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Conserved domains on  [gi|2050094043|ref|WP_215576749|]
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methionine ABC transporter ATP-binding protein [Bacillus mycoides]

Protein Classification

methionine ABC transporter ATP-binding protein( domain architecture ID 11438975)

methionine ABC transporter ATP-binding protein similar to the ATPase domain of MetN, an ABC-type transporter that is involved in methionine transport

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-334 0e+00

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


:

Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 599.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1135     1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1135    81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:COG1135   161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKE 317
Cdd:COG1135   241 LPTVLNDELPEELLARLReaaGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
                         330
                  ....*....|....*..
gi 2050094043 318 IQKALQHLRLQVQLKEV 334
Cdd:COG1135   321 IDAALAYLREQGVVVEV 337
 
Name Accession Description Interval E-value
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-334 0e+00

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 599.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1135     1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1135    81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:COG1135   161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKE 317
Cdd:COG1135   241 LPTVLNDELPEELLARLReaaGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
                         330
                  ....*....|....*..
gi 2050094043 318 IQKALQHLRLQVQLKEV 334
Cdd:COG1135   321 IDAALAYLREQGVVVEV 337
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-326 0e+00

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 528.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK11153    1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11153   81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK11153  161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ-----NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQ 315
Cdd:PRK11153  241 IQSTLHLDLPEDYLARLQaepttGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
                         330
                  ....*....|.
gi 2050094043 316 KEIQKALQHLR 326
Cdd:PRK11153  321 GDIQAAIAYLQ 331
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-233 1.71e-153

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: 430.08  E-value: 1.71e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:cd03258     1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03258    81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:cd03258   161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ABC_MetN TIGR02314
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ...
1-326 6.12e-130

D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.


Pssm-ID: 131367 [Multi-domain]  Cd Length: 343  Bit Score: 374.60  E-value: 6.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR02314   1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR02314  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQ--IYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQ 315
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQatpFADSvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
                         330
                  ....*....|.
gi 2050094043 316 KEIQKALQHLR 326
Cdd:TIGR02314 321 QDTQAAIAYLQ 331
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
21-169 3.99e-52

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: 169.37  E-value: 3.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsaKELRKLRQRIGMIFQSFNLFNSRTVF 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 101 GNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKAN----YYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:pfam00005  78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
20-223 1.01e-30

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 122.93  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTI-----SIDDKDITSlsakelrklRQRIGMIFQSFNLF 94
Cdd:NF033858  281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT---------RRRVGYMSQAFSLY 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:NF033858  352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:NF033858  432 ARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASD 479
NIL smart00930
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ...
260-334 9.34e-22

This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.


Pssm-ID: 197998 [Multi-domain]  Cd Length: 76  Bit Score: 87.57  E-value: 9.34e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043  260 GGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKEIQKALQHLR-LQVQLKEV 334
Cdd:smart00930   1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLReQGVEVEVL 76
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
17-173 4.55e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 85.18  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslSAKELRKLRQRIGMIFQSF--NLF 94
Cdd:NF033858   13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAYMPQGLgkNLY 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:NF033858   91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-221 5.68e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.37  E-value: 5.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDD-----KDItslSAKElrklRQRIGMIFQ 89
Cdd:NF040905   14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGevcrfKDI---RDSE----ALGIVIIHQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  90 SF----------NLF--NSRTVFGNIAYplrlaklpkNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:NF040905   86 ELalipylsiaeNIFlgNERAKRGVIDW---------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:NF040905  157 DVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
18-238 1.75e-16

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 79.39  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlRLVNMLERPTAGTisiDDKDITSLSAKElRKLRQRIG----MIFQSFNL 93
Cdd:NF000106   26 VKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANR-RALRRTIG*hrpVR*GRRES 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSRTvfgNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:NF000106  101 FSGRE---NLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 174 ETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQ 238
Cdd:NF000106  178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
GguA NF040905
sugar ABC transporter ATP-binding protein;
21-222 2.57e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 52.10  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSLS-----------AKELRKlrqRIGMi 87
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTvsdaidaglayVTEDRK---GYGL- 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  88 fqsfNLFNsrTVFGNIAyplrLAKLPK-------NEIKE-RVNE------LLKFVGLEDKAnyypEQLSGGQKQRVGIAR 153
Cdd:NF040905  352 ----NLID--DIKRNIT----LANLGKvsrrgviDENEEiKVAEeyrkkmNIKTPSVFQKV----GNLSGGNQQKVVLSK 417
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:NF040905  418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
 
Name Accession Description Interval E-value
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
1-334 0e+00

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 599.37  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1135     1 MIELENLSKTFPTKGGPVTALDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERELRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1135    81 RRKIGMIFQHFNLLSSRTVAENVALPLEIAGVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:COG1135   161 VLLCDEATSALDPETTRSILDLLKDINRELGLTIVLITHEMDVVRRICDRVAVLENGRIVEQGPVLDVFANPQSELTRRF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKE 317
Cdd:COG1135   241 LPTVLNDELPEELLARLReaaGGGRLVRLTFVGESADEPLLSELARRFGVDVNILSGGIEEIQGTPVGRLIVELEGDDAA 320
                         330
                  ....*....|....*..
gi 2050094043 318 IQKALQHLRLQVQLKEV 334
Cdd:COG1135   321 IDAALAYLREQGVVVEV 337
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
1-326 0e+00

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 528.99  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK11153    1 MIELKNISKVFPQGGRTIHALNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTALSEKELRKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11153   81 RRQIGMIFQHFNLLSSRTVFDNVALPLELAGTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK11153  161 VLLCDEATSALDPATTRSILELLKDINRELGLTIVLITHEMDVVKRICDRVAVIDAGRLVEQGTVSEVFSHPKHPLTREF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ-----NGGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQ 315
Cdd:PRK11153  241 IQSTLHLDLPEDYLARLQaepttGSGPLLRLEFTGESVDAPLLSETARRFGVDFNILSGQIDYIGGVKFGSLLVELTGDP 320
                         330
                  ....*....|.
gi 2050094043 316 KEIQKALQHLR 326
Cdd:PRK11153  321 GDIQAAIAYLQ 331
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
1-233 1.71e-153

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: 430.08  E-value: 1.71e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:cd03258     1 MIELKNVSKVFGDTGGKVTALKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKELRKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03258    81 RRRIGMIFQHFNLLSSRTVFENVALPLEIAGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPK 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:cd03258   161 VLLCDEATSALDPETTQSILALLRDINRELGLTIVLITHEMEVVKRICDRVAVMEKGEVVEEGTVEEVFANPQ 233
ABC_MetN TIGR02314
D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding ...
1-326 6.12e-130

D-methionine ABC transporter, ATP-binding protein; Members of this family are the ATP-binding protein of the D-methionine ABC transporter complex. Known members belong to the Proteobacteria.


Pssm-ID: 131367 [Multi-domain]  Cd Length: 343  Bit Score: 374.60  E-value: 6.12e-130
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR02314   1 MIKLSNITKVFHQGTKTIQALNNVSLHVPAGQIYGVIGASGAGKSTLIRCVNLLERPTSGSVIVDGQDLTTLSNSELTKA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR02314  81 RRQIGMIFQHFNLLSSRTVFGNVALPLELDNTPKDEIKRKVTELLALVGLGDKHDSYPSNLSGGQKQRVAIARALASNPK 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:TIGR02314 161 VLLCDEATSALDPATTQSILELLKEINRRLGLTILLITHEMDVVKRICDCVAVISNGELIEQGTVSEIFSHPKTPLAQKF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 241 VRSVINDHLPESVLAKIQ---NGGQ--IYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQ 315
Cdd:TIGR02314 241 IRSTLHLSIPEDYQERLQatpFADSvpMVRLEFTGQTVDAPLLSQTARRFNVDNSILSSQMDYAGGVKFGIMLAEMHGTQ 320
                         330
                  ....*....|.
gi 2050094043 316 KEIQKALQHLR 326
Cdd:TIGR02314 321 QDTQAAIAYLQ 331
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
1-244 3.85e-107

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 312.70  E-value: 3.85e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITsLSAKELRKL 80
Cdd:COG1126     1 MIEIENLHKSFGD----LEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLT-DSKKDINKL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAY-PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG1126    76 RRKVGMVFQQFNLFPHLTVLENVTLaPIKVKKMSKAEAEERAMELLERVGLADKADAYPAQLSGGQQQRVAIARALAMEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQN 239
Cdd:COG1126   156 KVMLFDEPTSALDPELVGEVLDVMRDLAKE-GMTMVVVTHEMGFAREVADRVVFMDGGRIVEEGPPEEFFENPQHERTRA 234

                  ....*
gi 2050094043 240 FVRSV 244
Cdd:COG1126   235 FLSKV 239
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-244 4.24e-106

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: 319.93  E-value: 4.24e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYES-GGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK 79
Cdd:COG1123   260 LLEVRNLSKRYPVrGKGGVRAVDDVSLTLRRGETLGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRSLRE 339
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQS-FNLFNSR-TVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:COG1123   340 LRRRVQMVFQDpYSSLNPRmTVGDIIAEPLRLHGlLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARAL 419
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:COG1123   420 ALEPKLLILDEPTSALDVSVQAQILNLLRDLQRELGLTYLFISHDLAVVRYIADRVAVMYDGRIVEDGPTEEVFANPQHP 499

                  ....*....
gi 2050094043 236 TTQNFVRSV 244
Cdd:COG1123   500 YTRALLAAV 508
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
1-222 1.28e-102

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 300.81  E-value: 1.28e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1136     4 LLELRNLTKSYGTGEGEVTALRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG1136    84 RrRHIGFVFQFFNLLPELTALENVALPLLLAGVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARALVNRP 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHvVKEICHRVAVMEKGKVIEE 222
Cdd:COG1136   164 KLILADEPTGNLDSKTGEEVLELLRELNRELGTTIVMVTHDPE-LAARADRVIRLRDGRIVSD 225
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
1-223 1.79e-100

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: 295.74  E-value: 1.79e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVHavEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1127     5 MIEVRNLTKSF--GDRVVL--DGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGLSEKELYEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG1127    81 RRRIGMLFQGGALFDSLTVFENVAFPLReHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARALALDP 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG1127   161 EILLYDEPTAGLDPITSAVIDELIRELRDELGLTSVVVTHDLDSAFAIADRVAVLADGKIIAEG 224
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-233 1.15e-95

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: 286.56  E-value: 1.15e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERP--TAGTISIDDKDITSLSAKEL 77
Cdd:COG0444     1 LLEVRNLKVYFPTRRGVVKAVDGVSFDVRRGETLGLVGESGSGKSTLARaILGLLPPPgiTSGEILFDGEDLLKLSEKEL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKLR-QRIGMIFQ-SFNLFNSR-TVFGNIAYPLRL-AKLPKNEIKERVNELLKFVGL---EDKANYYPEQLSGGQKQRVG 150
Cdd:COG0444    81 RKIRgREIQMIFQdPMTSLNPVmTVGDQIAEPLRIhGGLSKAEARERAIELLERVGLpdpERRLDRYPHELSGGMRQRVM 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:COG0444   161 IARALALEPKLLIADEPTTALDVTIQAQILNLLKDLQRELGLAILFITHDLGVVAEIADRVAVMYAGRIVEEGPVEELFE 240

                  ...
gi 2050094043 231 QPK 233
Cdd:COG0444   241 NPR 243
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
1-224 4.03e-95

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 281.56  E-value: 4.03e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG2884     1 MIRFENVSKRYPGG---REALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRLKRREIPYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG2884    78 RRRIGVVFQDFRLLPDRTVYENVALPLRVTGKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPE 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:COG2884   158 LLLADEPTGNLDPETSWEIMELLEEINRR-GTTVLIATHDLELVDRMPKRVLELEDGRLVRDEA 220
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
2-219 4.80e-95

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: 281.30  E-value: 4.80e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03255     1 IELKNLSKTYGGGGEKVQALKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKELAAFR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 -QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03255    81 rRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERAEELLERVGLGDRLNHYPSELSGGQQQRVAIARALANDPK 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:cd03255   161 IILADEPTGNLDSETGKEVMELLRELNKEAGTTIVVVTHDPELA-EYADRIIELRDGKI 218
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
1-223 9.01e-91

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: 270.92  E-value: 9.01e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:cd03257     1 LLEVKNLSVSFPTGGGSVKALDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLRKIR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQ-SFNLFN-SRTVFGNIAYPLRLAKLPKNE--IKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:cd03257    81 RKEIQMVFQdPMSSLNpRMTIGEQIAEPLRIHGKLSKKeaRKEAVLLLLVGVGLpEEVLNRYPHELSGGQRQRVAIARAL 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03257   161 ALNPKLLIADEPTSALDVSVQAQILDLLKKLQEELGLTLLFITHDLGVVAKIADRVAVMYAGKIVEEG 228
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
2-243 3.29e-90

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: 269.76  E-value: 3.29e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVHavEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03261     1 IELRGLTKSF--GGRTVL--KGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISGLSEAELYRLR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03261    77 RRMGMLFQSGALFDSLTVFENVAFPLReHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGklfdvfTQPKTKTTQN- 239
Cdd:cd03261   157 LLLYDEPTAGLDPIASGVIDDLIRSLKKELGLTSIMVTHDLDTAFAIADRIAVLYDGKIVAEG------TPEELRASDDp 230

                  ....
gi 2050094043 240 FVRS 243
Cdd:cd03261   231 LVRQ 234
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
1-245 6.84e-90

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: 269.37  E-value: 6.84e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKL 80
Cdd:COG1124     1 MLEVRNLSVSYGQGGRRVPVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVT---RRRRKAF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQ----SFNLFnsRTVFGNIAYPLRLAKLPknEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:COG1124    78 RRRVQMVFQdpyaSLHPR--HTVDRILAEPLRIHGLP--DREERIAELLEQVGLpPSFLDRYPHQLSGGQRQRVAIARAL 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:COG1124   154 ILEPELLLLDEPTSALDVSVQAEILNLLKDLREERGLTYLFVSHDLAVVAHLCDRVAVMQNGRIVEELTVADLLAGPKHP 233
                         250
                  ....*....|
gi 2050094043 236 TTQNFVRSVI 245
Cdd:COG1124   234 YTRELLAASL 243
ProV COG4175
ABC-type proline/glycine betaine transport system, ATPase component [Amino acid transport and ...
1-244 2.89e-86

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


Pssm-ID: 443334 [Multi-domain]  Cd Length: 389  Bit Score: 265.04  E-value: 2.89e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVY---------------------ESGGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTA 59
Cdd:COG4175     3 KIEVRNLYKIFgkrperalklldqgkskdeilEKTGQTV-GVNDASFDVEEGEIFVIMGLSGSGKSTLVRCLNRLIEPTA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  60 GTISIDDKDITSLSAKELRKLRQ-RIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYP 138
Cdd:COG4175    82 GEVLIDGEDITKLSKKELRELRRkKMSMVFQHFALLPHRTVLENVAFGLEIQGVPKAERRERAREALELVGLAGWEDSYP 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 139 EQLSGGQKQRVGIARALATSPDILICDEATSALDP----ETTTEILNLLKKVNReynlTILLITHEMHvvkE---ICHRV 211
Cdd:COG4175   162 DELSGGMQQRVGLARALATDPDILLMDEAFSALDPlirrEMQDELLELQAKLKK----TIVFITHDLD---EalrLGDRI 234
                         250       260       270
                  ....*....|....*....|....*....|...
gi 2050094043 212 AVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:COG4175   235 AIMKDGRIVQIGTPEEILTNPANDYVADFVEDV 267
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
1-227 1.43e-85

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 258.06  E-value: 1.43e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG3638     2 MLELRNLSKRYPGG---TPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRALRRL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIaypL--RLAKLP---------KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG3638    79 RRRIGMIFQQFNLVPRLSVLTNV---LagRLGRTStwrsllglfPPEDRERALEALERVGLADKAYQRADQLSGGQQQRV 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIeegklFD 227
Cdd:COG3638   156 AIARALVQEPKLILADEPVASLDPKTARQVMDLLRRIAREDGITVVVNLHQVDLARRYADRIIGLRDGRVV-----FD 228
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
2-219 1.69e-85

