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Conserved domains on  [gi|495112432|ref|WP_007837252|]
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ABC transporter ATP-binding protein [Phocaeicola dorei]

Protein Classification

ABC transporter ATP-binding protein( domain architecture ID 11438980)

ABC transporter ATP-binding protein is the ATPase catalytic subunit of an ABC transporter complex responsible for coupling the energy of ATP hydrolysis to the transport of one or more from a variety of substrates including hemin, bacitracin, and lipoproteins

CATH:  3.40.50.300
EC:  7.6.2.-
SCOP:  4003976
TCDB:  3.A.1

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-222 1.54e-132

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


:

Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 371.68  E-value: 1.54e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG1136    3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:COG1136   83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:COG1136  163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
 
Name Accession Description Interval E-value
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-222 1.54e-132

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 371.68  E-value: 1.54e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG1136    3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:COG1136   83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:COG1136  163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
4-220 5.55e-119

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: 337.15  E-value: 5.55e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03255    1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
3-220 3.85e-80

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 238.79  E-value: 3.85e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02211   1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   83 RNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02211  81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432  163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
2-222 2.70e-67

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 218.05  E-value: 2.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:PRK10535   3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK10535  83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
3-223 3.84e-44

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 151.00  E-value: 3.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTneietLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELAAF 82
Cdd:NF040840   1 MIRIENLSKDWKE-----FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDG------KDITNLPP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:NF040840  70 EKRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLAdRVGIMLNGRLSQ 211
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
23-171 1.18e-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: 141.25  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGtsvESMKDKELAAFRnKTLGFVFQSFHLINSLN 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKlIAGLLS-PTEGTILLDG---QDLTDDERKSLR-KEIGYVFQDPQLFPRLT 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432  102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH----RMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:pfam00005  76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
22-216 1.43e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 111.17  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGtsvesmkdkelaafrNKTLGFVFQSFHLINSL 100
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKvLAGVL-RPTSGTVRRAG---------------GARVAYVPQRSEVPDSL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 --NVIDNVELPL-----LYRKMAAKERTRLAkEVLERVGLsHRMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:NF040873  71 plTVRDLVAMGRwarrgLWRRLTRDDRAAVD-DALERVGL-ADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 173 NLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:NF040873 149 GLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
22-204 1.50e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 83.64  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDApSSGKIEINGTSVESmkdKELAAFRNktLGFVFQSFHLINSL 100
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLPA-SEGEAWLFGQPVDA---GDIATRRR--VGYMSQAFSLYGEL 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVEL-PLLYRkMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSkmG 179
Cdd:NF033858 355 TVRQNLELhARLFH-LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP--V 431
                        170       180
                 ....*....|....*....|....*....
gi 495112432 180 AEVM--ELLHKLNKEDGRTIVMVTH--NE 204
Cdd:NF033858 432 ARDMfwRLLIELSREDGVTIFISTHfmNE 460
GguA NF040905
sugar ABC transporter ATP-binding protein;
22-204 9.65e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 60.57  E-value: 9.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-SGKIEINGtsvesmkdkELAAFRN----KTLGFVF--QS 93
Cdd:NF040905  16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPHGSyEGEILFDG---------EVCRFKDirdsEALGIVIihQE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 FHLINSLNVIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:NF040905  87 LALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 171 TGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH--NE 204
Cdd:NF040905 167 TAALNEEDSAALLDLLLEL-KAQGITSIIISHklNE 201
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
115-222 1.04e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 57.44  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 115 MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKeDG 194
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DG 194
                         90       100
                 ....*....|....*....|....*....
gi 495112432 195 RTIVMVTHNEEQAKQTSRTIRFFD-GRQV 222
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDrGRVI 223
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
32-222 1.41e-08

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: 51.99  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    32 KGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGfvfqsfhlinslnvidnvelpl 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   111 lyrkmaakertrlakevlervglshrmrhmpTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMEL----L 186
Cdd:smart00382  59 -------------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrL 107
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 495112432   187 HKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-171 1.90e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.12  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDkelAAFR 83
Cdd:NF033858   2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMAD---ARHR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKT----------LGfvfqsFHLINSLNVIDNVELpllyrkMA------AKERTRLAKEVLERVGLsHRMRHMPT-QLSG 146
Cdd:NF033858  72 RAVcpriaympqgLG-----KNLYPTLSVFENLDF------FGrlfgqdAAERRRRIDELLRATGL-APFADRPAgKLSG 139
                        170       180
                 ....*....|....*....|....*
gi 495112432 147 GQCQRVAIARAIVGNPEIILADEPT 171
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPT 164
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-200 3.25e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLlnimglldAPS----------SGKIEINGTSVE--SMKDkelaAFRN------ 84
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL--------AMSvfgrsygrniSGTVFKDGKEVDvsTVSD----AIDAglayvt 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  85 ---KTLGFVFQ----------SFHLINSLNVIDNVElpllYRKMAAKERTRL---AKEVLERVGlshrmrhmptQLSGGQ 148
Cdd:NF040905 344 edrKGYGLNLIddikrnitlaNLGKVSRRGVIDENE----EIKVAEEYRKKMnikTPSVFQKVG----------NLSGGN 409
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495112432 149 CQRVAIARAIVGNPEIILADEPTGNLDskMGA--EVMELLHKLNKEdGRTIVMV 200
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGID--VGAkyEIYTIINELAAE-GKGVIVI 460
 
Name Accession Description Interval E-value
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
2-222 1.54e-132

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 371.68  E-value: 1.54e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG1136    3 PLLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELAR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:COG1136   83 LRRRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNR 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:COG1136  163 PKLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPELAARADRVIRLRDGRIV 223
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
4-220 5.55e-119

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: 337.15  E-value: 5.55e-119
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03255    1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03255   81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03255  161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELAEYADRIIELRDGK 217
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
2-223 3.66e-91

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: 267.38  E-value: 3.66e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG4181    7 PIIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARAR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMA-AKERtrlAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG4181   87 LRARHVGFVFQSFQLLPTLTALENVMLPLELAGRRdARAR---ARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFAT 163
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG4181  164 EPAILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAARCDRVLRLRAGRLVE 226
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
3-220 5.76e-90

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 263.84  E-value: 5.76e-90
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:COG2884    1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:COG2884   78 RRR-IGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQT-SRTIRFFDGR 220
Cdd:COG2884  157 ELLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMpKRVLELEDGR 214
LolD_lipo_ex TIGR02211
lipoprotein releasing system, ATP-binding protein; This model represents LolD, a member of the ...
3-220 3.85e-80

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


Pssm-ID: 131266 [Multi-domain]  Cd Length: 221  Bit Score: 238.79  E-value: 3.85e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02211   1 LLKCENLGKRYQEGKLDTRVLKGVSLSIGKGEIVAIVGSSGSGKSTLLHLLGGLDNPTSGEVLFNGQSLSKLSSNERAKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   83 RNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02211  81 RNKKLGFIYQFHHLLPDFTALENVAMPLLIGKKSVKEAKERAYEMLEKVGLEHRINHRPSELSGGERQRVAIARALVNQP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432  163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR02211 161 SLVLADEPTGNLDNNNAKIIFDLMLELNRELNTSFLVVTHDLELAKKLDRVLEMKDGQ 218
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-205 6.12e-79

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 237.30  E-value: 6.12e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkela 80
Cdd:COG1116    5 APALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTG------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG1116   78 --PGPDRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALAN 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EE 205
Cdd:COG1116  156 DPEVLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHDvDE 201
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
6-215 5.00e-77

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


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 230.58  E-value: 5.00e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNK 85
Cdd:TIGR03608   1 LKNISKKFGDKVI----LDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKKASKFRRE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   86 TLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:TIGR03608  77 KLGYLFQNFALIENETVEENLDLGLKYKKLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLI 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 495112432  166 LADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTSRTIR 215
Cdd:TIGR03608 157 LADEPTGSLDPKNRDEVLDLLLELNDE-GKTIIIVTHDPEVAKQADRVIE 205
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
3-219 1.45e-76

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 230.27  E-value: 1.45e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELAAF 82
Cdd:COG1126    1 MIEIENLHKSFGDLEV----LKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDL-TDSKKDINKL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKTlGFVFQSFHLINSLNVIDNVELPLLY-RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:COG1126   76 RRKV-GMVFQQFNLFPHLTVLENVTLAPIKvKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAME 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:COG1126  155 PKVMLFDEPTSALDPELVGEVLDVMRDL-AKEGMTMVVVTHEMGFAREVADRVVFMDG 211
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
4-207 6.81e-75

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: 225.43  E-value: 6.81e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkelaafR 83
Cdd:cd03293    1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTG---------P 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03293   72 GPDRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03293  152 VLLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEA 195
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
2-218 1.31e-74

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 225.71  E-value: 1.31e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG3638    1 PMLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTlGFVFQSFHLINSLNVIDNVELPLLYR--------KMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVA 153
Cdd:COG3638   78 LRRRI-GMIFQQFNLVPRLSVLTNVLAGRLGRtstwrsllGLFPPEDRERALEALERVGLADKAYQRADQLSGGQQQRVA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKqtsrtiRFFD 218
Cdd:COG3638  157 IARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLAR------RYAD 215
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
3-209 1.21e-73

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: 222.84  E-value: 1.21e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:cd03258    1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03258   81 RRR-IGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ 209
Cdd:cd03258  160 KVLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKR 206
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
3-202 1.37e-73

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 226.11  E-value: 1.37e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:COG1135    1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:COG1135   81 R-RKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:COG1135  160 KVLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITH 199
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
2-223 1.88e-71

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: 217.54  E-value: 1.88e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:COG1127    4 PMIEVRNLTKSFGDRVV----LDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKtLGFVFQSFHLINSLNVIDNVELPLL-YRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG1127   80 LRRR-IGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALAL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG1127  159 DPEILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKII 221
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
3-220 2.05e-71

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


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 216.35  E-value: 2.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02673   1 MIEFHNVSKAYPGG---VAALHDVSLHIRKGEFLFLTGPSGAGKTTLLKLLYGALTPSRGQVRIAGEDVNRLRGRQLPLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02673  78 RRR-IGVVFQDFRLLPDRTVYENVALPLEVRGKKEREIQRRVGAALRQVGLEHKADAFPEQLSGGEQQRVAIARAIVNSP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432  163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:TIGR02673 157 PLLLADEPTGNLDPDLSERILDLLKRLNKR-GTTVIVATHDLSLVDRVAhRVIILDDGR 214
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
4-220 1.22e-68

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: 210.05  E-value: 1.22e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03261    1 IELRGLTKSFGGRTV----LKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTlGFVFQSFHLINSLNVIDNVELPLL-YRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03261   77 RRM-GMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDP 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03261  156 ELLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIAdRIAVLYDGK 214
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-207 2.06e-68

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 213.42  E-value: 2.06e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelA 80
Cdd:COG3842    3 MPALELENVSKRYG----DVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLP----P 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG3842   75 EKRN--VGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAP 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG3842  153 EPRVLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQEEA 199
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
2-222 2.70e-67

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 218.05  E-value: 2.70e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAA 81
Cdd:PRK10535   3 ALLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK10535  83 LRREHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNG 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK10535 163 GQVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQAERVIEIRDGEIV 222
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-207 2.98e-65

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 205.31  E-value: 2.98e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKEla 80
Cdd:COG3839    1 MASLELENVSKSYGGVE----ALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afRNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG3839   75 --RN--IAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVR 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG3839  151 EPKVFLLDEPLSNLDAKLRVEMRAEIKRLHRRLGTTTIYVTHDQVEA 197
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
4-219 4.65e-64

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: 197.75  E-value: 4.65e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmKDKELAAFR 83
Cdd:cd03262    1 IEIKNLHKSFGDFHV----LKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTlGFVFQSFHLINSLNVIDNVELPLLY-RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03262   76 QKV-GMVFQQFNLFPHLTVLENITLAPIKvKGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNP 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03262  155 KVMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDD 210
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
4-220 7.60e-64

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: 197.25  E-value: 7.60e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03292    1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03292   78 RK-IGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPT 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03292  157 ILIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRhRVIALERGK 213
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
4-223 9.82e-64

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: 196.97  E-value: 9.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafR 83
Cdd:cd03259    1 LELKGLSKTYG----SVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPER----R 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03259   73 N--IGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPS 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQVQ 223
Cdd:cd03259  151 LLLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMnEGRIVQ 211
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
23-220 2.69e-63

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 196.54  E-value: 2.69e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINSLNV 102
Cdd:PRK10584  26 LTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKLRAKHVGFVFQSFMLIPTLNA 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEV 182
Cdd:PRK10584 106 LENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLDRQTGDKI 185
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 183 MELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK10584 186 ADLLFSLNREHGTTLILVTHDLQLAARCDRRLRLVNGQ 223
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
3-222 1.78e-62

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: 202.83  E-value: 1.78e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETL-ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELA 80
Cdd:COG1123  260 LLEVRNLSKRYPVRGKGGVrAVDDVSLTLRRGETLGLVGESGSGKSTLARlLLGLLR-PTSGSILFDGKDLTKLSRRSLR 338
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRnKTLGFVFQS-FHLIN-SLNVIDNVELPL-LYRKMAAKERTRLAKEVLERVGLSHRMRH-MPTQLSGGQCQRVAIAR 156
Cdd:COG1123  339 ELR-RRVQMVFQDpYSSLNpRMTVGDIIAEPLrLHGLLSRAERRERVAELLERVGLPPDLADrYPHELSGGQRQRVAIAR 417
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQV 222
Cdd:COG1123  418 ALALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIAdRVAVMYDGRIV 484
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
3-220 2.11e-62

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: 193.88  E-value: 2.11e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAA 81
Cdd:cd03257    1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARaILGLL-KPTSGSIIFDGKDLLKLSRRLRKI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKtLGFVFQsfHLINSLN----VIDNVELPLLYRKMAAKERTRLAK--EVLERVGLSHRMRHM-PTQLSGGQCQRVAI 154
Cdd:cd03257   80 RRKE-IQMVFQ--DPMSSLNprmtIGEQIAEPLRIHGKLSKKEARKEAvlLLLVGVGLPEEVLNRyPHELSGGQRQRVAI 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03257  157 ARALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIAdRVAVMYAGK 223
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
11-220 2.15e-62

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 194.26  E-value: 2.15e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  11 KIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFV 90
Cdd:PRK11629  13 KRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQKLGFI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  91 FQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK11629  93 YQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEP 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK11629 173 TGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRMSRQLEMRDGR 222
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
4-220 5.16e-62

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


Pssm-ID: 274374 [Multi-domain]  Cd Length: 220  Bit Score: 192.93  E-value: 5.16e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    4 IKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:TIGR02982   2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   84 nKTLGFVFQSFHLINSLNVIDNVELPL-LYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:TIGR02982  82 -RRIGYIFQAHNLLGFLTARQNVQMALeLQPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHP 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432  163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR02982 161 KLVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHDNRILDVADRILQMEDGK 218
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
3-202 1.10e-61

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 195.79  E-value: 1.10e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:PRK11153   1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:PRK11153  81 RRQ-IGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNP 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11153 160 KVLLCDEATSALDPATTRSILELLKDINRELGLTIVLITH 199
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
4-222 1.11e-61

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: 192.78  E-value: 1.11e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFR 83
Cdd:cd03256    1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTlGFVFQSFHLINSLNVIDNVELPLLYRK--------MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIA 155
Cdd:cd03256   78 RQI-GMIFQQFNLIERLSVLENVLSGRLGRRstwrslfgLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:cd03256  157 RALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREyADRIVGLKDGRIV 224
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
13-220 3.96e-60

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: 187.67  E-value: 3.96e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQ 92
Cdd:cd03225    7 FSYPDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELR----RKVGLVFQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 -SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:cd03225   83 nPDDQFFGPTVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPT 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ-TSRTIRFFDGR 220
Cdd:cd03225  163 AGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLElADRVIVLEDGK 211
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
20-223 3.17e-59

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: 187.47  E-value: 3.17e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINS 99
Cdd:cd03294   37 TVGVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRRKKISMVFQSFALLPH 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:cd03294  117 RTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAFSALDPLIR 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQVQ 223
Cdd:cd03294  197 REMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMkDGRLVQ 241
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
19-222 3.62e-59

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


Pssm-ID: 440739 [Multi-domain]  Cd Length: 230  Bit Score: 186.00  E-value: 3.62e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVesmKDKELAAFRnKTLGFVFQ-SFHL 96
Cdd:COG1122   13 GTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLnGLL-KPTSGEVLVDGKDI---TKKNLRELR-RKVGLVFQnPDDQ 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 INSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:COG1122   88 LFAPTVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDP 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 177 KMGAEVMELLHKLNKEdGRTIVMVTHN-EEQAKQTSRTIRFFDGRQV 222
Cdd:COG1122  168 RGRRELLELLKRLNKE-GKTVIIVTHDlDLVAELADRVIVLDDGRIV 213
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
3-203 5.51e-59

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: 186.16  E-value: 5.51e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKelaAF 82
Cdd:COG1124    1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVTRRRRK---AF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RnKTLGFVFQsfHLINSLN----VIDNVELPL-LYRKMAAKERtrlAKEVLERVGLSHRMRHM-PTQLSGGQCQRVAIAR 156
Cdd:COG1124   78 R-RRVQMVFQ--DPYASLHprhtVDRILAEPLrIHGLPDREER---IAELLEQVGLPPSFLDRyPHQLSGGQRQRVAIAR 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG1124  152 ALILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHD 198
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
3-202 6.13e-59

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: 186.02  E-value: 6.13e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAa 81
Cdd:COG1120    1 MLEAENLSVGYGGRPV----LDDVSLSLPPGEVTALLGPNGSGKSTLLRaLAGLL-KPSSGEVLLDGRDLASLSRRELA- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 frnKTLGFVFQSFHLINSLNVIDNVEL---PLL--YRKMAAKERtRLAKEVLERVGLSH-RMRHMpTQLSGGQCQRVAIA 155
Cdd:COG1120   75 ---RRIAYVPQEPPAPFGLTVRELVALgryPHLglFGRPSAEDR-EAVEEALERTGLEHlADRPV-DELSGGERQRVLIA 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:COG1120  150 RALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLH 196
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
3-203 7.04e-59

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: 187.95  E-value: 7.04e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDAP--SSGKIEINGTSVESMKDKEL 79
Cdd:COG0444    1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLaRAILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 AAFRNKTLGFVFQSfhLINSLN----VIDNVELPLLY-RKMAAKERTRLAKEVLERVGLSHRMRHM---PTQLSGGQCQR 151
Cdd:COG0444   81 RKIRGREIQMIFQD--PMTSLNpvmtVGDQIAEPLRIhGGLSKAEARERAIELLERVGLPDPERRLdryPHELSGGMRQR 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG0444  159 VMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHD 210
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-207 2.26e-57

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 182.37  E-value: 2.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelA 80
Cdd:COG4525    1 MSMLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGP-----G 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRnktlGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG4525   76 ADR----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAA 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 495112432 161 NPEIILADEPTGNLDSkMGAEVM-ELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG4525  152 DPRFLLMDEPFGALDA-LTREQMqELLLDVWQRTGKGVFLITHSVEEA 198
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
3-222 3.28e-57

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


Pssm-ID: 131368 [Multi-domain]  Cd Length: 243  Bit Score: 181.34  E-value: 3.28e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:TIGR02315   1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   83 RNKTlGFVFQSFHLINSLNVIDNVELPLLYRK--------MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAI 154
Cdd:TIGR02315  78 RRRI-GMIFQHYNLIERLTVLENVLHGRLGYKptwrsllgRFSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432  155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKyADRIVGLKAGEIV 225
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
4-220 1.95e-55

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: 174.68  E-value: 1.95e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkDKELAAFR 83
Cdd:cd03229    1 LELKNVSKRYG----QKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDL-EDELPPLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTlGFVFQSFHLINSLNVIDNVELPLlyrkmaakertrlakevlervglshrmrhmptqlSGGQCQRVAIARAIVGNPE 163
Cdd:cd03229   76 RRI-GMVFQDFALFPHLTVLENIALGL----------------------------------SGGQQQRVALARALAMDPD 120
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:cd03229  121 VLLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLAdRVVVLRDGK 178
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
19-222 5.08e-55

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: 183.18  E-value: 5.08e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPS--SGKIEINGTSVESMKDKElaafRNKTLGFVFQSF- 94
Cdd:COG1123   18 DVPAVDGVSLTIAPGETVALVGESGSGKSTLALaLMGLLPHGGriSGEVLLDGRDLLELSEAL----RGRRIGMVFQDPm 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  95 HLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:COG1123   94 TQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTAL 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 495112432 175 DSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGRQV 222
Cdd:COG1123  174 DVTTQAEILDLLRELQRERGTTVLLITHDlGVVAEIADRVVVMDDGRIV 222
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
4-214 8.19e-55

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: 174.73  E-value: 8.19e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkeLAAFR 83
Cdd:cd03300    1 IELENVSKFYGG----FVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITN-----LPPHK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03300   72 -RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPK 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:cd03300  151 VLLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRI 201
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
23-220 3.93e-54

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 172.31  E-value: 3.93e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQSFHLINSlNV 102
Cdd:COG4619   16 LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMP---PPEWRRQ-VAYVPQEPALWGG-TV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVELPLLYRKMAAKERTrlAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:COG4619   91 RDNLPFPFQLRERKFDRER--ALELLERLGLPPDILDKPVeRLSGGERQRLALIRALLLQPDVLLLDEPTSALDPENTRR 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 182 VMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:COG4619  169 VEELLREYLAEEGRAVLWVSHDPEQIERVAdRVLTLEAGR 208
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
4-207 8.95e-54

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: 171.67  E-value: 8.95e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafR 83
Cdd:cd03301    1 VELENVTKRFG----NVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD----R 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03301   73 D--IAMVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPK 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03301  151 VFLMDEPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEA 194
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
4-223 4.06e-53

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: 170.44  E-value: 4.06e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLD----APSSGKIEINGTSVESmKDKE 78
Cdd:cd03260    1 IELRDLNVYYGDKH----ALKDISLDIPKGEITALIGPSGCGKSTLLRLLnRLNDlipgAPDEGEVLLDGKDIYD-LDVD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  79 LAAFRnKTLGFVFQSFHLINsLNVIDNVELPLLYRKMA-AKERTRLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIA 155
Cdd:cd03260   76 VLELR-RRVGMVFQKPNPFP-GSIYDNVAYGLRLHGIKlKEELDERVEEALRKAALWDEVkdRLHALGLSGGQQQRLCLA 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:cd03260  154 RALANEPEVLLLDEPTSALDPISTAKIEELIAELKKE--YTIVIVTHNMQQAARVAdRTAFLLNGRLVE 220
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
4-203 7.95e-53

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 169.86  E-value: 7.95e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVesmkDKELAAF 82
Cdd:COG1131    1 IEVRGLTKRYG----DKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRmLLGLL-RPTSGEVRVLGEDV----ARDPAEV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:COG1131   72 R-RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDP 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG1131  151 ELLILDEPTSGLDPEARRELWELLREL-AAEGKTVLLSTHY 190
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-203 1.39e-52

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 169.50  E-value: 1.39e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESmkdkel 79
Cdd:COG1121    4 MPAIELENLTVSYG----GRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKaILGLL-PPTSGTVRLFGKPPRR------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 aafRNKTLGFVFQSFHLINS--LNVIDNVELPLLYR----KMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVA 153
Cdd:COG1121   73 ---ARRRIGYVPQRAEVDWDfpITVRDVVLMGRYGRrglfRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:COG1121  150 LARALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHD 198
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
4-207 7.52e-52

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 170.71  E-value: 7.52e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDkelaAFR 83
Cdd:COG1118    3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNG------RD----LFT 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTL-----GFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI 158
Cdd:COG1118   69 NLPPrerrvGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARAL 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:COG1118  149 AVEPEVLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEA 197
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
4-223 8.27e-51

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 164.80  E-value: 8.27e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV---ESMKDKELA 80
Cdd:COG4161    3 IQLKNINCFYGSHQ----ALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKtLGFVFQSFHLINSLNVIDN-VELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:COG4161   79 LLRQK-VGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALM 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDGRQVQ 223
Cdd:COG4161  158 MEPQVLLFDEPTAALDPEITAQVVEIIREL-SQTGITQVIVTHEVEFARKVaSQVVYMEKGRIIE 221
PhnT2 TIGR03265
putative 2-aminoethylphosphonate ABC transporter, ATP-binding protein; This ABC transporter ...
1-207 2.39e-50

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


Pssm-ID: 274496 [Multi-domain]  Cd Length: 353  Bit Score: 167.14  E-value: 2.39e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    1 MAMIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELA 80
Cdd:TIGR03265   2 SPYLSIDNIRKRFGA----FTALKDISLSVKKGEFVCLLGPSGCGKTTLLRIIAGLERQTAGTIYQGG------RDITRL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   81 AFRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:TIGR03265  72 PPQKRDYGIVFQSYALFPNLTVADNIAYGLKNRGMGRAEVAERVAELLDLVGLPGSERKYPGQLSGGQQQRVALARALAT 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 495112432  161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:TIGR03265 152 SPGLLLLDEPLSALDARVREHLRTEIRQLQRRLGVTTIMVTHDQEEA 198
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
5-207 4.40e-50

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: 161.06  E-value: 4.40e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   5 KLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAafr 83
Cdd:cd03214    1 EVENLSVGYGGRTV----LDDLSLSIEAGEIVGILGPNGAGKSTLLKtLAGLL-KPSSGEILLDGKDLASLSPKELA--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nKTLGFVFQsfhlinslnvidnvelpllyrkmaakertrlakeVLERVGLSH-RMRHMpTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03214   73 -RKIAYVPQ----------------------------------ALELLGLAHlADRPF-NELSGGERQRVLLARALAQEP 116
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03214  117 PILLLDEPTSHLDIAHQIELLELLRRLARERGKTVVMVLHDLNLA 161
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
3-219 7.65e-50

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 162.57  E-value: 7.65e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:PRK09493   1 MIEFKNVSKHFGPTQV----LHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDERLIR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtlGFVFQSFHLINSLNVIDNVEL-PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK09493  77 QEA--GMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVK 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIrFFDG 219
Cdd:PRK09493 155 PKLMLFDEPTSALDPELRHEVLKVMQDL-AEEGMTMVIVTHEIGFAEKVaSRLI-FIDK 211
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
4-223 8.57e-49

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 159.79  E-value: 8.57e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV---ESMKDKELA 80
Cdd:PRK11124   3 IQLNGINCFYGAHQ----ALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKtLGFVFQSFHLINSLNVIDN-VELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK11124  79 ELRRN-VGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDGRQVQ 223
Cdd:PRK11124 158 MEPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTaSRVVYMENGHIVE 221
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
2-202 1.13e-48

