE 444
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 22-210 4.20e-16

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 76.61  E-value: 4.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFF-EGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDN 100
Cdd:PTZ00265  400 IYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKDINLKWWRSKIGVVSQDPLLFSNSIKNN 479

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  101 LLFPW-----------QIRHKTPDPE-----------RFSADL--------------ARFN------------------- 125
Cdd:PTZ00265  480 IKYSLyslkdlealsnYYNEDGNDSQenknkrnscraKCAGDLndmsnttdsnelieMRKNyqtikdsevvdvskkvlih 559

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  126 -----LPP--DTLTKS-VSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PTZ00265  560 dfvsaLPDkyETLVGSnASKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAHR 639

                         250
                  ....*....|...
gi 504695722  198 ANEITHADDVLTL 210
Cdd:PTZ00265  640 LSTIRYANTIFVL 652
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 7-201 4.79e-16

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: 4.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRT-GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQ-VS 84
Cdd:COG3845  257 VLEVENLSVRDdRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgVA 336

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 Y---------SVQtpslfDSTVYDNLLFPwqiRHKTP--------DP---ERFSADL-ARFNL-PPDTLTKsVSELSGGE 142
Cdd:COG3845  337 YipedrlgrgLVP-----DMSVAENLILG---RYRRPpfsrggflDRkaiRAFAEELiEEFDVrTPGPDTP-ARSLSGGN 407

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 143 KQRVSLIRNLQFLPKVLLLDEITSALDdankrnVN--EIIHRYV---REQNIAVLWVTHDANEI 201
Cdd:COG3845  408 QQKVILARELSRDPKLLIAAQPTRGLD------VGaiEFIHQRLlelRDAGAAVLLISEDLDEI 465
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 27-197 6.36e-16

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 75.98  E-value: 6.36e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  27 SFSLL--PGEFRL-----ITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrqqVSYSVQTPS-LFDSTVY 98
Cdd:COG1245  353 GFSLEveGGEIREgevlgIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLK-------------ISYKPQYISpDYDGTVE 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  99 DNLlfpwqirhKTPDPERFS-----ADLAR-FNLPPdTLTKSVSELSGGEKQRV----SLIRNLQflpkVLLLDEiTSAL 168
Cdd:COG1245  420 EFL--------RSANTDDFGssyykTEIIKpLGLEK-LLDKNVKDLSGGELQRVaiaaCLSRDAD----LYLLDE-PSAH 485

                        170       180       190
                 ....*....|....*....|....*....|
gi 504695722 169 DDANKR-NVNEIIHRYVREQNIAVLWVTHD 197
Cdd:COG1245  486 LDVEQRlAVAKAIRRFAENRGKTAMVVDHD 515
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 18-220 7.26e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 74.36  E-value: 7.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSG-----KIFFEGKDISTLSPE-AYRQQVSYSVQTPS 91
Cdd:PRK14271  32 AGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRDVlEFRRRVGMLFQRPN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  92 LFDSTVYDNLLFPWQIRHKTPDPERFSADLAR------FNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEIT 165
Cdd:PRK14271 112 PFPMSIMDNVLAGVRAHKLVPRKEFRGVAQARltevglWDAVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPT 191

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722 166 SALDDANKRNVNEIIHRYVreQNIAVLWVTHDANEITHADDVLTLQPHGGKMQEA 220
Cdd:PRK14271 192 SALDPTTTEKIEEFIRSLA--DRLTVIIVTHNLAQAARISDRAALFFDGRLVEEG 244
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
15-211 1.01e-15

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 73.67  E-value: 1.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  15 YRTG-----GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIsTLSPEAYR-QQVSYSVQ 88
Cdd:PRK15112  16 YRTGwfrrqTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPL-HFGDYSYRsQRIRMIFQ 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  89 TP--SLFDSTVYDNLL-FPWQIRHKTPDPER---FSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:PRK15112  95 DPstSLNPRQRISQILdFPLRLNTDLEPEQRekqIIETLRQVGLLPDHASYYPHMLAPGQKQRLGLARALILRPKVIIAD 174

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504695722 163 EITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQ 211
Cdd:PRK15112 175 EALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHiSDQVLVMH 224
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
27-197 1.43e-15

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 74.84  E-value: 1.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  27 SFSL--LPGEFRL-----ITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrqqVSYSVQ--TPSlFDSTV 97
Cdd:PRK13409 352 DFSLevEGGEIYEgevigIVGPNGIGKTTFAKLLAGVLKPDEGEVDPELK-------------ISYKPQyiKPD-YDGTV 417

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  98 YDNLLfpwQIRHKTPDPERFSADLARFNLPPdTLTKSVSELSGGEKQRVS----LIRNLQflpkVLLLDEITSALDDANK 173
Cdd:PRK13409 418 EDLLR---SITDDLGSSYYKSEIIKPLQLER-LLDKNVKDLSGGELQRVAiaacLSRDAD----LYLLDEPSAHLDVEQR 489

                        170       180
                 ....*....|....*....|....
gi 504695722 174 RNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK13409 490 LAVAKAIRRIAEEREATALVVDHD 513
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 14-171 2.71e-15

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: 71.52  E-value: 2.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  14 GYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPT---SGKIFFEGKDISTLSpEAYRQQVSYSVQT- 89
Cdd:cd03233   14 GKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANRTEGNvsvEGDIHYNGIPYKEFA-EKYPGEIIYVSEEd 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 ---PSLfdsTVYDNLlfpwqirhktpdpeRFSADLaRFNlppdtltKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITS 166
Cdd:cd03233   93 vhfPTL---TVRETL--------------DFALRC-KGN-------EFVRGISGGERKRVSIAEALVSRASVLCWDNSTR 147


                 ....*
gi 504695722 167 ALDDA 171
Cdd:cd03233  148 GLDSS 152
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 5-222 2.88e-15

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 73.97  E-value: 2.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIED--VGYRTGGT--TILNNVSFSLLPGEFRLITGPSGCGKS-TLLKIIASLLTP----TSGKIFFEGKDISTLS 75
Cdd:PRK15134   3 QPLLAIENlsVAFRQQQTvrTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHAS 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  76 PEAYRQ----QVSYSVQTP--SL-----FDSTVYDNLLFPWQIRHKTPDPERFSAdLARFNL--PPDTLTKSVSELSGGE 142
Cdd:PRK15134  83 EQTLRGvrgnKIAMIFQEPmvSLnplhtLEKQLYEVLSLHRGMRREAARGEILNC-LDRVGIrqAAKRLTDYPHQLSGGE 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 143 KQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLQphGGKMQEAN 221
Cdd:PRK15134 162 RQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKlADRVAVMQ--NGRCVEQN 239


                 .
gi 504695722 222 R 222
Cdd:PRK15134 240 R 240
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 8-219 2.97e-15

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 73.85  E-value: 2.97e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTI-LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSyS 86
Cdd:PRK10522 323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEQPEDYRKLFS-A 401

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTpslfDSTVYDNLLFPwqiRHKTPDPERFSADLARFNLpPDTLTK-----SVSELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:PRK10522 402 VFT----DFHLFDQLLGP---EGKPANPALVEKWLERLKM-AHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLL 473

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 162 DEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:PRK10522 474 DEWAADQDPHFRREFYQVLLPLLQEMGKTIFAISHDDHYFIHADRLLEMR--NGQLSE 529
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 7-169 3.80e-15

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 73.43  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFeGKDIstlspeayrqQVSYS 86
Cdd:TIGR03719 322 VIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEI-GETV----------KLAYV 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   87 VQTPSLFDS--TVYDNL--------LFPWQIrhktpdPERfsADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLP 156
Cdd:TIGR03719 391 DQSRDALDPnkTVWEEIsggldiikLGKREI------PSR--AYVGRFNFKGSDQQKKVGQLSGGERNRVHLAKTLKSGG 462

                         170
                  ....*....|...
gi 504695722  157 KVLLLDEITSALD 169
Cdd:TIGR03719 463 NVLLLDEPTNDLD 475
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 21-201 4.51e-15

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: 71.41  E-value: 4.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSpeayrqqVSYSVQtPSLfdsTVYDN 100
Cdd:cd03220   36 WALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVTVRGRVSSLLG-------LGGGFN-PEL---TGREN 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 101 LLF--------PWQIRHKTPDPERFSADLARFNLPpdtltksVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:cd03220  105 IYLngrllglsRKEIDEKIDEIIEFSELGDFIDLP-------VKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAF 177

                        170       180
                 ....*....|....*....|....*....
gi 504695722 173 KRNVNEIIhRYVREQNIAVLWVTHDANEI 201
Cdd:cd03220  178 QEKCQRRL-RELLKQGKTVILVSHDPSSI 205
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 18-197 5.71e-15

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 73.05  E-value: 5.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFfegkdistLSPEAyrqQVSYSVQTPSLFDS-T 96
Cdd:TIGR03719  16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEAR--------PQPGI---KVGYLPQEPQLDPTkT 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   97 VYDNLLFpwQIRHKTPDPERFSADLARFNLPPDTLTK--------------------------------------SVSEL 138
Cdd:TIGR03719  85 VRENVEE--GVAEIKDALDRFNEISAKYAEPDADFDKlaaeqaelqeiidaadawdldsqleiamdalrcppwdaDVTKL 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722  139 SGGEKQRVSLIRNLQFLPKVLLLDEITSALDdanKRNVnEIIHRYVREQNIAVLWVTHD 197
Cdd:TIGR03719 163 SGGERRRVALCRLLLSKPDMLLLDEPTNHLD---AESV-AWLERHLQEYPGTVVAVTHD 217
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 8-196 2.23e-14