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: 256.69  E-value: 1.69e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlSAKELRKLR 81
Cdd:cd03262     1 IEIKNLHKSF--GDF--HVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLTD-DKKNINELR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLA-KLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03262    76 QKVGMVFQQFNLFPHLTVLENITLAPIKVkGMSKAEAEERALELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03262   156 VMLFDEPTSALDPELVGEVLDVMKDLAEE-GMTMVVVTHEMGFAREVADRVIFMDDGRI 213
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
1-241 5.27e-85

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 260.42  E-value: 5.27e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkELRkl 80
Cdd:COG3842     5 ALELENVSKRYGD----VTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVTGLPP-EKR-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG3842    78 --NVGMVFQDYALFPHLTVAENVAFGLRMRGVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQRVALARALAPEPR 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHvvkE---ICHRVAVMEKGKVIEEGKLFDVFTQPKTKTT 237
Cdd:COG3842   156 VLLLDEPLSALDAKLREEMREELRRLQRELGITFIYVTHDQE---EalaLADRIAVMNDGRIEQVGTPEEIYERPATRFV 232

                  ....
gi 2050094043 238 QNFV 241
Cdd:COG3842   233 ADFI 236
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
1-222 9.92e-85

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 256.55  E-value: 9.92e-85
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelrkl 80
Cdd:COG1116     7 ALELRGVSKRFPTGGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVTGPGP------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1116    81 --DRGVVFQEPALLPWLTVLDNVALGLELRGVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALANDPE 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEmhvVKE---ICHRVAVMEK--GKVIEE 222
Cdd:COG1116   159 VLLMDEPFGALDALTRERLQDELLRLWQETGKTVLFVTHD---VDEavfLADRVVVLSArpGRIVEE 222
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
5-233 1.58e-84

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 258.51  E-value: 1.58e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   5 NNISKVYESGG-------QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKEL 77
Cdd:COG4608    11 RDLKKHFPVRGglfgrtvGVVKAVDGVSFDIRRGETLGLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGREL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKLRQRIGMIFQ-SFNLFNSR-TVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIAR 153
Cdd:COG4608    91 RPLRRRMQMVFQdPYASLNPRmTVGDIIAEPLRIHGLaSKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIAR 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:COG4608   171 ALALNPKLIVCDEPVSALDVSIQAQVLNLLEDLQDELGLTYLFISHDLSVVRHISDRVAVMYLGKIVEIAPRDELYARPL 250
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
10-244 2.53e-84

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: 256.03  E-value: 2.53e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  10 VYESGGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR-QRIGMIF 88
Cdd:cd03294    30 ILKKTGQTV-GVNDVSLDVREGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAMSRKELRELRrKKISMVF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 QSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:cd03294   109 QSFALLPHRTVLENVAFGLEVQGVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRVGLARALAVDPDILLMDEAF 188
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 169 SALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:cd03294   189 SALDPLIRREMQDELLRLQAELQKTIVFITHDLDEALRLGDRIAIMKDGRLVQVGTPEEILTNPANDYVREFFRGV 264
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
2-234 4.01e-83

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: 251.48  E-value: 4.01e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKLR 81
Cdd:COG1122     1 IELENLSFSYPGG---TPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDIT---KKNLRELR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQsfN----LFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:COG1122    75 RKVGLVFQ--NpddqLFAP-TVEEDVAFGPENLGLPREEIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAM 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:COG1122   152 EPEVLVLDEPTAGLDPRGRRELLELLKRLNKE-GKTVIIVTHDLDLVAELADRVIVLDDGRIVADGTPREVFSDYEL 227
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
2-223 6.73e-82

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: 247.43  E-value: 6.73e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklR 81
Cdd:cd03259     1 LELKGLSKTY----GSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDVTGVPPE-----R 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03259    72 RNIGMVFQDYALFPHLTVAENIAFGLKLRGVPKAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03259   152 LLLDEPLSALDAKLREELREELKELQRELGITTIYVTHDQEEALALADRIAVMNEGRIVQVG 213
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
2-222 2.09e-81

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: 246.61  E-value: 2.09e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelrklr 81
Cdd:cd03293     1 LEVRNVSKTYGGGGGAVTALEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVTGPGP------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03293    74 -DRGYVFQQDALLPWLTVLDNVALGLELQGVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEK--GKVIEE 222
Cdd:cd03293   153 LLLDEPFSALDALTREQLQEELLDIWRETGKTVLLVTHDIDEAVFLADRVVVLSArpGRIVAE 215
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
2-225 5.52e-79

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 241.12  E-value: 5.52e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKLR 81
Cdd:COG1131     1 IEVRGLTKRY----GDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDV----ARDPAEVR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:COG1131    73 RRIGYVPQEPALYPDLTVRENLRFFARLYGLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPEL 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKL 225
Cdd:COG1131   153 LILDEPTSGLDPEARRELWELLRELAAE-GKTVLLSTHYLEEAERLCDRVAIIDKGRIVADGTP 215
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
1-233 1.91e-77

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: 245.97  E-value: 1.91e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgqSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTA---GTISIDDKDITSLSAKEL 77
Cdd:COG1123     4 LLEVRDLSVRYPGG--DVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGGrisGEVLLDGRDLLELSEALR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKlrqRIGMIFQSF-NLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:COG1123    82 GR---RIGMVFQDPmTQLNPVTVGDQIAEALENLGLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:COG1123   159 LDPDLLIADEPTTALDVTTQAEILDLLRELQRERGTTVLLITHDLGVVAEIADRVVVMDDGRIVEDGPPEEILAAPQ 235
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
2-224 3.43e-77

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: 236.70  E-value: 3.43e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03256     1 IEVENLSKTYPNG---KKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGKALRQLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNI-----AY--PLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIAR 153
Cdd:cd03256    78 RQIGMIFQQFNLIERLSVLENVlsgrlGRrsTWRsLFGLFPKEEKQRALAALERVGLLDKAYQRADQLSGGQQQRVAIAR 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:cd03256   158 ALMQQPKLILADEPVASLDPASSRQVMDLLKRINREEGITVIVSLHQVDLAREYADRIVGLKDGRIVFDGP 228
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
2-233 2.68e-76

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: 235.42  E-value: 2.68e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR04521   1 IKLKNVSYIYQPGTPfEKKALDDVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKKKLKDL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQsF---NLFnSRTVFGNIAY-PLRLaKLPKNEIKERVNELLKFVGLEDKanYY---PEQLSGGQKQRVGIAR 153
Cdd:TIGR04521  81 RKKVGLVFQ-FpehQLF-EETVYKDIAFgPKNL-GLSEEEAEERVKEALELVGLDEE--YLersPFELSGGQMRRVAIAG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:TIGR04521 156 VLAMEPEVLILDEPTAGLDPKGRKEILDLFKRLHKEKGLTVILVTHSMEDVAEYADRVIVMHKGKIVLDGTPREVFSDVD 235
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
3-218 1.09e-74

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: 229.28  E-value: 1.09e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   3 SFNNISKVYESGGQSvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrq 82
Cdd:cd03225     1 ELKNLSFSYPDGARP--ALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLTKLSLKELRR--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIGMIFQSFN--LFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03225    76 KVGLVFQNPDdqFFGP-TVEEEVAFGLENLGLPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPD 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd03225   155 ILLLDEPTAGLDPAGRRELLELLKKLKAE-GKTIIIVTHDLDLLLELADRVIVLEDGK 211
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
1-224 1.37e-73

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: 227.57  E-value: 1.37e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:TIGR02315   1 MLEVENLSKVYPNG---KQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGKKLRKL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPlRLAKLP---------KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGI 151
Cdd:TIGR02315  78 RRRIGMIFQHYNLIERLTVLENVLHG-RLGYKPtwrsllgrfSEEDKERALSALERVGLADKAYQRADQLSGGQQQRVAI 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:TIGR02315 157 ARALAQQPDLILADEPIASLDPKTSKQVMDYLKRINKEDGITVIINLHQVDLAKKYADRIVGLKAGEIVFDGA 229
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
18-244 1.47e-73

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: 236.50  E-value: 1.47e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTL----LRLVnmlerPTAGTISIDDKDITSLSAKELRKLRQRIGMIFQS-FN 92
Cdd:COG4172   299 VKAVDGVSLTLRRGETLGLVGESGSGKSTLglalLRLI-----PSEGEIRFDGQDLDGLSRRALRPLRRRMQVVFQDpFG 373
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  93 LFNSR-TVFGNIAYPLRL--AKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:COG4172   374 SLSPRmTVGQIIAEGLRVhgPGLSAAERRARVAEALEEVGLdPAARHRYPHEFSGGQRQRIAIARALILEPKLLVLDEPT 453
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 169 SALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:COG4172   454 SALDVSVQAQILDLLRDLQREHGLAYLFISHDLAVVRALAHRVMVMKDGKVVEQGPTEQVFDAPQHPYTRALLAAA 529
ectoine_ehuA TIGR03005
ectoine/hydroxyectoine ABC transporter, ATP-binding protein; Members of this family are the ...
2-245 7.55e-73

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


Pssm-ID: 132050 [Multi-domain]  Cd Length: 252  Bit Score: 225.86  E-value: 7.55e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSL--------- 72
Cdd:TIGR03005   1 VRFSDVTKRFGI----LTVLDGLNFSVAAGEKVALIGPSGSGKSTILRILMTLEPIDEGQIQVEGEQLYHMpgrngplvp 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  73 -SAKELRKLRQRIGMIFQSFNLFNSRTVFGNIAY-PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVG 150
Cdd:TIGR03005  77 aDEKHLRQMRNKIGMVFQSFNLFPHKTVLDNVTEaPVLVLGMARAEAEKRAMELLDMVGLADKADHMPAQLSGGQQQRVA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:TIGR03005 157 IARALAMRPKVMLFDEVTSALDPELVGEVLNVIRRLASEHDLTMLLVTHEMGFAREFADRVCFFDKGRIVEQGKPDEIFR 236
                         250
                  ....*....|....*
gi 2050094043 231 QPKTKTTQNFVRSVI 245
Cdd:TIGR03005 237 QPKEERTREFLSKVI 251
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
1-241 2.08e-72

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 228.03  E-value: 2.08e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:COG3839     3 SLELENVSKSY----GGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDVTDLPPKD---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG3839    75 R-NIAMVFQSYALYPHMTVYENIAFPLKLRKVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPK 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDP----ETTTEIlnllKKVNREYNLTILLITHEMHvvkE---ICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:COG3839   154 VFLLDEPLSNLDAklrvEMRAEI----KRLHRRLGTTTIYVTHDQV---EamtLADRIAVMNDGRIQQVGTPEELYDRPA 226

                  ....*...
gi 2050094043 234 TKttqnFV 241
Cdd:COG3839   227 NL----FV 230
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
2-231 2.31e-72

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: 225.39  E-value: 2.31e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitSLSAKELRKLR 81
Cdd:TIGR04520   1 IEVENVSFSYP--ESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLD--TLDEENLWEIR 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR04520  77 KKVGMVFQNpDNQFVGATVEDDVAFGLENLGVPREEMRKRVDEALKLVGMEDFRDREPHLLSGGQKQRVAIAGVLAMRPD 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMhvvKEI--CHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:TIGR04520 157 IIILDEATSMLDPKGRKEVLETIRKLNKEEGITVISITHDM---EEAvlADRVIVMNKGKIVAEGTPREIFSQ 226
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
2-234 3.96e-72

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 227.34  E-value: 3.96e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI-TSLSAKElrkl 80
Cdd:COG1118     3 IEVRNISKRFGS----FTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLfTNLPPRE---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RqRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG1118    75 R-RVGFVFQHYALFPHMTVAENIAFGLRVRPPSKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQRVALARALAVEPE 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:COG1118   154 VLLLDEPFGALDAKVRKELRRWLRRLHDELGGTTVFVTHDQEEALELADRVVVMNQGRIEQVGTPDEVYDRPAT 227
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
1-233 8.73e-72

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: 231.88  E-value: 8.73e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERPTA---GTISIDDKDITSLSAKE 76
Cdd:COG4172     6 LLSVEDLSVAFGQGGGTVEAVKGVSFDIAAGETLALVGESGSGKSvTALSILRLLPDPAAhpsGSILFDGQDLLGLSERE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  77 LRKLR-QRIGMIFQ----SFN-LFnsrTVFGNIAYPLRL-AKLPKNEIKERVNELLKFVGL---EDKANYYPEQLSGGQK 146
Cdd:COG4172    86 LRRIRgNRIAMIFQepmtSLNpLH---TIGKQIAEVLRLhRGLSGAAARARALELLERVGIpdpERRLDAYPHQLSGGQR 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:COG4172   163 QRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLQRELGMALLLITHDLGVVRRFADRVAVMRQGEIVEQGPTA 242

                  ....*..
gi 2050094043 227 DVFTQPK 233
Cdd:COG4172   243 ELFAAPQ 249
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
1-243 3.89e-71

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 221.60  E-value: 3.89e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDIT---------- 70
Cdd:COG4598     8 ALEVRDLHKSF--GDLEV--LKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRlkpdrdgelv 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  71 SLSAKELRKLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG4598    84 PADRRQLQRIRTRLGMVFQSFNLWSHMTVLENvIEAPVHVLGRPKAEAIERAEALLAKVGLADKRDAYPAHLSGGQQQRA 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVF 229
Cdd:COG4598   164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGR-TMLVVTHEMGFARDVSSHVVFLHQGRIEEQGPPAEVF 242
                         250
                  ....*....|....
gi 2050094043 230 TQPKTKTTQNFVRS 243
Cdd:COG4598   243 GNPKSERLRQFLSS 256
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
2-242 6.05e-71

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 220.65  E-value: 6.05e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI---TSLSAKELR 78
Cdd:COG4161     3 IQLKNINCFY----GSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsQKPSEKAIR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:COG4161    79 LLRQKVGMVFQQYNLWPHLTVMENlIEAPCKVLGLSKEQAREKAMKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNrEYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLfDVFTQPKTKTT 237
Cdd:COG4161   159 EPQVLLFDEPTAALDPEITAQVVEIIRELS-QTGITQVIVTHEVEFARKVASQVVYMEKGRIIEQGDA-SHFTQPQTEAF 236

                  ....*
gi 2050094043 238 QNFVR 242
Cdd:COG4161   237 AHYLS 241
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
2-218 6.68e-71

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: 218.21  E-value: 6.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesgGQsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSaKELRKLR 81
Cdd:cd03229     1 LELKNVSKRY---GQ-KTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLE-DELPPLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPlrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03229    76 RRIGMVFQDFALFPHLTVLENIALG----------------------------------LSGGQQQRVALARALAMDPDV 121
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd03229   122 LLLDEPTSALDPITRREVRALLKSLQAQLGITVVLVTHDLDEAARLADRVVVLRDGK 178
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
2-219 1.94e-70

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: 218.43  E-value: 1.94e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:cd03292     1 IEFINVTKTYPNG---TAALDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRAIPYLR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03292    78 RKIGVVFQDFRLLPDRNVYENVAFALEVTGVPPREIRKRVPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTI 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03292   158 LIADEPTGNLDPDTTWEIMNLLKKINKA-GTTVVVATHAKELVDTTRHRVIALERGKL 214
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
2-224 3.43e-69

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: 215.51  E-value: 3.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKE 76
Cdd:cd03260     1 IELRDLNVYYGDK----HALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRLndlipGAPDEGEVLLDGKDIYDLDVDV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  77 LRkLRQRIGMIFQSFNLFNSrTVFGNIAYPLRLA-KLPKNEIKERVNELLKFVGLED--KANYYPEQLSGGQKQRVGIAR 153
Cdd:cd03260    77 LE-LRRRVGMVFQKPNPFPG-SIYDNVAYGLRLHgIKLKEELDERVEEALRKAALWDevKDRLHALGLSGGQQQRLCLAR 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:cd03260   155 ALANEPEVLLLDEPTSALDPISTAKIEELIAELKKEY--TIVIVTHNMQQAARVADRTAFLLNGRLVEFGP 223
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
2-241 3.71e-69

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: 215.95  E-value: 3.71e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklR 81
Cdd:cd03300     1 IELENVSKFYGGF----VALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDITNLPPH-----K 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03300    72 RPVNTVFQNYALFPHLTVFENIAFGLRLKKLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:cd03300   152 LLLDEPLGALDLKLRKDMQLELKRLQKELGITFVFVTHDQEEALTMSDRIAVMNKGKIQQIGTPEEIYEEPANRFVADFI 231
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
2-240 6.43e-69