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 159.97  E-value: 1.13e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKD----- 76
Cdd:COG4598    7 PALEVRDLHKSFGDLEV----LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDrdgel 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  77 -----KELAAFRNKtLGFVFQSFHLINSLNVIDNV-ELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQ 150
Cdd:COG4598   83 vpadrRQLQRIRTR-LGMVFQSFNLWSHMTVLENViEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQ 161
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:COG4598  162 RAAIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEE-GRTMLVVTH 212
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
4-220 1.03e-47

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: 157.59  E-value: 1.03e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    4 IKLTGINKIYRtnEIETLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDaPSSGKIEINGtsVESMKDKELAAF 82
Cdd:TIGR04520   1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLaKLLNGLLL-PTSGKVTVDG--LDTLDEENLWEI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   83 RNKtLGFVFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIAR 156
Cdd:TIGR04520  76 RKK-VGMVFQ-----NPDNqfvgatVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAG 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432  157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR04520 150 VLAMRPDIIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDMEEAVLADRVIVMNKGK 213
OpuBA COG1125
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
3-202 1.60e-47

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


Pssm-ID: 440742 [Multi-domain]  Cd Length: 306  Bit Score: 158.33  E-value: 1.60e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAaf 82
Cdd:COG1125    1 MIEFENVTKRYPDG---TVAVDDLSLTIPAGEFTVLVGPSGCGKTTTLRMINRLIEPTSGRILIDGEDIRDLDPVELR-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNktLGFVFQSFHLINSLNVIDNVEL-PLLYRKMAAKERTRlAKEVLERVGLSH-RMRH-MPTQLSGGQCQRVAIARAIV 159
Cdd:COG1125   76 RR--IGYVIQQIGLFPHMTVAENIATvPRLLGWDKERIRAR-VDELLELVGLDPeEYRDrYPHELSGGQQQRVGVARALA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLD----SKMGAEVMELLHKLNKedgrTIVMVTH 202
Cdd:COG1125  153 ADPPILLMDEPFGALDpitrEQLQDELLRLQRELGK----TIVFVTH 195
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
4-220 2.36e-47

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 159.73  E-value: 2.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelAAFR 83
Cdd:PRK09452  15 VELRGISKSFDGKEV----ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVP----AENR 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK09452  87 H--VNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:PRK09452 165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSdRIVVMRDGR 222
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-222 4.62e-47

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 155.68  E-value: 4.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKI-----EINGTSVESMK 75
Cdd:PRK11264   1 MSAIEVKNLVKKFHGQTV----LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIrvgdiTIDTARSLSQQ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  76 DKELAAFRNKtLGFVFQSFHLINSLNVIDNV-ELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAI 154
Cdd:PRK11264  77 KGLIRQLRQH-VGFVFQNFNLFPHRTVLENIiEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAI 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDgRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK11264 156 ARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEK-RTMVIVTHEMSFARDVADRAIFMDQGRI 222
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
22-203 1.76e-46

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 153.07  E-value: 1.76e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGtsvesmkdKELAAFRNKtLGFVFQSFHlINS- 99
Cdd:cd03235   14 VLEDVSFEVKPGEFLAIVGPNGAGKSTLLKaILGLLK-PTSGSIRVFG--------KPLEKERKR-IGYVPQRRS-IDRd 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 --LNVIDNVELPLLYR----KMAAKERTRLAKEVLERVGLSHrMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:cd03235   83 fpISVRDVVLMGLYGHkglfRRLSKADKAKVDEALERVGLSE-LADRQiGELSGGQQQRVLLARALVQDPDLLLLDEPFA 161
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:cd03235  162 GVDPKTQEDIYELLRELRRE-GMTILVVTHD 191
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
3-223 2.11e-46

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 153.37  E-value: 2.11e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYrtneiETLALeNVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVE---------S 73
Cdd:COG3840    1 MLRLDDLTYRY-----GDFPL-RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTalppaerpvS 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  74 MkdkelaafrnktlgfVFQSFHLINSLNVIDNVEL---PLLyrKMAAKERTRLAkEVLERVGLSHRMRHMPTQLSGGQCQ 150
Cdd:COG3840   75 M---------------LFQENNLFPHLTVAQNIGLglrPGL--KLTAEQRAQVE-QALERVGLAGLLDRLPGQLSGGQRQ 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQVQ 223
Cdd:COG3840  137 RVALARCLVRKRPILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARiADRVLLVADGRIAA 210
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
4-220 2.20e-46

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


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 154.53  E-value: 2.20e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    4 IKLTGINKIYRTN-EIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAA 81
Cdd:TIGR04521   1 IKLKNVSYIYQPGtPFEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLnGLL-KPTSGTVTIDGRDITAKKKKKLKD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   82 FRnKTLGFVFQsF--HLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHM-PTQLSGGQCQRVAIARAI 158
Cdd:TIGR04521  80 LR-KKVGLVFQ-FpeHQLFEETVYKDIAFGPKNLGLSEEEAEERVKEALELVGLDEEYLERsPFELSGGQMRRVAIAGVL 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432  159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:TIGR04521 158 AMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSmEDVAEYADRVIVMHKGK 220
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
4-207 4.28e-46

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 156.01  E-value: 4.28e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDkelaafR 83
Cdd:PRK10851   3 IEIANIKKSFGRTQV----LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHA------R 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTLGFVFQSFHLINSLNVIDNVE-----LPLLYRKMAAKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI 158
Cdd:PRK10851  73 DRKVGFVFQHYALFRHMTVFDNIAfgltvLPRRERPNAAAIKAKVTQ-LLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK10851 152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEA 200
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
22-207 4.77e-46

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: 152.49  E-value: 4.77e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafRNktLGFVFQSFHLINSLN 101
Cdd:cd03296   17 ALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----RN--VGFVFQHYALFRHMT 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAK----ERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:cd03296   91 VFDNVAFGLRVKPRSERppeaEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPKVLLLDEPFGALDAK 170
                        170       180       190
                 ....*....|....*....|....*....|
gi 495112432 178 MGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:cd03296  171 VRKELRRWLRRLHDELHVTTVFVTHDQEEA 200
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
4-223 1.31e-45

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: 151.68  E-value: 1.31e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafR 83
Cdd:cd03295    1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVEL---R 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKtLGFVFQSFHLINSLNVIDNVEL-PLLYRKMAAKERTRlAKEVLERVGL--SHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:cd03295   75 RK-IGYVIQQIGLFPHMTVEENIALvPKLLKWPKEKIRER-ADELLALVGLdpAEFADRYPHELSGGQQQRVGVARALAA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA-KQTSRTIRFFDGRQVQ 223
Cdd:cd03295  153 DPPLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAfRLADRIAIMKNGEIVQ 216
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
22-223 1.33e-45

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: 159.16  E-value: 1.33e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAfrnkTLGFVFQSFHLINSl 100
Cdd:COG4987  350 VLDGLSLTLPPGERVAIVGPSGSGKSTLLAlLLRFLD-PQSGSITLGGVDLRDLDEDDLRR----RIAVVPQRPHLFDT- 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:COG4987  424 TLRENL---RLARPDATDEE---LWAALERVGLGDWLAALPdgldtwlgeggRRLSGGERRRLALARALLRDAPILLLDE 497
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG4987  498 PTEGLDAATEQALLADLLEALA--GRTVLLITHRLAGLERMDRILVLEDGRIVE 549
tungstate_WtpC NF040840
tungstate ABC transporter ATP-binding protein WtpC;
3-223 3.84e-44

tungstate ABC transporter ATP-binding protein WtpC;


Pssm-ID: 468779 [Multi-domain]  Cd Length: 347  Bit Score: 151.00  E-value: 3.84e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTneietLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELAAF 82
Cdd:NF040840   1 MIRIENLSKDWKE-----FKLRDISLEVKEGEYFIILGPSGAGKTVLLELIAGIWPPDSGKIYLDG------KDITNLPP 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:NF040840  70 EKRGIAYVYQNYMLFPHKTVFENIAFGLKLRKVPKEEIERKVKEIMELLGISHLLHRKPRTLSGGEQQRVALARALIIEP 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:NF040840 150 KLLLLDEPLSALDVQTRDELIREMKRWHREFGFTAIHVTHNFEEALSLAdRVGIMLNGRLSQ 211
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
4-220 1.06e-43

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: 144.45  E-value: 1.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAaf 82
Cdd:cd03228    1 IEFKNVSFSYPGRP--KPVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKlLLRLYD-PTSGEILIDGVDLRDLDLESLR-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 rnKTLGFVFQSFHLINSlNVIDNVelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNP 162
Cdd:cd03228   76 --KNIAYVPQDPFLFSG-TIRENI-------------------------------------LSGGQRQRIAIARALLRDP 115
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnkEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03228  116 PILILDEATSALDPETEALILEALRAL--AKGKTVIVIAHRLSTIRDADRIIVLDDGR 171
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
4-223 2.05e-43

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: 145.94  E-value: 2.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKElaaf 82
Cdd:cd03299    1 LKVENLSKDWKEFK-----LKNVSLEVERGDYFVILGPTGSGKSVLLEtIAGFI-KPDSGKILLNGKDITNLPPEK---- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtlGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03299   71 RDI--SYVPQNYALFPHMTVYKNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNP 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:cd03299  149 KILLLDEPFSALDVRTKEKLREELKKIRKEFGVTVLHVTHDFEEAWALAdKVAIMLNGKLIQ 210
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
19-223 2.46e-43

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: 152.99  E-value: 2.46e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLI 97
Cdd:COG4988  349 GRPALDGLSLTIPPGERVALVGPSGAGKSTLLNlLLGFLP-PYSGSILINGVDLSDLDPASWR----RQIAWVPQNPYLF 423
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSlNVIDNVelpLLYRKMAAKERTRlakEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:COG4988  424 AG-TIRENL---RLGRPDASDEELE---AALEAAGLDEFVAALPdgldtplgeggRGLSGGQAQRLALARALLRDAPLLL 496
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 167 ADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG4988  497 LDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQADRILVLDDGRIVE 551
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
22-203 5.94e-43

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 147.19  E-value: 5.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAFRnKTLGFVFQ-SFhliNS 99
Cdd:COG4608   33 AVDGVSFDIRRGETLGLVGESGCGKSTLGRlLLRLEE-PTSGEILFDGQDITGLSGRELRPLR-RRMQMVFQdPY---AS 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LN----VIDNVELPLLYRKMA-AKERTRLAKEVLERVGL--SHRMRHmPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:COG4608  108 LNprmtVGDIIAEPLRIHGLAsKAERRERVAELLELVGLrpEHADRY-PHEFSGGQRQRIGIARALALNPKLIVCDEPVS 186
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4608  187 ALDVSIQAQVLNLLEDLQDELGLTYLFISHD 217
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
4-223 7.39e-43

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: 153.07  E-value: 7.39e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINkiYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMkdkELAAF 82
Cdd:COG2274  474 IELENVS--FRYPGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKlLLGLYE-PTSGRILIDGIDLRQI---DPASL 547
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQSFHLINSlNVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQR 151
Cdd:COG2274  548 RRQ-IGVVLQDVFLFSG-TIRENI---TLGDPDATDEE---IIEAARLAGLHDFIEALPmgydtvvgeggSNLSGGQRQR 619
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:COG2274  620 LAIARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIRLADRIIVLDKGRIVE 689
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
4-209 7.62e-43

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: 142.15  E-value: 7.62e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVesmkDKELAAF 82
Cdd:cd03230    1 IEVRNLSKRYGKKT----ALDDISLTVEKGEIYGLLGPNGAGKTTLIKiILGLL-KPDSGEIKVLGKDI----KKEPEEV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQSFHLINSLNVIDNVELpllyrkmaakertrlakevlervglshrmrhmptqlSGGQCQRVAIARAIVGNP 162
Cdd:cd03230   72 KRR-IGYLPEEPSLYENLTVRENLKL------------------------------------SGGMKQRLALAQALLHDP 114
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ 209
Cdd:cd03230  115 ELLILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAER 160
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
22-203 9.20e-43

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 144.80  E-value: 9.20e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAAfrnktLGFV--FQSFHLIN 98
Cdd:COG0411   19 AVDDVSLEVERGEIVGLIGPNGAGKTTLFNlITGFY-RPTSGRILFDGRDITGLPPHRIAR-----LGIArtFQNPRLFP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLLYR-------------KMAAKER--TRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:COG0411   93 ELTVLENVLVAAHARlgrgllaallrlpRARREEReaRERAEELLERVGLADRADEPAGNLSYGQQRRLEIARALATEPK 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG0411  173 LLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHD 212
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
22-207 1.12e-42

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 144.46  E-value: 1.12e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelAAFRnktlGFVFQSFHLINSLN 101
Cdd:PRK11248  16 ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGP-----GAER----GVVFQNEGLLPWRN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK11248  87 VQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDEPFGALDAFTREQ 166
                        170       180
                 ....*....|....*....|....*.
gi 495112432 182 VMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK11248 167 MQTLLLKLWQETGKQVLLITHDIEEA 192
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
23-171 1.18e-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: 141.25  E-value: 1.18e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGtsvESMKDKELAAFRnKTLGFVFQSFHLINSLN 101
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKlIAGLLS-PTEGTILLDG---QDLTDDERKSLR-KEIGYVFQDPQLFPRLT 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432  102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH----RMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:pfam00005  76 VRENLRLGLLLKGLSKREKDARAEEALEKLGLGDladrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
3-220 1.79e-42

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 143.09  E-value: 1.79e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEietLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAF 82
Cdd:PRK10908   1 MIRFEHVSKAYLGGR---QALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:PRK10908  78 R-RQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQ-AKQTSRTIRFFDGR 220
Cdd:PRK10908 157 AVLLADEPTGNLDDALSEGILRLFEEFNRV-GVTVLMATHDIGLiSRRSYRMLTLSDGH 214
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
1-207 1.33e-41

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 144.79  E-value: 1.33e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIEtlalENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELA 80
Cdd:PRK11000   1 MASVTLRNVTKAYGDVVIS----KDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGE---KRMNDVPPA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afrNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:PRK11000  74 ---ERGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVA 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK11000 151 EPSVFLLDEPLSNLDAALRVQMRIEISRLHKRLGRTMIYVTHDQVEA 197
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
22-203 6.53e-41

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: 139.49  E-value: 6.53e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAAfrnktLGFV--FQSFHLIN 98
Cdd:cd03219   15 ALDDVSFSVRPGEIHGLIGPNGAGKTTLFNlISGFL-RPTSGSVLFDGEDITGLPPHEIAR-----LGIGrtFQIPRLFP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLLYRK-------MAAKERTRL---AKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:cd03219   89 ELTVLENVMVAAQARTgsglllaRARREEREArerAEELLERVGLADLADRPAGELSYGQQRRLEIARALATDPKLLLLD 168
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTHN 203
Cdd:cd03219  169 EPAAGLNPEETEELAELIRELR-ERGITVLLVEHD 202
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
5-220 7.07e-41

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: 136.61  E-value: 7.07e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   5 KLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrn 84
Cdd:cd00267    1 EIENLSFRYGGRTA----LDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLPLEELR---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  85 KTLGFVFQsfhlinslnvidnvelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNPEI 164
Cdd:cd00267   73 RRIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDL 101
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 165 ILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ-TSRTIRFFDGR 220
Cdd:cd00267  102 LLLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELaADRVIVLKDGK 157
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
23-207 1.21e-40

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: 138.37  E-value: 1.21e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV-ESMKDKELaafrnktlgfVFQSFHLINSLN 101
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQItEPGPDRMV----------VFQNYSLLPWLT 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  102 VIDNVELPL--LYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:TIGR01184  71 VRENIALAVdrVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTR 150
                         170       180
                  ....*....|....*....|....*...
gi 495112432  180 AEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:TIGR01184 151 GNLQEELMQIWEEHRVTVLMVTHDVDEA 178
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
23-220 1.93e-40

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: 137.43  E-value: 1.93e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDV---IKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTS-VESMKDKELAAFRNKtLGFVFQSFHLIN 98
Cdd:cd03297   10 LPDFTLKIdfdLNEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVlFDSRKKINLPPQQRK-IGLVFQQYALFP 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLlyRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03297   89 HLNVRENLAFGL--KRKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRAL 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 179 GAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:cd03297  167 RLQLLPELKQIKKNLNIPVIFVTHDlSEAEYLADRIVVMEDGR 209
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
19-220 6.49e-40

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 137.48  E-value: 6.49e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLL---NIMGLL--DAPSSGKIEINGTSVESmKDKELAAFRnKTLGFVFQS 93
Cdd:COG1117   23 DKQALKDINLDIPENKVTALIGPSGCGKSTLLrclNRMNDLipGARVEGEILLDGEDIYD-PDVDVVELR-RRVGMVFQK 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 ---FhlinSLNVIDNVELPLlyRKMAAKERTRLAKEV---LERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:COG1117  101 pnpF----PKSIYDNVAYGL--RLHGIKSKSELDEIVeesLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPE 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLnKEDgRTIVMVTHNEEQAKQTS-RTIRFFDGR 220
Cdd:COG1117  175 VLLMDEPTSALDPISTAKIEELILEL-KKD-YTIVIVTHNMQQAARVSdYTAFFYLGE 230
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
38-223 1.40e-39

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


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 138.40  E-value: 1.40e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   38 IMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdkeLAAFRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAA 117
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDVT------NVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMRKVPR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  118 KERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK----MGAEVMELLHKLnked 193
Cdd:TIGR01187  75 AEIKPRVLEALRLVQLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKlrdqMQLELKTIQEQL---- 150
                         170       180       190
                  ....*....|....*....|....*....|.
gi 495112432  194 GRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:TIGR01187 151 GITFVFVTHDQEEAMTMSdRIAIMRKGKIAQ 181
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
6-207 1.98e-39

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 136.35  E-value: 1.98e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIeINGTSvesmkdkELAAFRNK 85
Cdd:PRK11247  15 LNAVSKRYGERTV----LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGTA-------PLAEARED 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  86 TLgFVFQSFHLINSLNVIDNVELPLlyrkmAAKERTRlAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:PRK11247  83 TR-LMFQDARLLPWKKVIDNVGLGL-----KGQWRDA-ALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLL 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA 207
Cdd:PRK11247 156 LLDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHDVSEA 197
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
22-203 7.51e-39

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: 140.20  E-value: 7.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdaPSSGKIEINGTSVESMKDKELAAFRNKtLGFVFQS-FhliNS 99
Cdd:COG4172  301 AVDGVSLTLRRGETLGLVGESGSGKSTLgLALLRLI--PSEGEIRFDGQDLDGLSRRALRPLRRR-MQVVFQDpF---GS 374
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LN----VIDNVELPL--LYRKMAAKERTRLAKEVLERVGLSHRMRH-MPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:COG4172  375 LSprmtVGQIIAEGLrvHGPGLSAAERRARVAEALEEVGLDPAARHrYPHEFSGGQRQRIAIARALILEPKLLVLDEPTS 454
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4172  455 ALDVSVQAQILDLLRDLQREHGLAYLFISHD 485
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
28-222 1.78e-38

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: 132.23  E-value: 1.78e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  28 LDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafrnKTLGFVFQSFHLINSLNVIDNVE 107
Cdd:cd03298   19 LTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD------RPVSMLFQENNLFAHLTVEQNVG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 108 LPLLYR-KMAAKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELL 186
Cdd:cd03298   93 LGLSPGlKLTAEDRQAIEV-ALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLV 171
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 495112432 187 HKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFD-GRQV 222
Cdd:cd03298  172 LDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDnGRIA 208
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
23-216 3.30e-38

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 131.45  E-value: 3.30e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAP--SSGKIEINGTSVESMKdkelAAFRNktLGFVFQSFHLINS 99
Cdd:COG4136   17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALP----AEQRR--IGILFQDDLLFPH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNveLPL-LYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:COG4136   91 LSVGEN--LAFaLPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAAL 168
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 179 GAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:COG4136  169 RAQFREFVFEQIRQRGIPALLVTHDEEDAPAAGRVLDL 206
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
4-217 4.44e-38

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 132.79  E-value: 4.44e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDK--ELAA 81
Cdd:PRK10619   6 LNVIDLHKRYGEHEV----LKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVRDKdgQLKV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTL-------GFVFQSFHLINSLNVIDNV-ELPLLYRKMAAKERTRLAKEVLERVGLSHRMR-HMPTQLSGGQCQRV 152
Cdd:PRK10619  82 ADKNQLrllrtrlTMVFQHFNLWSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRV 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF 217
Cdd:PRK10619 162 SIARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQL-AEEGKTMVVVTHEMGFARHVSSHVIFL 225
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
3-219 9.58e-38

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 132.06  E-value: 9.58e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLL--DAPSSGKIEINGTSV--ESMKDK 77
Cdd:PRK09984   4 IIRVEKLAKTFNQHQ----ALHAVDLNIHHGEMVALLGPSGSGKSTLLrHLSGLItgDKSAGSHIELLGRTVqrEGRLAR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  78 ELAAFRNKTlGFVFQSFHLINSLNVIDNVELPLL---------YRKMAAKERTRlAKEVLERVGLSHRMRHMPTQLSGGQ 148
Cdd:PRK09984  80 DIRKSRANT-GYIFQQFNLVNRLSVLENVLIGALgstpfwrtcFSWFTREQKQR-ALQALTRVGMVHFAHQRVSTLSGGQ 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 149 CQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI-------RFFDG 219
Cdd:PRK09984 158 QQRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIvalrqghVFYDG 235
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
2-202 1.03e-37

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: 130.29  E-value: 1.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkDKELAA 81
Cdd:COG4133    1 MMLEAENLSCRRG----ERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDARED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRnKTLGFVFQSFHLINSLNVIDNVELpllYRKMAAKERTRLA-KEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:COG4133   73 YR-RRLAYLGHADGLKPELTVRENLRF---WAALYGLRADREAiDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLS 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG4133  149 PAPLWLLDEPFTALDAAGVALLAELIAAH-LARGGAVLLTTH 189
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
22-203 1.25e-37

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: 130.63  E-value: 1.25e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKELAAfrnKTLGFVFQSFHLINSL 100
Cdd:cd03224   15 ILFGVSLTVPEGEIVALLGRNGAGKTTLLKtIMGLL-PPRSGSIRFDGRDITGLPPHERAR---AGIGYVPEGRRIFPEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAKERTRlaKEVLERV-GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:cd03224   91 TVEENLLLGAYARRRAKRKARL--ERVYELFpRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIV 168
                        170       180
                 ....*....|....*....|....
gi 495112432 180 AEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:cd03224  169 EEIFEAIRELRDE-GVTILLVEQN 191
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-202 1.56e-37

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 133.82  E-value: 1.56e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKEla 80
Cdd:PRK11650   1 MAGLKLQAVRKSYDGK---TQVIKGIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD-- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afRNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:PRK11650  76 --RD--IAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVR 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEvMEL-LHKLNKEDGRTIVMVTH 202
Cdd:PRK11650 152 EPAVFLFDEPLSNLDAKLRVQ-MRLeIQRLHRRLKTTSLYVTH 193
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
3-202 1.80e-37

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 130.97  E-value: 1.80e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAaf 82
Cdd:COG4604    1 MIEIKNVSKRYGGKVV----LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELA-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 rnKTLGFVFQSFHLINSLNVIDNVEL---PllYRKmaakerTRLAKE-------VLERVGLSH-RMRHMpTQLSGGQCQR 151
Cdd:COG4604   75 --KRLAILRQENHINSRLTVRELVAFgrfP--YSK------GRLTAEdreiideAIAYLDLEDlADRYL-DELSGGQRQR 143
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:COG4604  144 AFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLH 194
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
13-203 3.51e-37

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: 135.97  E-value: 3.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDAPS---SGKIEINGTSVESMKDKELAAFRNKTLG 88
Cdd:COG4172   16 FGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAahpSGSILFDGQDLLGLSERELRRIRGNRIA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  89 FVFQ---SfhlinSLNVIDNV-----ELPLLYRKMAAKERTRLAKEVLERVGLSH---RMRHMPTQLSGGQCQRVAIARA 157
Cdd:COG4172   96 MIFQepmT-----SLNPLHTIgkqiaEVLRLHRGLSGAAARARALELLERVGIPDperRLDAYPHQLSGGQRQRVMIAMA 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4172  171 LANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHD 216
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
3-220 6.32e-37

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 128.93  E-value: 6.32e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYrtneiETLALEnVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvesmKDKELAAF 82
Cdd:PRK10771   1 MLKLTDITWLY-----HHLPMR-FDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNG------QDHTTTPP 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKTLGFVFQSFHLINSLNVIDNVEL---PLLyrKMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK10771  69 SRRPVSMLFQENNLFSHLTVAQNIGLglnPGL--KLNAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLV 145
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:PRK10771 146 REQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSlEDAARIAPRSLVVADGR 207
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
3-222 6.89e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 130.21  E-value: 6.89e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNE--IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDkeLA 80
Cdd:PRK13633   4 MIKCKNVSYKYESNEesTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEEN--LW 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKTlGFVFQsfhliNSLNVI------DNVELPLLYRKMAAKE-RTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVA 153
Cdd:PRK13633  82 DIRNKA-GMVFQ-----NPDNQIvativeEDVAFGPENLGIPPEEiRERV-DESLKKVGMYEYRRHAPHLLSGGQKQRVA 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK13633 155 IAGILAMRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVEADRIIVMDSGKVV 223
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
24-203 1.63e-36

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 129.11  E-value: 1.63e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRnKTLGFVFQSFHLINSLNVI 103
Cdd:PRK11831  24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVR-KRMSMLFQSGALFTDMNVF 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNVELPLlyrkmaaKERTRLAKEV--------LERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP-TGNL 174
Cdd:PRK11831 103 DNVAYPL-------REHTQLPAPLlhstvmmkLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPfVGQD 175
                        170       180
                 ....*....|....*....|....*....
gi 495112432 175 DSKMGAEVmELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11831 176 PITMGVLV-KLISELNSALGVTCVVVSHD 203
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
3-220 2.57e-36

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 128.28  E-value: 2.57e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEI-ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKEla 80
Cdd:COG1101    1 MLELKNLSKTFNPGTVnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNaIAGSL-PPDSGSILIDGKDVTKLPEYK-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afRNKTLGFVFQsfhliN-------SLNVIDNveLPLLYRKMAA--------KERTRLAKEVLERV--GLSHRMrHMPT- 142
Cdd:COG1101   78 --RAKYIGRVFQ-----DpmmgtapSMTIEEN--LALAYRRGKRrglrrgltKKRRELFRELLATLglGLENRL-DTKVg 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQA-KQTSRTIRFFDGR 220
Cdd:COG1101  148 LLSGGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQAlDYGNRLIMMHEGR 226
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
22-223 2.61e-36