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 71.37  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL--LTPTSGKIF----------------FEGK 69
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMdqYEPTSGRIIyhvalcekcgyverpsKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   70 DI----STLSPE-------------AYRQQVSYSVQ-TPSLF-DSTVYDNLLFPW-QIRHKTPDPERFSADLARFNLPPD 129
Cdd:TIGR03269  81 PCpvcgGTLEPEevdfwnlsdklrrRIRKRIAIMLQrTFALYgDDTVLDNVLEALeEIGYEGKEAVGRAVDLIEMVQLSH 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722  130 TLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTH 196
Cdd:TIGR03269 161 RITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
cbiO PRK13645
energy-coupling factor transporter ATPase;
23-217 2.72e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 70.04  E-value: 2.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSG-------KIFFEGKDISTLspEAYRQQVSYSVQTP--SLF 93
Cdd:PRK13645  27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGqtivgdyAIPANLKKIKEV--KRLRKEIGLVFQFPeyQLF 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DSTVYDNLLF-PWQIRHKTPDPERFSADLARF-NLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDA 171
Cdd:PRK13645 105 QETIEKDIAFgPVNLGENKQEAYKKVPELLKLvQLPEDYVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPK 184

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 504695722 172 NKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTLqpHGGKM 217
Cdd:PRK13645 185 GEEDFINLFERLNKEYKKRIIMVTHNMDQVLRiADEVIVM--HEGKV 229
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 21-169 3.16e-14

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 70.85  E-value: 3.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP---TSGKIFFEGKDIStlSPE-----AYRQQVSYSVqtPSL 92
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKgvkGSGSVLLNGMPID--AKEmraisAYVQQDDLFI--PTL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   93 fdsTVYDNLLFPWQIRHKTPDP-----ERFSADLARFNLPP--DTLTKS---VSELSGGEKQRVSLIRNLQFLPKVLLLD 162
Cdd:TIGR00955 115 ---TVREHLMFQAHLRMPRRVTkkekrERVDEVLQALGLRKcaNTRIGVpgrVKGLSGGERKRLAFASELLTDPPLLFCD 191


                  ....*..
gi 504695722  163 EITSALD 169
Cdd:TIGR00955 192 EPTSGLD 198
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 26-219 3.57e-14

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: 70.60  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  26 VSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQqvsysvqtpsLFdSTVY-DNLLFP 104
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVTADNREAYRQ----------LF-SAVFsDFHLFD 419

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 105 --WQIrHKTPDPERFSADLARFNLppDTLTK------SVSELSGGEKQRVSLIrnLQFL---PkVLLLDEItsALD-DAN 172
Cdd:COG4615  420 rlLGL-DGEADPARARELLERLEL--DHKVSvedgrfSTTDLSQGQRKRLALL--VALLedrP-ILVFDEW--AADqDPE 491

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504695722 173 KRNV--NEIIHRyVREQNIAVLWVTHDANEITHADDVLTLqpHGGKMQE 219
Cdd:COG4615  492 FRRVfyTELLPE-LKARGKTVIAISHDDRYFDLADRVLKM--DYGKLVE 537
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 4-210 3.75e-14

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 70.80  E-value: 3.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   4 NSAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAyRQQV 83
Cdd:PRK10762   1 MQALLQLKGIDKAFPGVKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKS-SQEA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSV--QTPSLFDS-TVYDNLLF------PW-QIRHKTPDPErfsAD--LARFNLP--PDTLtksVSELSGGEKQRVSLI 149
Cdd:PRK10762  80 GIGIihQELNLIPQlTIAENIFLgrefvnRFgRIDWKKMYAE---ADklLARLNLRfsSDKL---VGELSIGEQQMVEIA 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 150 RNLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEI-THADDVLTL 210
Cdd:PRK10762 154 KVLSFESKVIIMDEPTDALTDTETESLFRVI-RELKSQGRGIVYISHRLKEIfEICDDVTVF 214
cbiO PRK13643
energy-coupling factor transporter ATPase;
23-211 3.85e-14

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 69.76  E-value: 3.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEA----YRQQVSYSVQTP--SLFDST 96
Cdd:PRK13643  22 LFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKQKeikpVRKKVGVVFQFPesQLFEET 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLLF-PWQIRHKTPDPERFSAD-LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKR 174
Cdd:PRK13643 102 VLKDVAFgPQNFGIPKEKAEKIAAEkLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARI 181

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 175 NVNEIIHRyVREQNIAVLWVTHDANEIT-HADDVLTLQ 211
Cdd:PRK13643 182 EMMQLFES-IHQSGQTVVLVTHLMDDVAdYADYVYLLE 218
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 7-197 4.58e-14

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 70.36  E-value: 4.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrQQVSYS 86
Cdd:PRK11147 319 VFEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHCGTK-----------LEVAYF 387

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLFD--STVYDNL-------LFPWQIRHKTpdperfsADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPK 157
Cdd:PRK11147 388 DQHRAELDpeKTVMDNLaegkqevMVNGRPRHVL-------GYLQDFLFHPKRAMTPVKALSGGERNRLLLARLFLKPSN 460

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 158 VLLLDEITSALDDANKRNVNEIIHRYvreQNiAVLWVTHD 197
Cdd:PRK11147 461 LLILDEPTNDLDVETLELLEELLDSY---QG-TVLLVSHD 496
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 27-197 5.67e-14

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: 68.93  E-value: 5.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  27 SFSL--LP----GEFRLITGPSGCGKSTLLKIIASLLTPTSGKifFEGKDISTLSPEAYR-------------------Q 81
Cdd:cd03236   14 SFKLhrLPvpreGQVLGLVGPNGIGKSTALKILAGKLKPNLGK--FDDPPDWDEILDEFRgselqnyftkllegdvkviV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSVQTPSLFDSTVYDNLlfpwqirHKTPDPERFSADLARFNLPPdTLTKSVSELSGGEKQRV----SLIRNLQFlpk 157
Cdd:cd03236   92 KPQYVDLIPKAVKGKVGELL-------KKKDERGKLDELVDQLELRH-VLDRNIDQLSGGELQRVaiaaALARDADF--- 160

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 504695722 158 vLLLDEITSALDDANKRNVNEIIHRYVREQNiAVLWVTHD 197
Cdd:cd03236  161 -YFFDEPSSYLDIKQRLNAARLIRELAEDDN-YVLVVEHD 198
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
6-198 5.95e-14

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 67.95  E-value: 5.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYrqqVSY 85
Cdd:PRK13543  10 PLLAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRF---MAY 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSL-FDSTVYDNLLF--PWQIRHKTPDPerfSADLARFNLP--PDTLtksVSELSGGEKQRVSLIRnLQFLPKVL- 159
Cdd:PRK13543  87 LGHLPGLkADLSTLENLHFlcGLHGRRAKQMP---GSALAIVGLAgyEDTL---VRQLSAGQKKRLALAR-LWLSPAPLw 159

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRYVREQNiAVLWVTHDA 198
Cdd:PRK13543 160 LLDEPYANLDLEGITLVNRMISAHLRGGG-AALVTTHGA 197
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 40-200 8.93e-14

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: 70.04  E-value: 8.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    40 GPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlSPEAYRQQVSYSVQTPSLFDS-TVYDNLLFPWQIRHKTPDperfS 118
Cdd:TIGR01257  963 GHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET-NLDAVRQSLGMCPQHNILFHHlTVAEHILFYAQLKGRSWE----E 1037

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   119 ADLARFNLPPDT-----LTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIavLW 193
Cdd:TIGR01257 1038 AQLEMEAMLEDTglhhkRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIWDLLLKYRSGRTI--IM 1115


                   ....*..
gi 504695722   194 VTHDANE 200
Cdd:TIGR01257 1116 STHHMDE 1122
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 18-209 2.73e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 68.03  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIaSLLTPT---SGKIFFEGKDISTLS-PEAYRQQVSYSVQTPSLF 93
Cdd:PRK13549  16 GGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVL-SGVYPHgtyEGEIIFEGEELQASNiRDTERAGIAIIHQELALV 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 -DSTVYDNLLFPWQIRHK--TPDPE---RFSADLARFNLPPDTLTKsVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSA 167
Cdd:PRK13549  95 kELSVLENIFLGNEITPGgiMDYDAmylRAQKLLAQLKLDINPATP-VGNLGLGQQQLVEIAKALNKQARLLILDEPTAS 173

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504695722 168 LDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITHADDVLT 209
Cdd:PRK13549 174 LTESETAVLLDII-RDLKAHGIACIYISHKLNEVKAISDTIC 214
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 19-215 3.88e-13

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: 68.01  E-value: 3.88e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrqqVSYSVQTPSLFDSTVY 98
Cdd:TIGR01271  438 VTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSGR-------------ISFSPQTSWIMPGTIK 504

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    99 DNLLFPWqirhkTPDPERFSA---------DLARFNLPPDT-LTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:TIGR01271  505 DNIIFGL-----SYDEYRYTSvikacqleeDIALFPEKDKTvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFTHL 579

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 504695722   169 DDANKRnvnEIIHRYVRE--QNIAVLWVTHDANEITHADDVLTLqpHGG 215
Cdd:TIGR01271  580 DVVTEK---EIFESCLCKlmSNKTRILVTSKLEHLKKADKILLL--HEG 623
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 8-169 4.05e-13

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 67.61  E-value: 4.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKI-FFEGKDISTlspeaYRQQVSYS 86
Cdd:PRK15064 320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVkWSENANIGY-----YAQDHAYD 394

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 vqtpslFDStvyDNLLFPWQIRHKTP--DPERFSADLARFNLPPDTLTKSVSELSGGEKQRV---SLIrnLQfLPKVLLL 161
Cdd:PRK15064 395 ------FEN---DLTLFDWMSQWRQEgdDEQAVRGTLGRLLFSQDDIKKSVKVLSGGEKGRMlfgKLM--MQ-KPNVLVM 462


                 ....*...
gi 504695722 162 DEITSALD 169
Cdd:PRK15064 463 DEPTNHMD 470
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
6-200 4.11e-13

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 66.06  E-value: 4.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   6 AVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTL-SPEAYRQQVS 84
Cdd:PRK11614   4 VMLSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWqTAKIMREAVA 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  85 YSVQTPSLFDS-TVYDNLLFPWQIRHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:PRK11614  84 IVPEGRRVFSRmTVEENLAMGGFFAERDQFQERIKWVYELFPRLHERRIQRAGTMSGGEQQMLAIGRALMSQPRLLLLDE 163