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 215.65  E-value: 6.43e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI---TSLSAKELR 78
Cdd:PRK11124    3 IQLNGINCFYGAH-QALF---DITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNHFdfsKTPSDKAIR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK11124   79 ELRRNVGMVFQQYNLWPHLTVQQNlIEAPCRVLGLSKDQALARAEKLLERLRLKPYADRFPLHLSGGQQQRVAIARALMM 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLfDVFTQPKTKTT 237
Cdd:PRK11124  159 EPQVLLFDEPTAALDPEITAQIVSIIREL-AETGITQVIVTHEVEVARKTASRVVYMENGHIVEQGDA-SCFTQPQTEAF 236

                  ...
gi 2050094043 238 QNF 240
Cdd:PRK11124  237 KNY 239
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
2-245 3.24e-68

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: 213.70  E-value: 3.24e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:cd03295     1 IEFENVTKRYGGGKK---AVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDIREQDPVELRR-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDK--ANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:cd03295    76 -KIGYVIQQIGLFPHMTVEENIALVPKLLKWPKEKIRERADELLALVGLDPAefADRYPHELSGGQQQRVGVARALAADP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTkttqN 239
Cdd:cd03295   155 PLLLMDEPFGALDPITRDQLQEEFKRLQQELGKTIVFVTHDIDEAFRLADRIAIMKNGEIVQVGTPDEILRSPAN----D 230

                  ....*.
gi 2050094043 240 FVRSVI 245
Cdd:cd03295   231 FVAEFV 236
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
1-244 9.04e-68

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 212.65  E-value: 9.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesgGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElRKL 80
Cdd:PRK09493    1 MIEFKNVSKHF---GPTQ-VLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVNDPKVDE-RLI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAY-PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK09493   76 RQEAGMVFQQFYLFPHLTALENVMFgPLRVRGASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQN 239
Cdd:PRK09493  156 KLMLFDEPTSALDPELRHEVLKVMQDLAEE-GMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVLIKNPPSQRLQE 234

                  ....*
gi 2050094043 240 FVRSV 244
Cdd:PRK09493  235 FLQHV 239
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
1-247 5.52e-67

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 210.76  E-value: 5.52e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYEsgGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDIT---SLSAKE- 76
Cdd:PRK11264    3 AIEVKNLVKKFH--GQTV--LHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDtarSLSQQKg 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  77 -LRKLRQRIGMIFQSFNLFNSRTVFGN-IAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK11264   79 lIRQLRQHVGFVFQNFNLFPHRTVLENiIEGPVIVKGEPKEEATARARELLAKVGLAGKETSYPRRLSGGQQQRVAIARA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK11264  159 LAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQE-KRTMVIVTHEMSFARDVADRAIFMDQGRIVEQGPAKALFADPQQ 237
                         250
                  ....*....|...
gi 2050094043 235 KTTQNFVRSVIND 247
Cdd:PRK11264  238 PRTRQFLEKFLLQ 250
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
1-222 1.16e-66

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: 209.21  E-value: 1.16e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG4181     8 IIELRGLTKTVGTGAGELTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFALDEDARARL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPknEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG4181    88 RaRHVGFVFQSFQLLPTLTALENVMLPLELAGRR--DARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAFATEP 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEE 222
Cdd:COG4181   166 AILFADEPTGNLDAATGEQIIDLLFELNRERGTTLVLVTHDPALAAR-CDRVLRLRAGRLVED 227
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
1-224 4.12e-66

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: 208.74  E-value: 4.12e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRkl 80
Cdd:COG0411     4 LLEVRGLTKRF--GG--LVAVDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIA-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNI-------------AYPLRLAKLPKNE--IKERVNELLKFVGLEDKANYYPEQLSGGQ 145
Cdd:COG0411    78 RLGIARTFQNPRLFPELTVLENVlvaaharlgrgllAALLRLPRARREEreARERAEELLERVGLADRADEPAGNLSYGQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 146 KQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:COG0411   158 QRRLEIARALATEPKLLLLDEPAAGLNPEETEELAELIRRLRDERGITILLIEHDMDLVMGLADRIVVLDFGRVIAEGT 236
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
2-241 4.03e-65

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: 205.65  E-value: 4.03e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklR 81
Cdd:cd03296     3 IEVRNVSKRFGD----FVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDATDVPVQE----R 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QrIGMIFQSFNLFNSRTVFGNIAYPLRLAK----LPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:cd03296    75 N-VGFVFQHYALFRHMTVFDNVAFGLRVKPrserPPEAEIRAKVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAV 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTT 237
Cdd:cd03296   154 EPKVLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVFVTHDQEEALEVADRVVVMNKGRIEQVGTPDEVYDHPASPFV 233

                  ....
gi 2050094043 238 QNFV 241
Cdd:cd03296   234 YSFL 237
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
6-233 8.47e-64

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: 202.28  E-value: 8.47e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklRQRIG 85
Cdd:cd03219     5 GLTKRF--GG--LVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIA--RLGIG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIFQSFNLFNSRTVFGNIA--------YPLRLAKLPKNE--IKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:cd03219    79 RTFQIPRLFPELTVLENVMvaaqartgSGLLLARARREEreARERAEELLERVGLADLADRPAGELSYGQQRRLEIARAL 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:cd03219   159 ATDPKLLLLDEPAAGLNPEETEELAELIRELRER-GITVLLVEHDMDVVMSLADRVTVLDQGRVIAEGTPDEVRNNPR 235
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
1-223 1.41e-63

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: 202.01  E-value: 1.41e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitslSAKELRKL 80
Cdd:COG4555     1 MIEVENLSKKY----GKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGED----VRKEPREA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG4555    73 RRQIGVLPDERGLYDRLTVRENIRYFAELYGLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPK 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG4555   153 VLLLDEPTNGLDVMARRLLREILRALKKE-GKTVLFSSHIMQEVEALCDRVVILHKGKVVAQG 214
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
6-219 8.49e-62

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: 196.32  E-value: 8.49e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklrQRIG 85
Cdd:cd03301     5 NVTKRFGN----VTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKD-----RDIA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:cd03301    76 MVFQNYALYPHMTVYDNIAFGLKLRKVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMD 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03301   156 EPLSNLDAKLRVQMRAELKRLQQRLGTTTIYVTHDQVEAMTMADRIAVMNDGQI 209
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
1-227 7.63e-61

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 194.59  E-value: 7.63e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVHAvedvTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElRKl 80
Cdd:COG3840     1 MLRLDDLTYRY--GDFPLRF----DLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQDLTALPPAE-RP- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqrIGMIFQSFNLFNSRTVFGNIAYPLRLA-KLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:COG3840    73 ---VSMLFQENNLFPHLTVAQNIGLGLRPGlKLTAEQ-RAQVEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKR 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG---KLFD 227
Cdd:COG3840   149 PILLLDEPFSALDPALRQEMLDLVDELCRERGLTVLMVTHDPEDAARIADRVLLVADGRIAADGptaALLD 219
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
19-241 1.19e-60

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 194.87  E-value: 1.19e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVN-MLER-PTA---GTISIDDKDITSLSAkELRKLRQRIGMIFQSFNL 93
Cdd:COG1117    25 QALKDINLDIPENKVTALIGPSGCGKSTLLRCLNrMNDLiPGArveGEILLDGEDIYDPDV-DVVELRRRVGMVFQKPNP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FnSRTVFGNIAYPLRLA-KLPKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:COG1117   104 F-PKSIYDNVAYGLRLHgIKSKSELDEIVEESLRKAALwdevKDRLKKSALGLSGGQQQRLCIARALAVEPEVLLMDEPT 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 169 SALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:COG1117   183 SALDPISTAKIEELILELKKDY--TIVIVTHNMQQAARVSDYTAFFYLGELVEFGPTEQIFTNPKDKRTEDYI 253
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
21-241 6.32e-60

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: 192.17  E-value: 6.32e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklRQRIGMIFQSFNLFNSRTVF 100
Cdd:cd03299    15 LKNVSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDITNLPPE-----KRDISYVPQNYALFPHMTVY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:cd03299    90 KNIAYGLKKRKVDKKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSALDVRTKEKLR 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:cd03299   170 EELKKIRKEFGVTVLHVTHDFEEAWALADKVAIMLNGKLIQVGKPEEVFKKPKNEFVAEFL 230
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
1-241 2.72e-59

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 191.82  E-value: 2.72e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGG-----QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK 75
Cdd:PRK10419    3 LLNVSGLSHHYAHGGlsgkhQHQTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKLNRA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  76 ELRKLRQRIGMIFQ-SFNLFNSR-TVFGNIAYPLR-LAKLPKNEIKERVNELLKFVGLEDK-ANYYPEQLSGGQKQRVGI 151
Cdd:PRK10419   83 QRKAFRRDIQMVFQdSISAVNPRkTVREIIREPLRhLLSLDKAERLARASEMLRAVDLDDSvLDKRPPQLSGGQLQRVCL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV--F 229
Cdd:PRK10419  163 ARALAVEPKLLILDEAVSNLDLVLQAGVIRLLKKLQQQFGTACLFITHDLRLVERFCQRVMVMDNGQIVETQPVGDKltF 242
                         250
                  ....*....|..
gi 2050094043 230 TQPKTKTTQNFV 241
Cdd:PRK10419  243 SSPAGRVLQNAV 254
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
2-223 3.83e-59

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: 189.64  E-value: 3.83e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsakELRKLR 81
Cdd:cd03263     1 LQIRNLTKTYKKG--TKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRT----DRKAAR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03263    75 QSLGYCPQFDALFDELTVREHLRFYARLKGLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03263   155 LLLDEPTSGLDPASRRAIWDLILEVRK--GRSIILTTHSMDEAEALCDRIAIMSDGKLRCIG 214
heterocyst_DevA TIGR02982
ABC exporter ATP-binding subunit, DevA family; Members of this protein family are found mostly ...
2-219 4.12e-59

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: 189.46  E-value: 4.12e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:TIGR02982   2 ISIRNLNHYYGHGSLRKQVLFDINLEINPGEIVILTGPSGSGKTTLLTLIGGLRSVQEGSLKVLGQELHGASKKQLVQLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRL-AKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR02982  82 RRIGYIFQAHNLLGFLTARQNVQMALELqPNLSYQEARERARAMLEAVGLGDHLNYYPHNLSGGQKQRVAIARALVHHPK 161
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEmHVVKEICHRVAVMEKGKV 219
Cdd:TIGR02982 162 LVLADEPTAALDSKSGRDVVELMQKLAKEQGCTILMVTHD-NRILDVADRILQMEDGKL 219
SapF COG4167
ABC-type antimicrobial peptide export system, ATPase component SapF [Defense mechanisms];
5-243 4.41e-59

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


Pssm-ID: 443328 [Multi-domain]  Cd Length: 265  Bit Score: 191.20  E-value: 4.41e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   5 NNISKVYESGG-----QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRK 79
Cdd:COG4167     8 RNLSKTFKYRTglfrrQQFEAVKPVSFTLEAGQTLAIIGENGSGKSTLAKMLAGIIEPTSGEILINGH---KLEYGDYKY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQ-SFNLFNSRTVFGNI-AYPLRLA-KLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:COG4167    85 RCKHIRMIFQdPNTSLNPRLNIGQIlEEPLRLNtDLTAEEREERIFATLRLVGLlPEHANFYPHMLSSGQKQRVALARAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:COG4167   165 ILQPKIIIADEALAALDMSVRSQIINLMLELQEKLGISYIYVSQHLGIVKHISDKVLVMHQGEVVEYGKTAEVFANPQHE 244

                  ....*...
gi 2050094043 236 TTQNFVRS 243
Cdd:COG4167   245 VTKRLIES 252
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
2-223 1.13e-58

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 190.61  E-value: 1.13e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRKLR 81
Cdd:PRK13635    6 IRVEHISFRYP--DAATYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGM---VLSEETVWDVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK13635   81 RQVGMVFQNpDNQFVGATVQDDVAFGLENIGVPREEMVERVDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPD 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PRK13635  161 IIILDEATSMLDPRGRREVLETVRQLKEQKGITVLSITHDLDEAAQ-ADRVIVMNKGEILEEG 222
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
1-230 1.30e-58

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: 189.48  E-value: 1.30e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKl 80
Cdd:COG1120     1 MLEAENLSVGY--GGRPV--LDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLASLSRRELAR- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQS----FNLfnsrTVF-----GNIAYPLRLAKLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGI 151
Cdd:COG1120    76 --RIAYVPQEppapFGL----TVRelvalGRYPHLGLFGRPSAED-REAVEEALERTGLEHLADRPVDELSGGERQRVLI 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:COG1120   149 ARALAQEPPLLLLDEPTSHLDLAHQLEVLELLRRLARERGRTVVMVLHDLNLAARYADRLVLLKDGRIVAQGPPEEVLT 227
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
16-244 1.34e-58

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 191.84  E-value: 1.34e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  16 QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQRIGMIFQS-FNLF 94
Cdd:PRK15079   32 KTLKAVDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLLGMKDDEWRAVRSDIQMIFQDpLASL 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 NSRTVFGNI-AYPLRL--AKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK15079  112 NPRMTIGEIiAEPLRTyhPKLSRQEVKDRVKAMMLKVGLlPNLINRYPHEFSGGQCQRIGIARALILEPKLIICDEPVSA 191
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 171 LDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:PRK15079  192 LDVSIQAQVVNLLQQLQREMGLSLIFIAHDLAVVKHISDRVLVMYLGHAVELGTYDEVYHNPLHPYTKALMSAV 265
cbiO PRK13637
energy-coupling factor transporter ATPase;
2-234 1.12e-57

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 188.33  E-value: 1.12e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKeLRKL 80
Cdd:PRK13637    3 IKIENLTHIYMEGTPfEKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVK-LSDI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQ--SFNLFnSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL--EDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13637   82 RKKVGLVFQypEYQLF-EETIEKDIAFGPINLGLSEEEIENRVKRAMNIVGLdyEDYKDKSPFELSGGQKRRVAIAGVVA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK13637  161 MEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSMEDVAKLADRIIVMNKGKCELQGTPREVFKEVET 238
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
1-263 1.41e-57

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 190.82  E-value: 1.41e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYEsgGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelrkL 80
Cdd:PRK11607   19 LLEIRNLTKSFD--GQ--HAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPP-----Y 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11607   90 QRPINMMFQSYALFPHMTVEQNIAFGLKQDKLPKAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPK 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPE----TTTEILNLLKKVnreyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKT 236
Cdd:PRK11607  170 LLLLDEPMGALDKKlrdrMQLEVVDILERV----GVTCVMVTHDQEEAMTMAGRIAIMNRGKFVQIGEPEEIYEHPTTRY 245
                         250       260
                  ....*....|....*....|....*..
gi 2050094043 237 TQNFVRSVindHLPESVLAKIQNGGQI 263
Cdd:PRK11607  246 SAEFIGSV---NVFEGVLKERQEDGLV 269
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
6-238 4.18e-57

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 187.86  E-value: 4.18e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYE------SGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK 79
Cdd:PRK11308   10 DLKKHYPvkrglfKPERLVKALDGVSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLLKADPEAQKL 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQS-FNLFNSRTVFGNI-AYPLRL-AKLPKNEIKERVNELLKFVGLE-DKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK11308   90 LRQKIQIVFQNpYGSLNPRKKVGQIlEEPLLInTSLSAAERREKALAMMAKVGLRpEHYDRYPHMFSGGQRQRIAIARAL 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK11308  170 MLDPDVVVADEPVSALDVSVQAQVLNLMMDLQQELGLSYVFISHDLSVVEHIADEVMVMYLGRCVEKGTKEQIFNNPRHP 249

                  ...
gi 2050094043 236 TTQ 238
Cdd:PRK11308  250 YTQ 252
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
2-223 1.81e-56

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: 182.95  E-value: 1.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLR 81
Cdd:cd03265     1 IEVENLVKKYGD----FEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVV----REPREVR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03265    73 RRIGIVFQDLSVDDELTGWENLYIHARLYGVPGAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEV 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03265   153 LFLDEPTIGLDPQTRAHVWEYIEKLKEEFGMTILLTTHYMEEAEQLCDRVAIIDHGRIIAEG 214
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
20-244 1.95e-56