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 131.11  E-value: 2.61e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaafrnKTLGFVFQSFHLINSLN 101
Cdd:PRK11607  34 AVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQ------RPINMMFQSYALFPHMT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK---- 177
Cdd:PRK11607 108 VEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLDEPMGALDKKlrdr 187
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 178 MGAEVMELLHKLnkedGRTIVMVTHNEEQAKQTSRTIRFFD-GRQVQ 223
Cdd:PRK11607 188 MQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNrGKFVQ 230
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
19-202 3.04e-36

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 133.75  E-value: 3.04e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQSFHLI 97
Cdd:COG1132  352 DRPVLKDISLTIPPGETVALVGPSGSGKSTLVNlLLRFYD-PTSGRILIDGVDIRDLT---LESLRRQ-IGVVPQDTFLF 426
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 nSLNVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:COG1132  427 -SGTIRENI---RYGRPDATDEE---VEEAAKAAQAHEFIEALPdgydtvvgergVNLSGGQRQRIAIARALLKDPPILI 499
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 167 ADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:COG1132  500 LDEATSALDTETEALIQEALERLMK--GRTTIVIAH 533
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
22-204 3.08e-36

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: 133.25  E-value: 3.08e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAfrnkTLGFVFQSFHLINSl 100
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLAtLAGLLD-PLQGEVTLDGVPVSSLDQDEVRR----RVSVCAQDAHLFDT- 423
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  101 NVIDNVelpLLYRKMAAKERtrlAKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:TIGR02868 424 TVRENL---RLARPDATDEE---LWAALERVGLADWLRALPdgldtvlgeggARLSGGERQRLALARALLADAPILLLDE 497
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 495112432  170 PTGNLDSKMGAEVMELLhkLNKEDGRTIVMVTHNE 204
Cdd:TIGR02868 498 PTEHLDAETADELLEDL--LAALSGRTVVLITHHL 530
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
6-214 4.13e-36

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 129.84  E-value: 4.13e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkelAAFRNK 85
Cdd:PRK11432   9 LKNITKRFGSNTV----IDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  86 TLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:PRK11432  79 DICMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVL 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK11432 159 LFDEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTV 207
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
4-202 7.06e-36

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: 125.77  E-value: 7.06e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVsIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKelaaFR 83
Cdd:cd03264    1 LQLENLTKRYG----KKRALDGVSLTLGPGMYG-LLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQK----LR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03264   72 -RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPS 150
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:cd03264  151 ILIVDEPTAGLDPEERIRFRNLLSELGED--RIVILSTH 187
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
2-222 1.12e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 126.64  E-value: 1.12e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINkiYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaa 81
Cdd:PRK13632   6 VMIKVENVS--FSYPNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKENLKEI-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 fRNKtLGFVFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIA 155
Cdd:PRK13632  82 -RKK-IGIIFQ-----NPDNqfigatVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIA 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK13632 155 SVLALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMDEAILADKVIVFSEGKLI 221
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
9-222 1.14e-35

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


Pssm-ID: 213193 [Multi-domain]  Cd Length: 205  Bit Score: 125.06  E-value: 1.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   9 INKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDaPSSGKIEINGtsvESMKDKElaafRNKTL 87
Cdd:cd03226    2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKIlAGLIK-ESSGSILLNG---KPIKAKE----RRKSI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  88 GFVFQS--FHLINslnviDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:cd03226   74 GYVMQDvdYQLFT-----DSVREELLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLL 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEE-QAKQTSRTIRFFDGRQV 222
Cdd:cd03226  149 IFDEPTSGLDYKNMERVGELIRELAAQ-GKAVIVITHDYEfLAKVCDRVLLLANGAIV 205
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
3-203 1.51e-35

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: 125.74  E-value: 1.51e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEINGTSVEsmkdKELAA 81
Cdd:COG4555    1 MIEVENLSKKYGKVP----ALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLaGLLK-PDSGSILIDGEDVR----KEPRE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKtLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLShRMRHMPTQ-LSGGQCQRVAIARAIVG 160
Cdd:COG4555   72 ARRQ-IGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLE-EFLDRRVGeLSTGMKKKVALARALVH 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 161 NPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG4555  150 DPKVLLLDEPTNGLDVMARRLLREILRAL-KKEGKTVLFSSHI 191
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
19-209 2.59e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 126.29  E-value: 2.59e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKD-KELAAFRNKtLGFVFQsF--H 95
Cdd:PRK13634  19 ERRALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAGKKnKKLKPLRKK-VGIVFQ-FpeH 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMR-HMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK13634  97 QLFEETVEKDICFGPMNFGVSEEDAKQKAREMIELVGLPEELLaRSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGL 176
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495112432 175 DSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ 209
Cdd:PRK13634 177 DPKGRKEMMEMFYKLHKEKGLTTVLVTHSMEDAAR 211
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-207 3.39e-35

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: 124.71  E-value: 3.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYrtNEIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKEL 79
Cdd:COG0410    1 MPMLEVENLHAGY--GGIH--VLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRI 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 AAfrnKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAkEVLE---RvgLSHRMRHMPTQLSGGQCQRVAIAR 156
Cdd:COG0410   76 AR---LGIGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLE-RVYElfpR--LKERRRQRAGTLSGGEQQMLAIGR 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 157 AIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQA 207
Cdd:COG0410  150 ALMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFA 199
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
20-203 3.50e-35

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 125.58  E-value: 3.50e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  20 TLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDaPSSGKIEINGTSVESMKdKELAAFRnKTLGFVFQ-SFHLI 97
Cdd:PRK13639  15 TEALKGINFKAEKGEMVALLGPNGAGKSTLfLHFNGILK-PTSGEVLIKGEPIKYDK-KSLLEVR-KTVGIVFQnPDDQL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:PRK13639  92 FAPTVEEDVAFGPLNLGLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPM 171
                        170       180
                 ....*....|....*....|....*.
gi 495112432 178 MGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:PRK13639 172 GASQIMKLLYDLNKE-GITIIISTHD 196
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
13-220 3.92e-35

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 125.51  E-value: 3.92e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLdAPSSGKIEINGT--SVESMKDkelaaFRNKtLGF 89
Cdd:PRK13635  13 FRYPDAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAkLLNGLL-LPEAGTITVGGMvlSEETVWD-----VRRQ-VGM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  90 VFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK13635  86 VFQ-----NPDNqfvgatVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK13635 161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQADRVIVMNKGE 217
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
2-222 4.05e-35

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: 125.30  E-value: 4.05e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    2 AMIKLTGINKIYRTNEI-----ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKD 76
Cdd:TIGR02769   1 SLLEVRDVTHTYRTGGLfgakqRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   77 KELAAFRnKTLGFVFQSfhLINSLNVIDNVEL----PLL-YRKMAAKERTRLAKEVLERVGL-SHRMRHMPTQLSGGQCQ 150
Cdd:TIGR02769  81 KQRRAFR-RDVQLVFQD--SPSAVNPRMTVRQiigePLRhLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432  151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:TIGR02769 158 RINIARALAVKPKLIVLDEAVSNLDMVLQAVILELLRKLQQAFGTAYLFITHDLRLVQSFCQRVAVMDKGQI 229
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-222 4.97e-35

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: 124.43  E-value: 4.97e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGK-IEI-----NGTSVESM 74
Cdd:COG1119    1 DPLLELRNVTVRRGGKTI----LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNdVRLfgerrGGEDVWEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  75 KdkelaafrnKTLGFVFQSFHL-----INSLNVI-----DNVELpllYRKMAAKERTRlAKEVLERVGLSHRMRHMPTQL 144
Cdd:COG1119   77 R---------KRIGLVSPALQLrfprdETVLDVVlsgffDSIGL---YREPTDEQRER-ARELLELLGLAHLADRPFGTL 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGRQV 222
Cdd:COG1119  144 SQGEQRRVLIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHvEEIPPGITHVLLLKDGRVV 222
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
25-202 2.19e-34

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: 125.60  E-value: 2.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTS-VESMKDKELAAFRNKtLGFVFQSFHLINSLNVI 103
Cdd:COG4148   17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVlQDSARGIFLPPHRRR-IGYVFQEARLFPHLSVR 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNvelpLLY--RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:COG4148   96 GN----LLYgrKRAPRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAE 171
                        170       180
                 ....*....|....*....|.
gi 495112432 182 VMELLHKLNKEDGRTIVMVTH 202
Cdd:COG4148  172 ILPYLERLRDELDIPILYVSH 192
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
26-220 7.79e-34

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: 124.07  E-value: 7.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   26 VNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV-ESMKDKELAAFRNKtLGFVFQSFHLINSLNVID 104
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLfDSRKGIFLPPEKRR-IGYVFQEARLFPHLSVRG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  105 NvelpLLY--RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEV 182
Cdd:TIGR02142  95 N----LRYgmKRARPSERRISFERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 495112432  183 MELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:TIGR02142 171 LPYLERLHAEFGIPILYVSHSlQEVLRLADRVVVLEDGR 209
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-203 9.11e-34

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 121.72  E-value: 9.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIETLA-----LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMK 75
Cdd:PRK10419   1 MTLLNVSGLSHHYAHGGLSGKHqhqtvLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLN 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  76 DKELAAFRnKTLGFVFQ-SFHLINSLNVI-DNVELPLLY-RKMAAKERTRLAKEVLERVGL--SHRMRhMPTQLSGGQCQ 150
Cdd:PRK10419  81 RAQRKAFR-RDIQMVFQdSISAVNPRKTVrEIIREPLRHlLSLDKAERLARASEMLRAVDLddSVLDK-RPPQLSGGQLQ 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10419 159 RVCLARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHD 211
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
2-205 1.02e-33

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: 120.62  E-value: 1.02e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINK---IYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-----NIMglldaPSSGKIEIN--GTSV 71
Cdd:COG4778    3 TLLEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLkciygNYL-----PDSGSILVRhdGGWV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  72 E--SMKDKELAAFRNKTLGFVFQsFhlinsLNVI------DNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHM-PT 142
Cdd:COG4778   78 DlaQASPREILALRRRTIGYVSQ-F-----LRVIprvsalDVVAEPLLERGVDREEARARARELLARLNLPERLWDLpPA 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:COG4778  152 TFSGGEQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEA-KARGTAIIGIFHDEE 213
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
4-222 1.12e-33

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 119.97  E-value: 1.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    4 IKLTGINKIYRTNEIEtlalenVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkeLAAFR 83
Cdd:TIGR01277   1 LALDKVRYEYEHLPME------FDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQSHTG-----LAPYQ 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   84 nKTLGFVFQSFHLINSLNVIDNVEL---PLLyrKMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVG 160
Cdd:TIGR01277  70 -RPVSMLFQENNLFAHLTVRQNIGLglhPGL--KLNAEQQEKV-VDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVR 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432  161 NPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:TIGR01277 146 PNPILLLDEPFSALDPLLREEMLALVKQLCSERQRTLLMVTHHLSDARAIASQIAVVSQGKI 207
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
20-222 1.63e-33

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 123.99  E-value: 1.63e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINS 99
Cdd:PRK10070  41 SLGVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRRKKIAMVFQSFALMPH 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:PRK10070 121 MTVLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIR 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK10070 201 TEMQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEV 243
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
4-220 2.53e-33

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 121.73  E-value: 2.53e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIY-RTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI---------NGTSVES 73
Cdd:PRK13651   3 IKVKNIVKIFnKKLPTELKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkdeknkkKTKEKEK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  74 MKDK---ELAAFRN--------KTLGFVFQ--SFHLINSLNVIDNVELPLLY--RKMAAKERtrlAKEVLERVGLSHR-M 137
Cdd:PRK13651  83 VLEKlviQKTRFKKikkikeirRRVGVVFQfaEYQLFEQTIEKDIIFGPVSMgvSKEEAKKR---AAKYIELVGLDESyL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 138 RHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQA-KQTSRTIRF 216
Cdd:PRK13651 160 QRSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVlEWTKRTIFF 238

                 ....
gi 495112432 217 FDGR 220
Cdd:PRK13651 239 KDGK 242
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
22-203 5.37e-33

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 121.22  E-value: 5.37e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELAAFRNKTLGFVFQSFHliNSLN 101
Cdd:PRK11308  30 ALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDL-LKADPEAQKLLRQKIQIVFQNPY--GSLN 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 ----VIDNVELPLLYR-KMAAKERTRLAKEVLERVGL----SHRMRHMptqLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK11308 107 prkkVGQILEEPLLINtSLSAAERREKALAMMAKVGLrpehYDRYPHM---FSGGQRQRIAIARALMLDPDVVVADEPVS 183
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11308 184 ALDVSVQAQVLNLMMDLQQELGLSYVFISHD 214
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
4-207 7.16e-33

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: 117.99  E-value: 7.16e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDaPSSGKIEINGTSVESMKDKelaAF 82
Cdd:cd03263    1 LQIRNLTKTYKKGT--KPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMlTGELR-PTSGTAYINGYSIRTDRKA---AR 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03263   75 QS--LGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGP 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQA 207
Cdd:cd03263  153 SVLLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEA 195
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
23-218 7.87e-33

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: 117.27  E-value: 7.87e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDAPS-SGKIEINGTSVEsmkdkeLAAFRnKTLGFVFQSFHLINSL 100
Cdd:cd03213   25 LKNVSGKAKPGELTAIMGPSGAGKSTLLNAlAGRRTGLGvSGEVLINGRPLD------KRSFR-KIIGYVPQDDILHPTL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVElpllyrkMAAKERtrlakevlervglshrmrhmptQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGA 180
Cdd:cd03213   98 TVRETLM-------FAAKLR----------------------GLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSAL 148
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495112432 181 EVMELLHKLNKeDGRTIVMVTHneeqakQTSRTI-RFFD 218
Cdd:cd03213  149 QVMSLLRRLAD-TGRTIICSIH------QPSSEIfELFD 180
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
23-202 1.66e-32

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 118.34  E-value: 1.66e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLINSLN 101
Cdd:PRK13548  18 LDDVSLTLRPGEVVAILGPNGAGKSTLLRALsGEL-SPDSGEVRLNGRPLADWSPAELA----RRRAVLPQHSSLSFPFT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH-RMRHMPtQLSGGQCQRVAIARAIV------GNPEIILADEPTGNL 174
Cdd:PRK13548  93 VEEVVAMGRAPHGLSRAEDDALVAAALAQVDLAHlAGRDYP-QLSGGEQQRVQLARVLAqlwepdGPPRWLLLDEPTSAL 171
                        170       180
                 ....*....|....*....|....*...
gi 495112432 175 DSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK13548 172 DLAHQHHVLRLARQLAHERGLAVIVVLH 199
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
1-203 1.73e-32

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 118.40  E-value: 1.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTN-------EIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVES 73
Cdd:COG4167    2 SALLEVRNLSKTFKYRtglfrrqQFE--AVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGHKLEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  74 MKDKelaaFRNKTLGFVFQsfHLINSLNVIDNV----ELPL-LYRKMAAKERTRLAKEVLERVGL----SHRMRHMptqL 144
Cdd:COG4167   80 GDYK----YRCKHIRMIFQ--DPNTSLNPRLNIgqilEEPLrLNTDLTAEEREERIFATLRLVGLlpehANFYPHM---L 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4167  151 SSGQKQRVALARALILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQH 209
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-202 2.95e-32

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 122.05  E-value: 2.95e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdkela 80
Cdd:COG1129    2 EPLLEMRGISKSFGG----VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVR-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 aFRN----KTLG--FVFQSFHLINSLNVIDNVELPLLYRKMAA---KERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQR 151
Cdd:COG1129   70 -FRSprdaQAAGiaIIHQELNLVPNLSVAENIFLGREPRRGGLidwRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQL 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG1129  149 VEIARALSRDARVLILDEPTASLTEREVERLFRIIRRL-KAQGVAIIYISH 198
cbiO PRK13637
energy-coupling factor transporter ATPase;
4-220 3.12e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 118.23  E-value: 3.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNE-IETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVESMKDKeLAA 81
Cdd:PRK13637   3 IKIENLTHIYMEGTpFEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIqHLNGLLK-PTSGKIIIDGVDITDKKVK-LSD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRnKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH-RMRHM-PTQLSGGQCQRVAIARAI 158
Cdd:PRK13637  81 IR-KKVGLVFQyPEYQLFEETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLDYeDYKDKsPFELSGGQKRRVAIAGVV 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 159 VGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGR 220
Cdd:PRK13637 160 AMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmEDVAKLADRIIVMNKGK 222
cbiO PRK13641
energy-coupling factor transporter ATPase;
4-203 4.03e-32

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 118.01  E-value: 4.03e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRT-NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVES-MKDKELAA 81
Cdd:PRK13641   3 IKFENVDYIYSPgTPMEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNK-TLGFVFQSFHLINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK13641  83 LRKKvSLVFQFPEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLSEDlISKSPFELSGGQMRRVAIAGVMA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:PRK13641 162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKA-GHTVILVTHN 204
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
13-221 5.26e-32

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: 114.62  E-value: 5.26e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAAFrnktLGFVF 91
Cdd:cd03246    8 FRYPGAEPPVLRNVSFSIEPGESLAIIGPSGSGKSTLARLIlGLL-RPTSGRVRLDGADISQWDPNELGDH----VGYLP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  92 QSFHLInSLNVIDNVelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:cd03246   83 QDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRILVLDEPN 124
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQ 221
Cdd:cd03246  125 SHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETLASADRILVLEDGRV 173
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
23-222 8.39e-32

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 116.17  E-value: 8.39e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLL-----DAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQSFHLI 97
Cdd:PRK14247  19 LDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIEL----RRRVQMVFQIPNPI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNVIDNVELPLLYRKMAA--KERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK14247  95 PNLSIFENVALGLKLNRLVKskKELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLADEPT 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK14247 175 ANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQI 223
cbiO PRK13646
energy-coupling factor transporter ATPase;
4-223 1.85e-31

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 116.42  E-value: 1.85e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRT-NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVES-MKDKELA 80
Cdd:PRK13646   3 IRFDNVSYTYQKgTPYEHQAIHDVNTEFEQGKYYAIVGQTGSGKSTLIqNINALLK-PTTGTVTVDDITITHkTKDKYIR 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRnKTLGFVFQsfhLINSLNVIDNVELPLLYR----KMAAKERTRLAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIA 155
Cdd:PRK13646  82 PVR-KRIGMVFQ---FPESQLFEDTVEREIIFGpknfKMNLDEVKNYAHRLLMDLGFSRDvMSQSPFQMSGGQMRKIAIV 157
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN-EEQAKQTSRTIRFFDGRQVQ 223
Cdd:PRK13646 158 SILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDmNEVARYADEVIVMKEGSIVS 226
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
4-216 1.88e-31

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 115.32  E-value: 1.88e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLL-----DAPSSGKIEINGTSVESMKDKE 78
Cdd:PRK14267   5 IETVNLRVYYGSNHV----IKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  79 LAAfrNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAA--KERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRV 152
Cdd:PRK14267  81 IEV--RREVGMVFQYPNPFPHLTIYDNVAIGVKLNGLVKskKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRL 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:PRK14267 159 VIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKE--YTIVLVTHSPAQAARVSDYVAF 220
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
19-202 4.41e-31

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


Pssm-ID: 213218 [Multi-domain]  Cd Length: 234  Bit Score: 113.86  E-value: 4.41e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmKDKELAAFRNKtLGFVFQSFHLIN 98
Cdd:cd03251   14 GPPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDV---RDYTLASLRRQ-IGLVSQDVFLFN 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 slnviDNVELPLLYRKMAAKE-------RTRLAKEVLERV--GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:cd03251   90 -----DTVAENIAYGRPGATReeveeaaRAANAHEFIMELpeGYDTVIGERGVKLSGGQRQRIAIARALLKDPPILILDE 164
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03251  165 ATSALDTESERLVQAALERLMK--NRTTFVIAH 195
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
23-202 6.82e-31

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 114.06  E-value: 6.82e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAAFR-----NKTLGFVFqsfhl 96
Cdd:COG4559   17 LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLtGEL-TPSSGEVRLNGRPLAAWSPWELARRRavlpqHSSLAFPF----- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 inslNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSH-RMRHMPTqLSGGQCQRVAIARAIV-------GNPEIILAD 168
Cdd:COG4559   91 ----TVEEVVALGRAPHGSSAAQDRQIVREALALVGLAHlAGRSYQT-LSGGEQQRVQLARVLAqlwepvdGGPRWLFLD 165
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:COG4559  166 EPTSALDLAHQHAVLRLARQLARR-GGGVVAVLH 198
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
22-223 8.86e-31

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 115.57  E-value: 8.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINGTSVESMKDKELAAFRnKTLGFVFQSfhLINSL 100
Cdd:PRK15079  36 AVDGVTLRLYEGETLGVVGESGCGKSTFARaIIGLVKA-TDGEVAWLGKDLLGMKDDEWRAVR-SDIQMIFQD--PLASL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 N----VIDNVELPL--LYRKMAAKERTRLAKEVLERVGLSHRM--RHmPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK15079 112 NprmtIGEIIAEPLrtYHPKLSRQEVKDRVKAMMLKVGLLPNLinRY-PHEFSGGQCQRIGIARALILEPKLIICDEPVS 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:PRK15079 191 ALDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISdRVLVMYLGHAVE 242
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
4-202 1.04e-30

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: 112.31  E-value: 1.04e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkdkelaafr 83
Cdd:cd03268    1 LKTNDLTKTYGKKR----VLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSY------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nktlgfvfqsFHLINSLNVIDN-VELPLLYRKMAAKERTRLA-----------KEVLERVGLSHRMRHMPTQLSGGQCQR 151
Cdd:cd03268   65 ----------QKNIEALRRIGAlIEAPGFYPNLTARENLRLLarllgirkkriDEVLDVVGLKDSAKKKVKGFSLGMKQR 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:cd03268  135 LGIALALLGNPDLLILDEPTNGLDPDGIKELRELILSLRDQ-GITVLISSH 184
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
4-222 1.37e-30

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


Pssm-ID: 213183 [Multi-domain]  Cd Length: 163  Bit Score: 110.60  E-value: 1.37e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKElaAF 82
Cdd:cd03216    1 LELRGITKRFG----GVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILsGLY-KPDSGEILVDGKEVSFASPRD--AR 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQsfhlinslnvidnvelpllyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNP 162
Cdd:cd03216   74 RAG-IAMVYQ---------------------------------------------------LSVGERQMVEIARALARNA 101
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTI---RffDGRQV 222
Cdd:cd03216  102 RLLILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVtvlR--DGRVV 161
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
22-216 1.43e-30

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 111.17  E-value: 1.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGtsvesmkdkelaafrNKTLGFVFQSFHLINSL 100
Cdd:NF040873   7 VLHGVDLTIPAGSLTAVVGPNGSGKSTLLKvLAGVL-RPTSGTVRRAG---------------GARVAYVPQRSEVPDSL 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 --NVIDNVELPL-----LYRKMAAKERTRLAkEVLERVGLsHRMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:NF040873  71 plTVRDLVAMGRwarrgLWRRLTRDDRAAVD-DALERVGL-ADLAGRQLGeLSGGQRQRALLAQGLAQEADLLLLDEPTT 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 173 NLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:NF040873 149 GLDAESRERIIALLAEE-HARGATVVVVTHDLELVRRADPCVLL 191
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
22-215 1.62e-30

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: 117.39  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKdkelAAFRNKTLGFVFQSFHLINSl 100
Cdd:TIGR02857 337 ALRPVSFTVPPGERVALVGPSGAGKSTLLNlLLGFVD-PTEGSIAVNGVPLADAD----ADSWRDQIAWVPQHPFLFAG- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  101 NVIDNVelpLLYRKMAAKERTRlakEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:TIGR02857 411 TIAENI---RLARPDASDAEIR---EALERAGLDEFVAALPqgldtpigeggAGLSGGQAQRLALARAFLRDAPLLLLDE 484
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 495112432  170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIR 215
Cdd:TIGR02857 485 PTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALAALADRIVV 528
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
22-202 2.43e-30

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: 111.93  E-value: 2.43e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELaafRNKtLGFVFQSFHLINSl 100
Cdd:cd03254   18 VLKDINFSIKPGETVAIVGPTGAGKTTLINlLMRFYD-PQKGQILIDGIDIRDISRKSL---RSM-IGVVLQDTFLFSG- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVelpLLYRKMAAKERTrlaKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:cd03254   92 TIMENI---RLGRPNATDEEV---IEAAKEAGAHDFIMKLPngydtvlgengGNLSQGERQLLAIARAMLRDPKILILDE 165
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03254  166 ATSNIDTETEKLIQEALEKLMK--GRTSIIIAH 196
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
20-203 4.47e-30

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 112.63  E-value: 4.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVESMKdKELAAFRnKTLGFVFQS-FHLI 97
Cdd:PRK13636  19 THALKGININIKKGEVTAILGGNGAGKSTLFqNLNGILK-PSSGRILFDGKPIDYSR-KGLMKLR-ESVGMVFQDpDNQL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHrMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PRK13636  96 FSASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEH-LKDKPTHcLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDP 174
                        170       180
                 ....*....|....*....|....*..
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK13636 175 MGVSEIMKLLVEMQKELGLTIIIATHD 201
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
13-222 6.20e-30

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: 110.37  E-value: 6.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELaafrNKTLGFVF 91
Cdd:cd03245   10 FSYPNQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKlLAGLYK-PTSGSVLLDGTDIRQLDPADL----RRNIGYVP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  92 QSFHLINSlNVIDNVELPLLY----RKMAAKERTRLAKEVLER-VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:cd03245   85 QDVTLFYG-TLRDNITLGAPLaddeRILRAAELAGVTDFVNKHpNGLDLQIGERGRGLSGGQRQAVALARALLNDPPILL 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 167 ADEPTGNLDskMGAEvMELLHKLNKE-DGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:cd03245  164 LDEPTSAMD--MNSE-ERLKERLRQLlGDKTLIIITHRPSLLDLVDRIIVMDSGRIV 217
cbiO PRK13649
energy-coupling factor transporter ATPase;
4-202 6.89e-30

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 112.15  E-value: 6.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRT-NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESM-KDKELAA 81
Cdd:PRK13649   3 INLQNVSYTYQAgTPFEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTsKNKDIKQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRnKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHM-PTQLSGGQCQRVAIARAIV 159
Cdd:PRK13649  83 IR-KKVGLVFQfPESQLFEETVLKDVAFGPQNFGVSQEEAEALAREKLALVGISESLFEKnPFELSGGQMRRVAIAGILA 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTH 202
Cdd:PRK13649 162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLH-QSGMTIVLVTH 203
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
19-209 1.04e-29

Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein component of a bacterial exporter complex that confers resistance to the antibiotics daunorubicin and doxorubicin. In addition to DrrA, the complex includes an integral membrane protein called DrrB. DrrA belongs to the ABC family of transporters and shares sequence and functional similarities with a protein found in cancer cells called P-glycoprotein. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region in addition to the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 109.77  E-value: 1.04e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdKELAAFRnKTLGFVFQSFHLIN 98
Cdd:cd03265   12 DFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR-RRIGIVFQDLSVDD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03265   87 ELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDEPTIGLDPQT 166
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 179 GAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ 209
Cdd:cd03265  167 RAHVWEYIEKLKEEFGMTILLTTHYMEEAEQ 197
cbiO PRK13643
energy-coupling factor transporter ATPase;
3-202 1.07e-29

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 111.75  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNE-IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESM-KDKELA 80
Cdd:PRK13643   1 MIKFEKVNYTYQPNSpFASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTsKQKEIK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKtLGFVFQ--SFHLINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRM-RHMPTQLSGGQCQRVAIARA 157
Cdd:PRK13643  81 PVRKK-VGVVFQfpESQLFEE-TVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGI 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTH 202
Cdd:PRK13643 159 LAMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTH 202
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
3-207 2.22e-29

ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of a single ATP-binding protein and a single integral membrane protein.