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504695722 164 ITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANE 200
Cdd:PRK11614 164 PSLGLAPIIIQQIFDTIEQ-LREQGMTIFLVEQNANQ 199
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
5-202 5.53e-13

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 66.06  E-value: 5.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIED--VGYRTGGTTiLNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIStlspEAYRQQ 82
Cdd:PRK15056   4 QAGIVVNDvtVTWRNGHTA-LRDASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISILGQPTR----QALQKN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  83 -VSYSVQT-------PSLFDSTV----YDNLlfPWQIRHKTPDPERFSADLARFNLpPDTLTKSVSELSGGEKQRVSLIR 150
Cdd:PRK15056  79 lVAYVPQSeevdwsfPVLVEDVVmmgrYGHM--GWLRRAKKRDRQIVTAALARVDM-VEFRHRQIGELSGGQKKRVFLAR 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 504695722 151 NLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEIT 202
Cdd:PRK15056 156 AIAQQGQVILLDEPFTGVDVKTEARIISLL-RELRDEGKTMLVSTHNLGSVT 206
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 34-210 6.17e-13

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 67.36  E-value: 6.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   34 EFRLITGPSGCGKSTLLKiiaslltpTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDSTVYDNLLFPWQ--IRHKT 111
Cdd:PTZ00265 1257 EFSLTKEGGSGEDSTVFK--------NSGKILLDGVDICDYNLKDLRNLFSIVSQEPMLFNMSIYENIKFGKEdaTREDV 1328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  112 PDPERFSADLARFNLPPDTLTKSV----SELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQ 187
Cdd:PTZ00265 1329 KRACKFAAIDEFIESLPNKYDTNVgpygKSLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKA 1408

                         170       180
                  ....*....|....*....|...
gi 504695722  188 NIAVLWVTHDANEITHADDVLTL 210
Cdd:PTZ00265 1409 DKTIITIAHRIASIKRSDKIVVF 1431
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
16-169 1.01e-12

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 66.69  E-value: 1.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  16 RTGGTTILNNVSFSLLPGE-FRLItGPSGCGKSTLLKIIASLLTPTSG--KIF---FEGKDISTlspeayRQQVSYSVQT 89
Cdd:NF033858 275 RFGDFTAVDHVSFRIRRGEiFGFL-GSNGCGKSTTMKMLTGLLPASEGeaWLFgqpVDAGDIAT------RRRVGYMSQA 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  90 PSLF-DSTVYDNL-----LFpwqirHKTPD--PERFSADLARFNLPP--DTLTksvSELSGGEKQRVSL----IRNlqfl 155
Cdd:NF033858 348 FSLYgELTVRQNLelharLF-----HLPAAeiAARVAEMLERFDLADvaDALP---DSLPLGIRQRLSLavavIHK---- 415

                        170
                 ....*....|....
gi 504695722 156 PKVLLLDEITSALD 169
Cdd:NF033858 416 PELLILDEPTSGVD 429
PTZ00243 PTZ00243
ABC transporter; Provisional
 22-211 1.50e-12

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 66.34  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEgkdistlspeayrQQVSYSVQTPSLFDSTVYDNL 101
Cdd:PTZ00243  675 LLRDVSVSVPRGKLTVVLGATGSGKSTLLQSLLSQFEISEGRVWAE-------------RSIAYVPQQAWIMNATVRGNI 741

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  102 LFpwqirhktPDPER------------FSADLARFN--LPPDTLTKSVSeLSGGEKQRVSLIRNLQFLPKVLLLDEITSA 167
Cdd:PTZ00243  742 LF--------FDEEDaarladavrvsqLEADLAQLGggLETEIGEKGVN-LSGGQKARVSLARAVYANRDVYLLDDPLSA 812

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 504695722  168 LD-DANKRNVNEIIHRYVREQNiAVLwVTHDANEITHADDVLTLQ 211
Cdd:PTZ00243  813 LDaHVGERVVEECFLGALAGKT-RVL-ATHQVHVVPRADYVVALG 855
PLN03073 PLN03073
ABC transporter F family; Provisional
 14-208 1.78e-12

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 66.04  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  14 GYrTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVqTPSLF 93
Cdd:PLN03073 517 GY-PGGPLLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTVFRSAKVRMAVFSQHHVDGLDLSS-NPLLY 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  94 DSTVYDNLlfpwqirhktpdPE-RFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALD-DA 171
Cdd:PLN03073 595 MMRCFPGV------------PEqKLRAHLGSFGVTGNLALQPMYTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDlDA 662

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 504695722 172 nkrnVNEIIHRYVREQNiAVLWVTHDANEITHADDVL 208
Cdd:PLN03073 663 ----VEALIQGLVLFQG-GVLMVSHDEHLISGSVDEL 694
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
5-209 1.87e-12

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 65.70  E-value: 1.87e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   5 SAVLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIS-TLSPEAYRQQV 83
Cdd:PRK11288   2 SPYLSFDGIGKTFPGVKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRfASTTAALAAGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 SYSVQ----TPSLfdsTVYDNLL---FPWQ--IRHKTPDPERFSADLARFNLPPDTLTKsVSELSGGEKQRV----SLIR 150
Cdd:PRK11288  82 AIIYQelhlVPEM---TVAENLYlgqLPHKggIVNRRLLNYEAREQLEHLGVDIDPDTP-LKYLSIGQRQMVeiakALAR 157

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722 151 NlqflPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADDVLT 209
Cdd:PRK11288 158 N----ARVIAFDEPTSSLSAREIEQLFRVIRE-LRAEGRVILYVSHRMEEIFALCDAIT 211
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 18-197 1.91e-12

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.53  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFfegkdistLSPEAyrqQVSYSVQTPSLFDS-T 96
Cdd:PRK11819  18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEAR--------PAPGI---KVGYLPQEPQLDPEkT 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLLFPWQ-IRHK------------TPDPErFSADLAR-------------FNL--------------PPDTltkSVS 136
Cdd:PRK11819  87 VRENVEEGVAeVKAAldrfneiyaayaEPDAD-FDALAAEqgelqeiidaadaWDLdsqleiamdalrcpPWDA---KVT 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 137 ELSGGEKQRVSLIRNLQFLPKVLLLDEITSALdDAnkrnvnEIIH---RYVREQNIAVLWVTHD 197
Cdd:PRK11819 163 KLSGGERRRVALCRLLLEKPDMLLLDEPTNHL-DA------ESVAwleQFLHDYPGTVVAVTHD 219
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
 19-196 1.95e-12

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: 65.54  E-value: 1.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL-------LT-PTSGKIFFEGKDiSTLSPEAYRQQVSYSVQTP 90
Cdd:TIGR00954 464 GDVLIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELwpvyggrLTkPAKGKLFYVPQR-PYMTLGTLRDQIIYPDSSE 542

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   91 SLFDSTVYDNLLFpwQIrhktpdperfsadLARFNLPpDTLTKSVS---------ELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:TIGR00954 543 DMKRRGLSDKDLE--QI-------------LDNVQLT-HILEREGGwsavqdwmdVLSGGEKQRIAMARLFYHKPQFAIL 606

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 504695722  162 DEITSALddanKRNVNEIIHRYVREQNIAVLWVTH 196
Cdd:TIGR00954 607 DECTSAV----SVDVEGYMYRLCREFGITLFSVSH 637
cyc_pep_trnsptr TIGR01194
cyclic peptide transporter; This model describes cyclic peptide transporter in bacteria. ...
 23-210 2.59e-12

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


Pssm-ID: 130262 [Multi-domain]  Cd Length: 555  Bit Score: 65.36  E-value: 2.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSysvqtpSLF-DSTVYDNL 101
Cdd:TIGR01194 358 LGPIDLRIAQGDIVFIVGENGCGKSTLAKLFCGLYIPQEGEILLDGAAVSADSRDDYRDLFS------AIFaDFHLFDDL 431

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  102 LFPWQIRHktPDPERFSADLARFNLP-----PDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNV 176
Cdd:TIGR01194 432 IGPDEGEH--ASLDNAQQYLQRLEIAdkvkiEDGGFSTTTALSTGQQKRLALICAWLEDRPILLFDEWAADQDPAFKRFF 509

                         170       180       190
                  ....*....|....*....|....*....|....
gi 504695722  177 NEIIHRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:TIGR01194 510 YEELLPDLKRQGKTIIIISHDDQYFELADQIIKL 543
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 38-197 7.75e-12

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: 64.04  E-value: 7.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  38 ITGPSGCGKSTLLKIIASLLTPTSGKI-----------FFEGKDISTlspeaYRQQ-------VSYSVQ----TPSLFDS 95
Cdd:COG1245  104 ILGPNGIGKSTALKILSGELKPNLGDYdeepswdevlkRFRGTELQD-----YFKKlangeikVAHKPQyvdlIPKVFKG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 TVYDnLLfpwqirhKTPDpERFSAD--LARFNLPPdTLTKSVSELSGGEKQRV----SLIRNLQFlpkvLLLDEITSALD 169
Cdd:COG1245  179 TVRE-LL-------EKVD-ERGKLDelAEKLGLEN-ILDRDISELSGGELQRVaiaaALLRDADF----YFFDEPSSYLD 244

                        170       180
                 ....*....|....*....|....*...
gi 504695722 170 DANKRNVNEIIHRYVREqNIAVLWVTHD 197
Cdd:COG1245  245 IYQRLNVARLIRELAEE-GKYVLVVEHD 271
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 22-215 8.49e-12

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 63.88  E-value: 8.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLkiiaSLLT---PT--SGKIFFEGK---------DI--------STLSPEaY 79
Cdd:PRK10938 275 ILHNLSWQVNPGEHWQIVGPNGAGKSTLL----SLITgdhPQgySNDLTLFGRrrgsgetiwDIkkhigyvsSSLHLD-Y 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  80 RqqVSYSVQTPSL---FDST-VYdnllfpwqirHKTPDPERFSAD--LARFNLPPDTLTKSVSELSGGEkQRVSLI-RNL 152
Cdd:PRK10938 350 R--VSTSVRNVILsgfFDSIgIY----------QAVSDRQQKLAQqwLDILGIDKRTADAPFHSLSWGQ-QRLALIvRAL 416