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 188.32  E-value: 1.95e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR-QRIGMIFQSFNLFNSRT 98
Cdd:PRK10070   43 GVKDASLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAELREVRrKKIAMVFQSFALMPHMT 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  99 VFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:PRK10070  123 VLDNTAFGMELAGINAEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTE 202
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:PRK10070  203 MQDELVKLQAKHQRTIVFISHDLDEAMRIGDRIAIMQNGEVVQVGTPDEILNNPANDYVRTFFRGV 268
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
1-232 3.04e-56

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 182.98  E-value: 3.04e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakelRKL 80
Cdd:COG1121     6 AIELENLTVSYGG----RPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPP--------RRA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNlFNSR---TVF-----GNIAYpLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIA 152
Cdd:COG1121    74 RRRIGYVPQRAE-VDWDfpiTVRdvvlmGRYGR-RGLFRRPSRADREAVDEALERVGLEDLADRPIGELSGGQQQRVLLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGkVIEEGKLFDVFTQP 232
Cdd:COG1121   152 RALAQDPDLLLLDEPFAGVDAATEEALYELLRELRRE-GKTILVVTHDLGAVREYFDRVLLLNRG-LVAHGPPEEVLTPE 229
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
1-219 3.92e-56

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 182.00  E-value: 3.92e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK10908    1 MIRFEHVSKAYLGGRQ---ALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDITRLKNREVPFL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK10908   78 RRQIGMIFQDHHLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPA 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNReYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10908  158 VLLADEPTGNLDDALSEGILRLFEEFNR-VGVTVLMATHDIGLISRRSYRMLTLSDGHL 215
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
24-242 4.94e-56

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 182.86  E-value: 4.94e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  24 VTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSL----------SAKELRKLRQRIGMIFQSFNL 93
Cdd:PRK10619   24 VSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINLVrdkdgqlkvaDKNQLRLLRTRLTMVFQHFNL 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSRTVFGNI-AYPLRLAKLPKNEIKERVNELLKFVGLEDKAN-YYPEQLSGGQKQRVGIARALATSPDILICDEATSAL 171
Cdd:PRK10619  104 WSHMTVLENVmEAPIQVLGLSKQEARERAVKYLAKVGIDERAQgKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSAL 183
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 172 DPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVR 242
Cdd:PRK10619  184 DPELVGEVLRIMQQLAEE-GKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFGNPQSPRLQQFLK 253
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
2-269 5.66e-56

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 185.67  E-value: 5.66e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklr 81
Cdd:PRK10851    3 IEIANIKKSF--GRTQV--LNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARD----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLakLPKNE------IKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK10851   74 RKVGFVFQHYALFRHMTVFDNIAFGLTV--LPRRErpnaaaIKAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK10851  152 AVEPQILLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVFVTHDQEEAMEVADRVVVMSQGNIEQAGTPDQVWREPATR 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 2050094043 236 TTQNFVRSVinDHLPESVL-AKIQNGGQIYRLTFT 269
Cdd:PRK10851  232 FVLEFMGEV--NRLQGTIRgGQFHVGAHRWPLGYT 264
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
23-329 7.01e-56

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: 185.69  E-value: 7.01e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQR-IGMIFQSFNLFNSRTVFG 101
Cdd:COG4148    17 DVDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLGGEVLQDSARGIFLPPHRRrIGYVFQEARLFPHLSVRG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLAklPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILN 181
Cdd:COG4148    97 NLLYGRKRA--PRAERRISFDEVVELLGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLARKAEILP 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 182 LLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF--VRSVIN----DHLPESVLA 255
Cdd:COG4148   175 YLERLRDELDIPILYVSHSLDEVARLADHVVLLEQGRVVASGPLAEVLSRPDLLPLAGGeeAGSVLEatvaAHDPDYGLT 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 256 KIQNGGQIYRLTFTGEETGQPVLSYIAKNynvDV-------------NVLYGNIIELQNVLFGNLLVELQ-GEQK---EI 318
Cdd:COG4148   255 RLALGGGRLWVPRLDLPPGTRVRVRIRAR---DVslaleppegssilNILPGRVVEIEPADGGQVLVRLDlGGQTllaRI 331
                         330
                  ....*....|..
gi 2050094043 319 -QKALQHLRLQV 329
Cdd:COG4148   332 tRRSADELGLAP 343
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
1-199 2.14e-55

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 181.60  E-value: 2.14e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:COG4525     3 MLTVRHVSVRYPGGGQPQPALQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPVTGPGADR---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqriGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG4525    79 ----GVVFQKDALLPWLNVLDNVAFGLRLRGVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPR 154
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITH 199
Cdd:COG4525   155 FLLMDEPFGALDALTREQMQELLLDVWQRTGKGVFLITH 193
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
2-219 2.62e-55

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: 177.97  E-value: 2.62e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLR 81
Cdd:cd03230     1 IEVRNLSKRY----GKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIK----KEPEEVK 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIayplrlaklpkneikervnellkfvgledkanyypeQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03230    73 RRIGYLPEEPSLYENLTVRENL------------------------------------KLSGGMKQRLALAQALLHDPEL 116
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03230   117 LILDEPTSGLDPESRREFWELLRELKKE-GKTILLSSHILEEAERLCDRVAILNNGRI 173
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
2-223 6.85e-55

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: 190.43  E-value: 6.85e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:COG2274   474 IELENVSFRY--PGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQID---PASLR 548
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFnSRTVFGNIAyplrLAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG2274   549 RQIGVVLQDVFLF-SGTIRENIT----LGDPDATD--EEIIEAARLAGLHDFIEALPMgydtvvgeggsNLSGGQRQRLA 621
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKeICHRVAVMEKGKVIEEG 223
Cdd:COG2274   622 IARALLRNPRILILDEATSALDAETEAIILENLRRLLK--GRTVIIIAHRLSTIR-LADRIIVLDKGRIVEDG 691
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
2-241 7.56e-55

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 183.61  E-value: 7.56e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklr 81
Cdd:PRK09452   15 VELRGISKSF--DGKEV--ISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDITHVPAE------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QR-IGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK09452   85 NRhVNTVFQSYALFPHMTVFENVAFGLRMQKTPAAEITPRVMEALRMVQLEEFAQRKPHQLSGGQQQRVAIARAVVNKPK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK09452  165 VLLLDESLSALDYKLRKQMQNELKALQRKLGITFVFVTHDQEEALTMSDRIVVMRDGRIEQDGTPREIYEEPKNLFVARF 244

                  .
gi 2050094043 241 V 241
Cdd:PRK09452  245 I 245
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
2-219 1.32e-54

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 177.70  E-value: 1.32e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:COG4619     1 LELEGLS--FRVGGKPI--LSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPLSAMPPPEWRR-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFNLFnSRTVFGNIAYPLRLAKLPKNEikERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSPD 160
Cdd:COG4619    75 -QVAYVPQEPALW-GGTVRDNLPFPFQLRERKFDR--ERALELLERLGLPPDILDKPvERLSGGERQRLALIRALLLQPD 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:COG4619   151 VLLLDEPTSALDPENTRRVEELLREYLAEEGRAVLWVSHDPEQIERVADRVLTLEAGRL 209
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
1-231 1.71e-54

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 179.90  E-value: 1.71e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESG--GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitSLSAKELR 78
Cdd:PRK13633    4 MIKCKNVSYKYESNeeSTEKLALDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLD--TSDEENLW 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQS-FNLFNSRTVFGNIAY-PLRLAKLPKnEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13633   82 DIRNKAGMVFQNpDNQIVATIVEEDVAFgPENLGIPPE-EIRERVDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILA 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13633  161 MRPECIIFDEPTAMLDPSGRREVVNTIKELNKKYGITIILITHYMEEAVE-ADRIIVMDSGKVVMEGTPKEIFKE 234
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
2-218 2.43e-53

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: 172.95  E-value: 2.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:cd03228     1 IEFKNVSFSYPGRPKPV--LKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDLD---LESLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNsRTVFGNIayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03228    76 KNIAYVPQDPFLFS-GTIRENI-------------------------------------LSGGQRQRIAIARALLRDPPI 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKeICHRVAVMEKGK 218
Cdd:cd03228   118 LILDEATSALDPETEALILEALRALAK--GKTVIVIAHRLSTIR-DADRIIVLDDGR 171
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
1-230 1.55e-52

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 174.41  E-value: 1.55e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslSAKELRKL 80
Cdd:PRK13632    7 MIKVENVSFSY--PNSENNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITI---SKENLKEI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13632   82 RKKIGIIFQNpDNQFIGATVEDDIAFGLENKKVPPKKMKDIIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASVLALNP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEM-HVVKeiCHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13632  162 EIIIFDESTSMLDPKGKREIKKIMVDLRKTRKKTLISITHDMdEAIL--ADKVIVFSEGKLIAQGKPKEILN 231
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
3-219 2.80e-52

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: 171.95  E-value: 2.80e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   3 SFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakelRKLRQ 82
Cdd:cd03235     1 EVEDLTVSY----GGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPL--------EKERK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIGMIFQSFNL-FNSR-TVFGNIA----YPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:cd03235    69 RIGYVPQRRSIdRDFPiSVRDVVLmglyGHKGLFRRLSKADKAKVDEALERVGLSELADRQIGELSGGQQQRVLLARALV 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03235   149 QDPDLLLLDEPFAGVDPKTQEDIYELLRELRRE-GMTILVVTHDLGLVLEYFDRVLLLNRTVV 210
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
21-169 3.99e-52

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: 169.37  E-value: 3.99e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsaKELRKLRQRIGMIFQSFNLFNSRTVF 100
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTD---DERKSLRKEIGYVFQDPQLFPRLTVR 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 101 GNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKAN----YYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:pfam00005  78 ENLRLGLLLKGLSKREKDARAEEALEKLGLGDLADrpvgERPGTLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
2-223 4.21e-52

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 180.75  E-value: 4.21e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:COG1132   340 IEFENVSFSYPGD---RPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDLTLESLRR-- 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFNLFnSRTVFGNIAYplrlAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG1132   415 -QIGVVPQDTFLF-SGTIRENIRY----GRPDATD--EEVEEAAKAAQAHEFIEALPDgydtvvgergvNLSGGQRQRIA 486
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:COG1132   487 IARALLKDPPILILDEATSALDTETEALIQEALERLMK--GRTTIVIAHRLSTIRN-ADRILVLDDGRIVEQG 556
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
2-223 8.24e-52

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: 170.45  E-value: 8.24e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsvHAVEDVTLSVEKGeIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLR 81
Cdd:cd03264     1 LQLENLTKRYGKK----RALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVL----KQPQKLR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03264    72 RRIGYLPQEFGVYPNFTVREFLDYIAWLKGIPSKEVKARVDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSI 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03264   152 LIVDEPTAGLDPEERIRFRNLLSELGE--DRIVILSTHIVEDVESLCNQVAVLNKGKLVFEG 211
cbiO PRK13650
energy-coupling factor transporter ATPase;
1-219 6.61e-51

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 170.30  E-value: 6.61e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRKL 80
Cdd:PRK13650    4 IIEVKNLTFKYKED-QEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGD---LLTEENVWDI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13650   80 RHKIGMVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKERVNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRP 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKeICHRVAVMEKGKV 219
Cdd:PRK13650  160 KIIILDEATSMLDPEGRLELIKTIKGIRDDYQMTVISITHDLDEVA-LSDRVLVMKNGQV 218
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
1-224 9.38e-51

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 175.99  E-value: 9.38e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNML---ERPTAGTISIDDKDITSLSAKEL 77
Cdd:COG3845     5 ALELRGITKRF--GG--VVANDDVSLTVRPGEIHALLGENGAGKSTL---MKILyglYQPDSGEILIDGKPVRIRSPRDA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKLRqrIGMIFQSFNLFNSRTVFGNIAY---PLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:COG3845    78 IALG--IGMVHQHFMLVPNLTVAENIVLglePTKGGRLDRKAARARIRELSERYGLDVDPDAKVEDLSVGEQQRVEILKA 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:COG3845   156 LYRGARILILDEPTAVLTPQEADELFEILRRLAAE-GKSIIFITHKLREVMAIADRVTVLRRGKVVGTVD 224
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
1-229 1.02e-50

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 169.55  E-value: 1.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsaKELRKL 80
Cdd:PRK13648    7 IIVFKNVSFQYQS--DASFTLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITD---DNFEKL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13648   82 RKHIGIVFQNpDNQFVGSIVKYDVAFGLENHAVPYDEMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNP 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHrVAVMEKGKVIEEGKLFDVF 229
Cdd:PRK13648  162 SVIILDEATSMLDPDARQNLLDLVRKVKSEHNITIISITHDLSEAMEADH-VIVMNKGTVYKEGTPTEIF 230
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
30-223 2.11e-50

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: 167.09  E-value: 2.11e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  30 KGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK-ELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLR 108
Cdd:cd03297    22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGTVLFDSRKKiNLPPQQRKIGLVFQQYALFPHLNVRENLAFGLK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 109 laKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNR 188
Cdd:cd03297   102 --RKRNREDRISVDELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKK 179
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2050094043 189 EYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03297   180 NLNIPVIFVTHDLSEAEYLADRIVVMEDGRLQYIG 214
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
1-223 3.82e-50

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: 166.39  E-value: 3.82e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKL 80
Cdd:cd03266     1 MITADALTKRFRDVKKTVQAVDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDV----VKEPAEA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03266    77 RRRLGFVSDSTGLYDRLTARENLEYFAGLYGLKGDELTARLEELADRLGMEELLDRRVGGFSTGMRQKVAIARALVHDPP 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03266   157 VLLLDEPTTGLDVMATRALREFIRQL-RALGKCILFSTHIMQEVERLCDRVVVLHRGRVVYEG 218
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-287 4.52e-50

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 168.75  E-value: 4.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakelRKL 80
Cdd:COG4152     1 MLELKGLTKRFGD----KTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLD-------PED 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIG-----------MifqsfnlfnsrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG4152    70 RRRIGylpeerglypkM-----------KVGEQLVYLARLKGLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTteilNLLKKVNREYNL---TILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:COG4152   139 QLIAALLHDPELLILDEPFSGLDPVNV----ELLKDVIRELAAkgtTVIFSSHQMELVEELCDRIVIINKGRKVLSGSVD 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 227 DVFTQPKTKTtqnFVRSVIND-----HLPESVLAKIQNGGqiYRLTFTGEETGQPVLSYIAKNYNV 287
Cdd:COG4152   215 EIRRQFGRNT---LRLEADGDagwlrALPGVTVVEEDGDG--AELKLEDGADAQELLRALLARGPV 275
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
1-234 5.61e-50

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 167.95  E-value: 5.61e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItSLSAKELRKL 80
Cdd:PRK13639    1 ILETRDLKYSYPDGTE---ALKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPI-KYDKKSLLEV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFN--LFnSRTVFGNIAY-PLRLaKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK13639   77 RKTVGIVFQNPDdqLF-APTVEEDVAFgPLNL-GLSKEEVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILAM 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK13639  155 KPEIIVLDEPTSGLDPMGASQIMKLLYDLNKE-GITIIISTHDVDLVPVYADKVYVMSDGKIIKEGTPKEVFSDIET 230
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
21-223 3.47e-49

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: 162.60  E-value: 3.47e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLrqrigmifqsfnlfnsrtvf 100
Cdd:cd03214    15 LDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLASLSPKELARK-------------------- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 gnIAYplrlaklpkneikerVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:cd03214    75 --IAY---------------VPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHLDIAHQIELL 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03214   138 ELLRRLARERGKTVVMVLHDLNLAARYADRVILLKDGRIVAQG 180
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
6-240 1.61e-48

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 166.43  E-value: 1.61e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYesgGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsakelRKLRQR-I 84
Cdd:PRK11432   11 NITKRF---GSNT-VIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDVTH------RSIQQRdI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  85 GMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:PRK11432   81 CMVFQSYALFPHMSLGENVGYGLKMLGVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLF 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNF 240
Cdd:PRK11432  161 DEPLSNLDANLRRSMREKIRELQQQFNITSLYVTHDQSEAFAVSDTVIVMNKGKIMQIGSPQELYRQPASRFMASF 236
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
20-232 3.07e-48

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 163.65  E-value: 3.07e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITS-LSAKELRKLRQRIGMIFQ--SFNLFnS 96
Cdd:PRK13634   22 ALYDVNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVITAgKKNKKLKPLRKKVGIVFQfpEHQLF-E 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  97 RTVFGNIAY-PLRLAkLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:PRK13634  101 ETVEKDICFgPMNFG-VSEEDAKQKAREMIELVGLpEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPK 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK13634  180 GRKEMMEMFYKLHKEKGLTTVLVTHSMEDAARYADQIVVMHKGTVFLQGTPREIFADP 237
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
3-218 4.69e-48