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 108.99  E-value: 2.22e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAF 82
Cdd:cd03266    1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEP---AEAR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNktLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03266   78 RR--LGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDP 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:cd03266  156 PVLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEV 199
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
23-203 6.63e-29

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


Pssm-ID: 213220 [Multi-domain]  Cd Length: 236  Bit Score: 108.09  E-value: 6.63e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELAAFRnKTLGFVFQSFHLINslnv 102
Cdd:cd03253   17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDG---QDIREVTLDSLR-RAIGVVPQDTVLFN---- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 iDNVELPLLYRKMAAKErtrlaKEVLE--RVGLSH-RMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:cd03253   89 -DTIGYNIRYGRPDATD-----EEVIEaaKAAQIHdKIMRFPdgydtivgergLKLSGGEKQRVAIARAILKNPPILLLD 162
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHN 203
Cdd:cd03253  163 EATSALDTHTEREIQAALRDVSK--GRTTIVIAHR 195
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
23-207 9.02e-29

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 108.56  E-value: 9.02e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSfHLI-NSLN 101
Cdd:PRK11231  18 LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLA----RRLALLPQH-HLTpEGIT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVE------LPlLYRKMAAKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK11231  93 VRELVAygrspwLS-LWGRLSAEDNARVNQ-AMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYLD 170
                        170       180       190
                 ....*....|....*....|....*....|..
gi 495112432 176 SKMGAEVMELLHKLNKEdGRTIVMVTHNEEQA 207
Cdd:PRK11231 171 INHQVELMRLMRELNTQ-GKTVVTVLHDLNQA 201
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
4-203 9.32e-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: 107.63  E-value: 9.32e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAfr 83
Cdd:cd03218    1 LRAENLSKRYGKRKV----VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRAR-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03218   75 -LGIGYLPQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:cd03218  154 FLLLDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHN 192
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
13-214 2.12e-28

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 106.72  E-value: 2.12e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKelaAFRnKTLGFVFQ 92
Cdd:PRK10247  15 YLAGD--AKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPE---IYR-QQVSYCAQ 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 SFHLINSlNVIDNVELPLLYRKMAAkERTRLAKEvLERVGLSHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK10247  89 TPTLFGD-TVYDNLIFPWQIRNQQP-DPAIFLDD-LERFALPDTILTKNiAELSGGEKQRISLIRNLQFMPKVLLLDEIT 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK10247 166 SALDESNKHNVNEIIHRYVREQNIAVLWVTHDKDEINHADKVI 208
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
22-219 4.18e-28

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 106.78  E-value: 4.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLL---NIMGLL--DAPSSGKIEINGTSVESMKdKELAAFRnKTLGFVFQS--- 93
Cdd:PRK14239  20 ALNSVSLDFYPNEITALIGPSGSGKSTLLrsiNRMNDLnpEVTITGSIVYNGHNIYSPR-TDTVDLR-KEIGMVFQQpnp 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 FHLINSLNVIDNVELPLLYRKM---AAKERTRLAKEVLERVglSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK14239  98 FPMSIYENVVYGLRLKGIKDKQvldEAVEKSLKGASIWDEV--KDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEP 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 171 TGNLDSKMGAEVMELLHKLnkEDGRTIVMVTHNEEQAKQTS-RTIRFFDG 219
Cdd:PRK14239 176 TSALDPISAGKIEETLLGL--KDDYTMLLVTRSMQQASRISdRTGFFLDG 223
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
22-203 4.80e-28

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 110.68  E-value: 4.80e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNimgLLD---APSSGKIEINGTSVESMKDKELAAfrnkTLGFVFQSFHLIN 98
Cdd:PRK11160 355 VLKGLSLQIKAGEKVALLGRTGCGKSTLLQ---LLTrawDPQQGEILLNGQPIADYSEAALRQ----AISVVSQRVHLFS 427
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 -SLNviDNVelpllyrKMAAKERT--RLAkEVLERVGLSH----------------RmrhmptQLSGGQCQRVAIARAIV 159
Cdd:PRK11160 428 aTLR--DNL-------LLAAPNASdeALI-EVLQQVGLEKlleddkglnawlgeggR------QLSGGEQRRLGIARALL 491
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHN 203
Cdd:PRK11160 492 HDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHR 533
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
22-202 6.67e-28

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: 110.28  E-value: 6.67e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDA--PSSGKIEIN-----------------------GTSVESMK- 75
Cdd:TIGR03269  15 VLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIIYHvalcekcgyverpskvgepcpvcGGTLEPEEv 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   76 ------DKELAAFRnKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQ 148
Cdd:TIGR03269  95 dfwnlsDKLRRRIR-KRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMVQLSHRITHIARDLSGGE 173
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 495112432  149 CQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR03269 174 KQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSH 227
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
19-202 1.07e-27

ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 (also known as ABCB6) is a mitochondrial ATP-binding cassette protein involved in iron homeostasis and one of four ABC transporters expressed in the mitochondrial inner membrane, the other three being MDL1(ABC7), MDL2, and ATM1. In fact, the yeast MDL1 (multidrug resistance-like protein 1) and MDL2 (multidrug resistance-like protein 2) transporters are also included in this CD. MDL1 is an ATP-dependent permease that acts as a high-copy suppressor of ATM1 and is thought to have a role in resistance to oxidative stress. Interestingly, subfamily B is more closely related to the carboxyl-terminal component of subfamily C than the two halves of ABCC molecules are with one another.


Pssm-ID: 213216 [Multi-domain]  Cd Length: 238  Bit Score: 105.31  E-value: 1.07e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTllnIMGLLD---APSSGKIEINGtsvESMKDKELAAFRNKtLGFVFQSFH 95
Cdd:cd03249   15 DVPILKGLSLTIPPGKTVALVGSSGCGKST---VVSLLErfyDPTSGEILLDG---VDIRDLNLRWLRSQ-IGLVSQEPV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERV-GLSHRMRHM----PTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:cd03249   88 LFDG-TIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDGYDTLvgerGSQLSGGQKQRIAIARALLRNPKILLLDEA 166
                        170       180       190
                 ....*....|....*....|....*....|..
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03249  167 TSALDAESEKLVQEALDRAMK--GRTTIVIAH 196
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
19-219 1.24e-27

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 105.60  E-value: 1.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQS--FHL 96
Cdd:PRK13648  21 ASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFEKL----RKHIGIVFQNpdNQF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 INSLNVIDnVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PRK13648  97 VGSIVKYD-VAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPSVIILDEATSMLDP 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PRK13648 176 DARQNLLDLVRKVKSEHNITIISITHDLSEAMEADHVIVMNKG 218
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
22-203 1.71e-27

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 106.73  E-value: 1.71e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLdaPSSGKIE----INGTSVESMKDKELAAFRNKTLGFVFQSfhL 96
Cdd:PRK09473  31 AVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLL--AANGRIGgsatFNGREILNLPEKELNKLRAEQISMIFQD--P 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 INSLNVIDNV-----ELPLLYRKMAAKERTRLAKEVLERVGLSH---RMRHMPTQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:PRK09473 107 MTSLNPYMRVgeqlmEVLMLHKGMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 495112432 169 EPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK09473 187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHD 221
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
19-211 1.81e-27

urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC transporter ATP-binding subunits associated with urea transport and metabolism. This protein is found in a conserved five-gene transport operon typically found adjacent to urease genes. It was shown in Cyanobacteria that disruption leads to the loss of high-affinity urea transport activity. [Transport and binding proteins, Amino acids, peptides and amines]


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 104.14  E-value: 1.81e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELAAfrnKTLGFVFQSFHLI 97
Cdd:TIGR03410  12 QSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKtLMGLLP-VKSGSIRLDGEDITKLPPHERAR---AGIAYVPQGREIF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   98 NSLNVIDNVELPLLYRKMAAKErtrLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:TIGR03410  88 PRLTVEENLLTGLAALPRRSRK---IPDEIYELFPVLKEMLGRRGgDLSGGQQQQLAIARALVTRPKLLLLDEPTEGIQP 164
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 495112432  177 KMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS 211
Cdd:TIGR03410 165 SIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELA 199
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
13-203 3.35e-27

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 108.25  E-value: 3.35e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDAPS----SGKIEINGTSVESMKDKELAAFRNKTL 87
Cdd:PRK15134  15 FRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPPvvypSGDIRFHGESLLHASEQTLRGVRGNKI 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  88 GFVFQsfHLINSLNVIDNVELPL-----LYRKMAAKERTRLAKEVLERVGLSH---RMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK15134  95 AMIFQ--EPMVSLNPLHTLEKQLyevlsLHRGMRREAARGEILNCLDRVGIRQaakRLTDYPHQLSGGERQRVMIAMALL 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK15134 173 TRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHN 216
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
23-223 3.92e-27

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 104.36  E-value: 3.92e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDK-ELAAFR-NKTLGFVFQSFHLINSL 100
Cdd:PRK14246  26 LKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKVLYFGKDIfQIDAIKlRKEVGMVFQQPNPFPHL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAK-ERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK14246 106 SIYDNIAYPLKSHGIKEKrEIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARALALKPKVLLMDEPTSMID 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 495112432 176 SKMGAEVMELLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRF-FDGRQVQ 223
Cdd:PRK14246 186 IVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFlYNGELVE 232
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
22-203 3.99e-27

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 105.59  E-value: 3.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDAP---SSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSfhLI 97
Cdd:PRK11022  22 AVDRISYSVKQGEVVGIVGESGSGKSvSSLAIMGLIDYPgrvMAEKLEFNGQDLQRISEKERRNLVGAEVAMIFQD--PM 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNVIDNVElpllYRKMAA---------KERTRLAKEVLERVGL---SHRMRHMPTQLSGGQCQRVAIARAIVGNPEII 165
Cdd:PRK11022 100 TSLNPCYTVG----FQIMEAikvhqggnkKTRRQRAIDLLNQVGIpdpASRLDVYPHQLSGGMSQRVMIAMAIACRPKLL 175
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 166 LADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11022 176 IADEPTTALDVTIQAQIIELLLELQQKENMALVLITHD 213
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
3-202 4.34e-27

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 107.81  E-value: 4.34e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLdAPSSGKIEINGTSVE--SMKDkel 79
Cdd:COG3845    5 ALELRGITKRFGG----VVANDDVSLTVRPGEIHALLGENGAGKSTLMKIlYGLY-QPDSGEILIDGKPVRirSPRD--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 aAFRNKtLGFVFQSFHLINSLNVIDNV-----ELPLLYRKMaAKERTRLaKEVLERVGLS---HRMRHmptQLSGGQCQR 151
Cdd:COG3845   77 -AIALG-IGMVHQHFMLVPNLTVAENIvlglePTKGGRLDR-KAARARI-RELSERYGLDvdpDAKVE---DLSVGEQQR 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 152 VAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG3845  150 VEILKALYRGARILILDEPTAVLTPQEADELFEILRRL-AAEGKSIIFITH 199
cbiO PRK13644
energy-coupling factor transporter ATPase;
3-222 5.87e-27

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 104.30  E-value: 5.87e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdAPSSGKIEINGtsVESMKDKELAA 81
Cdd:PRK13644   1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLaLHLNGLL-RPQKGKVLVSG--IDTGDFSKLQG 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRnKTLGFVFQSfhlINSLNVIDNVELPLLYRK----MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARA 157
Cdd:PRK13644  75 IR-KLVGIVFQN---PETQFVGRTVEEDLAFGPenlcLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGI 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNkEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:PRK13644 151 LTMEPECLIFDEVTSMLDPDSGIAVLERIKKLH-EKGKTIVYITHNLEELHDADRIIVMDRGKIV 214
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
19-202 7.63e-27

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


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 107.64  E-value: 7.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFrnktLGFVFQSFHLIN 98
Cdd:TIGR03375 477 ETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQIDPADLRRN----IGYVPQDPRLFY 552
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   99 -SLNviDNvelpLLYRKMAAKERTRLakEVLERVGLSHRMRHMPT-----------QLSGGQCQRVAIARAIVGNPEIIL 166
Cdd:TIGR03375 553 gTLR--DN----IALGAPYADDEEIL--RAAELAGVTEFVRRHPDgldmqigergrSLSGGQRQAVALARALLRDPPILL 624
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 495112432  167 ADEPTGNLDskMGAEvMELLHKLNKE-DGRTIVMVTH 202
Cdd:TIGR03375 625 LDEPTSAMD--NRSE-ERFKDRLKRWlAGKTLVLVTH 658
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
24-222 1.00e-26

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 103.14  E-value: 1.00e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLINSLNVI 103
Cdd:PRK10253  24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVA----RRIGLLAQNATTPGDITVQ 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNV------ELPLLYRkmAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:PRK10253 100 ELVargrypHQPLFTR--WRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDIS 177
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 495112432 178 MGAEVMELLHKLNKEDGRTIVMVTHNEEQA-KQTSRTIRFFDGRQV 222
Cdd:PRK10253 178 HQIDLLELLSELNREKGYTLAAVLHDLNQAcRYASHLIALREGKIV 223
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
20-222 3.07e-26

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 102.12  E-value: 3.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafRNKtLGFVFQS-FHLIN 98
Cdd:PRK13647  18 TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWV---RSK-VGLVFQDpDDQVF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:PRK13647  94 SSTVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDPDVIVLDEPMAYLDPRG 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 179 GAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:PRK13647 174 QETLMEILDRLHNQ-GKTVIVATHDVDLAAEwADQVIVLKEGRVL 217
type_I_sec_HlyB TIGR01846
type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in ...
4-223 5.27e-26

type I secretion system ABC transporter, HlyB family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273831 [Multi-domain]  Cd Length: 694  Bit Score: 105.21  E-value: 5.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    4 IKLTGINKIYRTNEIETLAleNVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafr 83
Cdd:TIGR01846 456 ITFENIRFRYAPDSPEVLS--NLNLDIKPGEFIGIVGPSGSGKSTLTKLLQRLYTPQHGQVLVDGVDLAIADPAWL---- 529
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   84 NKTLGFVFQSFHLINSlNVIDNVELPllyRKMAAKERTRLAKEVLERVGLSHRMRHMPTQ--------LSGGQCQRVAIA 155
Cdd:TIGR01846 530 RRQMGVVLQENVLFSR-SIRDNIALC---NPGAPFEHVIHAAKLAGAHDFISELPQGYNTevgekganLSGGQRQRIAIA 605
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432  156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:TIGR01846 606 RALVGNPRILIFDEATSALDYESEALIMRNMREICR--GRTVIIIAHRLSTVRACDRIIVLEKGQIAE 671
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
21-220 7.05e-26

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 101.01  E-value: 7.05e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLD-----APSSGKIEINGTSVESmKDKELAAFRNKtLGFVFQSFH 95
Cdd:PRK14243  24 LAVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNdlipgFRVEGKVTFHGKNLYA-PDVDPVEVRRR-IGMVFQKPN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LInSLNVIDNVEL------------PLLYRKMAAKERTRLAKEVLERVGLShrmrhmptqLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK14243 102 PF-PKSIYDNIAYgaringykgdmdELVERSLRQAALWDEVKDKLKQSGLS---------LSGGQQQRLCIARAIAVQPE 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLnKEDgRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK14243 172 VILMDEPCSALDPISTLRIEELMHEL-KEQ-YTIIIVTHNMQQAARVSDMTAFFNVE 226
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
33-218 1.07e-25

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 104.36  E-value: 1.07e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   33 GEFVSIMGPSGCGKSTLLNIMGLLDAPS---SGKIEINGTSVESMKDKELAAFrnktlgfVFQSFHLINSLNVIDN---- 105
Cdd:TIGR00955  51 GELLAVMGSSGAGKTTLMNALAFRSPKGvkgSGSVLLNGMPIDAKEMRAISAY-------VQQDDLFIPTLTVREHlmfq 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  106 --VELPllyRKMAAKERTRLAKEVLERVGLS----------HRMRhmptQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:TIGR00955 124 ahLRMP---RRVTKKEKRERVDEVLQALGLRkcantrigvpGRVK----GLSGGERKRLAFASELLTDPPLLFCDEPTSG 196
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 495112432  174 LDSKMGAEVMELLHKL-NKedGRTIVMVTHneeqaKQTSRTIRFFD 218
Cdd:TIGR00955 197 LDSFMAYSVVQVLKGLaQK--GKTIICTIH-----QPSSELFELFD 235
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
17-202 1.87e-25

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: 97.77  E-value: 1.87e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  17 EIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKelaafRNKTLGFVFQSFH 95
Cdd:cd03247   12 EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQlLTGDLK-PQQGEITLDGVPVSDLEKA-----LSSLISVLNQRPY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSlnvidnvelpllyrkmaakertrlakEVLERVGlshrmrhmpTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:cd03247   86 LFDT--------------------------TLRNNLG---------RRFSGGERQRLALARILLQDAPIVLLDEPTVGLD 130
                        170       180
                 ....*....|....*....|....*..
gi 495112432 176 SKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:cd03247  131 PITERQLLSLIFEVLKD--KTLIWITH 155
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
6-202 3.22e-25

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 102.45  E-value: 3.22e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   6 LTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINgtsvesmkdkelaafRNK 85
Cdd:COG0488    1 LENLSKSFGGRPL----LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIP---------------KGL 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  86 TLGFVFQSFHLINSLNVIDNV------------ELPLLYRKMAAKER-----TRL---------------AKEVLERVGL 133
Cdd:COG0488   62 RIGYLPQEPPLDDDLTVLDTVldgdaelraleaELEELEAKLAEPDEdlerlAELqeefealggweaearAEEILSGLGF 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 134 SHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDskmgAEVMELLHK-LNKEDGrTIVMVTH 202
Cdd:COG0488  142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLD----LESIEWLEEfLKNYPG-TVLVVSH 207
cbiO PRK13640
energy-coupling factor transporter ATPase;
22-220 5.25e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 99.10  E-value: 5.25e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKST---LLNIMGLLDAPSSGKIEINGTSVESmkdKELAAFRNKtLGFVFQsfhliN 98
Cdd:PRK13640  22 ALNDISFSIPRGSWTALIGHNGSGKSTiskLINGLLLPDDNPNSKITVDGITLTA---KTVWDIREK-VGIVFQ-----N 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK13640  93 PDNqfvgatVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPKIIILDESTS 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 495112432 173 NLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK13640 173 MLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEANMADQVLVLDDGK 220
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
4-222 5.92e-25

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: 97.35  E-value: 5.92e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLdAPSSGKIEINGTSVEsmkdkelAAF 82
Cdd:cd03269    1 LEVENVTKRFGRVT----ALDDISFSVEKGEIFGLLGPNGAGKTTTIrMILGII-LPDSGEVLFDGKPLD-------IAA 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKtLGFVFQSFHLINSLNVIDNvelpLLY----RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI 158
Cdd:cd03269   69 RNR-IGYLPEERGLYPKMKVIDQ----LVYlaqlKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAV 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 159 VGNPEIILADEPTGNLDSkMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQ-TSRTIRFFDGRQV 222
Cdd:cd03269  144 IHDPELLILDEPFSGLDP-VNVELLKDVIRELARAGKTVILSTHQMELVEElCDRVLLLNKGRAV 207
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
9-203 8.21e-25

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 101.86  E-value: 8.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   9 INKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRnKTLG 88
Cdd:PRK10261 330 LNRVTR----EVHAVEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTLSPGKLQALR-RDIQ 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  89 FVFQSFH--LINSLNVIDNVELPL-LYRKMAAKERTRLAKEVLERVGL--SHRMRHmPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK10261 405 FIFQDPYasLDPRQTVGDSIMEPLrVHGLLPGKAAAARVAWLLERVGLlpEHAWRY-PHEFSGGQRQRICIARALALNPK 483
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10261 484 VIIADEAVSALDVSIRGQIINLLLDLQRDFGIAYLFISHD 523
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
4-203 9.47e-25

ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; NatA is the ATPase component of a bacterial ABC-type Na+ transport system called NatAB, which catalyzes ATP-dependent electrogenic Na+ extrusion without mechanically coupled to proton or K+ uptake. NatB possess six putative membrane spanning regions at its C-terminus. In B. subtilis, NatAB is inducible by agents such as ethanol and protonophores, which lower the proton-motive force across the membrane. The closest sequence similarity to NatA is exhibited by DrrA of the two-component daunorubicin- and doxorubicin-efflux system. Hence, the functional NatAB is presumably assembled with two copies of the single ATP-binding protein and the single integral membrane protein.


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 97.40  E-value: 9.47e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNE-----IETL------------ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI 66
Cdd:cd03267    1 IEVSNLSKSYRVYSkepglIGSLkslfkrkyreveALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  67 NGTSVESMKDKELaafrnKTLGFVF-QSFHLINSLNVIDNVEL-PLLYRKMAAKERTRLAK--EVLErvgLSHRMRHMPT 142
Cdd:cd03267   81 AGLVPWKRRKKFL-----RRIGVVFgQKTQLWWDLPVIDSFYLlAAIYDLPPARFKKRLDElsELLD---LEELLDTPVR 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:cd03267  153 QLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENIRNFLKEYNRERGTTVLLTSHY 213
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
22-203 1.04e-24

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 101.32  E-value: 1.04e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdaPSSGKIEINGTSVESMKDKELAAFRNKtLGFVFQSFHliNSL 100
Cdd:PRK15134 301 VVKNISFTLRPGETLGLVGESGSGKSTTgLALLRLI--NSQGEIWFDGQPLHNLNRRQLLPVRHR-IQVVFQDPN--SSL 375
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVE------LPLLYRKMAAKERTRLAKEVLERVGLSHRMRH-MPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK15134 376 NPRLNVLqiieegLRVHQPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTSS 455
                        170       180       190
                 ....*....|....*....|....*....|
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK15134 456 LDKTVQAQILALLKSLQQKHQLAYLFISHD 485
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
21-218 1.67e-24

White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ABC transporters homologous to the Drosophila white gene, which acts as a dimeric importer for eye pigment precursors. The eye pigmentation of Drosophila is developed from the synthesis and deposition in the cells of red pigments, which are synthesized from guanine, and brown pigments, which are synthesized from tryptophan. The pigment precursors are encoded by the white, brown, and scarlet genes, respectively. Evidence from genetic and biochemical studies suggest that the White and Brown proteins function as heterodimers to import guanine, while the White and Scarlet proteins function to import tryptophan. However, a recent study also suggests that White may be involved in the transport of a metabolite, such as 3-hydroxykynurenine, across intracellular membranes. Mammalian ABC transporters belonging to the White subfamily (ABCG1, ABCG5, and ABCG8) have been shown to be involved in the regulation of lipid-trafficking mechanisms in macrophages, hepatocytes, and intestinal mucosa cells. ABCG1 (ABC8), the human homolog of the Drosophila white gene is induced in monocyte-derived macrophages during cholesterol influx mediated by acetylated low-density lipoprotein. It is possible that human ABCG1 forms heterodimers with several heterologous partners.