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 153 QFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTH---DA-NEITHAddvLTLQPHGG 215
Cdd:PRK10938 417 VKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETQLLFVSHhaeDApACITHR---LEFVPDGD 480
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 13-219 1.17e-11

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 63.81  E-value: 1.17e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    13 VGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSL 92
Cdd:TIGR00957 1292 LRYREDLDLVLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNIAKIGLHDLRFKITIIPQDPVL 1371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    93 FDSTVYDNlLFPWQirhKTPDPERFSA-DLARF----NLPPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:TIGR00957 1372 FSGSLRMN-LDPFS---QYSDEEVWWAlELAHLktfvSALPDKLDHECAEggenLSVGQRQLVCLARALLRKTKILVLDE 1447

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722   164 ITSALDdankRNVNEIIHRYVREQ--NIAVLWVTHDANEITHADDVLTLQPhgGKMQE 219
Cdd:TIGR00957 1448 ATAAVD----LETDNLIQSTIRTQfeDCTVLTIAHRLNTIMDYTRVIVLDK--GEVAE 1499
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 19-215 1.81e-11

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 62.18  E-value: 1.81e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKdistlspeayrqqVSYSVQTPSLFDSTVY 98
Cdd:cd03291   49 GAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSGR-------------ISFSSQFSWIMPGTIK 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  99 DNLLFPW---QIRHKTP-DPERFSADLARFNLPPDT-LTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANK 173
Cdd:cd03291  116 ENIIFGVsydEYRYKSVvKACQLEEDITKFPEKDNTvLGEGGITLSGGQRARISLARAVYKDADLYLLDSPFGYLDVFTE 195

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 504695722 174 RNVNEIIHRYVREQNIAVLwVTHDANEITHADDVLTLqpHGG 215
Cdd:cd03291  196 KEIFESCVCKLMANKTRIL-VTSKMEHLKKADKILIL--HEG 234
PLN03211 PLN03211
ABC transporter G-25; Provisional
 9-169 1.84e-11

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 62.97  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   9 TIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTS--GKIFFEGKDIStlspEAYRQQVSYS 86
Cdd:PLN03211  70 KISDETRQIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGRIQGNNftGTILANNRKPT----KQILKRTGFV 145

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQtpslfdstvyDNLLFPwqirHKTPDPERFSADLARFnlpPDTLTKS---------VSEL------------------S 139
Cdd:PLN03211 146 TQ----------DDILYP----HLTVRETLVFCSLLRL---PKSLTKQekilvaesvISELgltkcentiignsfirgiS 208

                        170       180       190
                 ....*....|....*....|....*....|
gi 504695722 140 GGEKQRVSLIRNLQFLPKVLLLDEITSALD 169
Cdd:PLN03211 209 GGERKRVSIAHEMLINPSLLILDEPTSGLD 238
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 1-197 2.36e-11

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 62.05  E-value: 2.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   1 MKDNSAVLTIED--VGYRT--GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP---TSGKIFFEGKDIST 73
Cdd:PRK09473   6 QQQADALLDVKDlrVTFSTpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSQTAFALMGLLAAngrIGGSATFNGREILN 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  74 LsPEAY-----RQQVSYSVQTP--SLFDST-VYDNLLFPWQIRHKTPDPERFSADL------------ARFNLPPdtltk 133
Cdd:PRK09473  86 L-PEKElnklrAEQISMIFQDPmtSLNPYMrVGEQLMEVLMLHKGMSKAEAFEESVrmldavkmpearKRMKMYP----- 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 134 svSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK09473 160 --HEFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 7-217 2.72e-11

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 60.33  E-value: 2.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGY----RTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP--TSGKIFFEGKDIstlsPEAYR 80
Cdd:cd03232    3 VLTWKNLNYtvpvKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPL----DKNFQ 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 QQVSYSVQTPSLFD-STVYDNLlfpwqirhktpdpeRFSADLarfnlppdtltksvSELSGGEKQRVSLIRNLQFLPKVL 159
Cdd:cd03232   79 RSTGYVEQQDVHSPnLTVREAL--------------RFSALL--------------RGLSVEQRKRLTIGVELAAKPSIL 130

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 160 LLDEITSALDDANKRNVNEIIHRYVREqNIAVLWVTHDANE--ITHADDVLTLQPhGGKM 217
Cdd:cd03232  131 FLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQPSAsiFEKFDRLLLLKR-GGKT 188
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 21-171 3.03e-11

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.43  E-value: 3.03e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIAS----LLTPTSGKIFFEGKDISTLSPEaYRQQVSYSVQT----PSL 92
Cdd:TIGR00956   75 DILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIASntdgFHIGVEGVITYDGITPEEIKKH-YRGDVVYNAETdvhfPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    93 fdsTVYDNLLFpwQIRHKTPD--PERFSAD----------LARFNLPPDTLTKS----VSELSGGEKQRVSLIRNLQFLP 156
Cdd:TIGR00956  154 ---TVGETLDF--AARCKTPQnrPDGVSREeyakhiadvyMATYGLSHTRNTKVgndfVRGVSGGERKRVSIAEASLGGA 228

                          170
                   ....*....|....*
gi 504695722   157 KVLLLDEITSALDDA 171
Cdd:TIGR00956  229 KIQCWDNATRGLDSA 243
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 19-210 3.93e-11

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 61.67  E-value: 3.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  19 GTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDIS-TLSPEAYRQQVSYSVQTPSLF-DST 96
Cdd:PRK10982  10 GVKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDfKSSKEALENGISMVHQELNLVlQRS 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLlfpWQIRHKTP-----------DPERFSADLArFNLPPdtlTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEIT 165
Cdd:PRK10982  90 VMDNM---WLGRYPTKgmfvdqdkmyrDTKAIFDELD-IDIDP---RAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPT 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 504695722 166 SALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITHADDVLTL 210
Cdd:PRK10982 163 SSLTEKEVNHLFTII-RKLKERGCGIVYISHKMEEIFQLCDEITI 206
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 32-201 4.96e-11

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: 58.92  E-value: 4.96e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    32 PGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFegkdistLSPEAYRQQvsysvqtpslfdstvydnllfpwqirhkt 111
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGVIY-------IDGEDILEE----------------------------- 44

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   112 pdperfsadlARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYV-----RE 186
Cdd:smart00382  45 ----------VLDQLLLIIVGGKKASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLEELRLllllkSE 114

                          170
                   ....*....|....*
gi 504695722   187 QNIAVLWVTHDANEI 201
Cdd:smart00382 115 KNLTVILTTNDEKDL 129
PTZ00243 PTZ00243
ABC transporter; Provisional
 8-101 5.17e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 61.72  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    8 LTIEDVG--YRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:PTZ00243 1309 LVFEGVQmrYREGLPLVLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGAYGLRELRRQFSM 1388

                          90
                  ....*....|....*.
gi 504695722   86 SVQTPSLFDSTVYDNL 101
Cdd:PTZ00243 1389 IPQDPVLFDGTVRQNV 1404
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 8-169 5.48e-11

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: 60.64  E-value: 5.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIED--VGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTpTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:cd03289    3 MTVKDltAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLSAFLRLLN-TEGDIQIDGVSWNSVPLQKWRKAFGV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNLlfpwqirhktpDPERFSADLARFNLPPDTLTKSVSE----------------LSGGEKQRVSLI 149
Cdd:cd03289   82 IPQKVFIFSGTFRKNL-----------DPYGKWSDEEIWKVAEEVGLKSVIEqfpgqldfvlvdggcvLSHGHKQLMCLA 150

                        170       180
                 ....*....|....*....|
gi 504695722 150 RNLQFLPKVLLLDEITSALD 169
Cdd:cd03289  151 RSVLSKAKILLLDEPSAHLD 170
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 23-219 6.15e-11

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


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 61.50  E-value: 6.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGkdistlspeayrqQVSYSVQTPSLFDSTVYDNLL 102
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG-------------SVAYVPQQAWIQNDSLRENIL 720

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   103 FPWQIrhktpDPERFSADLARFNLPPD----------TLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDAN 172
Cdd:TIGR00957  721 FGKAL-----NEKYYQQVLEACALLPDleilpsgdrtEIGEKGVNLSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 504695722   173 KRNVNE-IIHRYVREQNIAVLWVTHDANEITHADDVLTLQphGGKMQE 219
Cdd:TIGR00957  796 GKHIFEhVIGPEGVLKNKTRILVTHGISYLPQVDVIIVMS--GGKISE 841
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 23-216 7.31e-11

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: 59.58  E-value: 7.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTL----------LKIIASLltPTSGKIFFEGKD------ISTLSPEAYRQQVSYS 86
Cdd:cd03270   11 LKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVESL--SAYARQFLGQMDkpdvdsIEGLSPAIAIDQKTTS 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 vQTPSlfdSTV------YD--NLLFPwqirhKTPDPERFSAdLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQF-LPK 157
Cdd:cd03270   89 -RNPR---STVgtvteiYDylRLLFA-----RVGIRERLGF-LVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSgLTG 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504695722 158 VL-LLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEITHADDVLTLQP----HGGK 216
Cdd:cd03270  159 VLyVLDEPSIGLHPRDNDRLIETLKR-LRDLGNTVLVVEHDEDTIRAADHVIDIGPgagvHGGE 221
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 13-169 9.49e-11

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: 61.08  E-value: 9.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    13 VGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTpTSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSL 92
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSVTLQTWRKAFGVIPQKVFI 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    93 FDSTVYDNLlfpwqirhktpDPERFSADLARFNLPPDTLTKSVSE----------------LSGGEKQRVSLIRNLQFLP 156
Cdd:TIGR01271 1304 FSGTFRKNL-----------DPYEQWSDEEIWKVAEEVGLKSVIEqfpdkldfvlvdggyvLSNGHKQLMCLARSILSKA 1372