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: 158.95  E-value: 4.69e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   3 SFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLRQ 82
Cdd:cd00267     1 EIENLSFRYGGR----TALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKLP---LEELRR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIGMIFQsfnlfnsrtvfgniayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDIL 162
Cdd:cd00267    74 RIGYVPQ---------------------------------------------------LSGGQRQRVALARALLLNPDLL 102
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd00267   103 LLDEPTSGLDPASRERLLELLRELAEE-GRTVIIVTHDPELAELAADRVIVLKDGK 157
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
5-225 4.80e-48

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 161.52  E-value: 4.80e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   5 NNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQR- 83
Cdd:PRK11629    9 DNLCKRYQEGSVQTDVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSKLSSAAKAELRNQk 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  84 IGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK11629   89 LGFIYQFHHLLPDFTALENVAMPLLIGKKKPAEINSRALEMLAAVGLEHRANHRPSELSGGERQRVAIARALVNNPRLVL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEGKL 225
Cdd:PRK11629  169 ADEPTGNLDARNADSIFQLLGELNRLQGTAFLVVTHDLQLAKRM-SRQLEMRDGRLTAELSL 229
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
18-273 5.68e-48

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 170.42  E-value: 5.68e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKST----LLRLVNMlerpTAGTISIDDKDITSLSAKELRKLRQRIGMIFQS--F 91
Cdd:PRK10261  337 VHAVEKVSFDLWPGETLSLVGESGSGKSTtgraLLRLVES----QGGEIIFNGQRIDTLSPGKLQALRRDIQFIFQDpyA 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  92 NLFNSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGLE-DKANYYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK10261  413 SLDPRQTVGDSIMEPLRVHGLlPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVS 492
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 170 ALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSV-IND- 247
Cdd:PRK10261  493 ALDVSIRGQIINLLLDLQRDFGIAYLFISHDMAVVERISHRVAVMYLGQIVEIGPRRAVFENPQHPYTRKLMAAVpVADp 572
                         250       260
                  ....*....|....*....|....*...
gi 2050094043 248 --HLPESVLAKIQNGGQIYRltfTGEET 273
Cdd:PRK10261  573 srQRPQRVLLSDDLPSNIHL---RGEEV 597
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
2-224 1.69e-47

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: 168.41  E-value: 1.69e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:COG4987   334 LELEDVSFRYP--GAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDEDDLR--- 408
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSrTVFGNiaypLRLAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG4987   409 RRIAVVPQRPHLFDT-TLREN----LRLARPDATD--EELWAALERVGLGDWLAALPDgldtwlgeggrRLSGGERRRLA 481
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKV--NReynlTILLITHEMHVVkEICHRVAVMEKGKVIEEGK 224
Cdd:COG4987   482 LARALLRDAPILLLDEPTEGLDAATEQALLADLLEAlaGR----TVLLITHRLAGL-ERMDRILVLEDGRIVEQGT 552
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
19-231 2.65e-47

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 161.17  E-value: 2.65e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItSLSAKELRKLRQRIGMIFQS--FNLFnS 96
Cdd:PRK13636   20 HALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPI-DYSRKGLMKLRESVGMVFQDpdNQLF-S 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  97 RTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETT 176
Cdd:PRK13636   98 ASVYQDVSFGAVNLKLPEDEVRKRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVMEPKVLVLDEPTAGLDPMGV 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 177 TEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13636  178 SEIMKLLVEMQKELGLTIIIATHDIDIVPLYCDNVFVMKEGRVILQGNPKEVFAE 232
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
23-319 6.91e-47

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: 162.20  E-value: 6.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK-ELRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:TIGR02142  15 DADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGiFLPPEKRRIGYVFQEARLFPHLSVRG 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLAKLPKNEIK-ERVNELLkfvGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:TIGR02142  95 NLRYGMKRARPSERRISfERVIELL---GIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEIL 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSVIN-----DHLPESVLA 255
Cdd:TIGR02142 172 PYLERLHAEFGIPILYVSHSLQEVLRLADRVVVLEDGRVAAAGPIAEVWASPDLPWLAREDQGSLIegvvaEHDQHYGLT 251
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 256 KIQNGGQIYRLTFTGEETGQPVLSYIAKNynvDV-------------NVLYGNIIELQNVLFGNLLVELQGEQKEIQ 319
Cdd:TIGR02142 252 ALRLGGGHLWVPENLGPTGARLRLRVPAR---DVslalqkpeatsirNILPARVVEIEDSDIGRVGVVLESGGKTLW 325
cbiO PRK13646
energy-coupling factor transporter ATPase;
2-233 9.22e-47

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 159.95  E-value: 9.22e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVH-AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA-KELRK 79
Cdd:PRK13646    3 IRFDNVSYTYQKGTPYEHqAIHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHKTKdKYIRP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQ--SFNLFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLE-DKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13646   83 VRKRIGMVFQfpESQLFED-TVEREIIFGPKNFKMNLDEVKNYAHRLLMDLGFSrDVMSQSPFQMSGGQMRKIAIVSILA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:PRK13646  162 MNPDIIVLDEPTAGLDPQSKRQVMRLLKSLQTDENKTIILVSHDMNEVARYADEVIVMKEGSIVSQTSPKELFKDKK 238
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
1-220 1.04e-46

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 167.59  E-value: 1.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK10535    4 LLELKDIRRSYPSGEEQVEVLKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATLDADALAQL 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK10535   84 RrEHFGFIFQRYHLLSHLTAAQNVEVPAVYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGG 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEiCHRVAVMEKGKVI 220
Cdd:PRK10535  164 QVILADEPTGALDSHSGEEVMAILHQL-RDRGHTVIIVTHDPQVAAQ-AERVIEIRDGEIV 222
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
1-256 2.27e-46

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 159.91  E-value: 2.27e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS----TLLRLVNMLERPTAGTISIDDKDITSLSAKE 76
Cdd:PRK11022    3 LLNVDKLSVHFGDESAPFRAVDRISYSVKQGEVVGIVGESGSGKSvsslAIMGLIDYPGRVMAEKLEFNGQDLQRISEKE 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  77 LRKL-RQRIGMIFQ----SFNlfNSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGLEDKA---NYYPEQLSGGQKQ 147
Cdd:PRK11022   83 RRNLvGAEVAMIFQdpmtSLN--PCYTVGFQIMEAIKVHQGgNKKTRRQRAIDLLNQVGIPDPAsrlDVYPHQLSGGMSQ 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFD 227
Cdd:PRK11022  161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVLITHDLALVAEAAHKIIVMYAGQVVETGKAHD 240
                         250       260
                  ....*....|....*....|....*....
gi 2050094043 228 VFTQPKTKTTQNFVRSvindhLPESVLAK 256
Cdd:PRK11022  241 IFRAPRHPYTQALLRA-----LPEFAQDK 264
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
5-255 6.79e-46

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 156.87  E-value: 6.79e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   5 NNISKV--YESG---GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditSLSAKELRK 79
Cdd:PRK15112    8 RNLSKTfrYRTGwfrRQTVEAVKPLSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDH---PLHFGDYSY 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQ-SFNLFNSRTVFGNIA-YPLRL-AKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK15112   85 RSQRIRMIFQdPSTSLNPRQRISQILdFPLRLnTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARAL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK15112  165 ILRPKVIIADEALASLDMSMRSQLINLMLELQEKQGISYIYVTQHLGMMKHISDQVLVMHQGEVVERGSTADVLASPLHE 244
                         250       260
                  ....*....|....*....|
gi 2050094043 236 TTqnfvRSVINDHLPESVLA 255
Cdd:PRK15112  245 LT----KRLIAGHFGEALTA 260
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
18-224 8.14e-46

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: 155.28  E-value: 8.14e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELrkLRQRIGMIFQSFNLFNSR 97
Cdd:cd03224    13 SQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHER--ARAGIGYVPEGRRIFPEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 TVFGNiaypLRLA--KLPKNEIKERVNELLK-FVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:cd03224    91 TVEEN----LLLGayARRRAKRKARLERVYElFPRLKERRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPK 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2050094043 175 TTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:cd03224   167 IVEEIFEAIRELRDE-GVTILLVEQNARFALEIADRAYVLERGRVVLEGT 215
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
2-223 1.15e-45

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: 154.68  E-value: 1.15e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrklR 81
Cdd:cd03268     1 LKTNDLTKTY--GKK--RVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEA-----L 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKneikERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03268    72 RRIGALIEAPGFYPNLTARENLRLLARLLGIRK----KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03268   148 LILDEPTNGLDPDGIKELRELILSL-RDQGITVLISSHLLSEIQKVADRIGIINKGKLIEEG 208
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
2-224 1.56e-45

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


Pssm-ID: 444012 [Multi-domain]  Cd Length: 563  Bit Score: 163.01  E-value: 1.56e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:COG4988   337 IELEDVSFSYPGGRP---ALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDLDPASWR--- 410
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNsrtvfGNIAYPLRLAKLPKNEikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:COG4988   411 RQIAWVPQNPYLFA-----GTIRENLRLGRPDASD--EELEAALEAAGLDEFVAALPDgldtplgeggrGLSGGQAQRLA 483
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:COG4988   484 LARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLAK--GRTVILITHRLALLAQ-ADRILVLDDGRIVEQGT 554
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
2-224 4.43e-45

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: 153.93  E-value: 4.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:cd03253     1 IEFENVTFAYDPGRP---VLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDIREVT---LDSLR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSrTVFGNIAYplrlAKLPKNEikERVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVG 150
Cdd:cd03253    75 RAIGVVPQDTVLFND-TIGYNIRY----GRPDATD--EEVIEAAKAAQIHDKIMRFPDGydtivgerglkLSGGEKQRVA 147
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:cd03253   148 IARAILKNPPILLLDEATSALDTHTEREIQAALRDVSK--GRTTIVIAHRLSTIVN-ADKIIVLKDGRIVERGT 218
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
19-238 7.49e-45

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 160.64  E-value: 7.49e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKST----LLRLVNmlerpTAGTISIDDKDITSLSAKELRKLRQRIGMIFQSFN-L 93
Cdd:PRK15134  300 VVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNLNRRQLLPVRHRIQVVFQDPNsS 374
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSR-TVFGNIAYPLRL--AKLPKNEIKERVNELLKFVGLEDKANY-YPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK15134  375 LNPRlNVLQIIEEGLRVhqPTLSAAQREQQVIAVMEEVGLDPETRHrYPAEFSGGQRQRIAIARALILKPSLIILDEPTS 454
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 170 ALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQ 238
Cdd:PRK15134  455 SLDKTVQAQILALLKSLQQKHQLAYLFISHDLHVVRALCHQVIVLRQGEVVEQGDCERVFAAPQQEYTR 523
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-291 9.71e-45

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 155.63  E-value: 9.71e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVY-----ESGG------------QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIS 63
Cdd:COG4586     1 IIEVENLSKTYrvyekEPGLkgalkglfrreyREVEAVDDISFTIEPGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  64 IDDKDITslsaKELRKLRQRIGMIF-------------QSFNLFnsRTVFGniayplrlakLPKNEIKERVNELLKFVGL 130
Cdd:COG4586    81 VLGYVPF----KRRKEFARRIGVVFgqrsqlwwdlpaiDSFRLL--KAIYR----------IPDAEYKKRLDELVELLDL 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 131 EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHR 210
Cdd:COG4586   145 GELLDTPVRQLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYNRERGTTILLTSHDMDDIEALCDR 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 211 VAVMEKGKVIEEG---KLFDVFTQPKTkttqnfVRSVINDHLPESVLAK----IQNGGQIYRLTFTGEETGQPVLSYIAK 283
Cdd:COG4586   225 VIVIDHGRIIYDGsleELKERFGPYKT------IVLELAEPVPPLELPRggevIEREGNRVRLEVDPRESLAEVLARLLA 298

                  ....*....
gi 2050094043 284 NYNV-DVNV 291
Cdd:COG4586   299 RYPVrDLTI 307
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
1-223 1.83e-44

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 159.03  E-value: 1.83e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:COG1129     4 LLEMRGISKSF--GG--VKALDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGEPVRFRSPRDAQAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFNSRTVFGNIA---YPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:COG1129    80 --GIAIIHQELNLVPNLSVAENIFlgrEPRRGGLIDWRAMRRRARELLARLGLDIDPDTPVGDLSVAQQQLVEIARALSR 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 158 SPDILICDEATSALDPEtttEILNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG1129   158 DARVLILDEPTASLTER---EVERLFRIIRrlKAQGVAIIYISHRLDEVFEIADRVTVLRDGRLVGTG 222
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
2-223 2.22e-44

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: 151.28  E-value: 2.22e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakelrklR 81
Cdd:cd03269     1 LEVENVTKRF----GRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIAA-------R 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03269    70 NRIGYLPEERGLYPKMKVIDQLVYLAQLKGLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPEL 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 162 LICDEATSALDPETTteilNLLKKVNREY---NLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03269   150 LILDEPFSGLDPVNV----ELLKDVIRELaraGKTVILSTHQMELVEELCDRVLLLNKGRAVLYG 210
cbiO PRK13649
energy-coupling factor transporter ATPase;
2-250 3.14e-44

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 152.98  E-value: 3.14e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA-KELRK 79
Cdd:PRK13649    3 INLQNVSYTYQAGTPfEGRALFDVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLITSTSKnKDIKQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQ--SFNLFnSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13649   83 IRKKVGLVFQfpESQLF-EETVLKDVAFGPQNFGVSQEEAEALAREKLALVGIsESLFEKNPFELSGGQMRRVAIAGILA 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ----- 231
Cdd:PRK13649  162 MEPKILVLDEPTAGLDPKGRKELMTLFKKLHQS-GMTIVLVTHLMDDVANYADFVYVLEKGKLVLSGKPKDIFQDvdfle 240
                         250       260
                  ....*....|....*....|....*..
gi 2050094043 232 ------PK-TKTTQNFVRSVIN-DHLP 250
Cdd:PRK13649  241 ekqlgvPKiTKFAQRLADRGISfSSLP 267
cbiO PRK13640
energy-coupling factor transporter ATPase;
2-253 9.49e-44

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 151.88  E-value: 9.49e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLR 81
Cdd:PRK13640    6 VEFKHVSFTYPD--SKKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPDDNPNSKITVDGITLTAKTVWDIR 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQS-FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK13640   84 EKVGIVFQNpDNQFVGATVGDDVAFGLENRAVPRPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEPK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEGKLFDVFtqPKTKTTQN- 239
Cdd:PRK13640  164 IIILDESTSMLDPAGKEQILKLIRKLKKKNNLTVISITHDIDEA-NMADQVLVLDDGKLLAQGSPVEIF--SKVEMLKEi 240
                         250       260
                  ....*....|....*....|....*
gi 2050094043 240 -----FVRSVIND------HLPESV 253
Cdd:PRK13640  241 gldipFVYKLKNKlkekgiSVPQEI 265
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
1-245 9.58e-44

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 153.85  E-value: 9.58e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:PRK11650    3 GLKLQAVRKSYDGKTQVIK---GIDLDVADGEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPAD---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqR-IGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK11650   76 --RdIAMVFQNYALYPHMSVRENMAYGLKIRGMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHE----MhvvkEICHRVAVMEKGkVIEE-GKLFDVFTQPKT 234
Cdd:PRK11650  154 AVFLFDEPLSNLDAKLRVQMRLEIQRLHRRLKTTSLYVTHDqveaM----TLADRVVVMNGG-VAEQiGTPVEVYEKPAS 228
                         250
                  ....*....|.
gi 2050094043 235 KttqnFVRSVI 245
Cdd:PRK11650  229 T----FVASFI 235
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
17-241 1.16e-43

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 150.83  E-value: 1.16e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSF 91
Cdd:PRK14247   15 QVEVLDGVNLEIPDNTITALMGPSGSGKSTLLRVFNRLielypEARVSGEVYLDGQDIFKMDVIELRR---RVQMVFQIP 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  92 NLFNSRTVFGNIAYPLRLAKLPKN--EIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:PRK14247   92 NPIPNLSIFENVALGLKLNRLVKSkkELQERVRWALEKAQLwdevKDRLDAPAGKLSGGQQQRLCIARALAFQPEVLLAD 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREynLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK14247  172 EPTANLDPENTAKIESLFLELKKD--MTIVLVTHFPQQAARISDYVAFLYKGQIVEWGPTREVFTNPRHELTEKYV 245
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
2-220 3.14e-43