Pssm-ID: 213201 [Multi-domain]  Cd Length: 226  Bit Score: 96.57  E-value: 1.67e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPS--SGKIEINGtsVESMKDKELaafrnKTLGFVFQSFHLI 97
Cdd:cd03234   21 RILNDVSLHVESGQVMAILGSSGSGKTTLLDaISGRVEGGGttSGQILFNG--QPRKPDQFQ-----KCVAYVRQDDILL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNV------IDNVELPllyRKMAAKERT-RLAKEVLERVGLShRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:cd03234   94 PGLTVretltyTAILRLP---RKSSDAIRKkRVEDVLLRDLALT-RIGGNLvKGISGGERRRVSIAVQLLWDPKVLILDE 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 495112432 170 PTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHneeqaKQTSRTIRFFD 218
Cdd:cd03234  170 PTSGLDSFTALNLVSTLSQLARR-NRIVILTIH-----QPRSDLFRLFD 212
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
21-203 1.79e-24

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 96.98  E-value: 1.79e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrNKTLGFVFQSFHLINSL 100
Cdd:PRK11300  19 LAVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIA---RMGVVRTFQHVRLFREM 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDN--------VELPLL--------YRKmAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEI 164
Cdd:PRK11300  96 TVIENllvaqhqqLKTGLFsgllktpaFRR-AESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEI 174
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495112432 165 ILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK11300 175 LMLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHD 213
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-170 2.02e-24

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 96.64  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESmkdkeL 79
Cdd:COG1137    1 MMTLEAENLVKSYGKRTV----VKDVSLEVNQGEIVGLLGPNGAGKTTTFYmIVGLV-KPDSGRIFLDGEDITH-----L 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 AAFRNKTLGF--------VFQSfhlinsLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQR 151
Cdd:COG1137   71 PMHKRARLGIgylpqeasIFRK------LTVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRR 144
                        170
                 ....*....|....*....
gi 495112432 152 VAIARAIVGNPEIILADEP 170
Cdd:COG1137  145 VEIARALATNPKFILLDEP 163
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
16-220 2.89e-24

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: 95.23  E-value: 2.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  16 NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTsvesmkdkelaafrnktLGFVFQSF 94
Cdd:cd03250   14 EQETSFTLKDINLEVPKGELVAIVGPVGSGKSSLLSaLLGELE-KLSGSVSVPGS-----------------IAYVSQEP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  95 HLINSlNVIDNVelpLLYRKMAaKERTrlaKEVLERVGLSHRMRHMP----TQ-------LSGGQCQRVAIARAIVGNPE 163
Cdd:cd03250   76 WIQNG-TIRENI---LFGKPFD-EERY---EKVIKACALEPDLEILPdgdlTEigekginLSGGQKQRISLARAVYSDAD 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 164 IILADEPTGNLDSKMGAEVME--LLHKLnkEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:cd03250  148 IYLLDDPLSAVDAHVGRHIFEncILGLL--LNNKTRILVTHQLQLLPHADQIVVLDNGR 204
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
4-223 3.27e-24

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: 96.02  E-value: 3.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkELAAFR 83
Cdd:cd03252    1 ITFEHVRFRYKPDG--PVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLR 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nKTLGFVFQSFHLINSlNVIDNVELPllyRKMAAKERTrlaKEVLERVGLSHRMRHMP-----------TQLSGGQCQRV 152
Cdd:cd03252   76 -RQVGVVLQENVLFNR-SIRDNIALA---DPGMSMERV---IEAAKLAGAHDFISELPegydtivgeqgAGLSGGQRQRI 147
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 495112432 153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNkeDGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:cd03252  148 AIARALIHNPRILIFDEATSALDYESEHAIMRNMHDIC--AGRTVIIIAHRLSTVKNADRIIVMEKGRIVE 216
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
23-223 3.92e-24

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 96.70  E-value: 3.92e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSG-----KIEINGTSVESMKDkeLAAFRNKtLGFVFQSFHLI 97
Cdd:PRK14271  37 LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGyrysgDVLLGGRSIFNYRD--VLEFRRR-VGMLFQRPNPF 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 nSLNVIDNVELPLLYRKMAAKERTR-LAKEVLERVGL----SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:PRK14271 114 -PMSIMDNVLAGVRAHKLVPRKEFRgVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTS 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 173 NLDSKMGAEVMELLHKLnkEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:PRK14271 193 ALDPTTTEKIEEFIRSL--ADRLTVIIVTHNLAQAARISdRAALFFDGRLVE 242
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
20-223 7.43e-24

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 98.76  E-value: 7.43e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdaPSSGKIEINGtsVEsMKDKELAAFRnKTLGFVFQSFHLIN 98
Cdd:PRK11174 363 KTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNaLLGFL--PYQGSLKING--IE-LRELDPESWR-KHLSWVGQNPQLPH 436
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SlNVIDNVelpLLYRKMAAKERTRLA------KEVLERV--GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK11174 437 G-TLRDNV---LLGNPDASDEQLQQAlenawvSEFLPLLpqGLDTPIGDQAAGLSVGQAQRLALARALLQPCQLLLLDEP 512
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:PRK11174 513 TASLDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQWDQIWVMQDGQIVQ 563
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-220 1.16e-23

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 95.57  E-value: 1.16e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELA 80
Cdd:PRK13650   2 SNIIEVKNLTFKYKEDQ-EKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDG---DLLTEENVW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKtLGFVFQsfhliNSLN------VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAI 154
Cdd:PRK13650  78 DIRHK-IGMVFQ-----NPDNqfvgatVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAI 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495112432 155 ARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:PRK13650 152 AGAVAMRPKIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVALSDRVLVMKNGQ 217
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
3-207 2.59e-23

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 94.79  E-value: 2.59e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLdAPSSGKIEINGtsvESMKDKELAA 81
Cdd:COG4152    1 MLELKGLTKRFG----DKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIrIILGIL-APDSGEVLWDG---EPLDPEDRRR 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FrnktlGFvfqsfhlinslnvidnveLPL---LYRKM------------------AAKERtrlAKEVLERVGLSHRMRHM 140
Cdd:COG4152   73 I-----GY------------------LPEergLYPKMkvgeqlvylarlkglskaEAKRR---ADEWLERLGLGDRANKK 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 141 PTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSkMGAEVM-ELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:COG4152  127 VEELSKGNQQKVQLIAALLHDPELLILDEPFSGLDP-VNVELLkDVIREL-AAKGTTVIFSSHQMELV 192
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
23-203 3.61e-23

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 93.37  E-value: 3.61e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdaPSSGKIEINGTSVESMKDKELAAFR-----NKTLGFVFQSFHL 96
Cdd:COG4138   12 LGPISAQVNAGELIHLIGPNGAGKSTLLARMaGLL--PGQGEILLNGRPLSDWSAAELARHRaylsqQQSPPFAMPVFQY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 InSLNvidnvelplLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV-----GNPE--IILADE 169
Cdd:COG4138   90 L-ALH---------QPAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLLqvwptINPEgqLLLLDE 159
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495112432 170 PTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG4138  160 PMNSLDVAQQAALDRLLREL-CQQGITVVMSSHD 192
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
4-221 3.99e-23

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 93.56  E-value: 3.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTL---LNIMGLLDAPS--SGKIEINGTSVESMKdKE 78
Cdd:PRK14258   8 IKVNNLSFYYDTQKI----LEGVSMEIYQSKVTAIIGPSGCGKSTFlkcLNRMNELESEVrvEGRVEFFNQNIYERR-VN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  79 LAAFRnKTLGFVFQSFHLInSLNVIDNVELPLLYRKMAAK-ERTRLAKEVLERVGL----SHRMRHMPTQLSGGQCQRVA 153
Cdd:PRK14258  83 LNRLR-RQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWRPKlEIDDIVESALKDADLwdeiKHKIHKSALDLSGGQQQRLC 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQ 221
Cdd:PRK14258 161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGNE 228
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
1-223 4.20e-23

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 96.52  E-value: 4.20e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTneieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkdkela 80
Cdd:PRK11288   2 SPYLSFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEM--------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKTLGF------VFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEV---LERVGL----SHRMRHmptqLSGG 147
Cdd:PRK11288  69 RFASTTAALaagvaiIYQELHLVPEMTVAENLYLGQLPHKGGIVNRRLLNYEAreqLEHLGVdidpDTPLKY----LSIG 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 148 QCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQVQ 223
Cdd:PRK11288 145 QRQMVEIAKALARNARVIAFDEPTSSLSAREIEQLFRVIREL-RAEGRVILYVSHRMEEIFALCDAITVFkDGRYVA 220
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
19-206 4.66e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 94.53  E-value: 4.66e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI----------NGTSVESMKDKELAAFRN--KT 86
Cdd:PRK13631  38 ELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVgdiyigdkknNHELITNPYSKKIKNFKElrRR 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  87 LGFVFQ--SFHLINslnviDNVELPLLYRKMA---AKERTR-LAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK13631 118 VSMVFQfpEYQLFK-----DTIEKDIMFGPVAlgvKKSEAKkLAKFYLNKMGLDDSyLERSPFGLSGGQKRRVAIAGILA 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLhKLNKEDGRTIVMVTHNEEQ 206
Cdd:PRK13631 193 IQPEILIFDEPTAGLDPKGEHEMMQLI-LDAKANNKTVFVITHTMEH 238
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
3-203 9.76e-23

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 93.61  E-value: 9.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNE-----------------IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKI 64
Cdd:COG4586    1 IIEVENLSKTYRVYEkepglkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLtGIL-VPTSGEV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  65 EINGTsVESMKDKELAafrnKTLGFVF-QSFHLINSLNVIDNVELpllYRKM----AAKERTRLaKEVLERVGLSHRMrH 139
Cdd:COG4586   80 RVLGY-VPFKRRKEFA----RRIGVVFgQRSQLWWDLPAIDSFRL---LKAIyripDAEYKKRL-DELVELLDLGELL-D 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 140 MPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:COG4586  150 TPVrQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHD 214
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
22-202 2.15e-22

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 91.53  E-value: 2.15e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTL-----GFVFQsfHL 96
Cdd:PRK11701  21 GCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRDGQLRDLYALSEAERRRLlrtewGFVHQ--HP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 INSL--------NVIDnvelpllyRKMAAKER-----TRLAKEVLERVGL-SHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:PRK11701  99 RDGLrmqvsaggNIGE--------RLMAVGARhygdiRATAGDWLERVEIdAARIDDLPTTFSGGMQQRLQIARNLVTHP 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11701 171 RLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTH 210
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
15-214 2.53e-22

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 92.66  E-value: 2.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  15 TNEIET-----LALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAP---SSGKIEINGTSVESMKDKELAAFRNK 85
Cdd:COG4170   10 TIEIDTpqgrvKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKDNwhvTADRFRWNGIDLLKLSPRERRKIIGR 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  86 TLGFVFQsfHLINSLN-----------VIDNVEL--PLLYRKMAAKERtrlAKEVLERVGL-SHR--MRHMPTQLSGGQC 149
Cdd:COG4170   90 EIAMIFQ--EPSSCLDpsakigdqlieAIPSWTFkgKWWQRFKWRKKR---AIELLHRVGIkDHKdiMNSYPHELTEGEC 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 150 QRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:COG4170  165 QKVMIAMAIANQPRLLIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTI 229
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
4-223 2.72e-22

lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide chain transporter in the ATP-binding cassette (ABC) transporter family, MsbA, which exports lipid A. It may also act in multidrug resistance. Lipid A, a part of lipopolysaccharide, is found in the outer leaflet of the outer membrane of most Gram-negative bacteria. Members of this family are restricted to the Proteobacteria (although lipid A is more broadly distributed) and often are clustered with lipid A biosynthesis genes. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 94.40  E-value: 2.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    4 IKLTGINKIYRTNEIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkDKELAAFR 83
Cdd:TIGR02203 331 VEFRNVTFRYPGRDRP--ALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLA---DYTLASLR 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   84 NKtLGFVFQSFHLINSlNVIDNVElpllYRKMAAKERTRL--------AKEVLERV--GLSHRMRHMPTQLSGGQCQRVA 153
Cdd:TIGR02203 406 RQ-VALVSQDVVLFND-TIANNIA----YGRTEQADRAEIeralaaayAQDFVDKLplGLDTPIGENGVLLSGGQRQRLA 479
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  154 IARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:TIGR02203 480 IARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEKADRIVVMDDGRIVE 547
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
38-203 3.36e-22

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 92.63  E-value: 3.36e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  38 IMGPSGCGKSTLLNIMGLLDAPSSGKIEING-TSVESMKDKELAAFRNKtLGFVFQSFHLINSLNVIDNvelpLLYrKMA 116
Cdd:PRK11144  29 IFGRSGAGKTSLINAISGLTRPQKGRIVLNGrVLFDAEKGICLPPEKRR-IGYVFQDARLFPHYKVRGN----LRY-GMA 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 117 AKERTRLAKeVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRT 196
Cdd:PRK11144 103 KSMVAQFDK-IVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKRELLPYLERLAREINIP 181

                 ....*..
gi 495112432 197 IVMVTHN 203
Cdd:PRK11144 182 ILYVSHS 188
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
23-202 3.90e-22

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: 93.66  E-value: 3.90e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKELAAFrnktLGFVFQSFHL----- 96
Cdd:COG4618  348 LRGVSFSLEPGEVLGVIGPSGSGKSTLARLLvGVW-PPTAGSVRLDGADLSQWDREELGRH----IGYLPQDVELfdgti 422
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 ---------INSLNVIDnvelpllyrkmAAKertrlakevleRVGLsHRM-RHMP-----------TQLSGGQCQRVAIA 155
Cdd:COG4618  423 aeniarfgdADPEKVVA-----------AAK-----------LAGV-HEMiLRLPdgydtrigeggARLSGGQRQRIGLA 479
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG4618  480 RALYGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITH 525
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
3-203 7.09e-22

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 92.94  E-value: 7.09e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    3 MIKLTGINKIYRTNEIETL-ALENVNLDVIKGEFVSIMGPSGCGKSTLLNI-MGLLDaPSSGKIEIN-GTSVESMKDK-- 77
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVVkAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIiAGVLE-PTSGEVNVRvGDEWVDMTKPgp 357
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   78 ELAAFRNKTLGFVFQSFHLINSLNVIDN------VELPLLYRKMAAKERTRL-------AKEVLERvglshrmrhMPTQL 144
Cdd:TIGR03269 358 DGRGRAKRYIGILHQEYDLYPHRTVLDNlteaigLELPDELARMKAVITLKMvgfdeekAEEILDK---------YPDEL 428
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432  145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:TIGR03269 429 SEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHD 487
cbiO PRK13645
energy-coupling factor transporter ATPase;
19-206 1.71e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 90.07  E-value: 1.71e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVES--MKDKELAAFRnKTLGFVFQ--SF 94
Cdd:PRK13645  23 EFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVKRLR-KEIGLVFQfpEY 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  95 HLINSlNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHR-MRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK13645 102 QLFQE-TIEKDIAFGPVNLGENKQEAYKKVPELLKLVQLPEDyVKRSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGG 180
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQ 206
Cdd:PRK13645 181 LDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQ 213
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
22-202 2.46e-21

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 91.38  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkDKELAAfrNKTLGFVFQSFHLINSLN 101
Cdd:PRK09700  20 ALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKL-DHKLAA--QLGIGIIYQELSVIDELT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVEL-PLLYRKMAA------KERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK09700  97 VLENLYIgRHLTKKVCGvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSL 176
                        170       180
                 ....*....|....*....|....*...
gi 495112432 175 DSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:PRK09700 177 TNKEVDYLFLIMNQLRKE-GTAIVYISH 203
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1-203 2.62e-21

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 89.09  E-value: 2.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNeieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELa 80
Cdd:PRK13652   1 MHLIETRDLCYSYSGS---KEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREV- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afrNKTLGFVFQ-SFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK13652  77 ---RKFVGLVFQnPDDQIFSPTVEQDIAFGPINLGLDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK13652 154 MEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQ 197
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
22-207 4.43e-21

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: 91.23  E-value: 4.43e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkdkELAAFRnKTLGFVFQSFHLINSLN 101
Cdd:TIGR01257  945 AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIET----NLDAVR-QSLGMCPQHNILFHHLT 1019
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   102 VIDNVelpLLYRKMAAK--ERTRLAKE-VLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:TIGR01257 1020 VAEHI---LFYAQLKGRswEEAQLEMEaMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYS 1096
                          170       180
                   ....*....|....*....|....*....
gi 495112432   179 GAEVMELLhkLNKEDGRTIVMVTHNEEQA 207
Cdd:TIGR01257 1097 RRSIWDLL--LKYRSGRTIIMSTHHMDEA 1123
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
19-207 5.09e-21

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 89.90  E-value: 5.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLIN 98
Cdd:PRK09536  15 DTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARAAS----RRVASVPQDTSLSF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVEL---PLLYRKMAAKERTRLA-KEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK09536  91 EFDVRQVVEMgrtPHRSRFDTWTETDRAAvERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASL 170
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 175 DSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:PRK09536 171 DINHQVRTLELVRRL-VDDGKTAVAAIHDLDLA 202
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
1-203 6.77e-21

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 87.26  E-value: 6.77e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELA 80
Cdd:PRK10895   1 MATLTAKNLAKAYKGRRV----VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afrNKTLGFVFQSFHLINSLNVIDNVELPLLYRK-MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK10895  77 ---RRGIGYLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALA 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:PRK10895 154 ANPKFILLDEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHN 196
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
4-220 7.14e-21

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: 86.82  E-value: 7.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNE------------------IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIE 65
Cdd:cd03220    1 IELENVSKSYPTYKggssslkklgilgrkgevGEFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  66 INGTSVESMkdkELAAFrnktlgfvfqsFHliNSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMrHMPT-QL 144
Cdd:cd03220   81 VRGRVSSLL---GLGGG-----------FN--PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFI-DLPVkTY 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDGR 220
Cdd:cd03220  144 SSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLREL-LKQGKTVILVSHDPSSIKRLcDRALVLEKGK 219
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-223 7.90e-21

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 87.06  E-value: 7.90e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MA-MIKLTGINKIYRTNEI------------------ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSS 61
Cdd:COG1134    1 MSsMIEVENVSKSYRLYHEpsrslkelllrrrrtrreEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  62 GKIEINGtSVESMkdkeLAafrnktLGFVFQsfhliNSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMrHMP 141
Cdd:COG1134   81 GRVEVNG-RVSAL----LE------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFI-DQP 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 142 TQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQT-SRTIRFFDG 219
Cdd:COG1134  144 VKtYSSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLcDRAIWLEKG 222

                 ....
gi 495112432 220 RQVQ 223
Cdd:COG1134  223 RLVM 226
CP_lyasePhnK TIGR02323
phosphonate C-P lyase system protein PhnK; Members of this family are the PhnK protein of C-P ...
25-223 1.17e-20

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


Pssm-ID: 188208 [Multi-domain]  Cd Length: 253  Bit Score: 86.81  E-value: 1.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEI---NGTSVE--SMKDKELAAFRNKTLGFVFQsfHLINS 99
Cdd:TIGR02323  21 DVSFDLYPGEVLGIVGESGSGKSTLLGCLAGRLAPDHGTATYimrSGAELElyQLSEAERRRLMRTEWGFVHQ--NPRDG 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  100 LNVIDNVELPLLYRKMAAKER-----TRLAKEVLERVGLS-HRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:TIGR02323  99 LRMRVSAGANIGERLMAIGARhygniRATAQDWLEEVEIDpTRIDDLPRAFSGGMQQRLQIARNLVTRPRLVFMDEPTGG 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495112432  174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS-RTIRFFDGRQVQ 223
Cdd:TIGR02323 179 LDVSVQARLLDLLRGLVRDLGLAVIIVTHDLGVARLLAqRLLVMQQGRVVE 229
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
22-223 1.42e-20

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 89.25  E-value: 1.42e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQSFHLINSlN 101
Cdd:PRK13657 350 GVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTVT---RASLR-RNIAVVFQDAGLFNR-S 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPllyRKMAAKERTRLAKEV------LER--VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK13657 425 IEDNIRVG---RPDATDEEMRAAAERaqahdfIERkpDGYDTVVGERGRQLSGGERQRLAIARALLKDPPILILDEATSA 501
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 174 LDSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:PRK13657 502 LDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRNADRILVFDNGRVVE 549
cbiO PRK13642
energy-coupling factor transporter ATPase;
23-214 3.94e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 85.91  E-value: 3.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDKELAAFRNKtLGFVFQS-FHLINSLN 101
Cdd:PRK13642  23 LNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDG---ELLTAENVWNLRRK-IGMVFQNpDNQFVGAT 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK13642  99 VEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGRQE 178
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 182 VMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK13642 179 IMRVIHEIKEKYQLTVLSITHDLDEAASSDRIL 211
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
23-202 5.49e-20

type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in some Gram-negative bacteria to export proteins (often proteases) across both inner and outer membranes to the extracellular medium. This is one of three proteins of the type I secretion apparatus. Targeted proteins are not cleaved at the N-terminus, but rather carry signals located toward the extreme C-terminus to direct type I secretion. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 87.79  E-value: 5.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkDKElaaFRNKTLGFVFQSFHLI----- 97
Cdd:TIGR01842 334 LRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQW-DRE---TFGKHIGYLPQDVELFpgtva 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   98 -NSLNVIDNVElpllYRKMAAKERTRLAKEVLERV--GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:TIGR01842 410 eNIARFGENAD----PEKIIEAAKLAGVHELILRLpdGYDTVIGPGGATLSGGQRQRIALARALYGDPKLVVLDEPNSNL 485
                         170       180
                  ....*....|....*....|....*...
gi 495112432  175 DSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:TIGR01842 486 DEEGEQALANAIKAL-KARGITVVVITH 512
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
22-201 1.30e-19

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


Pssm-ID: 213182 [Multi-domain]  Cd Length: 182  Bit Score: 82.48  E-value: 1.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLlDAPSSGKIEINGtsvESMKDKELAAFRNKTLGFVFQSFH---LI 97
Cdd:cd03215   15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEaLFGL-RPPASGEITLDG---KPVTRRSPRDAIRAGIAYVPEDRKregLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNVIDNVELPLLyrkmaakertrlakevlervglshrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:cd03215   91 LDLSVAENIALSSL--------------------------------LSGGNQQKVVLARWLARDPRVLILDEPTRGVDVG 138
                        170       180
                 ....*....|....*....|....
gi 495112432 178 MGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:cd03215  139 AKAEIYRLIREL-ADAGKAVLLIS 161
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
19-210 2.55e-19

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: 82.02  E-value: 2.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkdkELAAFRNKTLGFVFQSFHLIN 98
Cdd:TIGR01189  12 ERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHENILYLGHLPGLKP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   99 SLNVIDNVELpllYRKMAAKERtRLAKEVLERVGLSHRmRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDsK 177
Cdd:TIGR01189  87 ELSALENLHF---WAAIHGGAQ-RTIEDALAAVGLTGF-EDLPAaQLSAGQQRRLALARLWLSRRPLWILDEPTTALD-K 160
                         170       180       190
                  ....*....|....*....|....*....|...
gi 495112432  178 MGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQT 210
Cdd:TIGR01189 161 AGVALLAGLLRAHLARGGIVLLTTHQDLGLVEA 193
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
23-202 3.08e-19

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 83.06  E-value: 3.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdaPSSGKIEINGTSVESMKDKELAAFR-----NKTLGF---VFQ- 92
Cdd:PRK03695  12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMaGLL--PGSGSIQFAGQPLEAWSAAELARHRaylsqQQTPPFampVFQy 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 -SFHLiNSLNVIDNVELPLlyrkmaakertrlaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI-----VGNPE--I 164
Cdd:PRK03695  90 lTLHQ-PDKTRTEAVASAL--------------NEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVVlqvwpDINPAgqL 154
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 165 ILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:PRK03695 155 LLLDEPMNSLDVAQQAALDRLLSEL-CQQGIAVVMSSH 191
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
19-202 3.56e-19

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 85.46  E-value: 3.56e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmKDKELAAFRNKtLGFVFQSFHLIN 98
Cdd:PRK11176 355 EVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDL---RDYTLASLRNQ-VALVSQNVHLFN 430
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 slnviDNVELPLLYrkmAAKER-TRlaKEVLERVGLSHRM---RHMP-----------TQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK11176 431 -----DTIANNIAY---ARTEQySR--EQIEEAARMAYAMdfiNKMDngldtvigengVLLSGGQRQRIAIARALLRDSP 500
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:PRK11176 501 ILILDEATSALDTESERAIQAALDELQKN--RTSLVIAH 537
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
16-205 4.28e-19

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 81.93  E-value: 4.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  16 NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMG-LLDAPSSGKIEIngtsvesmkdKELAAFRNKTLgfvfqs 93
Cdd:COG2401   39 RVVERYVLRDLNLEIEPGEIVLIVGASGSGKSTLLRlLAGaLKGTPVAGCVDV----------PDNQFGREASL------ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 fhlinslnvIDNVelpllYRKMAAKErtrlAKEVLERVGLSHR--MRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:COG2401  103 ---------IDAI-----GRKGDFKD----AVELLNAVGLSDAvlWLRRFKELSTGQKFRFRLALLLAERPKLLVIDEFC 164
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495112432 172 GNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEE 205
Cdd:COG2401  165 SHLDRQTAKRVARNLQKLARRAGITLVVATHHYD 198
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
19-204 4.69e-19

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 81.46  E-value: 4.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFrnktLGfvfqsfH--- 95
Cdd:PRK13539  14 GRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDIDDPDVAEACHY----LG------Hrna 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSLNVIDNVElplLYRKMAAKERTRLAkEVLERVGLSHrMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PRK13539  84 MKPALTVAENLE---FWAAFLGGEELDIA-AALEAVGLAP-LAHLPFGyLSAGQKRRVALARLLVSNRPIWILDEPTAAL 158
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 175 DS---KMGAEVMEllHKLNKedGRTIVMVTHNE 204
Cdd:PRK13539 159 DAaavALFAELIR--AHLAQ--GGIVIAATHIP 187
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-209 6.85e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 82.93  E-value: 6.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelAA 81
Cdd:PRK13537   6 APIDFRNVEKRYG----DKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSR-----AR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:PRK13537  77 HARQRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVND 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ 209
Cdd:PRK13537 157 PDVLVLDEPTTGLDPQARHLMWERLRSLLAR-GKTILLTTHFMEEAER 203
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
4-209 9.42e-19

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 82.96  E-value: 9.42e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMkdkelAAFR 83
Cdd:PRK13536  42 IDLAGVSKSYGDKAV----VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPAR-----ARLA 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKTLGFVFQSFHLINSLNVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK13536 113 RARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQ 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAKQ 209
Cdd:PRK13536 193 LLILDEPTTGLDPHARHLIWERLRSLLAR-GKTILLTTHFMEEAER 237
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
3-203 1.17e-18

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 83.75  E-value: 1.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIETLALENVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDApSSGKIEING----------TSV 71
Cdd:PRK10261  12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKmllrrrsrqvIEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  72 ESMKDKELAAFRNKTLGFVFQsfHLINSLNVIDNV-----ELPLLYRKMAAKERTRLAKEVLERVGL--SHRM-RHMPTQ 143
Cdd:PRK10261  91 SEQSAAQMRHVRGADMAMIFQ--EPMTSLNPVFTVgeqiaESIRLHQGASREEAMVEAKRMLDQVRIpeAQTIlSRYPHQ 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 144 LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10261 169 LSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHD 228
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
22-203 1.32e-18

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 81.85  E-value: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINGTSVESmkdkelaAFRNKTLGFVFQSFHLINSL 100
Cdd:PRK15056  22 ALRDASFTVPGGSIAALVGVNGSGKSTLFKaLMGFVRL-ASGKISILGQPTRQ-------ALQKNLVAYVPQSEEVDWSF 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NV-IDNVELPLLYRKMA----AKERTR-LAKEVLERVG-LSHRMRHMpTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK15056  94 PVlVEDVVMMGRYGHMGwlrrAKKRDRqIVTAALARVDmVEFRHRQI-GELSGGQKKRVFLARAIAQQGQVILLDEPFTG 172
                        170       180       190
                 ....*....|....*....|....*....|
gi 495112432 174 LDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:PRK15056 173 VDVKTEARIISLLREL-RDEGKTMLVSTHN 201
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
22-204 1.50e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 83.64  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDApSSGKIEINGTSVESmkdKELAAFRNktLGFVFQSFHLINSL 100
Cdd:NF033858 281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLtGLLPA-SEGEAWLFGQPVDA---GDIATRRR--VGYMSQAFSLYGEL 354
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVEL-PLLYRkMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSkmG 179
Cdd:NF033858 355 TVRQNLELhARLFH-LPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDP--V 431
                        170       180
                 ....*....|....*....|....*....
gi 495112432 180 AEVM--ELLHKLNKEDGRTIVMVTH--NE 204
Cdd:NF033858 432 ARDMfwRLLIELSREDGVTIFISTHfmNE 460
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
23-203 2.50e-18