                          170
                   ....*....|...
gi 504695722   157 KVLLLDEITSALD 169
Cdd:TIGR01271 1373 KILLLDEPSAHLD 1385
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 7-169 9.50e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 60.52  E-value: 9.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIffegkDI-STLspeayrqQVSY 85
Cdd:PRK11819 324 VIEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI-----KIgETV-------KLAY 391

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDS--TVY-------DNLLFpwqirHKTPDPERfsADLARFNLP-PDTlTKSVSELSGGEKQRVSLIRNLQFL 155
Cdd:PRK11819 392 VDQSRDALDPnkTVWeeisgglDIIKV-----GNREIPSR--AYVGRFNFKgGDQ-QKKVGVLSGGERNRLHLAKTLKQG 463

                        170
                 ....*....|....
gi 504695722 156 PKVLLLDEITSALD 169
Cdd:PRK11819 464 GNVLLLDEPTNDLD 477
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
23-199 1.54e-10

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 59.26  E-value: 1.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLT---PTSGKIFFEGKDISTLSPEA-----YRQQVSYSVQTPSLFD 94
Cdd:PRK09984  20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRHLSGLITgdkSAGSHIELLGRTVQREGRLArdirkSRANTGYIFQQFNLVN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  95 S-TVYDNLLFP-------WQ--IRHKTP-DPERFSADLARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:PRK09984 100 RlSVLENVLIGalgstpfWRtcFSWFTReQKQRALQALTRVGMV-HFAHQRVSTLSGGQQQRVAIARALMQQAKVILADE 178

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504695722 164 ITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDAN 199
Cdd:PRK09984 179 PIASLDPESARIVMDTLRDINQNDGITVVVTLHQVD 214
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
38-197 2.33e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 59.44  E-value: 2.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  38 ITGPSGCGKSTLLKIIASLLTPTSGKI-----------FFEGKDISTlspeaYRQQVS-----------YSVQTPSLFDS 95
Cdd:PRK13409 104 ILGPNGIGKTTAVKILSGELIPNLGDYeeepswdevlkRFRGTELQN-----YFKKLYngeikvvhkpqYVDLIPKVFKG 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 TVYDnLLfpwqirhKTPDpERFSAD--LARFNLPPdTLTKSVSELSGGEKQRV----SLIRNLQFlpkvLLLDEITSALD 169
Cdd:PRK13409 179 KVRE-LL-------KKVD-ERGKLDevVERLGLEN-ILDRDISELSGGELQRVaiaaALLRDADF----YFFDEPTSYLD 244

                        170       180
                 ....*....|....*....|....*...
gi 504695722 170 DANKRNVNEIIHRYVreQNIAVLWVTHD 197
Cdd:PRK13409 245 IRQRLNVARLIRELA--EGKYVLVVEHD 270
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
24-201 3.38e-10

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 59.03  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  24 NNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSYSvqTPSLFDSTVYDNL- 101
Cdd:PRK09700 280 RDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRSPlDAVKKGMAYI--TESRRDNGFFPNFs 357

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 ---------------------LFPWQIRHKTPDPERfsadlARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLL 160
Cdd:PRK09700 358 iaqnmaisrslkdggykgamgLFHEVDEQRTAENQR-----ELLALKCHSVNQNITELSGGNQQKVLISKWLCCCPEVII 432

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504695722 161 LDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEI 201
Cdd:PRK09700 433 FDEPTRGIDVGAKAEIYKVM-RQLADDGKVILMVSSELPEI 472
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 8-211 5.53e-10

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 57.61  E-value: 5.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIED--VGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVSY 85
Cdd:cd03288   20 IKIHDlcVRYENNLKPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDISKLPLHTLRSRLSI 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQTPSLFDSTVYDNLlfpwqirhktpDPERFSAD--------LARFNLP----PDTLTKSVSE----LSGGEKQRVSLI 149
Cdd:cd03288  100 ILQDPILFSGSIRFNL-----------DPECKCTDdrlwealeIAQLKNMvkslPGGLDAVVTEggenFSVGQRQLFCLA 168

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504695722 150 RNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQniAVLWVTHDANEITHADDVLTLQ 211
Cdd:cd03288  169 RAFVRKSSILIMDEATASIDMATENILQKVVMTAFADR--TVVTIAHRVSTILDADLVLVLS 228
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 23-216 7.83e-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: 56.18  E-value: 7.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLkiiaslltptsgkifFEGkdistlspeAYRQQVSYSVQTPSLFDstvYDNLL 102
Cdd:cd03238   11 LQNLDVSIPLNVLVVVTGVSGSGKSTLV---------------NEG---------LYASGKARLISFLPKFS---RNKLI 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 103 FPWQIRHktpdperfsadLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPK--VLLLDEITSALDDANKRNVNEII 180
Cdd:cd03238   64 FIDQLQF-----------LIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQDINQLLEVI 132

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 504695722 181 HRyVREQNIAVLWVTHDANEITHADDVLTLQPHGGK 216
Cdd:cd03238  133 KG-LIDLGNTVILIEHNLDVLSSADWIIDFGPGSGK 167
PLN03130 PLN03130
ABC transporter C family member; Provisional
 23-219 8.37e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 58.21  E-value: 8.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFfegkdistlspeAYRQQVSYSVQTPSLFDSTVYDNLL 102
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASV------------VIRGTVAYVPQVSWIFNATVRDNIL 700

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  103 F--PWqirhktpDPERFSA---------DLARfnLPPDTLTKsVSE----LSGGEKQRVSLIRNLQFLPKVLLLDEITSA 167
Cdd:PLN03130  701 FgsPF-------DPERYERaidvtalqhDLDL--LPGGDLTE-IGErgvnISGGQKQRVSMARAVYSNSDVYIFDDPLSA 770

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 504695722  168 LDDANKRNV-NEIIHRYVReQNIAVLwVTHDANEITHADDVLTLqpHGGKMQE 219
Cdd:PLN03130  771 LDAHVGRQVfDKCIKDELR-GKTRVL-VTNQLHFLSQVDRIILV--HEGMIKE 819
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 25-207 1.32e-09

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 56.63  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  25 NVSFSLLPGEFRLITGPSGCGKS----TLLKIIASLLTPTSGKIFFEGKDIStlsPEAYR-QQVSYSVQTP-SLFDS--T 96
Cdd:PRK10418  21 GVSLTLQRGRVLALVGGSGSGKSltcaAALGILPAGVRQTAGRVLLDGKPVA---PCALRgRKIATIMQNPrSAFNPlhT 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  97 VYDNLLFPWQIRHKTPDPERFSADLARFNLP-PDTLTKSVS-ELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKR 174
Cdd:PRK10418  98 MHTHARETCLALGKPADDATLTAALEAVGLEnAARVLKLYPfEMSGGMLQRMMIALALLCEAPFIIADEPTTDLDVVAQA 177

                        170       180       190
                 ....*....|....*....|....*....|....
gi 504695722 175 NVNEIIHRYVREQNIAVLWVTHDANEITH-ADDV 207
Cdd:PRK10418 178 RILDLLESIVQKRALGMLLVTHDMGVVARlADDV 211
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 18-169 5.08e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.73  E-value: 5.08e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  18 GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEgKD--ISTLS---P---------------- 76
Cdd:PRK11147  14 SDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYE-QDliVARLQqdpPrnvegtvydfvaegie 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  77 ------EAYrQQVSYSVQT-PS---------LFDSTVYDNLlfpWQIRhktpdpERFSADLARFNLPPDTltkSVSELSG 140
Cdd:PRK11147  93 eqaeylKRY-HDISHLVETdPSeknlnelakLQEQLDHHNL---WQLE------NRINEVLAQLGLDPDA---ALSSLSG 159

                        170       180
                 ....*....|....*....|....*....
gi 504695722 141 GEKQRVSLIRNLQFLPKVLLLDEITSALD 169
Cdd:PRK11147 160 GWLRKAALGRALVSNPDVLLLDEPTNHLD 188
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 7-218 7.50e-09

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 55.18  E-value: 7.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFeGKDIstlspeayrqQVSYS 86
Cdd:PRK10636 312 LLKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIGL-AKGI----------KLGYF 380

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  87 VQTPSLF---DSTVYDNL--LFPWQIRHKTPDPerfsadLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLL 161
Cdd:PRK10636 381 AQHQLEFlraDESPLQHLarLAPQELEQKLRDY------LGGFGFQGDKVTEETRRFSGGEKARLVLALIVWQRPNLLLL 454

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722 162 DEITSALDDANKRNVNEIIHRYvreqNIAVLWVTHDANEITHADDVLTLQpHGGKMQ 218
Cdd:PRK10636 455 DEPTNHLDLDMRQALTEALIDF----EGALVVVSHDRHLLRSTTDDLYLV-HDGKVE 506
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 23-197 2.40e-08

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 53.21  E-value: 2.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKS-TLLKIIASLLTP---TSGKIFFEGKDISTLSPEAYRQQVSYSV----QTP--SL 92
Cdd:PRK11022  23 VDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVamifQDPmtSL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  93 FDS-TVydnllfPWQI----------RHKT--------------PDPErfsadlARFNLPPdtltksvSELSGGEKQRVS 147
Cdd:PRK11022 103 NPCyTV------GFQImeaikvhqggNKKTrrqraidllnqvgiPDPA------SRLDVYP-------HQLSGGMSQRVM 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 504695722 148 LIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHD 197
Cdd:PRK11022 164 IAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 3-210 4.74e-08

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 52.55  E-value: 4.74e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   3 DNSAVLTIEDVGYR----TGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGkdisTLSPEA 78
Cdd:PRK10261   8 DARDVLAVENLNIAfmqeQQKIAAVRNLSFSLQRGETLAIVGESGSGKSVTALALMRLLEQAGGLVQCDK----MLLRRR 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 YRQQVSYSVQTPS------------LFDSTVYD-NLLFPW------QIR-HKTPDPERFSA------DLARFNLPPDTLT 132
Cdd:PRK10261  84 SRQVIELSEQSAAqmrhvrgadmamIFQEPMTSlNPVFTVgeqiaeSIRlHQGASREEAMVeakrmlDQVRIPEAQTILS 163