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: 146.80  E-value: 3.14e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLR 81
Cdd:cd03216     1 LELRGITKRF--GG--VKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKEVSFASPRD--ARR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQsfnlfnsrtvfgniayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03216    75 AGIAMVYQ---------------------------------------------------LSVGERQMVEIARALARNARL 103
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:cd03216   104 LILDEPTAALTPAEVERLFKVIRRL-RAQGVAVIFISHRLDEVFEIADRVTVLRDGRVV 161
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
2-223 4.76e-43

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: 148.53  E-value: 4.76e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLr 81
Cdd:cd03251     1 VEFKNVTFRYPGDGPPV--LRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDYTLASLRRQ- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qrIGMIFQSFNLFNSrTVFGNIAYPLRlaklpkNEIKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:cd03251    78 --IGLVSQDVFLFND-TVAENIAYGRP------GATREEVEEAARAANAHEFIMELPEgydtvigergvKLSGGQRQRIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:cd03251   149 IARALLKDPPILILDEATSALDTESERLVQAALERLMK--NRTTFVIAHRLSTIENA-DRIVVLEDGKIVERG 218
cbiO PRK13644
energy-coupling factor transporter ATPase;
1-236 1.17e-42

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 148.98  E-value: 1.17e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakELRKL 80
Cdd:PRK13644    1 MIRLENVSYSYPDG---TPALENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTGDFS--KLQGI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNL-FNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13644   76 RKLVGIVFQNPETqFVGRTVEEDLAFGPENLCLPPIEIRKRVDRALAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITH---EMHVVKeichRVAVMEKGKVIEEGKLFDVFTQPKTKT 236
Cdd:PRK13644  156 ECLIFDEVTSMLDPDSGIAVLERIKKLHEK-GKTIVYITHnleELHDAD----RIIVMDRGKIVLEGEPENVLSDVSLQT 230
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
19-241 1.69e-42

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 147.68  E-value: 1.69e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKELRkLRQRIGMIFQSFNL 93
Cdd:PRK14267   18 HVIKGVDLKIPQNGVFALMGPSGCGKSTLLRTFNRLlelneEARVEGEVRLFGRNIYSPDVDPIE-VRREVGMVFQYPNP 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSRTVFGNIAYPLRLAKL--PKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEA 167
Cdd:PRK14267   97 FPHLTIYDNVAIGVKLNGLvkSKKELDERVEWALKKAALwdevKDRLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEP 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 168 TSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK14267  177 TANIDPVGTAKIEELLFELKKEY--TIVLVTHSPAQAARVSDYVAFLYLGKLIEVGPTRKVFENPEHELTEKYV 248
cbiO PRK13641
energy-coupling factor transporter ATPase;
2-233 1.87e-42

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 148.82  E-value: 1.87e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITS-LSAKELRK 79
Cdd:PRK13641    3 IKFENVDYIYSPGTPmEKKGLDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPeTGNKNLKK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQ--SFNLFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:PRK13641   83 LRKKVSLVFQfpEAQLFEN-TVLKDVEFGPKNFGFSEDEAKEKALKWLKKVGLsEDLISKSPFELSGGQMRRVAIAGVMA 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPK 233
Cdd:PRK13641  162 YEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGH-TVILVTHNMDDVAEYADDVLVLEHGKLIKHASPKEIFSDKE 237
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
23-223 2.48e-42

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: 146.10  E-value: 2.48e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklrQRIGMIFQSFNLFNSRTVFGN 102
Cdd:cd03298    16 HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPAD-----RPVSMLFQENNLFAHLTVEQN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 103 IAyplrLAKLP----KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:cd03298    91 VG----LGLSPglklTAEDRQAIEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAE 166
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03298   167 MLDLVLDLHAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
2-224 3.35e-42

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 148.41  E-value: 3.35e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakelRKLR 81
Cdd:PRK13537    8 IDFRNVEKRY--GDKLV--VDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRA----RHAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:PRK13537   80 QRVGVVPQFDNLDPDFTVRENLLVFGRYFGLSAAAARALVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDV 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:PRK13537  160 LVLDEPTTGLDPQARHLMWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVIEEGRKIAEGA 221
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
2-228 3.44e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 148.31  E-value: 3.44e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSV-HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI---DDKDITSLSAKE- 76
Cdd:PRK13651    3 IKVKNIVKIFNKKLPTElKALDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWifkDEKNKKKTKEKEk 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  77 -----------------LRKLRQRIGMIFQ--SFNLFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANY 136
Cdd:PRK13651   83 vleklviqktrfkkikkIKEIRRRVGVVFQfaEYQLFEQ-TIEKDIIFGPVSMGVSKEEAKKRAAKYIELVGLdESYLQR 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 137 YPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEK 216
Cdd:PRK13651  162 SPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQ-GKTIILVTHDLDNVLEWTKRTIFFKD 240
                         250
                  ....*....|..
gi 2050094043 217 GKVIEEGKLFDV 228
Cdd:PRK13651  241 GKIIKDGDTYDI 252
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
18-244 3.68e-42

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 148.90  E-value: 3.68e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLE---RPTAGTISIDDKDITSLSAKELRKL-RQRIGMIFQ--S 90
Cdd:COG4170    20 VKAVDRVSLTLNEGEIRGLVGESGSGKSLIAKaICGITKdnwHVTADRFRWNGIDLLKLSPRERRKIiGREIAMIFQepS 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  91 FNLFNSRTVFGNI--AYPLRLAKLP----KNEIKERVNELLKFVGLED-KA--NYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:COG4170   100 SCLDPSAKIGDQLieAIPSWTFKGKwwqrFKWRKKRAIELLHRVGIKDhKDimNSYPHELTEGECQKVMIAMAIANQPRL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:COG4170   180 LIADEPTNAMESTTQAQIFRLLARLNQLQGTSILLISHDLESISQWADTITVLYCGQTVESGPTEQILKSPHHPYTKALL 259

                  ...
gi 2050094043 242 RSV 244
Cdd:COG4170   260 RSM 262
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
21-233 5.94e-42

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: 145.69  E-value: 5.94e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELrklrqrigMIFQSFNLFNSRTVF 100
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQITEPGPDRM--------VVFQNYSLLPWLTVR 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLR--LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:TIGR01184  73 ENIALAVDrvLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGN 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV-FTQPK 233
Cdd:TIGR01184 153 LQEELMQIWEEHRVTVLMVTHDVDEALLLSDRVVMLTNGPAANIGQILEVpFPRPR 208
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
18-232 7.40e-42

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 148.33  E-value: 7.40e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERP--TAGTISIDDKDITSLSAKELRKLR-QRIGMIFQ---- 89
Cdd:PRK09473   29 VTAVNDLNFSLRAGETLGIVGESGSGKSqTAFALMGLLAANgrIGGSATFNGREILNLPEKELNKLRaEQISMIFQdpmt 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  90 SFNLFnsRTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLED---KANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:PRK09473  109 SLNPY--MRVGEQLMEVLMLHKgMSKAEAFEESVRMLDAVKMPEarkRMKMYPHEFSGGMRQRVMIAMALLCRPKLLIAD 186
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK09473  187 EPTTALDVTVQAQIMTLLNELKREFNTAIIMITHDLGVVAGICDKVLVMYAGRTMEYGNARDVFYQP 253
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
2-223 7.90e-42

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: 145.04  E-value: 7.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkLR 81
Cdd:cd03245     3 IEFRNVSFSYP--NQEIPALDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQLDPAD---LR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSrTVFGNIAYPLRLAKlpkneiKERVNELLKFVGLEDKANYYP-----------EQLSGGQKQRVG 150
Cdd:cd03245    78 RNIGYVPQDVTLFYG-TLRDNITLGAPLAD------DERILRAAELAGVTDFVNKHPngldlqigergRGLSGGQRQAVA 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:cd03245   151 LARALLNDPPILLLDEPTSAMDMNSEERLKERLRQLLGDK--TLIIITHRPSLL-DLVDRIIVMDSGRIVADG 220
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
1-247 8.19e-42

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 148.07  E-value: 8.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVY-ESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI---------- 69
Cdd:PRK13631   21 ILRVKNLYCVFdEKQENELVALNNISYTFEKNKIYFIIGNSGSGKSTLVTHFNGLIKSKYGTIQVGDIYIgdkknnheli 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  70 ---TSLSAKELRKLRQRIGMIFQ--SFNLFNSrTVFGNIAY-PLRLaKLPKNEIKERVNELLKFVGL-EDKANYYPEQLS 142
Cdd:PRK13631  101 tnpYSKKIKNFKELRRRVSMVFQfpEYQLFKD-TIEKDIMFgPVAL-GVKKSEAKKLAKFYLNKMGLdDSYLERSPFGLS 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 143 GGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK13631  179 GGQKRRVAIAGILAIQPEILIFDEPTAGLDPKGEHEMMQLILDAKAN-NKTVFVITHTMEHVLEVADEVIVMDKGKILKT 257
                         250       260
                  ....*....|....*....|....*....
gi 2050094043 223 GKLFDVFTQP----KTKTTQNFVRSVIND 247
Cdd:PRK13631  258 GTPYEIFTDQhiinSTSIQVPRVIQVIND 286
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
1-223 9.23e-42

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 145.17  E-value: 9.23e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:COG1137     3 TLEAENLVKSY--GKRTV--VKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHK---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGM--------IFQsfNLfnsrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIA 152
Cdd:COG1137    75 RARLGIgylpqeasIFR--KL----TVEDNILAVLELRKLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTIlLITHemHVVKE---ICHRVAVMEKGKVIEEG 223
Cdd:COG1137   149 RALATNPKFILLDEPFAGVDPIAVADIQKIIRHL-KERGIGV-LITD--HNVREtlgICDRAYIISEGKVLAEG 218
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
1-224 1.57e-41

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: 151.49  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSV-HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI---DD-KDITSLSAK 75
Cdd:TIGR03269 279 IIKVRNVSKRYISVDRGVvKAVDNVSLEVKEGEIFGIVGTSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEwVDMTKPGPD 358
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  76 ELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLRLaKLPKNEIKERVNELLKFVGLEDKA-----NYYPEQLSGGQKQRVG 150
Cdd:TIGR03269 359 GRGRAKRYIGILHQEYDLYPHRTVLDNLTEAIGL-ELPDELARMKAVITLKMVGFDEEKaeeilDKYPDELSEGERHRVA 437
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:TIGR03269 438 LAQVLIKEPRIVILDEPTGTMDPITKVDVTHSILKAREEMEQTFIIVSHDMDFVLDVCDRAALMRDGKIVKIGD 511
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
2-223 2.34e-41

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: 143.79  E-value: 2.34e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL-LRLVNMLErPTAGTISIDDKDITSLSakeLRKL 80
Cdd:cd03244     3 IEFKNVSLRYRPNLPPV--LKNISFSIKPGEKVGIVGRTGSGKSSLlLALFRLVE-LSSGSILIDGVDISKIG---LHDL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFnSRTVFGNIA----YP-------LRLAKLpkneiKERVNELLKfvGLEDKANYYPEQLSGGQKQRV 149
Cdd:cd03244    77 RSRISIIPQDPVLF-SGTIRSNLDpfgeYSdeelwqaLERVGL-----KEFVESLPG--GLDTVVEEGGENLSVGQRQLL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLkkvnREY--NLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:cd03244   149 CLARALLRKSKILVLDEATASVDPETDALIQKTI----REAfkDCTVLTIAHRLDTIID-SDRILVLDKGRVVEFD 219
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
6-235 6.18e-41

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: 143.07  E-value: 6.18e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklRQRIG 85
Cdd:cd03218     5 NLSKRY--GKRKV--VNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHK----RARLG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIF--QSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:cd03218    77 IGYlpQEASIFRKLTVEENILAVLEIRGLSKKEREEKLEELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:cd03218   157 LDEPFAGVDPIAVQDIQKIIKIL-KDRGIGVLITDHNVRETLSITDRAYIIYEGKVLAEGTPEEIAANELVR 227
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
2-223 1.07e-40

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: 142.36  E-value: 1.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:cd03254     3 IEFENVNFSYDEK---KPVLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDISRKSLRS-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFNLFnSRTVFGNIayplrlaKLPKNEIK-ERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRV 149
Cdd:cd03254    78 -MIGVVLQDTFLF-SGTIMENI-------RLGRPNATdEEVIEAAKEAGAHDFIMKLPNgydtvlgenggNLSQGERQLL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:cd03254   149 AIARAMLRDPKILILDEATSNIDTETEKLIQEALEKLMK--GRTSIIIAHRLSTIKN-ADKILVLDDGKIIEEG 219
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
22-223 1.26e-40

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 143.37  E-value: 1.26e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:PRK11831   24 DNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIPAMSRSRLYTVRKRMSMLFQSGALFTDMNVFD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:PRK11831  104 NVAYPLReHTQLPAPLLHSTVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPDLIMFDEPFVGQDPITMGVLV 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2050094043 181 NLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK11831  184 KLISELNSALGVTCVVVSHDVPEVLSIADHAYIVADKKIVAHG 226
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
2-224 1.63e-40

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: 141.91  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNMLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:cd03249     1 IEFKNVSFRYPSR-PDVPILKGLSLTIPPGKTVALVGSSGCGKSTV---VSLLERfydPTSGEILLDGVDIRDLN---LR 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQSFNLFNsRTVFGNIAYPLRLAKLPKNEIKERVNELLKFV-GLEDKanYYPE------QLSGGQKQRVGI 151
Cdd:cd03249    74 WLRSQIGLVSQEPVLFD-GTIAENIRYGKPDATDEEVEEAAKKANIHDFImSLPDG--YDTLvgergsQLSGGQKQRIAI 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:cd03249   151 ARALLRNPKILLLDEATSALDAESEKLVQEALDRAMK--GRTTIVIAHRLSTIRN-ADLIAVLQNGQVVEQGT 220
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
7-220 1.63e-40

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: 141.24  E-value: 1.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   7 ISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslSAKELRKlrqRIGM 86
Cdd:cd03226     2 IENISFSYKKGTEILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPI---KAKERRK---SIGY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  87 IFQS--FNLFnSRTVFGNiaypLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:cd03226    76 VMQDvdYQLF-TDSVREE----LLLGLKELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:cd03226   151 DEPTSGLDYKNMERVGELIRELAAQGK-AVIVITHDYEFLAKVCDRVLLLANGAIV 205
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
1-232 1.70e-40

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 143.40  E-value: 1.70e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggqSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK13652    3 LIETRDLCYSYSG---SKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKENIREVRKF 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqrIGMIFQSFN--LFnSRTVFGNIAY-PLRLAkLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK13652   80 ---VGLVFQNPDdqIF-SPTVEQDIAFgPINLG-LDEETVAHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAM 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK13652  155 EPQVLVLDEPTAGLDPQGVKELIDFLNDLPETYGMTVIFSTHQLDLVPEMADYIYVMDKGRIVAYGTVEEIFLQP 229
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
2-224 1.85e-40

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: 141.85  E-value: 1.85e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:cd03252     1 ITFEHVRFRY--KPDGPVILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALA---DPAWLR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNsRTVFGNIAYPLRLAKLpkneikERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:cd03252    76 RQVGVVLQENVLFN-RSIRDNIALADPGMSM------ERVIEAAKLAGAHDFISELPEgydtivgeqgaGLSGGQRQRIA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:cd03252   149 IARALIHNPRILIFDEATSALDYESEHAIMRNMHDICA--GRTVIIIAHRLSTVKN-ADRIIVMEKGRIVEQGS 219
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
1-223 2.07e-40

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: 141.66  E-value: 2.07e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesgGQSvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLeRPTAGTISIDDKDITSLSAKELrk 79
Cdd:COG0410     3 MLEVENLHAGY---GGI-HVLHGVSLEVEEGEIVALLGRNGAGKTTLLKaISGLL-PPRSGSIRFDGEDITGLPPHRI-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQSFNLFNSRTVFGNI---AYPLRLAKLPKnEIKERVNELlkFVGLEDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:COG0410    76 ARLGIGYVPEGRRIFPSLTVEENLllgAYARRDRAEVR-ADLERVYEL--FPRLKERRRQRAGTLSGGEQQMLAIGRALM 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:COG0410   153 SRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNRE-GVTILLVEQNARFALEIADRAYVLERGRIVLEG 218
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
1-201 2.32e-40