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 80.54  E-value: 2.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEingtsvesmKDKELaafrnkTLGFVFQSFHLinslnv 102
Cdd:PRK09544  20 LSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIK---------RNGKL------RIGYVPQKLYL------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 idNVELPL-LYRKMAAKERTRLAK--EVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:PRK09544  79 --DTTLPLtVNRFLRLRPGTKKEDilPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGVDVNGQ 156
                        170       180
                 ....*....|....*....|....
gi 495112432 180 AEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK09544 157 VALYDLIDQLRRELDCAVLMVSHD 180
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
22-223 2.74e-18

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: 82.87  E-value: 2.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNktlgFVFQSfHLINSLN 101
Cdd:TIGR01193 489 ILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLRQFIN----YLPQE-PYIFSGS 563
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  102 VIDNvelpLLyrkMAAKERTRLAK--EVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:TIGR01193 564 ILEN----LL---LGAKENVSQDEiwAACEIAEIKDDIENMPlgyqtelseegSSISGGQKQRIALARALLTDSKVLILD 636
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 495112432  169 EPTGNLDSKMGAEVMELLHKLNKedgRTIVMVTHNEEQAKQTSRTIRFFDGRQVQ 223
Cdd:TIGR01193 637 ESTSNLDTITEKKIVNNLLNLQD---KTIIFVAHRLSVAKQSDKIIVLDHGKIIE 688
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
3-202 3.46e-18

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 82.42  E-value: 3.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEInGTSVEsmkdkelaa 81
Cdd:COG0488  315 VLELEGLSKSYGDKTL----LDDLSLRIDRGDRIGLIGPNGAGKSTLLKlLAGEL-EPDSGTVKL-GETVK--------- 379
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 frnktLGFVFQSFHLIN-SLNVIDNVelpllyRKMAAKERTRLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIV 159
Cdd:COG0488  380 -----IGYFDQHQEELDpDKTVLDEL------RDGAPGGTEQEVRGYLGRFLFSGDDAFKPVgVLSGGEKARLALAKLLL 448
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLD--SKmgaEVMELLhkLNKEDGrTIVMVTH 202
Cdd:COG0488  449 SPPNVLLLDEPTNHLDieTL---EALEEA--LDDFPG-TVLLVSH 487
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
22-211 3.90e-18

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 80.22  E-value: 3.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelAAFRNKTLGFVFQSFHliNSLN 101
Cdd:PRK15112  28 AVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHFGD----YSYRSQRIRMIFQDPS--TSLN 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 ----VIDNVELPL-LYRKMAAKERTRLAKEVLERVGL-SHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK15112 102 prqrISQILDFPLrLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLD 181
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 176 SKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTS 211
Cdd:PRK15112 182 MSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHIS 217
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
17-203 6.32e-18

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 79.74  E-value: 6.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  17 EIETLALE-------NVNLDVIKGEFVSIMGPSGCGKS-TLLNIMGLLDA---PSSGKIEINGTSVEsmkdkeLAAFRNK 85
Cdd:PRK10418   6 ELRNIALQaaqplvhGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPAgvrQTAGRVLLDGKPVA------PCALRGR 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  86 TLGFVFQ----SFhliNSL-NVIDNVELPLLYRKMAAKERTRLAkeVLERVGLSHRMRHM---PTQLSGGQCQRVAIARA 157
Cdd:PRK10418  80 KIATIMQnprsAF---NPLhTMHTHARETCLALGKPADDATLTA--ALEAVGLENAARVLklyPFEMSGGMLQRMMIALA 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 495112432 158 IVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10418 155 LLCEAPFIIADEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHD 200
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
23-202 8.86e-18

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 81.31  E-value: 8.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQSFHLINSlNV 102
Cdd:TIGR00958 497 LKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQYDHHYL----HRQVALVGQEPVLFSG-SV 571
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  103 IDNVELPLLYRKMAakERTRLAKEVlervGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:TIGR00958 572 RENIAYGLTDTPDE--EIMAAAKAA----NAHDFIMEFPngydtevgekgSQLSGGQKQRIAIARALVRKPRVLILDEAT 645
                         170       180       190
                  ....*....|....*....|....*....|.
gi 495112432  172 GNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR00958 646 SALD----AECEQLLQESRSRASRTVLLIAH 672
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
23-203 2.49e-17

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 78.13  E-value: 2.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLdAPSSGKIEINGTSVESMKdKELAAFRNKtLGFVFQS-FHLINSL 100
Cdd:PRK13638  17 LKGLNLDFSLSPVTGLVGANGCGKSTLfMNLSGLL-RPQKGAVLWQGKPLDYSK-RGLLALRQQ-VATVFQDpEQQIFYT 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHrMRHMPTQ-LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMG 179
Cdd:PRK13638  94 DIDSDIAFSLRNLGVPEAEITRRVDEALTLVDAQH-FRHQPIQcLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGR 172
                        170       180
                 ....*....|....*....|....
gi 495112432 180 AEVMELLHKLNKEdGRTIVMVTHN 203
Cdd:PRK13638 173 TQMIAIIRRIVAQ-GNHVIISSHD 195
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
22-201 2.56e-17

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 79.68  E-value: 2.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLlDAPSSGKIEINGTSVE--SMKDkelaAFRN---------KTLGf 89
Cdd:COG1129  267 VVRDVSFSVRAGEILGIAGLVGAGRTELARaLFGA-DPADSGEIRLDGKPVRirSPRD----AIRAgiayvpedrKGEG- 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  90 vfqsfhLINSLNVIDNVELPLLyRKMA-------AKERtRLAKEVLERVGLSHRMRHMPTQ-LSGGQCQRVAIARAIVGN 161
Cdd:COG1129  341 ------LVLDLSIRENITLASL-DRLSrgglldrRRER-ALAEEYIKRLRIKTPSPEQPVGnLSGGNQQKVVLAKWLATD 412
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495112432 162 PEIILADEPTGNLD--SKmgAEVMELLHKLNKEdGRTIVMVT 201
Cdd:COG1129  413 PKVLILDEPTRGIDvgAK--AEIYRLIRELAAE-GKAVIVIS 451
PLN03211 PLN03211
ABC transporter G-25; Provisional
33-218 3.80e-17

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 79.54  E-value: 3.80e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  33 GEFVSIMGPSGCGKSTLLN-IMGLLDAPS-SGKIEINgtsvesmkDKELAAFRNKTLGFVFQSFHLINSLNVIDN---VE 107
Cdd:PLN03211  94 GEILAVLGPSGSGKSTLLNaLAGRIQGNNfTGTILAN--------NRKPTKQILKRTGFVTQDDILYPHLTVRETlvfCS 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 108 LPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQ-----LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEV 182
Cdd:PLN03211 166 LLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEPTSGLDATAAYRL 245
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 183 MELLHKLNKEdGRTIVMVTHneeqaKQTSRTIRFFD 218
Cdd:PLN03211 246 VLTLGSLAQK-GKTIVTSMH-----QPSSRVYQMFD 275
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
33-203 4.45e-17

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 77.52  E-value: 4.45e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  33 GEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAafrnKTLGFVFQSFHLINSLNVidnVELPLLY 112
Cdd:PRK10575  37 GKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFA----RKVAYLPQQLPAAEGMTV---RELVAIG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 113 R--------KMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVME 184
Cdd:PRK10575 110 RypwhgalgRFGAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVDVLA 188
                        170
                 ....*....|....*....
gi 495112432 185 LLHKLNKEDGRTIVMVTHN 203
Cdd:PRK10575 189 LVHRLSQERGLTVIAVLHD 207
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
23-215 7.71e-17

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 78.70  E-value: 7.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINgtsvesmKDKELAafrnktlgFVFQSFHLIN-SL 100
Cdd:COG4178  379 LEDLSLSLKPGERLLITGPSGSGKSTLLRaIAGLWPY-GSGRIARP-------AGARVL--------FLPQRPYLPLgTL 442
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 nvIDNVELPLLYRKMAAKErtrlAKEVLERVGLSHRMRHMPTQ------LSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:COG4178  443 --REALLYPATAEAFSDAE----LREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFARLLLHKPDWLFLDEATSAL 516
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495112432 175 DSKMGAEVMELLHKLNKedGRTIVMVTHNEEQAKQTSRTIR 215
Cdd:COG4178  517 DEENEAALYQLLREELP--GTTVISVGHRSTLAAFHDRVLE 555
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
23-204 9.38e-17

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 76.26  E-value: 9.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLD-APSSGKIEINGTSVESMKDKELAafrNKTLGFVFQ-------- 92
Cdd:COG0396   16 LKGVNLTIKPGEVHAIMGPNGSGKSTLAKvLMGHPKyEVTSGSILLDGEDILELSPDERA---RAGIFLAFQypveipgv 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 --SFHLINSLNVIDNVELPllyrkmaAKERTRLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:COG0396   93 svSNFLRTALNARRGEELS-------AREFLKLLKEKMKELGLDEDFldRYVNEGFSGGEKKRNEILQMLLLEPKLAILD 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 169 EPtgnlDS-------KMGAEVMELLHklnkEDGRTIVMVTHNE 204
Cdd:COG0396  166 ET----DSgldidalRIVAEGVNKLR----SPDRGILIITHYQ 200
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
24-215 1.01e-16

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 75.23  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEINGTSVESMKDkelaAFRNKTL--GfvfqsfHL--IN 98
Cdd:PRK13538  18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILaGLAR-PDAGEVLWQGEPIRRQRD----EYHQDLLylG------HQpgIK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 S-LNVIDNVelpLLYRKMAAKERTRLAKEVLERVGLSHRMrHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDs 176
Cdd:PRK13538  87 TeLTALENL---RFYQRLHGPGDDEALWEALAQVGLAGFE-DVPVrQLSAGQQRRVALARLWLTRAPLWILDEPFTAID- 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 177 KMGAEVMELLHKLNKEDGRTIVMVTHNE-EQAKQTSRTIR 215
Cdd:PRK13538 162 KQGVARLEALLAQHAEQGGMVILTTHQDlPVASDKVRKLR 201
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
23-219 2.47e-16

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: 74.67  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDApSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINSln 101
Cdd:cd03290   17 LSNINIRIPTGQLTMIVGQVGCGKSSLLlAILGEMQT-LEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNA-- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 vidNVELPLLYRKMAAKERTrlaKEVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:cd03290   94 ---TVEENITFGSPFNKQRY---KAVTDACSLQPDIDLLPfgdqteigergINLSGGQRQRICVARALYQNTNIVFLDDP 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112432 171 TGNLDSKMGAEVM-ELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03290  168 FSALDIHLSDHLMqEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
120-203 2.57e-16

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 75.99  E-value: 2.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 120 RTRLAKEVLERVGL-SHR--MRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRT 196
Cdd:PRK15093 132 RKRRAIELLHRVGIkDHKdaMRSFPYELTEGECQKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTT 211

                 ....*..
gi 495112432 197 IVMVTHN 203
Cdd:PRK15093 212 ILLISHD 218
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
8-202 2.87e-16

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: 76.90  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    8 GINKIYRTN-EIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGkieingtsvesmkdkELAAFRNKT 86
Cdd:TIGR03719   9 RVSKVVPPKkEI----LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNG---------------EARPQPGIK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   87 LGFVFQSFHLINSLNVIDNVELPL------------LYRKMA---------AKERTRLaKEVLERVG---LSHRM----- 137
Cdd:TIGR03719  70 VGYLPQEPQLDPTKTVRENVEEGVaeikdaldrfneISAKYAepdadfdklAAEQAEL-QEIIDAADawdLDSQLeiamd 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112432  138 --RHMP-----TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR03719 149 alRCPPwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLD----AESVAWLERHLQEYPGTVVAVTH 216
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
4-221 5.60e-16

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


Pssm-ID: 213188 [Multi-domain]  Cd Length: 144  Bit Score: 71.71  E-value: 5.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMglldapsSGKIEINGTSVESMKDKELAAFr 83
Cdd:cd03221    1 IELENLSKTYGGKLL----LKDISLTINPGDRIGLVGRNGAGKSTLLKLI-------AGELEPDEGIVTWGSTVKIGYF- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 nktlgfvfqsfhlinslnvidnvelpllyrkmaakertrlakevlervglshrmrhmpTQLSGGQCQRVAIARAIVGNPE 163
Cdd:cd03221   69 ----------------------------------------------------------EQLSGGEKMRLALAKLLLENPN 90
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 164 IILADEPTGNLDSKMGAEVMELLHKLNkedgRTIVMVTHNEEQAKQTSRTIRFFDGRQ 221
Cdd:cd03221   91 LLLLDEPTNHLDLESIEALEEALKEYP----GTVILVSHDRYFLDQVATKIIELEDGK 144
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
13-202 5.98e-16

ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; TAP (Transporter Associated with Antigen Processing) is essential for peptide delivery from the cytosol into the lumen of the endoplasmic reticulum (ER), where these peptides are loaded on major histocompatibility complex (MHC) I molecules. Loaded MHC I leave the ER and display their antigenic cargo on the cell surface to cytotoxic T cells. Subsequently, virus-infected or malignantly transformed cells can be eliminated. TAP belongs to the large family of ATP-binding cassette (ABC) transporters, which translocate a vast variety of solutes across membranes.


Pssm-ID: 213215 [Multi-domain]  Cd Length: 226  Bit Score: 73.66  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQ 92
Cdd:cd03248   21 YPTRP-DTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQYEHKYL----HSKVSLVGQ 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 SFHLInSLNVIDNVELPL----LYRKMAAKER-------TRLAKEVLERVGlshrmrHMPTQLSGGQCQRVAIARAIVGN 161
Cdd:cd03248   96 EPVLF-ARSLQDNIAYGLqscsFECVKEAAQKahahsfiSELASGYDTEVG------EKGSQLSGGQKQRVAIARALIRN 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLNKEdgRTIVMVTH 202
Cdd:cd03248  169 PQVLILDEATSALDAESEQQVQQALYDWPER--RTVLVIAH 207
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
13-202 2.28e-15

ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C is also known as MRP (multidrug resistance-associated protein). Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resistance lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions, such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 72.14  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEieTLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVESMKDKELaafRNKtLGFVF 91
Cdd:cd03244   12 YRPNL--PPVLKNISFSIKPGEKVGIVGRTGSGKSSLLLaLFRLVE-LSSGSILIDGVDISKIGLHDL---RSR-ISIIP 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  92 QSFHL--------INSLNVIDNVELpllyrkMAAKERTRLAKEVLE-RVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:cd03244   85 QDPVLfsgtirsnLDPFGEYSDEEL------WQALERVGLKEFVESlPGGLDTVVEEGGENLSVGQRQLLCLARALLRKS 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495112432 163 EIILADEPTGNLDSkmgaEVMELLHKLNKE--DGRTIVMVTH 202
Cdd:cd03244  159 KILVLDEATASVDP----ETDALIQKTIREafKDCTVLTIAH 196
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
23-202 2.36e-15

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: 74.09  E-value: 2.36e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEINGTSVesmKDKELAAFRnKTLGFVFQSFHLINsln 101
Cdd:COG5265  374 LKGVSFEVPAGKTVAIVGPSGAGKSTLARLLfRFYD-VTSGRILIDGQDI---RDVTQASLR-AAIGIVPQDTVLFN--- 445
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 viDNVELPLLYRKMAAKER-----TRLAK--------------EVLERvGLshrmrhmptQLSGGQCQRVAIARAIVGNP 162
Cdd:COG5265  446 --DTIAYNIAYGRPDASEEeveaaARAAQihdfieslpdgydtRVGER-GL---------KLSGGEKQRVAIARTLLKNP 513
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:COG5265  514 PILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAH 551
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
23-202 2.68e-15

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


Pssm-ID: 213198 [Multi-domain]  Cd Length: 201  Bit Score: 71.37  E-value: 2.68e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDkELAafrnKTLGFVFQSFHLINSLNV 102
Cdd:cd03231   16 FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRD-SIA----RGLLYLGHAPGIKTTLSV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 IDNVelpllyRKMAAKERTRLAKEVLERVGLSHrMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:cd03231   91 LENL------RFWHADHSDEQVEEALARVGLNG-FEDRPVaQLSAGQQRRVALARLLLSGRPLWILDEPTTALDKAGVAR 163
                        170       180
                 ....*....|....*....|.
gi 495112432 182 VMELLHKlNKEDGRTIVMVTH 202
Cdd:cd03231  164 FAEAMAG-HCARGGMVVLTTH 183
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
2-202 7.14e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 72.73  E-value: 7.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   2 AMIKLTGINKIYRTNEietlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV--ESMKDKEL 79
Cdd:PRK10762   3 ALLQLKGIDKAFPGVK----ALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVtfNGPKSSQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 AAfrnktLGFVFQSFHLINSLNVIDNVEL---------PLLYRKMAAKertrlAKEVLERVGLSHRMRHMPTQLSGGQCQ 150
Cdd:PRK10762  79 AG-----IGIIHQELNLIPQLTIAENIFLgrefvnrfgRIDWKKMYAE-----ADKLLARLNLRFSSDKLVGELSIGEQQ 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 151 RVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:PRK10762 149 MVEIAKVLSFESKVIIMDEPTDALTDTETESLFRVIREL-KSQGRGIVYISH 199
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
24-202 1.41e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 72.37  E-value: 1.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTsvESMKDKELAAFRNKtLGFVFQ----------- 92
Cdd:PTZ00265  402 KDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDS--HNLKDINLKWWRSK-IGVVSQdpllfsnsikn 478
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   93 ----SFHLINSLNVIDN------------------------VELPLLYRKMAAKERTRLAKE-----------VLERVGL 133
Cdd:PTZ00265  479 nikySLYSLKDLEALSNyynedgndsqenknkrnscrakcaGDLNDMSNTTDSNELIEMRKNyqtikdsevvdVSKKVLI 558
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  134 SHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PTZ00265  559 HDFVSALPdkyetlvgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLKGNENRITIIIAH 638
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
23-216 1.78e-14

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: 68.33  E-value: 1.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEIngtsvesmkdkelaAFRNKTLgFVFQsfhlinslnv 102
Cdd:cd03223   17 LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGM--------------PEGEDLL-FLPQ---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 103 idnveLPLLYRkmaakerTRLaKEVL----ERVglshrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03223   72 -----RPYLPL-------GTL-REQLiypwDDV------------LSGGEQQRLAFARLLLHKPKFVFLDEATSALDEES 126
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 179 GAEVMELLhklnKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:cd03223  127 EDRLYQLL----KELGITVISVGHRPSLWKFHDRVLDL 160
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
22-214 2.12e-14

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 71.30  E-value: 2.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKElaAFRNKtLGFVFQSFHLINSLN 101
Cdd:PRK10982  13 ALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENG-ISMVHQELNLVLQRS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:PRK10982  90 VMDNMWLgryPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEKE 169
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 179 GAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK10982 170 VNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEI 204
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
26-218 2.27e-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: 71.37  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  26 VNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkDKELAAFRNKtlgF--VFQSFHLINSLNVI 103
Cdd:COG4615  351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAYRQL---FsaVFSDFHLFDRLLGL 424
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNVELPllyrkmaakertRLAKEVLERVGLSHRMRHM-----PTQLSGGQCQRVAIARAIVGNPEIILADE------P-- 170
Cdd:COG4615  425 DGEADP------------ARARELLERLELDHKVSVEdgrfsTTDLSQGQRKRLALLVALLEDRPILVFDEwaadqdPef 492
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495112432 171 -----TgnldskmgaevmELLHKLnKEDGRTIVMVTHNEeqakqtsrtiRFFD 218
Cdd:COG4615  493 rrvfyT------------ELLPEL-KARGKTVIAISHDD----------RYFD 522
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
23-205 2.86e-14

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: 68.71  E-value: 2.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLD-APSSGKIEINGTSVESMKDKELAafrNKTLGFVFQSfhlinsl 100
Cdd:cd03217   16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKtIMGHPKyEVTEGEILFKGEDITDLPPEERA---RLGIFLAFQY------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 nvidNVELPllyrkmaakertrlakevleRVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGA 180
Cdd:cd03217   86 ----PPEIP--------------------GVKNADFLRYVNEGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALR 141
                        170       180
                 ....*....|....*....|....*
gi 495112432 181 EVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:cd03217  142 LVAEVINKL-REEGKSVLIITHYQR 165
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
23-218 3.94e-14

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: 68.04  E-value: 3.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNI------MGLLdapsSGKIEINGtsveSMKDKELAafrnKTLGFVFQSFHL 96
Cdd:cd03232   23 LNNISGYVKPGTLTALMGESGAGKTTLLDVlagrktAGVI----TGEILING----RPLDKNFQ----RSTGYVEQQDVH 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  97 INSLNVIDNVELPLLYRkmaakertrlakevlervGLSHRMRhmptqlsggqcQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:cd03232   91 SPNLTVREALRFSALLR------------------GLSVEQR-----------KRLTIGVELAAKPSILFLDEPTSGLDS 141
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 495112432 177 KMGAEVMELLHKLnKEDGRTIVMVTHneeqakQTSRTI-RFFD 218
Cdd:cd03232  142 QAAYNIVRFLKKL-ADSGQAILCTIH------QPSASIfEKFD 177
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-207 4.38e-14

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 68.75  E-value: 4.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   1 MAMIKLTGINKIYrtNEIEtlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmKDKELA 80
Cdd:PRK11614   3 KVMLSFDKVSAHY--GKIQ--ALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI---TDWQTA 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKTLGFVFQSFHLINSLNVIDNVELPLLY-RKMAAKERTRLAKEVLERvgLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:PRK11614  76 KIMREAVAIVPEGRRVFSRMTVEENLAMGGFFaERDQFQERIKWVYELFPR--LHERRIQRAGTMSGGEQQMLAIGRALM 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQA 207
Cdd:PRK11614 154 SQPRLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQA 200
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
13-202 1.63e-13

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 68.98  E-value: 1.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  13 YRTNEietLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKDKEL------------ 79
Cdd:PRK10790 350 YRDDN---LVLQNINLSVPSRGFVALVGHTGSGKSTLASlLMGYY-PLTEGEIRLDGRPLSSLSHSVLrqgvamvqqdpv 425
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 ----AAFRNKTLGFVFQSFHLinsLNVIDNVELPLLYRKMAAKERTRLAKEvlervglshrmrhmPTQLSGGQCQRVAIA 155
Cdd:PRK10790 426 vladTFLANVTLGRDISEEQV---WQALETVQLAELARSLPDGLYTPLGEQ--------------GNNLSVGQKQLLALA 488
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 495112432 156 RAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDgrTIVMVTH 202
Cdd:PRK10790 489 RVLVQTPQILILDEATANIDSGTEQAIQQALAAVREHT--TLVVIAH 533
sufC TIGR01978
FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six ...
23-205 2.42e-13

FeS assembly ATPase SufC; SufC is part of the SUF system, shown in E. coli to consist of six proteins and believed to act in Fe-S cluster formation during oxidative stress. SufC forms a complex with SufB and SufD. SufC belongs to the ATP-binding cassette transporter family (pfam00005) but is no longer thought to be part of a transporter. The complex is reported as cytosolic () or associated with the membrane (). The SUF system also includes a cysteine desulfurase (SufS, enhanced by SufE) and a probable iron-sulfur cluster assembly scaffold protein, SufA. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 273907 [Multi-domain]  Cd Length: 243  Bit Score: 66.90  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAP-SSGKIEINGTSVESMKDKELAAfrnKTLGFVFQSFHLINSL 100
Cdd:TIGR01978  16 LKGVNLTVKKGEIHAIMGPNGSGKSTLSKtIAGHPSYEvTSGTILFKGQDLLELEPDERAR---AGLFLAFQYPEEIPGV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  101 NVIDNVELPLLYRKMAAKERT-------RLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:TIGR01978  93 SNLEFLRSALNARRSARGEEPldlldfeKLLKEKLALLDMDEEFlnRSVNEGFSGGEKKRNEILQMALLEPKLAILDEID 172
                         170       180       190
                  ....*....|....*....|....*....|....
gi 495112432  172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:TIGR01978 173 SGLDIDALKIVAEGINRL-REPDRSFLIITHYQR 205
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
23-175 3.10e-13

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 67.73  E-value: 3.10e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGllDAPSS--------GKIEINGTSVESMKdkelaafrnKTLGFVFQS 93
Cdd:PRK10938 276 LHNLSWQVNPGEHWQIVGPNGAGKSTLLSlITG--DHPQGysndltlfGRRRGSGETIWDIK---------KHIGYVSSS 344
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 FHL-----INSLNVI-----DNVELpllYRKMAAKERtRLAKEVLERVGLSHRMRHMPTQ-LSGGQcQRVA-IARAIVGN 161
Cdd:PRK10938 345 LHLdyrvsTSVRNVIlsgffDSIGI---YQAVSDRQQ-KLAQQWLDILGIDKRTADAPFHsLSWGQ-QRLAlIVRALVKH 419
                        170
                 ....*....|....
gi 495112432 162 PEIILADEPTGNLD 175
Cdd:PRK10938 420 PTLLILDEPLQGLD 433
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
22-222 3.18e-13

D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose isomerase and xylulokinase enzymes for xylose utilization. Members of this protein family are the ATP-binding cassette (ABC) subunit of the known or predicted high-affinity xylose ABC transporter for xylose import. These genes, which closely resemble other sugar transport ABC transporter genes, typically are encoded near xylose utilization enzymes and regulatory proteins. Note that this form of the transporter contains two copies of the ABC transporter domain (pfam00005). [Transport and binding proteins, Carbohydrates, organic alcohols, and acids]


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 67.93  E-value: 3.18e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-SGKIEINGTSVE--SMKDKElaafrNKTLGFVFQSFHLI 97
Cdd:TIGR02633  16 ALDGIDLEVRPGECVGLCGENGAGKSTLMKILsGVYPHGTwDGEIYWSGSPLKasNIRDTE-----RAGIVIIHQELTLV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   98 NSLNVIDNV----ELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTG 172
Cdd:TIGR02633  91 PELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPVgDYGGGQQQLVEIAKALNKQARLLILDEPSS 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495112432  173 NLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQV 222
Cdd:TIGR02633 171 SLTEKETEILLDIIRDL-KAHGVACVYISHKLNEVKAVCDTICVIrDGQHV 220
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
19-204 3.31e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 68.07  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVEsmkDKELAAFRnKTLGFVFQSFHLIN 98
Cdd:PRK10522 335 NGFSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR-KLFSAVFTDFHLFD 410
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLnvidnvelpLLYRKMAAKErtRLAKEVLERVGLSHRMRH-----MPTQLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK10522 411 QL---------LGPEGKPANP--ALVEKWLERLKMAHKLELedgriSNLKLSKGQKKRLALLLALAEERDILLLDEWAAD 479
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 174 LDSKMGAEVMELLHKLNKEDGRTIVMVTHNE 204
Cdd:PRK10522 480 QDPHFRREFYQVLLPLLQEMGKTIFAISHDD 510
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
3-202 3.31e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 67.84  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTginKIYRTN-EIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGkieingtsvesmkdkELAA 81
Cdd:PRK11819   9 MNRVS---KVVPPKkQI----LKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEG---------------EARP 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  82 FRNKTLGFVFQSFHLINSLNVIDNVELPL------------LYRKMA---------AKERTRLaKEVLERVG---LSHRM 137
Cdd:PRK11819  67 APGIKVGYLPQEPQLDPEKTVRENVEEGVaevkaaldrfneIYAAYAepdadfdalAAEQGEL-QEIIDAADawdLDSQL 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 138 -RHM-----P------TQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDskmgAE-VMELLHKLNKEDGrTIVMVTH 202
Cdd:PRK11819 146 eIAMdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLD----AEsVAWLEQFLHDYPG-TVVAVTH 218
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
22-222 3.40e-13