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722 133 KSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITH-ADDVLTL 210
Cdd:PRK10261 164 RYPHQLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEiADRVLVM 242
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
7-169 8.36e-08

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 52.05  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   7 VLTIEDVGYRTGGTTILNNVSFSLLPGefR---LItGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTlspEAYRQQV 83
Cdd:NF033858   1 VARLEGVSHRYGKTVALDDVSLDIPAG--CmvgLI-GPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMAD---ARHRRAV 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  84 S----YSVQT------PSLfdsTVYDNL-----LF-------PWQIRHKTPdperfSADLARFnlppdtLTKSVSELSGG 141
Cdd:NF033858  75 CpriaYMPQGlgknlyPTL---SVFENLdffgrLFgqdaaerRRRIDELLR-----ATGLAPF------ADRPAGKLSGG 140

                        170       180       190
                 ....*....|....*....|....*....|..
gi 504695722 142 EKQRVS----LIRNlqflPKVLLLDEITSALD 169
Cdd:NF033858 141 MKQKLGlccaLIHD----PDLLILDEPTTGVD 168
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 23-218 9.67e-08

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: 51.75  E-value: 9.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLK-IIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSYSVQ-------TPSL- 92
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPaQAIRAGIAMVPEdrkrhgiVPILg 355

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   93 ----FDSTVYDNLLFPWQIrHKTPDPERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSAL 168
Cdd:TIGR02633 356 vgknITLSVLKSFCFKMRI-DAAAELQIIGSAIQRLKVKTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504695722  169 DDANKRNVNEIIHRYVREqNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQ 218
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGlSDRVLVI--GEGKLK 482
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 32-200 2.11e-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: 51.17  E-value: 2.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    32 PGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYrQQVSYSVQTPSLFDSTVYDNLLFPWQIRHKT 111
Cdd:TIGR01257 1964 PGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVH-QNMGYCPQFDAIDDLLTGREHLYLYARLRGV 2042

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   112 PDPE-----RFSADLARFNLPPDTLTKSvseLSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVRE 186
Cdd:TIGR01257 2043 PAEEiekvaNWSIQSLGLSLYADRLAGT---YSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE 2119

                          170
                   ....*....|....
gi 504695722   187 QNiAVLWVTHDANE 200
Cdd:TIGR01257 2120 GR-AVVLTSHSMEE 2132
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-209 2.37e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 50.56  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIaSLLTPT---SGKIFFEG-----KDIS--------------TLSPEAyr 80
Cdd:NF040905  17 LDDVNLSVREGEIHALCGENGAGKSTLMKVL-SGVYPHgsyEGEILFDGevcrfKDIRdsealgiviihqelALIPYL-- 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  81 qqvsysvqtpslfdsTVYDNL----------LFPWQIRHKtpdpeRFSADLARFNL--PPDTLtksVSELSGGEKQRVSL 148
Cdd:NF040905  94 ---------------SIAENIflgnerakrgVIDWNETNR-----RARELLAKVGLdeSPDTL---VTDIGVGKQQLVEI 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722 149 IRNLQFLPKVLLLDEITSALDDANKRNVNEIIhRYVREQNIAVLWVTHDANEITHADDVLT 209
Cdd:NF040905 151 AKALSKDVKLLILDEPTAALNEEDSAALLDLL-LELKAQGITSIIISHKLNEIRRVADSIT 210
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
23-201 2.67e-07

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 49.81  E-value: 2.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGkDISTLSPEAyrqqvSYSVQTpslfdsTVYDNLL 102
Cdd:PRK13546  40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-EVSVIAISA-----GLSGQL------TGIENIE 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 103 F--------PWQIRHKTPDPERFSaDLARFNLPPdtltksVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKR 174
Cdd:PRK13546 108 FkmlcmgfkRKEIKAMTPKIIEFS-ELGEFIYQP------VKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180

                        170       180
                 ....*....|....*....|....*..
gi 504695722 175 NVNEIIHRYvREQNIAVLWVTHDANEI 201
Cdd:PRK13546 181 KCLDKIYEF-KEQNKTIFFVSHNLGQV 206
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 24-197 3.73e-07

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: 48.12  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  24 NNVSFSllPGEFRLITGPSGCGKSTLLKIIASLLTptsgkiffegkdistlspEAYRQQVSYSVQTPSLFDSTVYDNLLF 103
Cdd:cd03227   14 NDVTFG--EGSLTIITGPNGSGKSTILDAIGLALG------------------GAQSATRRRSGVKAGCIVAAVSAELIF 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 104 pwqirhktpdperfsadlarfnlppdtltkSVSELSGGEKQRVSL-----IRNLQFLPkVLLLDEITSALDDANKRNVNE 178
Cdd:cd03227   74 ------------------------------TRLQLSGGEKELSALalilaLASLKPRP-LYILDEIDRGLDPRDGQALAE 122

                        170
                 ....*....|....*....
gi 504695722 179 IIHRYVREQNIaVLWVTHD 197
Cdd:cd03227  123 AILEHLVKGAQ-VIVITHL 140
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 22-218 4.09e-07

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 49.93  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  22 ILNNVSFSLLPGEFRLITGPSGCGKSTLLK-IIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSY-------------- 85
Cdd:PRK13549 277 RVDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPqQAIAQGIAMvpedrkrdgivpvm 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  86 SVQ---TPSLFDS----TVYDNLLFPWQIRH-------KTPDPErfsadlarfnLPpdtltksVSELSGGEKQRVSLIRN 151
Cdd:PRK13549 357 GVGkniTLAALDRftggSRIDDAAELKTILEsiqrlkvKTASPE----------LA-------IARLSGGNQQKAVLAKC 419

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504695722 152 LQFLPKVLLLDEITSALDDANKRNVNEIIHRYVrEQNIAVLWVTHDANEITH-ADDVLTLqpHGGKMQ 218
Cdd:PRK13549 420 LLLNPKILILDEPTRGIDVGAKYEIYKLINQLV-QQGVAIIVISSELPEVLGlSDRVLVM--HEGKLK 484
PLN03232 PLN03232
ABC transporter C family member; Provisional
 23-169 5.49e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 49.59  E-value: 5.49e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGkiffegkdistlSPEAYRQQVSYSVQTPSLFDSTVYDNLL 102
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAET------------SSVVIRGSVAYVPQVSWIFNATVRENIL 700

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504695722  103 FPWQIrhktpDPERF------SADLARFNLPPDTLTKSVSE----LSGGEKQRVSLIRNLQFLPKVLLLDEITSALD 169
Cdd:PLN03232  701 FGSDF-----ESERYwraidvTALQHDLDLLPGRDLTEIGErgvnISGGQKQRVSMARAVYSNSDIYIFDDPLSALD 772
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 33-208 8.25e-07

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: 47.57  E-value: 8.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  33 GEFRLITGPSGCGKSTLLKIIASLLTPTSGKIffegkdistlspEAYRQQVSYSVQTPSLfdstvydnllfpwqirhktp 112
Cdd:cd03222   25 GEVIGIVGPNGTGKTTAVKILAGQLIPNGDND------------EWDGITPVYKPQYIDL-------------------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 113 dperfsadlarfnlppdtltksvselSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVL 192
Cdd:cd03222   73 --------------------------SGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKKTAL 126

                        170
                 ....*....|....*.
gi 504695722 193 WVTHDANEITHADDVL 208
Cdd:cd03222  127 VVEHDLAVLDYLSDRI 142
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
8-206 1.45e-06

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 47.87  E-value: 1.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   8 LTIEdvgYRT--GGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASL----LTPTSGKIFFEGKDISTLSPEAYRQ 81
Cdd:PRK15093   9 LTIE---FKTsdGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVtkdnWRVTADRMRFDDIDLLRLSPRERRK 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  82 QVSYSV----QTP-SLFDST--VYDNLL---------------FPWQIRhktpdpeRFSADLARFNL--PPDTLTKSVSE 137
Cdd:PRK15093  86 LVGHNVsmifQEPqSCLDPSerVGRQLMqnipgwtykgrwwqrFGWRKR-------RAIELLHRVGIkdHKDAMRSFPYE 158

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722 138 LSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLWVTHDANEITHADD 206
Cdd:PRK15093 159 LTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWAD 227
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
26-201 1.65e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 47.98  E-value: 1.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  26 VSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSP-EAYRQQVSYS---------VQTPSlfds 95
Cdd:PRK11288 272 ISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPIDIRSPrDAIRAGIMLCpedrkaegiIPVHS---- 347

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  96 tVYDNLlfpwQI---RHKTP-----DP--ERFSAD--LARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDE 163
Cdd:PRK11288 348 -VADNI----NIsarRHHLRagcliNNrwEAENADrfIRSLNIKTPSREQLIMNLSGGNQQKAILGRWLSEDMKVILLDE 422

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 504695722 164 ITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDANEI 201
Cdd:PRK11288 423 PTRGIDVGAKHEIYNVIYE-LAAQGVAVLFVSSDLPEV 459
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 130-215 4.08e-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: 46.93  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  130 TLTKSVSELSGGEKQRVSLIRNLQFL---PKVLLLDEITSAL--DDANKrnVNEIIHRYVREQNIAVLwVTHDANEITHA 204
Cdd:TIGR00630 822 RLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLhfDDIKK--LLEVLQRLVDKGNTVVV-IEHNLDVIKTA 898

                          90
                  ....*....|.
gi 504695722  205 DDVLTLQPHGG 215
Cdd:TIGR00630 899 DYIIDLGPEGG 909
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 16-171 6.13e-06

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 46.32  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  16 RTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEG--------KDISTLSPEA--------- 78
Cdd:PRK10636  10 RRGVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGnwqlawvnQETPALPQPAleyvidgdr 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  79 -YRQQVSYSVQTPSLFD----STVYDNL--LFPWQIRhktpdpERFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRN 151
Cdd:PRK10636  90 eYRQLEAQLHDANERNDghaiATIHGKLdaIDAWTIR------SRAASLLHGLGFSNEQLERPVSDFSGGWRMRLNLAQA 163