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 142.15  E-value: 2.32e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkl 80
Cdd:PRK11248    1 MLQISHLYADY--GGKP--ALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPVEGPGAER---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqriGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK11248   73 ----GVVFQNEGLLPWRNVQDNVAFGLQLAGVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQ 148
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEM 201
Cdd:PRK11248  149 LLLLDEPFGALDAFTREQMQTLLLKLWQETGKQVLLITHDI 189
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
1-243 2.48e-40

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 148.31  E-value: 2.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERP----TAGTISIDDKDITSLSAK 75
Cdd:PRK15134    5 LLAIENLSVAFRQQQTVRTVVNDVSLQIEAGETLALVGESGSGKSvTALSILRLLPSPpvvyPSGDIRFHGESLLHASEQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  76 ELRKLR-QRIGMIFQ----SFNLFNsrTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLEDKA---NYYPEQLSGGQK 146
Cdd:PRK15134   85 TLRGVRgNKIAMIFQepmvSLNPLH--TLEKQLYEVLSLHRgMRREAARGEILNCLDRVGIRQAAkrlTDYPHQLSGGER 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:PRK15134  163 QRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNMGLLFITHNLSIVRKLADRVAVMQNGRCVEQNRAA 242
                         250
                  ....*....|....*..
gi 2050094043 227 DVFTQPKTKTTQNFVRS 243
Cdd:PRK15134  243 TLFSAPTHPYTQKLLNS 259
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
20-241 4.10e-40

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 141.45  E-value: 4.10e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKELrKLRQRIGMIFQSFNLF 94
Cdd:PRK14239   20 ALNSVSLDFYPNEITALIGPSGSGKSTLLRSINRMndlnpEVTITGSIVYNGHNIYSPRTDTV-DLRKEIGMVFQQPNPF 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 nSRTVFGNIAYPLRLAKLP-KNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK14239   99 -PMSIYENVVYGLRLKGIKdKQVLDEAVEKSLKGASIwdevKDRLHDSALGLSGGQQQRVCIARVLATSPKIILLDEPTS 177
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 170 ALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK14239  178 ALDPISAGKIEETLLGLKDDY--TMLLVTRSMQQASRISDRTGFFLDGDLIEYNDTKQMFMNPKHKETEDYI 247
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
1-224 4.71e-40

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 140.87  E-value: 4.71e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYEsggqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrkl 80
Cdd:PRK10771    1 MLKLTDITWLYH------HLPMRFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQDHTTTPPS----- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rQR-IGMIFQSFNLFNSRTVFGNIA---YP-LRLaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK10771   70 -RRpVSMLFQENNLFSHLTVAQNIGlglNPgLKL----NAAQREKLHAIARQMGIEDLLARLPGQLSGGQRQRVALARCL 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:PRK10771  145 VREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQLTLLMVSHSLEDAARIAPRSLVVADGRIAWDGP 213
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
1-228 5.11e-40

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 140.99  E-value: 5.11e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVY------------------ESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTI 62
Cdd:COG1134     4 MIEVENVSKSYrlyhepsrslkelllrrrRTRREEFWALKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  63 SIDDKdITSLSAkelrklrqrIGMIFQsfnlfNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKAN----YYp 138
Cdd:COG1134    84 EVNGR-VSALLE---------LGAGFH-----PELTGRENIYLNGRLLGLSRKEIDEKFDEIVEFAELGDFIDqpvkTY- 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 139 eqlSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:COG1134   148 ---SSGMRARLAFAVATAVDPDILLVDEVLAVGDAAFQKKCLARIREL-RESGRTVIFVSHSMGAVRRLCDRAIWLEKGR 223
                         250
                  ....*....|
gi 2050094043 219 VIEEGKLFDV 228
Cdd:COG1134   224 LVMDGDPEEV 233
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
1-220 1.23e-39

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 140.61  E-value: 1.23e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQS-VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelRK 79
Cdd:COG1101     1 MLELKNLSKTFNPGTVNeKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVTKLPE---YK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQ------SFNLfnsrTVFGN--IAY------PLRLAKLPKN--EIKERVNEL-LkfvGLEDKANYYPEQLS 142
Cdd:COG1101    78 RAKYIGRVFQdpmmgtAPSM----TIEENlaLAYrrgkrrGLRRGLTKKRreLFRELLATLgL---GLENRLDTKVGLLS 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 143 GGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:COG1101   151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLTTLMVTHNMEQALDYGNRLIMMHEGRII 228
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
6-241 1.50e-39

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 140.18  E-value: 1.50e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYESGGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK------DITSLSAKelrK 79
Cdd:PRK14246   12 NISRLYLYINDKA-ILKDITIKIPNNSIFGIMGPSGSGKSTLLKVLNRLIEIYDSKIKVDGKvlyfgkDIFQIDAI---K 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLP-KNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK14246   88 LRKEVGMVFQQPNPFPHLSIYDNIAYPLKSHGIKeKREIKKIVEECLRKVGLwkevYDRLNSPASQLSGGQQQRLTIARA 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREynLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK14246  168 LALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNE--IAIVIVSHNPQQVARVADYVAFLYNGELVEWGSSNEIFTSPKN 245

                  ....*..
gi 2050094043 235 KTTQNFV 241
Cdd:PRK14246  246 ELTEKYV 252
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
2-219 5.95e-39

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: 135.81  E-value: 5.95e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLR 81
Cdd:cd03246     1 LEVENVSFRYPGAEPPV--LRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWD---PNELG 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFnSRTVFGNIayplrlaklpkneikervnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDI 161
Cdd:cd03246    76 DHVGYLPQDDELF-SGSIAENI-------------------------------------LSGGQRQRLGLARALYGNPRI 117
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:cd03246   118 LVLDEPNSHLDVEGERALNQAIAAL-KAAGATRIVIAHRPETL-ASADRILVLEDGRV 173
cbiO PRK13645
energy-coupling factor transporter ATPase;
2-230 1.06e-38

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 138.99  E-value: 1.06e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITS--LSAKELR 78
Cdd:PRK13645    7 IILDNVSYTYAKKTPfEFKALNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlKKIKEVK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQ--SFNLFNSrTVFGNIAY-PLRLAKlPKNEIKERVNELLKFVGL-EDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK13645   87 RLRKEIGLVFQfpEYQLFQE-TIEKDIAFgPVNLGE-NKQEAYKKVPELLKLVQLpEDYVKRSPFELSGGQKRRVALAGI 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13645  165 IAMDGNTLVLDEPTGGLDPKGEEDFINLFERLNKEYKKRIIMVTHNMDQVLRIADEVIVMHEGKVISIGSPFEIFS 240
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
2-228 1.34e-38

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 139.97  E-value: 1.34e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSlsakELRKLR 81
Cdd:PRK13536   42 IDLAGVSKSY--GDKAV--VNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPA----RARLAR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:PRK13536  114 ARIGVVPQFDNLDLEFTVRENLLVFGRYFGMSTREIEAVIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQL 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV 228
Cdd:PRK13536  194 LILDEPTTGLDPHARHLIWERLRSL-LARGKTILLTTHFMEEAERLCDRLCVLEAGRKIAEGRPHAL 259
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
20-224 1.84e-38

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 137.43  E-value: 1.84e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELrklrQRIGMI--FQSFNLFNSR 97
Cdd:PRK11300   20 AVNNVNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQI----ARMGVVrtFQHVRLFREM 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 TVFGN--IAYPLR--------LAKLP-----KNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDIL 162
Cdd:PRK11300   96 TVIENllVAQHQQlktglfsgLLKTPafrraESEALDRAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEIL 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK 224
Cdd:PRK11300  176 MLDEPAAGLNPKETKELDELIAELRNEHNVTVLLIEHDMKLVMGISDRIYVVNQGTPLANGT 237
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
2-223 3.90e-38

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: 143.04  E-value: 3.90e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLvnmLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:COG5265   358 VRFENVSFGYDPERPILK---GVSFEVPAGKTVAIVGPSGAGKSTLARL---LFRfydVTSGRILIDGQDIRDVT---QA 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQSFNLFNSrTVFGNIAYP------------LRLA-------KLPK---NEIKERvnellkfvGLedkany 136
Cdd:COG5265   429 SLRAAIGIVPQDTVLFND-TIAYNIAYGrpdaseeeveaaARAAqihdfieSLPDgydTRVGER--------GL------ 493
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 137 ypeQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEK 216
Cdd:COG5265   494 ---KLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVAR--GRTTLVIAHRLSTIVD-ADEILVLEA 567

                  ....*..
gi 2050094043 217 GKVIEEG 223
Cdd:COG5265   568 GRIVERG 574
NHLM_micro_ABC2 TIGR03797
NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family ...
2-223 4.27e-38

NHLM bacteriocin system ABC transporter, ATP-binding protein; Members of this protein family are ABC transporter ATP-binding subunits, part of a three-gene putative bacteriocin transport operon. The other subunits include another ATP-binding subunit (TIGR03796), which has an N-terminal leader sequence cleavage domain, and an HlyD homolog (TIGR03794). In a number of genomes, members of protein families related to nitrile hydratase alpha subunit or to nif11 have undergone paralogous family expansions, with members possessing a putative bacteriocin cleavage region ending with a classic Gly-Gly motif. Those sets of putative bacteriocins, members of this protein family and its partners TIGR03794 and TIGR03796, and cyclodehydratase/docking scaffold fusion proteins of thiazole/oxazole biosynthesis frequently show correlated species distribution and co-clustering within many of those genomes. [Transport and binding proteins, Amino acids, peptides and amines, Cellular processes, Biosynthesis of natural products]


Pssm-ID: 274789 [Multi-domain]  Cd Length: 686  Bit Score: 143.56  E-value: 4.27e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:TIGR03797 452 IEVDRVTFRYRPDGPLI--LDDVSLQIEPGEFVAIVGPSGSGKSTLLRLLLGFETPESGSVFYDGQDLAGL---DVQAVR 526
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFnSRTVFGNIA--YPLRLaklpkneikERVNELLKFVGLEDKANYYP-----------EQLSGGQKQR 148
Cdd:TIGR03797 527 RQLGVVLQNGRLM-SGSIFENIAggAPLTL---------DEAWEAARMAGLAEDIRAMPmgmhtviseggGTLSGGQRQR 596
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 149 VGIARALATSPDILICDEATSALDPETTTEILNLLKKVnreyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:TIGR03797 597 LLIARALVRKPRILLFDEATSALDNRTQAIVSESLERL----KVTRIVIAHRLSTIRN-ADRIYVLDAGRVVQQG 666
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
1-222 7.77e-38

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 134.91  E-value: 7.77e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK10584    6 IVEVHHLKKSVGQGEHELSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQMDEEARAKL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 R-QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK10584   86 RaKHVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGAKALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNGRP 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEE 222
Cdd:PRK10584  166 DVLFADEPTGNLDRQTGDKIADLLFSLNREHGTTLILVTHDLQLAAR-CDRRLRLVNGQLQEE 227
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
2-223 2.42e-37

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: 140.62  E-value: 2.42e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNMLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:TIGR02203 331 VEFRNVTFRY--PGRDRPALDSISLVIEPGETVALVGRSGSGKSTL---VNLIPRfyePDSGQILLDGHDLADYT---LA 402
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQSFNLFNSrTVFGNIAYPlRLAKLPKNEIKERVNE--LLKFV-----GLEDKANYYPEQLSGGQKQRVGI 151
Cdd:TIGR02203 403 SLRRQVALVSQDVVLFND-TIANNIAYG-RTEQADRAEIERALAAayAQDFVdklplGLDTPIGENGVLLSGGQRQRLAI 480
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:TIGR02203 481 ARALLKDAPILILDEATSALDNESERLVQAALERLMQ--GRTTLVIAHRLSTIEK-ADRIVVMDDGRIVERG 549
cbiO PRK13642
energy-coupling factor transporter ATPase;
18-229 2.73e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 134.84  E-value: 2.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKLRQRIGMIFQS-FNLFNS 96
Cdd:PRK13642   20 VNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLT---AENVWNLRRKIGMVFQNpDNQFVG 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  97 RTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETT 176
Cdd:PRK13642   97 ATVEDDVAFGMENQGIPREEMIKRVDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEIIILDESTSMLDPTGR 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 177 TEILNLLKKVNREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKLFDVF 229
Cdd:PRK13642  177 QEIMRVIHEIKEKYQLTVLSITHDLDEAAS-SDRILVMKAGEIIKEAAPSELF 228
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
1-230 3.01e-37

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 134.06  E-value: 3.01e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK- 79
Cdd:COG4604     1 MIEIKNVSKRY--GGKVV--LDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVATTPSRELAKr 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 ---LRQRigmifqsfNLFNSR-TV-----FGNiaYPL---RLAKlpknEIKERVNELLKFVGLEDKANYYPEQLSGGQKQ 147
Cdd:COG4604    77 laiLRQE--------NHINSRlTVrelvaFGR--FPYskgRLTA----EDREIIDEAIAYLDLEDLADRYLDELSGGQRQ 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFD 227
Cdd:COG4604   143 RAFIAMVLAQDTDYVLLDEPLNNLDMKHSVQMMKLLRRLADELGKTVVIVLHDINFASCYADHIVAMKDGRVVAQGTPEE 222

                  ...
gi 2050094043 228 VFT 230
Cdd:COG4604   223 IIT 225
cbiO PRK13643
energy-coupling factor transporter ATPase;
1-231 3.52e-37

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 134.86  E-value: 3.52e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQ-SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA-KELR 78
Cdd:PRK13643    1 MIKFEKVNYTYQPNSPfASRALFDIDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVTVGDIVVSSTSKqKEIK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQ--SFNLFnSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKA-NYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK13643   81 PVRKKVGVVFQfpESQLF-EETVLKDVAFGPQNFGIPKEKAEKIAAEKLEMVGLADEFwEKSPFELSGGQMRRVAIAGIL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNrEYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13643  160 AMEPEVLVLDEPTAGLDPKARIEMMQLFESIH-QSGQTVVLVTHLMDDVADYADYVYLLEKGHIISCGTPSDVFQE 234
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
2-255 3.80e-37

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 136.70  E-value: 3.80e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklr 81
Cdd:PRK11000    4 VTLRNVTKAYGD----VVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAE----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDI 161
Cdd:PRK11000   75 RGVGMVFQSYALYPHLSVAENMSFGLKLAGAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 162 LICDEATSALDP----ETTTEILNLLKKVNReynlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTT 237
Cdd:PRK11000  155 FLLDEPLSNLDAalrvQMRIEISRLHKRLGR----TMIYVTHDQVEAMTLADKIVVLDAGRVAQVGKPLELYHYPANRFV 230
                         250
                  ....*....|....*...
gi 2050094043 238 QNFVRSVINDHLPESVLA 255
Cdd:PRK11000  231 AGFIGSPKMNFLPVKVTA 248
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
6-223 4.35e-37

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: 133.03  E-value: 4.35e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYESGGQSvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklRQRIG 85
Cdd:TIGR03410   2 EVSNLNVYYGQS-HILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHE----RARAG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIF--QSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELlkFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:TIGR03410  77 IAYvpQGREIFPRLTVEENLLTGLAALPRRSRKIPDEIYEL--FPVLKEMLGRRGGDLSGGQQQQLAIARALVTRPKLLL 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:TIGR03410 155 LDEPTEGIQPSIIKDIGRVIRRLRAEGGMAILLVEQYLDFARELADRYYVMERGRVVASG 214
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
1-200 4.91e-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: 131.83  E-value: 4.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKL 80
Cdd:COG4133     2 MLEAENLSCRR--GERLL--FSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPI----RDAREDY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEikERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:COG4133    74 RRRLAYLGHADGLKPELTVRENLRFWAALYGLRADR--EAIDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAP 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKvNREYNLTILLITHE 200
Cdd:COG4133   152 LWLLDEPFTALDAAGVALLAELIAA-HLARGGAVLLTTHQ 190
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
2-227 5.00e-37