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 67.65  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLlniMGLLDA--PS---SGKIEINGTSVE--SMKDKELAAfrnktLGFVFQSF 94
Cdd:PRK13549  20 ALDNVSLKVRAGEIVSLCGENGAGKSTL---MKVLSGvyPHgtyEGEIIFEGEELQasNIRDTERAG-----IAIIHQEL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  95 HLINSLNVIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK13549  92 ALVKELSVLENIFLgneITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQARLLILDEPT 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQV 222
Cdd:PRK13549 172 ASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIrDGRHI 222
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
22-208 4.55e-13

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 67.61  E-value: 4.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSvesmkdkelaafrnktlGFVFQSFHLINSLN 101
Cdd:PRK13545  39 ALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSA-----------------ALIAISSGLNGQLT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK13545 102 GIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKK 181
                        170       180
                 ....*....|....*....|....*..
gi 495112432 182 VMELLHKLnKEDGRTIVMVTHNEEQAK 208
Cdd:PRK13545 182 CLDKMNEF-KEQGKTIFFISHSLSQVK 207
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
33-203 4.69e-13

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: 66.24  E-value: 4.69e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  33 GEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEING---TSVESMKDKEL----AAFRNKTLGFVF--QSFHLINslNVI 103
Cdd:cd03236   26 GQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDDPPdwdEILDEFRGSELqnyfTKLLEGDVKVIVkpQYVDLIP--KAV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 104 DNVELPLLYRKmaaKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVM 183
Cdd:cd03236  104 KGKVGELLKKK---DERGKL-DELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQRLNAA 179
                        170       180
                 ....*....|....*....|
gi 495112432 184 ELLHKLNkEDGRTIVMVTHN 203
Cdd:cd03236  180 RLIRELA-EDDNYVLVVEHD 198
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
15-189 8.09e-13

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 66.59  E-value: 8.09e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  15 TNEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIEINGTSVESMKdkeLAAFRNKTLGFVFQS 93
Cdd:COG3845  266 RDDRGVPALKDVSLEVRAGEILGIAGVAGNGQSELAEaLAGLR-PPASGSIRLDGEDITGLS---PRERRRLGVAYIPED 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 FH---LINSLNVIDNVELPLLYRK-------MAAKERTRLAKEVLER-----VGLSHRMRhmptQLSGGQCQRVAIARAI 158
Cdd:COG3845  342 RLgrgLVPDMSVAENLILGRYRRPpfsrggfLDRKAIRAFAEELIEEfdvrtPGPDTPAR----SLSGGNQQKVILAREL 417
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 159 VGNPEIILADEPTGNLDskMGAevMELLHKL 189
Cdd:COG3845  418 SRDPKLLIAAQPTRGLD--VGA--IEFIHQR 444
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
23-220 1.02e-12

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: 66.89  E-value: 1.02e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDApSSGKIEINGTsvesmkdkelaafrnktLGFVFQSFHLINsln 101
Cdd:TIGR00957  654 LNGITFSIPEGALVAVVGQVGCGKSSLLSaLLAEMDK-VEGHVHMKGS-----------------VAYVPQQAWIQN--- 712
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   102 viDNVELPLLYRKMAAKERTRlakEVLERVGLSHRMRHMPT-----------QLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:TIGR00957  713 --DSLRENILFGKALNEKYYQ---QVLEACALLPDLEILPSgdrteigekgvNLSGGQKQRVSLARAVYSNADIYLFDDP 787
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 495112432   171 TGNLDSKMGAEVMEllHKLNKE---DGRTIVMVTHNEEQAKQTSRTIRFFDGR 220
Cdd:TIGR00957  788 LSAVDAHVGKHIFE--HVIGPEgvlKNKTRILVTHGISYLPQVDVIIVMSGGK 838
PLN03130 PLN03130
ABC transporter C family member; Provisional
23-219 2.01e-12

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 65.91  E-value: 2.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPSSGKIEINGTsvesmkdkelaafrnktLGFVFQSFHLINSlN 101
Cdd:PLN03130  633 LSNINLDVPVGSLVAIVGSTGEGKTSLISAMlGELPPRSDASVVIRGT-----------------VAYVPQVSWIFNA-T 694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  102 VIDNVELPLLYrkmaakERTRLAKeVLERVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PLN03130  695 VRDNILFGSPF------DPERYER-AIDVTALQHDLDLLPggdlteigergVNISGGQKQRVSMARAVYSNSDVYIFDDP 767
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 495112432  171 TGNLDSKMGAEVMEllhKLNKED--GRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PLN03130  768 LSALDAHVGRQVFD---KCIKDElrGKTRVLVTNQLHFLSQVDRIILVHEG 815
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
22-202 2.30e-12

ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type transporter 1). NFT1 belongs to the MRP (multidrug resistance-associated protein) family of ABC transporters. Some of the MRP members have five additional transmembrane segments in their N-terminus, but the function of these additional membrane-spanning domains is not clear. The MRP was found in the multidrug-resisting lung cancer cell in which p-glycoprotein was not overexpressed. MRP exports glutathione by drug stimulation, as well as, certain substrates in conjugated forms with anions such as glutathione, glucuronate, and sulfate.


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 63.59  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDaPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQ-----SFH 95
Cdd:cd03369   23 VLKNVSFKVKAGEKIGIVGRTGAGKSTLiLALFRFLE-AEEGKIEIDGIDISTIP---LEDLRSS-LTIIPQdptlfSGT 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSLNVIDNVELPLLYRKMAAKERtrlakevlervGLShrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:cd03369   98 IRSNLDPFDEYSDEEIYGALRVSEG-----------GLN---------LSQGQRQLLCLARALLKRPRVLVLDEATASID 157
                        170       180
                 ....*....|....*....|....*..
gi 495112432 176 SKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:cd03369  158 YATDALIQKTIREEFT--NSTILTIAH 182
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
22-219 7.24e-12

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 62.91  E-value: 7.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEingtsvesmkdkelaafRNKTLGFVFQSFHLINSLN 101
Cdd:PRK13546  39 ALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVD-----------------RNGEVSVIAISAGLSGQLT 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAE 181
Cdd:PRK13546 102 GIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQK 181
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 182 VMELLHKLnKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PRK13546 182 CLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEG 218
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
11-216 1.06e-11

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 63.89  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   11 KIYRTNEIETLALENVNldvikgEFVSIMGPSGCGKSTLLNimglldapSSGKIEINGTSVesmKDKELAAFRNkTLGFV 90
Cdd:PTZ00265 1240 QDYQGDEEQNVGMKNVN------EFSLTKEGGSGEDSTVFK--------NSGKILLDGVDI---CDYNLKDLRN-LFSIV 1301
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   91 FQSFHLINsLNVIDNVELPllyRKMAAKERTrlaKEVLERVGLSHRMRHMPTQ-----------LSGGQCQRVAIARAIV 159
Cdd:PTZ00265 1302 SQEPMLFN-MSIYENIKFG---KEDATREDV---KRACKFAAIDEFIESLPNKydtnvgpygksLSGGQKQRIAIARALL 1374
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432  160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:PTZ00265 1375 REPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIKRSDKIVVF 1431
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
32-202 1.66e-11

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: 62.88  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  32 KGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTsvesmKDKELAAFRNKTLGFVFQSfhLIN-SLNV---IDNV 106
Cdd:COG1245   98 KGKVTGILGPNGIGKSTALKILsGEL-KPNLGDYDEEPS-----WDEVLKRFRGTELQDYFKK--LANgEIKVahkPQYV 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 107 EL-P---------LLyrkMAAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:COG1245  170 DLiPkvfkgtvreLL---EKVDERGKL-DELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLDI 245
                        170       180
                 ....*....|....*....|....*.
gi 495112432 177 KMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:COG1245  246 YQRLNVARLIREL-AEEGKYVLVVEH 270
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
3-214 1.91e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 62.76  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkdKELAAF 82
Cdd:PRK15439  11 LLCARSISKQYSGVEV----LKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPC-----ARLTPA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  83 RNKTLG--FVFQSFHLINSLNVIDNVeLPLLYRKMAAKERTrlaKEVLERVGlSHRMRHMPT-QLSGGQCQRVAIARAIV 159
Cdd:PRK15439  82 KAHQLGiyLVPQEPLLFPNLSVKENI-LFGLPKRQASMQKM---KQLLAALG-CQLDLDSSAgSLEVADRQIVEILRGLM 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 495112432 160 GNPEIILADEPTGNLDSkmgAEVMELLHKLNK--EDGRTIVMVTHNEEQAKQTSRTI 214
Cdd:PRK15439 157 RDSRILILDEPTASLTP---AETERLFSRIREllAQGVGIVFISHKLPEIRQLADRI 210
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
29-219 4.55e-11

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: 60.50  E-value: 4.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  29 DVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELAAfrnKTLGFVFQsfhlinslnvidnvel 108
Cdd:cd03237   21 SISESEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTV-SYKPQYIKA---DYEGTVRD---------------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 pLLYRKMAAK-ERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLH 187
Cdd:cd03237   81 -LLSSITKDFyTHPYFKTEIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQRLMASKVIR 159
                        170       180       190
                 ....*....|....*....|....*....|..
gi 495112432 188 KLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03237  160 RFAENNEKTAFVVEHDIIMIDYLADRLIVFEG 191
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
23-205 4.59e-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: 60.35  E-value: 4.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLL---------------------NIMGLLDAPSSGKIEinGTSVE-SMKDKELA 80
Cdd:cd03270   11 LKNVDVDIPRNKLVVITGVSGSGKSSLAfdtiyaegqrryveslsayarQFLGQMDKPDVDSIE--GLSPAiAIDQKTTS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 AFRNKTLGFVFQsfhlINSLnvidnveLPLLYRKMAAKERTRLakevLERVGLSH-RM-RHMPTqLSGGQCQRVAIARAI 158
Cdd:cd03270   89 RNPRSTVGTVTE----IYDY-------LRLLFARVGIRERLGF----LVDVGLGYlTLsRSAPT-LSGGEAQRIRLATQI 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 159 ----VGnpEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHNEE 205
Cdd:cd03270  153 gsglTG--VLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDED 200
PLN03140 PLN03140
ABC transporter G family member; Provisional
33-202 4.86e-11

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 61.79  E-value: 4.86e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   33 GEFVSIMGPSGCGKSTLLNIM------GLLDapssGKIEINGTSvesmKDKELAAfrnKTLGFVFQSFhlINSLNVidNV 106
Cdd:PLN03140  906 GVLTALMGVSGAGKTTLMDVLagrktgGYIE----GDIRISGFP----KKQETFA---RISGYCEQND--IHSPQV--TV 970
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  107 ELPLLY-------RKMAAKERTRLAKEVLERV---GLSHRMRHMP--TQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:PLN03140  971 RESLIYsaflrlpKEVSKEEKMMFVDEVMELVeldNLKDAIVGLPgvTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGL 1050
                         170       180
                  ....*....|....*....|....*....
gi 495112432  175 DSKMGAEVMELLHklNKED-GRTIVMVTH 202
Cdd:PLN03140 1051 DARAAAIVMRTVR--NTVDtGRTVVCTIH 1077
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
6-208 4.89e-11

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: 61.95  E-value: 4.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432     6 LTGINK--IYRTNEIETL-------ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSV-ESMK 75
Cdd:TIGR01257 1929 ISGGNKtdILRLNELTKVysgtsspAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS 2008
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    76 DKelaafrNKTLGFVFQsFHLINSLnvIDNVELPLLY---RKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRV 152
Cdd:TIGR01257 2009 DV------HQNMGYCPQ-FDAIDDL--LTGREHLYLYarlRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKL 2079
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 495112432   153 AIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTHNEEQAK 208
Cdd:TIGR01257 2080 STAIALIGCPPLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECE 2134
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
25-201 5.53e-11

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 61.34  E-value: 5.53e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESmkDKELAAFRnKTLGFV---------FQSFH 95
Cdd:PRK09700 281 DISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISP--RSPLDAVK-KGMAYItesrrdngfFPNFS 357
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSLNVIDNVELPLLYRKMA---AKERTRLAKEVLERVGLS-HRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:PRK09700 358 IAQNMAISRSLKDGGYKGAMGlfhEVDEQRTAENQRELLALKcHSVNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPT 437
                        170       180       190
                 ....*....|....*....|....*....|
gi 495112432 172 GNLDSKMGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:PRK09700 438 RGIDVGAKAEIYKVMRQL-ADDGKVILMVS 466
PTZ00243 PTZ00243
ABC transporter; Provisional
23-202 5.90e-11

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 61.72  E-value: 5.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNimGLLdapssGKIEINGTSVesmkdkeLAAfrnKTLGFVFQSFHLINSlNV 102
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLLQ--SLL-----SQFEISEGRV-------WAE---RSIAYVPQQAWIMNA-TV 737
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  103 IDNVelpLLYrkmaAKERT-RLAKEVleRV------------GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:PTZ00243  738 RGNI---LFF----DEEDAaRLADAV--RVsqleadlaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDD 808
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 495112432  170 PTGNLDSKMGAEVME--LLHKLNkedGRTIVMVTH 202
Cdd:PTZ00243  809 PLSALDAHVGERVVEecFLGALA---GKTRVLATH 840
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
22-202 6.28e-11

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 61.27  E-value: 6.28e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRNKtLGFVFQSFHLInSLN 101
Cdd:PRK10789 330 ALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKLQ---LDSWRSR-LAVVSQTPFLF-SDT 404
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVELPllyRKMAAKER----TRLAK--------------EVLERvglshrmrhmPTQLSGGQCQRVAIARAIVGNPE 163
Cdd:PRK10789 405 VANNIALG---RPDATQQEiehvARLASvhddilrlpqgydtEVGER----------GVMLSGGQKQRISIARALLLNAE 471
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 164 IILADEPTGNLDskmGAEVMELLHKLNK-EDGRTIVMVTH 202
Cdd:PRK10789 472 ILILDDALSAVD---GRTEHQILHNLRQwGEGRTVIISAH 508
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
33-175 7.52e-11

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 59.48  E-value: 7.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  33 GEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGF-----VFQSFHLINSLNvidnve 107
Cdd:PRK13543  37 GEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDRSRFMAYLGHLPGLkadlsTLENLHFLCGLH------ 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 108 lpllyrkmaAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK13543 111 ---------GRRAKQMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLD 169
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
23-202 8.60e-11

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 60.73  E-value: 8.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMG---LLDapsSGKIEINGTSVESM------KDKELAAFRN-----KTLG 88
Cdd:PRK11147  19 LDNAELHIEDNERVCLVGRNGAGKSTLMKILNgevLLD---DGRIIYEQDLIVARlqqdppRNVEGTVYDFvaegiEEQA 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  89 FVFQSFHLINSLNVIDNVElPLLYRKMAAKER----------TRLaKEVLERVGLShrmRHMP-TQLSGGQCQRVAIARA 157
Cdd:PRK11147  96 EYLKRYHDISHLVETDPSE-KNLNELAKLQEQldhhnlwqleNRI-NEVLAQLGLD---PDAAlSSLSGGWLRKAALGRA 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 495112432 158 IVGNPEIILADEPTGNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11147 171 LVSNPDVLLLDEPTNHLD----IETIEWLEGFLKTFQGSIIFISH 211
GguA NF040905
sugar ABC transporter ATP-binding protein;
22-204 9.65e-11

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 60.57  E-value: 9.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-SGKIEINGtsvesmkdkELAAFRN----KTLGFVF--QS 93
Cdd:NF040905  16 ALDDVNLSVREGEIHALCGENGAGKSTLMKVLsGVYPHGSyEGEILFDG---------EVCRFKDirdsEALGIVIihQE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 FHLINSLNVIDNVEL---PLLYRKMAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:NF040905  87 LALIPYLSIAENIFLgneRAKRGVIDWNETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEP 166
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 171 TGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH--NE 204
Cdd:NF040905 167 TAALNEEDSAALLDLLLEL-KAQGITSIIISHklNE 201
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
30-202 1.23e-10

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 60.21  E-value: 1.23e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  30 VIKGEFVSIMGPSGCGKSTLLNIMglldapsSGKIEIN--GTSVESMKDKELAAFRNKTLGFVF--------------QS 93
Cdd:PRK13409  96 PKEGKVTGILGPNGIGKTTAVKIL-------SGELIPNlgDYEEEPSWDEVLKRFRGTELQNYFkklyngeikvvhkpQY 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 FHLINSL---NVIDnvelpLLYRkmaAKERTRLaKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PRK13409 169 VDLIPKVfkgKVRE-----LLKK---VDERGKL-DEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEP 239
                        170       180       190
                 ....*....|....*....|....*....|..
gi 495112432 171 TGNLDSKMGAEVMELLHKLNKedGRTIVMVTH 202
Cdd:PRK13409 240 TSYLDIRQRLNVARLIRELAE--GKYVLVVEH 269
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
20-219 1.92e-10

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 59.92  E-value: 1.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    20 TLALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDaPSSGKIEINGTSVES----------MKDkelaafrNKTLG 88
Cdd:TIGR01271  439 TPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMmIMGELE-PSEGKIKHSGRISFSpqtswimpgtIKD-------NIIFG 510
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    89 FVFQSFHLInslNVIDNVELPLLYRKMAAKERTrlakeVLERVGLShrmrhmptqLSGGQCQRVAIARAIVGNPEIILAD 168
Cdd:TIGR01271  511 LSYDEYRYT---SVIKACQLEEDIALFPEKDKT-----VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLD 573
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 495112432   169 EPTGNLDSKMGAEVME-LLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:TIGR01271  574 SPFTHLDVVTEKEIFEsCLCKLMSN--KTRILVTSKLEHLKKADKILLLHEG 623
hmuV PRK13547
heme ABC transporter ATP-binding protein;
23-222 1.98e-10

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 59.07  E-value: 1.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPS-------SGKIEINGTSVESMKDKELAAFR-----NKTLGF 89
Cdd:PRK13547  17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKALaGDLTGGGaprgarvTGDVTLNGEPLAAIDAPRLARLRavlpqAAQPAF 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  90 VFqSFHLINSLNvidnvELPLLYRKMAAKERTR-LAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAI---------V 159
Cdd:PRK13547  97 AF-SAREIVLLG-----RYPHARRAGALTHRDGeIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaA 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAKQTSRTIRFF-DGRQV 222
Cdd:PRK13547 171 QPPRYLLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLaDGAIV 234
ycf16 CHL00131
sulfate ABC transporter protein; Validated
19-202 2.74e-10

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 58.50  E-value: 2.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNImgLLDAPS----SGKIEINGTSVESMKDKELAafrnkTLGfVFQSF 94
Cdd:CHL00131  19 ENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKV--IAGHPAykilEGDILFKGESILDLEPEERA-----HLG-IFLAF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  95 HLINSLNVIDNVE-LPLLY---RKMAAK------ERTRLAKEVLERVGLSHRM--RHMPTQLSGGQCQRVAIARAIVGNP 162
Cdd:CHL00131  91 QYPIEIPGVSNADfLRLAYnskRKFQGLpeldplEFLEIINEKLKLVGMDPSFlsRNVNEGFSGGEKKRNEILQMALLDS 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 495112432 163 EIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:CHL00131 171 ELAILDETDSGLDIDALKIIAEGINKL-MTSENSIILITH 209
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
23-219 2.85e-10

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: 58.71  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLL-NIMGLLDaPSSGKIEINGTSVESMKDKEL---AAFRNKTLGFVFQSFHLin 98
Cdd:cd03291   53 LKNINLKIEKGEMLAITGSTGSGKTSLLmLILGELE-PSEGKIKHSGRISFSSQFSWImpgTIKENIIFGVSYDEYRY-- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 sLNVIDNVELPLLYRKMAAKERTrlakeVLERVGLShrmrhmptqLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKM 178
Cdd:cd03291  130 -KSVVKACQLEEDITKFPEKDNT-----VLGEGGIT---------LSGGQRARISLARAVYKDADLYLLDSPFGYLDVFT 194
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 495112432 179 GAEVME-LLHKLNKEdgRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03291  195 EKEIFEsCVCKLMAN--KTRILVTSKMEHLKKADKILILHEG 234
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
115-222 1.04e-09

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 57.44  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 115 MAAKERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKeDG 194
Cdd:NF000106 116 LSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDPRTRNEVWDEVRSMVR-DG 194
                         90       100
                 ....*....|....*....|....*....
gi 495112432 195 RTIVMVTHNEEQAKQTSRTIRFFD-GRQV 222
Cdd:NF000106 195 ATVLLTTQYMEEAEQLAHELTVIDrGRVI 223
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
23-175 1.89e-09

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: 56.02  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDapSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQSFhLINSLN 101
Cdd:cd03289   20 LENISFSISPGQRVGLLGRTGSGKSTLLSaFLRLLN--TEGDIQIDGVSWNSVP---LQKWR-KAFGVIPQKV-FIFSGT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 102 VIDNVElPllYRKMAAKERTRLAKEVlervGLSHRMRHMPTQL-----------SGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:cd03289   93 FRKNLD-P--YGKWSDEEIWKVAEEV----GLKSVIEQFPGQLdfvlvdggcvlSHGHKQLMCLARSVLSKAKILLLDEP 165

                 ....*
gi 495112432 171 TGNLD 175
Cdd:cd03289  166 SAHLD 170
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
23-175 1.94e-09

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: 57.23  E-value: 1.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLdAPSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQSFhLINSLNV 102
Cdd:TIGR01271 1235 LQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRL-LSTEGEIQIDGVSWNSVT---LQTWR-KAFGVIPQKV-FIFSGTF 1308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   103 IDNVElPllYRKMAAKERTRLAKEVlervGLSHRMRHMPTQL-----------SGGQCQRVAIARAIVGNPEIILADEPT 171
Cdd:TIGR01271 1309 RKNLD-P--YEQWSDEEIWKVAEEV----GLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKAKILLLDEPS 1381

                   ....
gi 495112432   172 GNLD 175
Cdd:TIGR01271 1382 AHLD 1385
PLN03232 PLN03232
ABC transporter C family member; Provisional
23-219 2.06e-09

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 56.91  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLDAPSSGKIEINGTsvesmkdkelaafrnktLGFVFQSFHLINSlN 101
Cdd:PLN03232  633 LSDINLEIPVGSLVAIVGGTGEGKTSLISAMlGELSHAETSSVVIRGS-----------------VAYVPQVSWIFNA-T 694
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  102 VIDNVelplLYRKMAAKERTRLAKEVlerVGLSHRMRHMP-----------TQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:PLN03232  695 VRENI----LFGSDFESERYWRAIDV---TALQHDLDLLPgrdlteigergVNISGGQKQRVSMARAVYSNSDIYIFDDP 767
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 495112432  171 TGNLDSKMGAEVMELLHKlNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:PLN03232  768 LSALDAHVAHQVFDSCMK-DELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
19-204 2.34e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 54.96  E-value: 2.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  19 ETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVesmkDKELAAFRnKTLGFVFQSFHLIN 98
Cdd:PRK13540  13 DQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSI----KKDLCTYQ-KQLCFVGHRSGINP 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLLYRK--MAAKERTRLAKevlervgLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PRK13540  88 YLTLRENCLYDIHFSPgaVGITELCRLFS-------LEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDE 160
                        170       180
                 ....*....|....*....|....*...
gi 495112432 177 KMGAEVMELLHKLNKEDGrTIVMVTHNE 204
Cdd:PRK13540 161 LSLLTIITKIQEHRAKGG-AVLLTSHQD 187
PLN03073 PLN03073
ABC transporter F family; Provisional
21-204 3.14e-09

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 56.41  E-value: 3.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIeingtsvesmkdkelaaFRNKTLGFVFQSFHLINSL 100
Cdd:PLN03073 523 LLFKNLNFGIDLDSRIAMVGPNGIGKSTILKLISGELQPSSGTV-----------------FRSAKVRMAVFSQHHVDGL 585
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNvelPLLY--RKMAAKERTRLaKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSK 177
Cdd:PLN03073 586 DLSSN---PLLYmmRCFPGVPEQKL-RAHLGSFGVTGNLALQPMyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLD 661
                        170       180
                 ....*....|....*....|....*..
gi 495112432 178 mgaEVMELLHKLNKEDGrTIVMVTHNE 204
Cdd:PLN03073 662 ---AVEALIQGLVLFQG-GVLMVSHDE 684
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
3-202 4.19e-09

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: 55.91  E-value: 4.19e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    3 MIKLTGINKIYRTNEIetlALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMG--------LLDAPSSGKI--------EI 66
Cdd:TIGR00954 451 GIKFENIPLVTPNGDV---LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGelwpvyggRLTKPAKGKLfyvpqrpyMT 527
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   67 NGT---------SVESMKDKelaAFRNKTLgfvfqsfhlinsLNVIDNVELpllyrkmaakertrlaKEVLERVGLSHRM 137
Cdd:TIGR00954 528 LGTlrdqiiypdSSEDMKRR---GLSDKDL------------EQILDNVQL----------------THILEREGGWSAV 576
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432  138 RHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTgnldSKMGAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:TIGR00954 577 QDWMDVLSGGEKQRIAMARLFYHKPQFAILDECT----SAVSVDVEGYMYRLCREFGITLFSVSH 637
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
21-175 5.30e-09

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: 55.33  E-value: 5.30e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGT----SVESMKDKeLAAfrNKTlgfVFQSFHL 96
Cdd:TIGR03719 336 LLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGETvklaYVDQSRDA-LDP--NKT---VWEEISG 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   97 INSLNVIDNVELPllyrkmaakERTRLAK------EVLERVGlshrmrhmptQLSGGQCQRVAIARAIVGNPEIILADEP 170
Cdd:TIGR03719 410 GLDIIKLGKREIP---------SRAYVGRfnfkgsDQQKKVG----------QLSGGERNRVHLAKTLKSGGNVLLLDEP 470