                        170       180
                 ....*....|....*....|.
gi 504695722 152 LQFLPKVLLLDEITSALD-DA 171
Cdd:PRK10636 164 LICRSDLLLLDEPTNHLDlDA 184
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 23-201 9.67e-06

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 45.65  E-value: 9.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  23 LNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPTSGKIFFEGKDISTLSPEAYRQQVS--YSVQTPSLFDStvydn 100
Cdd:PRK13545  40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISSGLNGQLTgiENIELKGLMMG----- 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 101 lLFPWQIRHKTPDPERFsADLARFnlppdtLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEII 180
Cdd:PRK13545 115 -LTKEKIKEIIPEIIEF-ADIGKF------IYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCLDKM 186

                        170       180
                 ....*....|....*....|.
gi 504695722 181 HRYvREQNIAVLWVTHDANEI 201
Cdd:PRK13545 187 NEF-KEQGKTIFFISHSLSQV 206
AAA_29 pfam13555
P-loop containing region of AAA domain;
24-66 1.51e-05

P-loop containing region of AAA domain;


Pssm-ID: 433304 [Multi-domain]  Cd Length: 61  Bit Score: 41.43  E-value: 1.51e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 504695722   24 NNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPtSGKIFF 66
Cdd:pfam13555  13 DGHTIPIDPRGNTLLTGPSGSGKSTLLDAIQTLLVP-AKRARF 54
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 12-169 1.98e-05

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 45.10  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    12 DVGYRTGGTTILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTP---TSGKIF--FEGKDISTLSPEAYRQQvsys 86
Cdd:TIGR00956  768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLvnGRPLDSSFQRSIGYVQQ---- 843

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722    87 vQTPSLFDSTVYDNLLFPWQIRH--KTPDPERFS-----ADLARFNLPPDTLTKSVSE-LSGGEKQRVSLIRNLQFLPKV 158
Cdd:TIGR00956  844 -QDLHLPTSTVRESLRFSAYLRQpkSVSKSEKMEyveevIKLLEMESYADAVVGVPGEgLNVEQRKRLTIGVELVAKPKL 922

                          170
                   ....*....|..
gi 504695722   159 LL-LDEITSALD 169
Cdd:TIGR00956  923 LLfLDEPTSGLD 934
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 130-215 2.08e-05

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: 44.14  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 130 TLTKSVSELSGGEKQRVSLIRNLQFL---PKVLLLDEITSALDDANKRNVNEIIHRYVREQNiAVLWVTHDANEITHADD 206
Cdd:cd03271  162 KLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIKCADW 240


                 ....*....
gi 504695722 207 VLTLQPHGG 215
Cdd:cd03271  241 IIDLGPEGG 249
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
138-216 9.74e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 9.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 138 LSGGEkqRVSLirNLQF-----LPKV-----LLLDEITSALDDANKRNVNEIIHRYVRE--QniaVLWVTHDANEITHAD 205
Cdd:PRK03918 789 LSGGE--RIAL--GLAFrlalsLYLAgniplLILDEPTPFLDEERRRKLVDIMERYLRKipQ---VIIVSHDEELKDAAD 861

                         90
                 ....*....|.
gi 504695722 206 DVLTLQPHGGK 216
Cdd:PRK03918 862 YVIRVSLEGGV 872
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 121-215 1.15e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.89  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  121 LARFNLPPDTLTKSVSELSGGEKQRVSLIRNL--QFLPKVLLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHDA 198
Cdd:PRK00635  460 LIDLGLPYLTPERALATLSGGEQERTALAKHLgaELIGITYILDEPSIGLHPQDTHKLINVIKK-LRDQGNTVLLVEHDE 538

                          90
                  ....*....|....*..
gi 504695722  199 NEITHADDVLTLQPHGG 215
Cdd:PRK00635  539 QMISLADRIIDIGPGAG 555
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 37-208 1.18e-04

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: 41.44  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  37 LITGPSGCGKSTLLKIIASLLT----PTSGKIFFEGKDISTLSPEAY-------RQQVSYSV-QTPSLFDSTVYdnllfp 104
Cdd:cd03240   26 LIVGQNGAGKTTIIEALKYALTgelpPNSKGGAHDPKLIREGEVRAQvklafenANGKKYTItRSLAILENVIF------ 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 105 wqIRHktpdpERFSADLARfnlPPDTLtksvselSGGEKQRVSLIRNL---QFLP---KVLLLDEITSALDDANKRNV-N 177
Cdd:cd03240  100 --CHQ-----GESNWPLLD---MRGRC-------SGGEKVLASLIIRLalaETFGsncGILALDEPTTNLDEENIEESlA 162

                        170       180       190
                 ....*....|....*....|....*....|.
gi 504695722 178 EIIHRYVREQNIAVLWVTHDANEITHADDVL 208
Cdd:cd03240  163 EIIEERKSQKNFQLIVITHDEELVDAADHIY 193
PLN03073 PLN03073
ABC transporter F family; Provisional
 116-169 1.37e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 42.54  E-value: 1.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504695722 116 RFSADLARFNLPPDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALD 169
Cdd:PLN03073 323 RAASILAGLSFTPEMQVKATKTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 131-216 1.70e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.12  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  131 LTKSVSELSGGEKQRVSLIRNLQFLPK---VLLLDEITSALDDANKRNVNEIIHRYVrEQNIAVLWVTHDANEITHADDV 207
Cdd:PRK00635 1693 LGQNLSSLSLSEKIAIKIAKFLYLPPKhptLFLLDEIATSLDNQQKSALLVQLRTLV-SLGHSVIYIDHDPALLKQADYL 1771


                  ....*....
gi 504695722  208 LTLQPHGGK 216
Cdd:PRK00635 1772 IEMGPGSGK 1780
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 130-215 3.67e-04

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


Pssm-ID: 273184 [Multi-domain]  Cd Length: 925  Bit Score: 41.15  E-value: 3.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  130 TLTKSVSELSGGEKQRVSLIRNL-QFLPKVL-LLDEITSALDDA-NKRNVNEIIHryVREQNIAVLWVTHDANEITHADD 206
Cdd:TIGR00630 481 SLSRAAGTLSGGEAQRIRLATQIgSGLTGVLyVLDEPSIGLHQRdNRRLINTLKR--LRDLGNTLIVVEHDEDTIRAADY 558

                          90
                  ....*....|...
gi 504695722  207 VLTLQP----HGG 215
Cdd:TIGR00630 559 VIDIGPgageHGG 571
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-219 3.81e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   127 PPDTLTKSVSELSGGEKQRVSL-----IRNLQFLPKVLLlDEITSALDDANKRNVNEIIHRYVRE-QNIAvlwVTHdaNE 200
Cdd:TIGR02168 1079 PPGKKNQNLSLLSGGEKALTALallfaIFKVKPAPFCIL-DEVDAPLDDANVERFANLLKEFSKNtQFIV---ITH--NK 1152

                           90       100
                   ....*....|....*....|.
gi 504695722   201 IT--HADdvltlQPHGGKMQE 219
Cdd:TIGR02168 1153 GTmeVAD-----QLYGVTMQE 1168
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 37-67 5.73e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 40.26  E-value: 5.73e-04
                         10        20        30
                 ....*....|....*....|....*....|.
gi 504695722  37 LItGPSGCGKSTLLKIIASLLTPTSGKIFFE 67
Cdd:PRK15064  32 LI-GANGCGKSTFMKILGGDLEPSAGNVSLD 61
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
37-65 6.15e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 6.15e-04
                          10        20
                  ....*....|....*....|....*....
gi 504695722   37 LITGPSGCGKSTLLKIIASLLTPTSGKIF 65
Cdd:COG4913    28 LLTGDNGSGKSTLLDAIQTLLVPAKRPRF 56
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 131-215 6.62e-04

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 40.58  E-value: 6.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  131 LTKSVSELSGGEKQRVSLIRNLQFL---PKVLLLDEITSALddaNKRNVNEIIH--RYVREQNIAVLWVTHDANEITHAD 205
Cdd:PRK00635  803 LGRPLSSLSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGL---HTHDIKALIYvlQSLTHQGHTVVIIEHNMHVVKVAD 879

                          90
                  ....*....|
gi 504695722  206 DVLTLQPHGG 215
Cdd:PRK00635  880 YVLELGPEGG 889
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 32-59 7.17e-04

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 40.32  E-value: 7.17e-04
                          10        20
                  ....*....|....*....|....*...
gi 504695722   32 PGEFRLITGPSGCGKSTLLKIIASLLTP 59
Cdd:TIGR00602 109 PKRILLITGPSGCGKSTTIKILSKELGI 136
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 127-183 8.76e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.95  E-value: 8.76e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504695722   127 PPDTLTKSVSELSGGEKQRV--SLIRNLQ-FLPKVL-LLDEITSALDDANKRNVNEIIHRY 183
Cdd:pfam02463 1067 PPGKGVKNLDLLSGGEKTLValALIFAIQkYKPAPFyLLDEIDAALDDQNVSRVANLLKEL 1127
ABC_SMC_barmotin cd03278
ATP-binding cassette domain of barmotin, a member of the SMC protein family; Barmotin is a ...
 132-202 1.00e-03

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


Pssm-ID: 213245 [Multi-domain]  Cd Length: 197  Bit Score: 38.60  E-value: 1.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504695722 132 TKSVSELSGGEKQ--RVSLIRNLQFL---PKVLLlDEITSALDDANKRNVNEIIHRYVREQNIAVlwVTHdaNEIT 202
Cdd:cd03278  108 VQRLSLLSGGEKAltALALLFAIFRVrpsPFCVL-DEVDAALDDANVERFARLLKEFSKETQFIV--ITH--RKGT 178
Rad17 pfam03215
Rad17 P-loop domain;
20-59 1.06e-03

Rad17 P-loop domain;


Pssm-ID: 367398 [Multi-domain]  Cd Length: 186  Bit Score: 38.79  E-value: 1.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 504695722   20 TTILNNVSFSLLpgefrLITGPSGCGKSTLLKIIASLLTP 59
Cdd:pfam03215  37 AMFLENAKHRIL-----LISGPSGCGKSTVIKELSKELGP 71
PLN03140 PLN03140
ABC transporter G family member; Provisional
 21-192 1.09e-03

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 39.83  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   21 TILNNVSFSLLPGEFRLITGPSGCGKSTLLKIIASLLTPT---SGKIFFEGKDISTLSPE---AYRQQVS-----YSVQT 89
Cdd:PLN03140  179 TILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLNEFVPRktsAYISQNDvhvgvMTVKE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   90 PSLFDS------TVYDnLLFPWQIRHKT----PDPE-------------------RFSADLARFNLPPDTLT--KSVSEL 138
Cdd:PLN03140  259 TLDFSArcqgvgTRYD-LLSELARREKDagifPEAEvdlfmkatamegvksslitDYTLKILGLDICKDTIVgdEMIRGI 337

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 504695722  139 SGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVL 192
Cdd:PLN03140  338 SGGQKKRVTTGEMIVGPTKTLFMDEISTGLDSSTTYQIVKCLQQIVHLTEATVL 391
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 26-197 1.36e-03

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


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 38.40  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722  26 VSFSLLPG-EFRLITGPSGCGKSTLLKIIASLL---TPTSGKiffEGKDISTLSPEAYRQQVSysvqtpslfdstvydnl 101
Cdd:cd03279   20 IDFTGLDNnGLFLICGPTGAGKSTILDAITYALygkTPRYGR---QENLRSVFAPGEDTAEVS----------------- 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 102 lFPWQIRHKTPDPERfsadlaRFNLPPDT---------------LTKSVSELSGGEKQRVS------LIRNLQFLPKV-- 158
Cdd:cd03279   80 -FTFQLGGKKYRVER------SRGLDYDQftrivllpqgefdrfLARPVSTLSGGETFLASlslalaLSEVLQNRGGArl 152

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 504695722 159 --LLLDEITSALDDANKRNVNEIIHRyVREQNIAVLWVTHD 197
Cdd:cd03279  153 eaLFIDEGFGTLDPEALEAVATALEL-IRTENRMVGVISHV 192
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
 37-164 1.74e-03

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


Pssm-ID: 433025 [Multi-domain]  Cd Length: 167  Bit Score: 37.87  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722   37 LITGPSGCGKSTLLKIIASLLTPtSGKIFFEGKDISTLSPEAYRQQVSYSVQTPSLFDstvydnllfpwqiRHKTPDPER 116
Cdd:pfam13191  28 LLTGEAGTGKTTLLRELLRALER-DGGYFLRGKCDENLPYSPLLEALTREGLLRQLLD-------------ELESSLLEA 93

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 504695722  117 FSADLarfnlppDTLTKSVSELSGGEKQRV--SLIRNLQFLPK-----VLLLDEI 164
Cdd:pfam13191  94 WRAAL-------LEALAPVPELPGDLAERLldLLLRLLDLLARgerplVLVLDDL 141
ABC_SMC2_euk cd03273
ATP-binding cassette domain of eukaryotic SMC2 proteins; The structural maintenance of ...
 133-182 1.97e-03

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


Pssm-ID: 213240 [Multi-domain]  Cd Length: 251  Bit Score: 38.43  E-value: 1.97e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504695722 133 KSVSELSGGEKQRV--SLIRN-LQFLPKVL-LLDEITSALDDANKRNVNEIIHR 182
Cdd:cd03273  162 ESLTELSGGQRSLValSLILAlLLFKPAPMyILDEVDAALDLSHTQNIGRMIKT 215
XRCC2 cd19490
XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells ...
 38-72 2.75e-03

XRCC2 recombinase; XRCC2 (X-ray repair complementing defective repair in Chinese hamster cells 2) recombinase, a RAD51 paralog, plays an important role in DNA repair by homologous recombination (HR). HR is an important error-free repair mechanism for chromosomal double-strand break (DSB) which otherwise leads to cell cycle arrest and death. XRCC2, together with the other RAD51 paralogs, RAD51B, RAD51C, RAD51D, and XRCC3, helps recruit RAD51 to the break site.


Pssm-ID: 410898 [Multi-domain]  Cd Length: 226  Bit Score: 37.71  E-value: 2.75e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 504695722  38 ITGPSGCGKSTLL-KIIASLLTPTS-GKIFFEGKDIS 72
Cdd:cd19490    6 ITGPSGSGKTELLyHLAARCILPSSwGGVPLGGLEAA 42
Twinkle_C cd01122
C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid ...
 21-50 3.58e-03

C-terminal domain of Twinkle; Twinkle ( T7 gp4-like protein with intramitochondrial nucleoid localization, also known as C10orf2, PEO1, SCA8, ATXN8, IOSCA, PEOA3 or SANDO) is a homohexameric DNA helicases which unwinds short stretches of double-stranded DNA in the 5' to 3' direction and, along with mitochondrial single-stranded DNA binding protein and mtDNA polymerase gamma, is thought to play a key role in mtDNA replication. Mutations in the human gene cause infantile onset spinocerebellar ataxia (IOSCA) and progressive external ophthalmoplegia (PEO) and are also associated with several mitochondrial depletion syndromes. This group also contains viral GP4-like and related bacterial helicases.


Pssm-ID: 410867  Cd Length: 266  Bit Score: 37.60  E-value: 3.58e-03
                         10        20        30
                 ....*....|....*....|....*....|
gi 504695722  21 TILNNVSFSLLPGEFRLITGPSGCGKSTLL 50
Cdd:cd01122   31 PSLNKLLKGHRRGELTIFTGPTGSGKTTFL 60
RNA_helicase pfam00910
RNA helicase; This family includes RNA helicases thought to be involved in duplex unwinding ...
 37-82 3.93e-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: 3.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 504695722   37 LITGPSGCGKSTLLKIIASLLTPTSGkifFEGKDISTLSPE-----AYRQQ 82
Cdd:pfam00910   2 WLYGPPGCGKSTLAKYLARALLKKLG---LPKDSVYSRNPDddfwdGYTGQ 49
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
116-203 4.08e-03

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 37.79  E-value: 4.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504695722 116 RFSAD--LARFNLPpDTLTKSVSELSGGEKQRVSLIRNLQFLPKVLLLDEITSALDDANKRNVNEIIHRYVREQNIAVLW 193
Cdd:NF000106 122 RARADelLERFSLT-EAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLT 200

                         90
                 ....*....|..
gi 504695722 194 VTH--DANEITH 203
Cdd:NF000106 201 TQYmeEAEQLAH 212
GntK cd02021
Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting ...
 37-71 4.41e-03

Gluconate kinase (GntK) catalyzes the phosphoryl transfer from ATP to gluconate. The resulting product gluconate-6-phoshate is an important precursor of gluconate metabolism. GntK acts as a dimmer composed of two identical subunits.


Pssm-ID: 238979 [Multi-domain]  Cd Length: 150  Bit Score: 36.46  E-value: 4.41e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 504695722  37 LITGPSGCGKSTLLKIIASLLtptsGKIFFEGKDI 71
Cdd:cd02021    3 VVMGVSGSGKSTVGKALAERL----GAPFIDGDDL 33
ATPase_2 pfam01637
ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is ...
 32-57 5.84e-03

ATPase domain predominantly from Archaea; This family contain a conserved P-loop motif that is involved in binding ATP. There are eukaryote members as well as archaeal members in this family.


Pssm-ID: 376582 [Multi-domain]  Cd Length: 222  Bit Score: 36.53  E-value: 5.84e-03
                          10        20
                  ....*....|....*....|....*.
gi 504695722   32 PGEFRLITGPSGCGKSTLLKIIASLL 57
Cdd:pfam01637  19 PNLIYVIYGPEGCGKTALLRESIENL 44
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 37-65 6.76e-03

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 35.97  E-value: 6.76e-03
                         10        20
                 ....*....|....*....|....*....
gi 504695722  37 LITGPSGCGKSTLLKIIASLLTPTSGKIF 65
Cdd:cd00009   23 LLYGPPGTGKTTLARAIANELFRPGAPFL 51
ABC_SMC4_euk cd03274
ATP-binding cassette domain of eukaryotic SMC4 proteins; The structural maintenance of ...
 133-187 8.00e-03

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


Pssm-ID: 213241 [Multi-domain]  Cd Length: 212  Bit Score: 36.12  E-value: 8.00e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 504695722 133 KSVSELSGGEKQRVS--LIRNL-QFLPKVL-LLDEITSALDdanKRNVNeIIHRYVREQ 187
Cdd:cd03274  123 KNISNLSGGEKTLSSlaLVFALhHYKPTPLyVMDEIDAALD---FRNVS-IVANYIKER 177
NK cd02019
Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of ...
 37-61 8.42e-03

Nucleoside/nucleotide kinase (NK) is a protein superfamily consisting of multiple families of enzymes that share structural similarity and are functionally related to the catalysis of the reversible phosphate group transfer from nucleoside triphosphates to nucleosides/nucleotides, nucleoside monophosphates, or sugars. Members of this family play a wide variety of essential roles in nucleotide metabolism, the biosynthesis of coenzymes and aromatic compounds, as well as the metabolism of sugar and sulfate.


Pssm-ID: 238977 [Multi-domain]  Cd Length: 69  Bit Score: 33.85  E-value: 8.42e-03
                         10        20
                 ....*....|....*....|....*
gi 504695722  37 LITGPSGCGKSTLLKIIASLLTPTS 61
Cdd:cd02019    3 AITGGSGSGKSTVAKKLAEQLGGRS 27
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 16-49 8.44e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 37.12  E-value: 8.44e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 504695722   16 RTGGTTI--LNNVSFSLLPGEFRLITGPSGCGKSTL 49
Cdd:PRK00635    7 RLSGITVrnLKNISIEFCPREIVLLTGVSGSGKSSL 42
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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