                  ....*
gi 495112432  171 TGNLD 175
Cdd:TIGR03719 471 TNDLD 475
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
23-202 7.24e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 55.50  E-value: 7.24e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNI------MGLLdapSSGKIEINGTSVESmkdkelaAFRNKTlGFVFQSFHL 96
Cdd:TIGR00956  779 LNNVDGWVKPGTLTALMGASGAGKTTLLNVlaervtTGVI---TGGDRLVNGRPLDS-------SFQRSI-GYVQQQDLH 847
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    97 INSLNVIDNVELPLLYR---KMAAKERTRLAKEVLERVGlshrMRHMPTQLSG--------GQCQRVAIARAIVGNPEII 165
Cdd:TIGR00956  848 LPTSTVRESLRFSAYLRqpkSVSKSEKMEYVEEVIKLLE----MESYADAVVGvpgeglnvEQRKRLTIGVELVAKPKLL 923
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 495112432   166 L-ADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMVTH 202
Cdd:TIGR00956  924 LfLDEPTSGLDSQTAWSICKLMRKLADH-GQAILCTIH 960
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
32-222 1.41e-08

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: 51.99  E-value: 1.41e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432    32 KGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGfvfqsfhlinslnvidnvelpl 110
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGKK---------------------- 58
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   111 lyrkmaakertrlakevlervglshrmrhmpTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMEL----L 186
Cdd:smart00382  59 -------------------------------ASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLLLeelrL 107
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 495112432   187 HKLNKEDGRTIVMVTHNEEQAKQTSRTIRFFDGRQV 222
Cdd:smart00382 108 LLLLKSEKNLTVILTTNDEKDLGPALLRRRFDRRIV 143
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
22-216 2.15e-08

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: 51.94  E-value: 2.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  22 ALENVNLDVIKGEFVSIMGPSGCGKSTLLNimglldapssgkiEINGTSVESMKDKELAAF-RNKTLgfvfqsfhLINSL 100
Cdd:cd03238   10 NLQNLDVSIPLNVLVVVTGVSGSGKSTLVN-------------EGLYASGKARLISFLPKFsRNKLI--------FIDQL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 101 NVIDNVELPLLyrkmaakertrlakevleRVGlshrmRHMPTqLSGGQCQRVAIARAIVGNPE--IILADEPTGNLDSKM 178
Cdd:cd03238   69 QFLIDVGLGYL------------------TLG-----QKLST-LSGGELQRVKLASELFSEPPgtLFILDEPSTGLHQQD 124
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 179 GAEVMELLHKLNKEdGRTIVMVTHNEEQAKQTSRTIRF 216
Cdd:cd03238  125 INQLLEVIKGLIDL-GNTVILIEHNLDVLSSADWIIDF 161
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
23-201 2.19e-08

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 53.47  E-value: 2.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEINGTSVESMKDKE-LAAfrnktlGFVFQSFH----- 95
Cdd:PRK10762 268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLyGAL-PRTSGYVTLDGHEVVTRSPQDgLAN------GIVYISEDrkrdg 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  96 LINSLNVIDNVELPLLYRKMAAKERTRLAKEVLErVGLSHRMRHMPT--------QLSGGQCQRVAIARAIVGNPEIILA 167
Cdd:PRK10762 341 LVLGMSVKENMSLTALRYFSRAGGSLKHADEQQA-VSDFIRLFNIKTpsmeqaigLLSGGNQQKVAIARGLMTRPKVLIL 419
                        170       180       190
                 ....*....|....*....|....*....|....
gi 495112432 168 DEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:PRK10762 420 DEPTRGVDVGAKKEIYQLINQF-KAEGLSIILVS 452
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
29-219 7.01e-08

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: 50.65  E-value: 7.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  29 DVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVeSMKDKELaafrnktlgfvfqsfhlinslnvidnvel 108
Cdd:cd03222   21 VVKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITP-VYKPQYI----------------------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 pllyrkmaakertrlakevlervglshrmrhmptQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHK 188
Cdd:cd03222   71 ----------------------------------DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
                        170       180       190
                 ....*....|....*....|....*....|.
gi 495112432 189 LNKEDGRTIVMVTHNEEQAKQTSRTIRFFDG 219
Cdd:cd03222  117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEG 147
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
23-202 1.02e-07

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 51.87  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIM-GLLdAPSSGKIEInGTSVE-SMKDKELAAFR-NKTlgfvfqsfhlins 99
Cdd:PRK11147 335 VKDFSAQVQRGDKIALIGPNGCGKTTLLKLMlGQL-QADSGRIHC-GTKLEvAYFDQHRAELDpEKT------------- 399
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 lnVIDNVelpllyrkmaAKERtrlaKEVL----ERVGLS-------HRMRHM-PTQ-LSGGQCQRVAIARAIVGNPEIIL 166
Cdd:PRK11147 400 --VMDNL----------AEGK----QEVMvngrPRHVLGylqdflfHPKRAMtPVKaLSGGERNRLLLARLFLKPSNLLI 463
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 495112432 167 ADEPTGNLDskmgAEVMELLHKLNKEDGRTIVMVTH 202
Cdd:PRK11147 464 LDEPTNDLD----VETLELLEELLDSYQGTVLLVSH 495
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
32-202 1.41e-07

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: 51.32  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  32 KGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEingTSVE-SMKDKELAAFRNKTlgfvfqsfhlinslnVIDnvelpL 110
Cdd:COG1245  365 EGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVD---EDLKiSYKPQYISPDYDGT---------------VEE-----F 421
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 111 LYRKMAAKERTRLAK-EVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKL 189
Cdd:COG1245  422 LRSANTDDFGSSYYKtEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRF 501
                        170
                 ....*....|...
gi 495112432 190 NKEDGRTIVMVTH 202
Cdd:COG1245  502 AENRGKTAMVVDH 514
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
32-203 1.44e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 51.35  E-value: 1.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  32 KGEFVSIMGPSGCGKSTLLNIM-GLLDaPSSGKIEingTSVE-SMKDKELAAFRNKTlgfvfqsfhlinslnvidnVELP 109
Cdd:PRK13409 364 EGEVIGIVGPNGIGKTTFAKLLaGVLK-PDEGEVD---PELKiSYKPQYIKPDYDGT-------------------VEDL 420
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 110 LlyRKMAAKERTRLAK-EVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHK 188
Cdd:PRK13409 421 L--RSITDDLGSSYYKsEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRR 498
                        170
                 ....*....|....*
gi 495112432 189 LNKEDGRTIVMVTHN 203
Cdd:PRK13409 499 IAEEREATALVVDHD 513
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
140-205 4.18e-07

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: 48.76  E-value: 4.18e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112432 140 MPTQLSGGQ------CQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVM-ELLHKLNKEDGRTIVMVTHNEE 205
Cdd:cd03240  112 MRGRCSGGEkvlaslIIRLALAETFGSNCGILALDEPTTNLDEENIEESLaEIIEERKSQKNFQLIVITHDEE 184
PLN03130 PLN03130
ABC transporter C family member; Provisional
23-199 2.82e-06

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 47.43  E-value: 2.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkeLAAFRnKTLGFVFQS--------- 93
Cdd:PLN03130 1255 LHGLSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLR-KVLGIIPQApvlfsgtvr 1330
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   94 FHL--INSLNVIDNVElpllyrkmaAKERTRLaKEVLER--VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADE 169
Cdd:PLN03130 1331 FNLdpFNEHNDADLWE---------SLERAHL-KDVIRRnsLGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDE 1400
                         170       180       190
                  ....*....|....*....|....*....|
gi 495112432  170 PTGNLDSKMGAevmeLLHKLNKEDGRTIVM 199
Cdd:PLN03130 1401 ATAAVDVRTDA----LIQKTIREEFKSCTM 1426
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
3-222 3.54e-06

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: 46.10  E-value: 3.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRT--NEIETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLdapSSGKIEINGT-SVESMKDKEL 79
Cdd:cd03233    1 ASTLSWRNISFTTgkGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANR---TEGNVSVEGDiHYNGIPYKEF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  80 AAFRNKTLGFVFQSFHLINSLNVidnvelpllyrkmaakertrlaKEVLERVgLSHRMRHMPTQLSGGQCQRVAIARAIV 159
Cdd:cd03233   78 AEKYPGEIIYVSEEDVHFPTLTV----------------------RETLDFA-LRCKGNEFVRGISGGERKRVSIAEALV 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112432 160 GNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDGRTIVMVTH--NEEQAKQTSRTIRFFDGRQV 222
Cdd:cd03233  135 SRASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYqaSDEIYDLFDKVLVLYEGRQI 199
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
25-211 4.28e-06

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 46.58  E-value: 4.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  25 NVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAfrnktLGFVF-----QSFHLINS 99
Cdd:PRK15439 281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLA-----RGLVYlpedrQSSGLYLD 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 100 LNVIDNVeLPLLYRKMAAKERTRLAKEVLER------VGLSHRMRHMPTqLSGGQCQRVAIARAIVGNPEIILADEPTGN 173
Cdd:PRK15439 356 APLAWNV-CALTHNRRGFWIKPARENAVLERyrralnIKFNHAEQAART-LSGGNQQKVLIAKCLEASPQLLIVDEPTRG 433
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 495112432 174 LDSKMGAEVMELLHKLnKEDGRTIVMVTHNEEQAKQTS 211
Cdd:PRK15439 434 VDVSARNDIYQLIRSI-AAQNVAVLFISSDLEEIEQMA 470
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
23-201 4.62e-06

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: 46.74  E-value: 4.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVFQSFHLINSLN 101
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNPAQAIRAGIAMVPEDRKRHGIVPILG 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  102 VIDNVELPLLyRKMAAKERTRLAKEV------LERVGLSHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILADEPTGNL 174
Cdd:TIGR02633 356 VGKNITLSVL-KSFCFKMRIDAAAELqiigsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGV 434
                         170       180
                  ....*....|....*....|....*..
gi 495112432  175 DSKMGAEVMELLHKLNKEdGRTIVMVT 201
Cdd:TIGR02633 435 DVGAKYEIYKLINQLAQE-GVAIIVVS 460
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
24-200 7.10e-06

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 46.06  E-value: 7.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEING--TSVESMKDkelaAFR---------NKTLGFVfq 92
Cdd:PRK11288 270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGkpIDIRSPRD----AIRagimlcpedRKAEGII-- 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 sfhLINSlnVIDNVELP----------LLYRKmaaKERtRLAKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGN 161
Cdd:PRK11288 344 ---PVHS--VADNINISarrhhlragcLINNR---WEA-ENADRFIRSLNIKTPSREQLImNLSGGNQQKAILGRWLSED 414
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495112432 162 PEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMV 200
Cdd:PRK11288 415 MKVILLDEPTRGIDVGAKHEIYNVIYEL-AAQGVAVLFV 452
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
3-202 1.30e-05

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 44.78  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   3 MIKLTGINKIYRTNEIetlaLENVNLDVIKGEFVSIMGPSGCGKSTL-LNIMGLLDAP-SSGKIEINGTSVESMKDKELA 80
Cdd:PRK09580   1 MLSIKDLHVSVEDKAI----LRGLNLEVRPGEVHAIMGPNGSGKSTLsATLAGREDYEvTGGTVEFKGKDLLELSPEDRA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 ------AFRNKT-LGFVFQSFHLINSLNVIDNvelpllYRKMAAKERTRLAKEVLERVglshRMRHMPTQL--------- 144
Cdd:PRK09580  77 gegifmAFQYPVeIPGVSNQFFLQTALNAVRS------YRGQEPLDRFDFQDLMEEKI----ALLKMPEDLltrsvnvgf 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 145 SGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTH 202
Cdd:PRK09580 147 SGGEKKRNDILQMAVLEPELCILDESDSGLDIDALKIVADGVNSL-RDGKRSFIIVTH 203
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
4-171 1.90e-05

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 45.12  E-value: 1.90e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   4 IKLTGINKIYRtneiETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGtsvESMKDkelAAFR 83
Cdd:NF033858   2 ARLEGVSHRYG----KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLG---GDMAD---ARHR 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  84 NKT----------LGfvfqsFHLINSLNVIDNVELpllyrkMA------AKERTRLAKEVLERVGLsHRMRHMPT-QLSG 146
Cdd:NF033858  72 RAVcpriaympqgLG-----KNLYPTLSVFENLDF------FGrlfgqdAAERRRRIDELLRATGL-APFADRPAgKLSG 139
                        170       180
                 ....*....|....*....|....*
gi 495112432 147 GQCQRVAIARAIVGNPEIILADEPT 171
Cdd:NF033858 140 GMKQKLGLCCALIHDPDLLILDEPT 164
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
25-200 2.06e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 44.53  E-value: 2.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  25 NVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLDAPSSGKIEINGTSVESMKDKElaAFRN---------KTLGFVFQsf 94
Cdd:PRK13549 280 DVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQ--AIAQgiamvpedrKRDGIVPV-- 355
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  95 hlinsLNVIDNVELPLLYRKM------AAKERTRLAKEVLE-RVGLSHRMRHMpTQLSGGQCQRVAIARAIVGNPEIILA 167
Cdd:PRK13549 356 -----MGVGKNITLAALDRFTggsridDAAELKTILESIQRlKVKTASPELAI-ARLSGGNQQKAVLAKCLLLNPKILIL 429
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 168 DEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMV 200
Cdd:PRK13549 430 DEPTRGIDVGAKYEIYKLINQLVQQ-GVAIIVI 461
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
21-175 2.18e-05

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 44.72  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  21 LALENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGlLDAPSSGKIEInGTSVEsmkdkelaafrnktLGFVFQSF-HLIN 98
Cdd:PRK11819 338 LLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKmITG-QEQPDSGTIKI-GETVK--------------LAYVDQSRdALDP 401
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  99 SLNVIDNVELPLLYRKMAAKE---RTRLAK------EVLERVGlshrmrhmptQLSGGQCQRVAIARAIV--GNpeIILA 167
Cdd:PRK11819 402 NKTVWEEISGGLDIIKVGNREipsRAYVGRfnfkggDQQKKVG----------VLSGGERNRLHLAKTLKqgGN--VLLL 469

                 ....*...
gi 495112432 168 DEPTGNLD 175
Cdd:PRK11819 470 DEPTNDLD 477
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
23-175 2.61e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.39  E-value: 2.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLGFVF----------Q 92
Cdd:PRK10636  17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWQLAWVNQETPALPQPALEYVIdgdreyrqleA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  93 SFHLINSLNviDNVELPLLYRKMAAKE----RTRlAKEVLERVGLSHRMRHMP-TQLSGGQCQRVAIARAIVGNPEIILA 167
Cdd:PRK10636  97 QLHDANERN--DGHAIATIHGKLDAIDawtiRSR-AASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRSDLLLL 173

                 ....*...
gi 495112432 168 DEPTGNLD 175
Cdd:PRK10636 174 DEPTNHLD 181
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
23-203 4.10e-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: 43.37  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNimGLLDAPSSGKIEINGTSVESMKDKELAAFRNKTLgFVFQS--------- 93
Cdd:cd03271   11 LKNIDVDIPLGVLTCVTGVSGSGKSSLIN--DTLYPALARRLHLKKEQPGNHDRIEGLEHIDKVI-VIDQSpigrtprsn 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  94 -------FHLINSL----------------------NVIDNVELP----LLYRKMAAKERTRLakEVLERVGLSH-RMRH 139
Cdd:cd03271   88 patytgvFDEIRELfcevckgkrynretlevrykgkSIADVLDMTveeaLEFFENIPKIARKL--QTLCDVGLGYiKLGQ 165
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 140 MPTQLSGGQCQRVAIARAIV----GNPEIILaDEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVTHN 203
Cdd:cd03271  166 PATTLSGGEAQRIKLAKELSkrstGKTLYIL-DEPTTGLHFHDVKKLLEVLQRL-VDKGNTVVVIEHN 231
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
144-201 4.11e-05

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 43.95  E-value: 4.11e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495112432 144 LSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEDgRTIVMVT 201
Cdd:PRK10982 392 LSGGNQQKVIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKD-KGIIIIS 448
PLN03232 PLN03232
ABC transporter C family member; Provisional
23-200 5.44e-05

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 43.81  E-value: 5.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKDKELaafrNKTLGFVFQSFHLInSLNV 102
Cdd:PLN03232 1252 LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDL----RRVLSIIPQSPVLF-SGTV 1326
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  103 IDNVElPLLYRKMA----AKERTRLaKEVLER--VGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDS 176
Cdd:PLN03232 1327 RFNID-PFSEHNDAdlweALERAHI-KDVIDRnpFGLDAEVSEGGENFSVGQRQLLSLARALLRRSKILVLDEATASVDV 1404
                         170       180
                  ....*....|....*....|....
gi 495112432  177 KMGAevmeLLHKLNKEDGRTIVMV 200
Cdd:PLN03232 1405 RTDS----LIQRTIREEFKSCTML 1424
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
24-175 9.06e-05

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 42.96  E-value: 9.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  24 ENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIeingtsvesMKDKelaafrNKTLG------FVFQSFhli 97
Cdd:PRK15064  18 ENISVKFGGGNRYGLIGANGCGKSTFMKILGGDLEPSAGNV---------SLDP------NERLGklrqdqFAFEEF--- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 nslNVIDNVELPllYRKM--AAKERTRL--------------------------------AKEVLERVGLSHRMRHMP-T 142
Cdd:PRK15064  80 ---TVLDTVIMG--HTELweVKQERDRIyalpemseedgmkvadlevkfaemdgytaearAGELLLGVGIPEEQHYGLmS 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 143 QLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PRK15064 155 EVAPGWKLRVLLAQALFSNPDILLLDEPTNNLD 187
PLN03073 PLN03073
ABC transporter F family; Provisional
124-175 2.12e-04

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 41.77  E-value: 2.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495112432 124 AKEVLERVGLSHRMRHMPT-QLSGGQCQRVAIARAIVGNPEIILADEPTGNLD 175
Cdd:PLN03073 324 AASILAGLSFTPEMQVKATkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
11-205 2.12e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 41.80  E-value: 2.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  11 KIYRTN-EIETLA--------LENVNLDVIKGEFVSIMGPSGCGKSTLLN-IMGLLdAPSSGKIeingtsvesmKDKEla 80
Cdd:PRK15064 314 KLHRNAlEVENLTkgfdngplFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGEL-EPDSGTV----------KWSE-- 380
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  81 afrNKTLGFVFQ--SFHLINSLNVIDNVElplLYRKmaAKERTRLAKEVLERVGLSH-RMRHMPTQLSGGQCQRVAIARA 157
Cdd:PRK15064 381 ---NANIGYYAQdhAYDFENDLTLFDWMS---QWRQ--EGDDEQAVRGTLGRLLFSQdDIKKSVKVLSGGEKGRMLFGKL 452
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112432 158 IVGNPEIILADEPTGNLDskmgaevMELLHKLN----KEDGrTIVMVTHNEE 205
Cdd:PRK15064 453 MMQKPNVLVMDEPTNHMD-------MESIESLNmaleKYEG-TLIFVSHDRE 496
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
11-216 2.20e-04

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: 40.42  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  11 KIYRTNEIETLALENVNLdvikgefvsIMGPSGCGKSTLLNIMGLLdapssgkieingtsvesmkdkelaafrnktlgfV 90
Cdd:cd03227    8 PSYFVPNDVTFGEGSLTI---------ITGPNGSGKSTILDAIGLA---------------------------------L 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  91 FQSFHLinslnvidnvelplLYRKMAAKERTRLAKEVLERVGLSHrmrhmptQLSGGQCQRVAIA-----RAIVGNPEII 165
Cdd:cd03227   46 GGAQSA--------------TRRRSGVKAGCIVAAVSAELIFTRL-------QLSGGEKELSALAlilalASLKPRPLYI 104
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112432 166 LaDEPTGNLDSKMGAEVMELLHKLNKEDGRTIVmVTHNEEQAKQTSRTIRF 216
Cdd:cd03227  105 L-DEIDRGLDPRDGQALAEAILEHLVKGAQVIV-ITHLPELAELADKLIHI 153
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
132-200 2.84e-04

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 41.15  E-value: 2.84e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112432 132 GLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLDSKMGAEVMELLHKLNKEdGRTIVMV 200
Cdd:PRK10938 124 GITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQLAELLASLHQS-GITLVLV 191
GguA NF040905
sugar ABC transporter ATP-binding protein;
23-200 3.25e-04

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 40.93  E-value: 3.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLlnimglldAPS----------SGKIEINGTSVE--SMKDkelaAFRN------ 84
Cdd:NF040905 276 VDDVSLNVRRGEIVGIAGLMGAGRTEL--------AMSvfgrsygrniSGTVFKDGKEVDvsTVSD----AIDAglayvt 343
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  85 ---KTLGFVFQ----------SFHLINSLNVIDNVElpllYRKMAAKERTRL---AKEVLERVGlshrmrhmptQLSGGQ 148
Cdd:NF040905 344 edrKGYGLNLIddikrnitlaNLGKVSRRGVIDENE----EIKVAEEYRKKMnikTPSVFQKVG----------NLSGGN 409
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495112432 149 CQRVAIARAIVGNPEIILADEPTGNLDskMGA--EVMELLHKLNKEdGRTIVMV 200
Cdd:NF040905 410 QQKVVLSKWLFTDPDVLILDEPTRGID--VGAkyEIYTIINELAAE-GKGVIVI 460
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
126-203 4.87e-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: 40.77  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  126 EVLERVGLSH-RMRHMPTQLSGGQCQRVAIARAI---VGNPEIILADEPTGNLDSKMGAEVMELLHKLnKEDGRTIVMVT 201
Cdd:TIGR00630 811 QTLCDVGLGYiRLGQPATTLSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRL-VDKGNTVVVIE 889

                  ..
gi 495112432  202 HN 203
Cdd:TIGR00630 890 HN 891
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
23-51 1.01e-03

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: 39.61  E-value: 1.01e-03
                          10        20
                  ....*....|....*....|....*....
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN 51
Cdd:TIGR00630 624 LKNITVSIPLGLFTCITGVSGSGKSTLIN 652
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
18-208 1.49e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 38.31  E-value: 1.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  18 IETLALENVNLDVIKGEFVSIMGPSGCGKSTLLNIMGLLDAPSSGKIEINGTSVESMKdkelaafrNKTLGFVFQSFHLI 97
Cdd:PRK13541  11 IEQKNLFDLSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA--------KPYCTYIGHNLGLK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432  98 NSLNVIDNVelpllyrKMAAK--ERTRLAKEVLERVGLSHRMRHMPTQLSGGQCQRVAIARAIVGNPEIILADEPTGNLd 175
Cdd:PRK13541  83 LEMTVFENL-------KFWSEiyNSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDEVETNL- 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 495112432 176 SKMGAEVMELLHKLNKEDGRTIVMVTHNEEQAK 208
Cdd:PRK13541 155 SKENRDLLNNLIVMKANSGGIVLLSSHLESSIK 187
PRK00098 PRK00098
GTPase RsgA; Reviewed
18-51 1.52e-03

GTPase RsgA; Reviewed


Pssm-ID: 234631 [Multi-domain]  Cd Length: 298  Bit Score: 38.65  E-value: 1.52e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 495112432  18 IETLALENVNLDVIKGEF---VSI-MGPSGCGKSTLLN 51
Cdd:PRK00098 145 LELSAKEGEGLDELKPLLagkVTVlAGQSGVGKSTLLN 182
uvrA PRK00349
excinuclease ABC subunit UvrA;
23-51 2.80e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 38.52  E-value: 2.80e-03
                         10        20
                 ....*....|....*....|....*....
gi 495112432  23 LENVNLDVIKGEFVSIMGPSGCGKSTLLN 51
Cdd:PRK00349 625 LKNVDVEIPLGKFTCVTGVSGSGKSTLIN 653
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
23-49 3.35e-03

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: 38.07  E-value: 3.35e-03
                          10        20
                  ....*....|....*....|....*..
gi 495112432   23 LENVNLDVIKGEFVSIMGPSGCGKSTL 49
Cdd:TIGR00630  12 LKNIDVEIPRDKLVVITGLSGSGKSSL 38
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
109-203 4.76e-03

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 37.70  E-value: 4.76e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 PLLYRKMaakertrlakEVLERVGLSHrMR---HMPTqLSGGQCQRVAIARAIV----GNPEIILaDEPTGNL---DSKM 178
Cdd:COG0178  801 PKIARKL----------QTLQDVGLGY-IKlgqPATT-LSGGEAQRVKLASELSkrstGKTLYIL-DEPTTGLhfhDIRK 867
                         90       100
                 ....*....|....*....|....*
gi 495112432 179 gaeVMELLHKLnKEDGRTIVMVTHN 203
Cdd:COG0178  868 ---LLEVLHRL-VDKGNTVVVIEHN 888
AAA_16 pfam13191
AAA ATPase domain; This family of domains contain a P-loop motif that is characteriztic of the ...
12-51 7.42e-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: 35.94  E-value: 7.42e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 495112432   12 IYRTNEIETL--ALENVNLDviKGEFVSIMGPSGCGKSTLLN 51
Cdd:pfam13191   3 VGREEELEQLldALDRVRSG--RPPSVLLTGEAGTGKTTLLR 42
RsgA_GTPase pfam03193
RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are ...
11-51 7.68e-03

RsgA GTPase; RsgA (also known as EngC and YjeQ) represents a protein family whose members are broadly conserved in bacteria and are indispensable for growth. The GTPase domain of RsgA is very similar to several P-loop GTPases, but differs in having a circular permutation of the GTPase structure described by a G4-G1-G3 pattern.


Pssm-ID: 427191 [Multi-domain]  Cd Length: 174  Bit Score: 35.98  E-value: 7.68e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 495112432   11 KIYRTNEIETLALENVN-------LDVIKGEFVSIMGPSGCGKSTLLN 51
Cdd:pfam03193  77 KIYRAIGYPVLFVSAKTgegiealKELLKGKTTVLAGQSGVGKSTLLN 124
uvrA PRK00349
excinuclease ABC subunit UvrA;
109-203 9.83e-03

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 36.59  E-value: 9.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112432 109 PLLYRKMaakertrlakEVLERVGLSH-RMRHMPTQLSGGQCQRVAIA-----RAiVGNPEIILaDEPTGNLDSKMGAEV 182
Cdd:PRK00349 805 PKIARKL----------QTLVDVGLGYiKLGQPATTLSGGEAQRVKLAkelskRS-TGKTLYIL-DEPTTGLHFEDIRKL 872
                         90       100
                 ....*....|....*....|.
gi 495112432 183 MELLHKLnKEDGRTIVMVTHN 203
Cdd:PRK00349 873 LEVLHRL-VDKGNTVVVIEHN 892
 
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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