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 140.10  E-value: 5.00e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLlrlVNMLER---PTAGTISIDDKDITSLSakeLR 78
Cdd:PRK13657  335 VEFDDVSFSYDNSRQ---GVEDVSFEAKPGQTVAIVGPTGAGKSTL---INLLQRvfdPQSGRILIDGTDIRTVT---RA 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 KLRQRIGMIFQSFNLFNsRTVFGNIayplRLAKlpKNEIKERVNELLK------FVglEDKANYYP-------EQLSGGQ 145
Cdd:PRK13657  406 SLRRNIAVVFQDAGLFN-RSIEDNI----RVGR--PDATDEEMRAAAEraqahdFI--ERKPDGYDtvvgergRQLSGGE 476
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 146 KQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKl 225
Cdd:PRK13657  477 RQRLAIARALLKDPPILILDEATSALDVETEAKVKAALDELMK--GRTTFIIAHRLSTVRN-ADRILVFDNGRVVESGS- 552

                  ..
gi 2050094043 226 FD 227
Cdd:PRK13657  553 FD 554
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
1-231 5.12e-37

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 133.36  E-value: 5.12e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK13548    2 MLEARNLS--VRLGGRTL--LDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLADWSPAELARR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RqriGMIFQSFNL---FNSRTVFGNIAYPLRLAKLPKNEIkerVNELLKFVGLEDKAN-YYPeQLSGGQKQRVGIARALA 156
Cdd:PRK13548   78 R---AVLPQHSSLsfpFTVEEVVAMGRAPHGLSRAEDDAL---VAAALAQVDLAHLAGrDYP-QLSGGEQQRVQLARVLA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 157 ------TSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13548  151 qlwepdGPPRWLLLDEPTSALDLAHQHHVLRLARQLAHERGLAVIVVLHDLNLAARYADRIVLLHQGRLVADGTPAEVLT 230

                  .
gi 2050094043 231 Q 231
Cdd:PRK13548  231 P 231
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
1-230 5.60e-37

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: 133.29  E-value: 5.60e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAG-TISIDDKDITSLSakeLRK 79
Cdd:COG1119     3 LLELRNVTVRR--GGKTI--LDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGnDVRLFGERRGGED---VWE 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIGMIFQSFNLFNSRTV----------FGNIAYPLRlaklPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:COG1119    76 LRKRIGLVSPALQLRFPRDEtvldvvlsgfFDSIGLYRE----PTDEQRERARELLELLGLAHLADRPFGTLSQGEQRRV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMH-VVKEIcHRVAVMEKGKVIEEGKLFDV 228
Cdd:COG1119   152 LIARALVKDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVLVTHHVEeIPPGI-THVLLLKDGRVVAAGPKEEV 230

                  ..
gi 2050094043 229 FT 230
Cdd:COG1119   231 LT 232
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
2-223 6.23e-37

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 133.71  E-value: 6.23e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:PRK13647    5 IEVEDLHFRYKDG---TKALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNAENEKWVRS-- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFN--LFNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK13647   80 -KVGLVFQDPDdqVFSS-TVWDDVAFGPVNMGLDKDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVLAMDP 157
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 160 DILICDEATSALDP---ETTTEILNLLKKVNReynlTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK13647  158 DVIVLDEPMAYLDPrgqETLMEILDRLHNQGK----TVIVATHDVDLAAEWADQVIVLKEGRVLAEG 220
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
5-225 1.44e-36

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 132.49  E-value: 1.44e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   5 NNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditsLS-AKELRKLRQR 83
Cdd:PRK11247   16 NAVSKRY--GERTV--LNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL---------LAgTAPLAEARED 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  84 IGMIFQSFNLFNSRTVFGNIAYPLrlaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK11247   83 TRLMFQDARLLPWKKVIDNVGLGL------KGQWRDAALQALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLL 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYNLTILLITHEmhvVKEichRVAVMEKGKVIEEGKL 225
Cdd:PRK11247  157 LDEPLGALDALTRIEMQDLIESLWQQHGFTVLLVTHD---VSE---AVAMADRVLLIEEGKI 212
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
21-199 1.55e-36

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 130.68  E-value: 1.55e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERP--TAGTISIDDKDITSLSAkELRklrqRIGMIFQSFNLFNSR 97
Cdd:COG4136    17 LAPLSLTVAPGEILTLMGPSGSGKSTLLAaIAGTLSPAfsASGEVLLNGRRLTALPA-EQR----RIGILFQDDLLFPHL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 TVFGNIAYPLRlAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:COG4136    92 SVGENLAFALP-PTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRALLLDEPFSKLDAALRA 170
                         170       180
                  ....*....|....*....|..
gi 2050094043 178 EILNLLKKVNREYNLTILLITH 199
Cdd:COG4136   171 QFREFVFEQIRQRGIPALLVTH 192
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
2-232 6.85e-36

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 137.55  E-value: 6.85e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:TIGR00958 479 IEFQDVSFSYPNR-PDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLVQY---DHHYLH 554
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFnSRTVFGNIAYPLRlaKLPKNEIKERVNELL--KFVGlEDKANYYPE------QLSGGQKQRVGIAR 153
Cdd:TIGR00958 555 RQVALVGQEPVLF-SGSVRENIAYGLT--DTPDEEIMAAAKAANahDFIM-EFPNGYDTEvgekgsQLSGGQKQRIAIAR 630
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDpettTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:TIGR00958 631 ALVRKPRVLILDEATSALD----AECEQLLQESRSRASRTVLLIAHRLSTV-ERADQILVLKKGSVVEMGTHKQLMEDQ 704
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
1-244 8.35e-36

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 136.91  E-value: 8.35e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLERpTAGTISIDDK----------DI 69
Cdd:PRK10261   12 VLAVENLNIAFMQEQQKIAAVRNLSFSLQRGETLAIVGESGSGKSvTALALMRLLEQ-AGGLVQCDKMllrrrsrqviEL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  70 TSLSAKELRKLR-QRIGMIFQ----SFN-LFnsrTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLEDKA---NYYPE 139
Cdd:PRK10261   91 SEQSAAQMRHVRgADMAMIFQepmtSLNpVF---TVGEQIAESIRLHQgASREEAMVEAKRMLDQVRIPEAQtilSRYPH 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 140 QLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10261  168 QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDVTIQAQILQLIKVLQKEMSMGVIFITHDMGVVAEIADRVLVMYQGEA 247
                         250       260
                  ....*....|....*....|....*
gi 2050094043 220 IEEGKLFDVFTQPKTKTTQNFVRSV 244
Cdd:PRK10261  248 VETGSVEQIFHAPQHPYTRALLAAV 272
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
16-223 9.90e-36

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: 129.37  E-value: 9.90e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  16 QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditsLSAKELRKLRQRIGMIF-QSFNLF 94
Cdd:cd03267    32 REVEALKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGL----VPWKRRKKFLRRIGVVFgQKTQLW 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:cd03267   108 WDLPVIDSFYLLAAIYDLPPARFKKRLDELSELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVV 187
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03267   188 AQENIRNFLKEYNRERGTTVLLTSHYMKDIEALARRVLVIDKGRLLYDG 236
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
21-241 1.75e-35

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 129.43  E-value: 1.75e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKS-TLLRLVNMLE---RPTAGTISIDDKDItslSAKELRKlrQRIGMIFQsfnlfNS 96
Cdd:PRK10418   19 VHGVSLTLQRGRVLALVGGSGSGKSlTCAAALGILPagvRQTAGRVLLDGKPV---APCALRG--RKIATIMQ-----NP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  97 RTVFGniayPLR---------LAKLPKNEIKERVNELLKFVGLEDKA---NYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:PRK10418   89 RSAFN----PLHtmhtharetCLALGKPADDATLTAALEAVGLENAArvlKLYPFEMSGGMLQRMMIALALLCEAPFIIA 164
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFV 241
Cdd:PRK10418  165 DEPTTDLDVVAQARILDLLESIVQKRALGMLLVTHDMGVVARLADDVAVMSHGRIVEQGDVETLFNAPKHAVTRSLV 241
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
2-223 2.41e-35

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: 128.03  E-value: 2.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQS------------------VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIS 63
Cdd:cd03220     1 IELENVSKSYPTYKGGssslkklgilgrkgevgeFWALKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGIYPPDSGTVT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  64 IdDKDITSLSAkelrklrqrIGMIFQsfnlfNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSG 143
Cdd:cd03220    81 V-RGRVSSLLG---------LGGGFN-----PELTGRENIYLNGRLLGLSRKEIDEKIDEIIEFSELGDFIDLPVKTYSS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:cd03220   146 GMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGK-TVILVSHDPSSIKRLCDRALVLEKGKIRFDG 224
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
6-244 1.08e-34

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 129.15  E-value: 1.08e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLE----RPTAGTISIDDKDITSLSAKELRKL- 80
Cdd:PRK15093    8 NLTIEFKTSDGWVKAVDRVSMTLTEGEIRGLVGESGSGKSLIAKAICGVTkdnwRVTADRMRFDDIDLLRLSPRERRKLv 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQ--------SFNLfnSRTVFGNI---AYPLRLAKLpKNEIKERVNELLKFVGLEDKANY---YPEQLSGGQK 146
Cdd:PRK15093   88 GHNVSMIFQepqscldpSERV--GRQLMQNIpgwTYKGRWWQR-FGWRKRRAIELLHRVGIKDHKDAmrsFPYELTEGEC 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:PRK15093  165 QKVMIAIALANQPRLLIADEPTNAMEPTTQAQIFRLLTRLNQNNNTTILLISHDLQMLSQWADKINVLYCGQTVETAPSK 244
                         250
                  ....*....|....*...
gi 2050094043 227 DVFTQPKTKTTQNFVRSV 244
Cdd:PRK15093  245 ELVTTPHHPYTQALIRAI 262
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
20-241 5.02e-34

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 125.66  E-value: 5.02e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLER--PTA---GTISIDDKDITSlSAKELRKLRQRIGMIFQSFNLF 94
Cdd:PRK14243   25 AVKNVWLDIPKNQITAFIGPSGCGKSTILRCFNRLNDliPGFrveGKVTFHGKNLYA-PDVDPVEVRRRIGMVFQKPNPF 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 nSRTVFGNIAYPLRLAKLpKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK14243  104 -PKSIYDNIAYGARINGY-KGDMDELVERSLRQAALwdevKDKLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 171 LDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEICHRVA-----VMEKGKVIEEGKLFD----VFTQPKTKTTQNFV 241
Cdd:PRK14243  182 LDPISTLRIEELMHELKEQY--TIIIVTHNMQQAARVSDMTAffnveLTEGGGRYGYLVEFDrtekIFNSPQQQATRDYV 259
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
2-223 6.94e-34

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: 130.31  E-value: 6.94e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLE--RPTAG------------------- 60
Cdd:TIGR03269   1 IEVKNLTKKFDG----KEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDqyEPTSGriiyhvalcekcgyverps 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  61 -----------TISIDDKDITSLSAKELRKLRQRIGMIFQ-SFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFV 128
Cdd:TIGR03269  77 kvgepcpvcggTLEPEEVDFWNLSDKLRRRIRKRIAIMLQrTFALYGDDTVLDNVLEALEEIGYEGKEAVGRAVDLIEMV 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 129 GLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEIC 208
Cdd:TIGR03269 157 QLSHRITHIARDLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWPEVIEDLS 236
                         250
                  ....*....|....*
gi 2050094043 209 HRVAVMEKGKVIEEG 223
Cdd:TIGR03269 237 DKAIWLENGEIKEEG 251
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
23-228 7.70e-34

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 127.30  E-value: 7.70e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAK-----ELRklrqRIGMIFQSFNLFNSR 97
Cdd:PRK11144   16 TVNLTLPAQGITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRVLFDAEKGiclppEKR----RIGYVFQDARLFPHY 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 TVFGNIAYPLrlaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK11144   92 KVRGNLRYGM------AKSMVAQFDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAPELLLMDEPLASLDLPRKR 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 178 EILNLLKKVNREYNLTILLITHEMhvvKEICH---RVAVMEKGKVIEEGKLFDV 228
Cdd:PRK11144  166 ELLPYLERLAREINIPILYVSHSL---DEILRladRVVVLEQGKVKAFGPLEEV 216
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
1-232 1.04e-33

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 124.84  E-value: 1.04e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRK- 79
Cdd:COG4559     1 MLEAENLS--VRLGGRTL--LDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAWSPWELARr 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 ---LRQRIGMIFQsfnlFNSRTV--FGniAYPLRLAKLPKNEIKERVNELlkfVGLEDKAN-YYPeQLSGGQKQRVGIAR 153
Cdd:COG4559    77 ravLPQHSSLAFP----FTVEEVvaLG--RAPHGSSAAQDRQIVREALAL---VGLAHLAGrSYQ-TLSGGEQQRVQLAR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 154 ALA-------TSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLF 226
Cdd:COG4559   147 VLAqlwepvdGGPRWLFLDEPTSALDLAHQHAVLRLARQLARR-GGGVVAVLHDLNLAAQYADRILLLHQGRLVAQGTPE 225

                  ....*.
gi 2050094043 227 DVFTQP 232
Cdd:COG4559   226 EVLTDE 231
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
6-235 1.30e-33

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 124.24  E-value: 1.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYEsgGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIG 85
Cdd:PRK10895    8 NLAKAYK--GRRV--VEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHA--RARRGIG 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIFQSFNLFNSRTVFGNIAYPLRLAK-LPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILIC 164
Cdd:PRK10895   82 YLPQEASIFRRLSVYDNLMAVLQIRDdLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 165 DEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTK 235
Cdd:PRK10895  162 DEPFAGVDPISVIDIKRIIEHL-RDSGLGVLITDHNVRETLAVCERAYIVSQGHLIAHGTPTEILQDEHVK 231
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
2-224 4.03e-33

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 128.79  E-value: 4.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:PRK11160  339 LTLNNVSFTYPDQPQPV--LKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPIADYSEAALR--- 413
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSrTVFGNiaypLRLAKLPKNEikERVNELLKFVGLEDKANYYP----------EQLSGGQKQRVGI 151
Cdd:PRK11160  414 QAISVVSQRVHLFSA-TLRDN----LLLAAPNASD--EALIEVLQQVGLEKLLEDDKglnawlgeggRQLSGGEQRRLGI 486
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVkEICHRVAVMEKGKVIEEGK 224
Cdd:PRK11160  487 ARALLHDAPLLLLDEPTEGLDAETERQILELLAEHAQ--NKTVLMITHRLTGL-EQFDRICVMDNGQIIEQGT 556
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
2-243 5.35e-33

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 123.22  E-value: 5.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNML-----ERPTAGTISIDDKDITSLSAKe 76
Cdd:PRK14258    8 IKVNNLSFYYDT--QKI--LEGVSMEIYQSKVTAIIGPSGCGKSTFLKCLNRMnelesEVRVEGRVEFFNQNIYERRVN- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  77 LRKLRQRIGMIFQSFNLFnSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGLED----KANYYPEQLSGGQKQRVGI 151
Cdd:PRK14258   83 LNRLRRQVSMVHPKPNLF-PMSVYDNVAYGVKIVGWrPKLEIDDIVESALKDADLWDeikhKIHKSALDLSGGQQQRLCI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 152 ARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEK-----GKVIEEGKLF 226
Cdd:PRK14258  162 ARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMVIVSHNLHQVSRLSDFTAFFKGnenriGQLVEFGLTK 241
                         250
                  ....*....|....*..
gi 2050094043 227 DVFTQPKTKTTQNFVRS 243
Cdd:PRK14258  242 KIFNSPHDSRTREYVLS 258
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
6-225 1.35e-32

gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 represents the family of all lantibiotics related to gallidermin, including epidermin, mutatin, and nisin. This protein family describes the ATP-binding subunit of a gallidermin/epidermin class lantibiotic protection transporter. It is largely restricted to gallidermin-family lantibiotic biosynthesis and export cassettes, but also occurs in orphan transporter cassettes in species that lack candidate lantibiotic precursor and synthetase genes.


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 120.97  E-value: 1.35e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYesGGQsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakelRKLRQRIG 85
Cdd:TIGR03740   5 NLSKRF--GKQ--TAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGHPWT-------RKDLHKIG 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIkervNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:TIGR03740  74 SLIESPPLYENLTARENLKVHTTLLGLPDSRI----DEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILD 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKL 225
Cdd:TIGR03740 150 EPTNGLDPIGIQELRELIRSFPEQ-GITVILSSHILSEVQQLADHIGIISEGVLGYQGKI 208
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
20-219 2.51e-32

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: 118.69  E-value: 2.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL--------RQRIGmifqsf 91
Cdd:cd03215    15 AVRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTRRSPRDAIRAgiayvpedRKREG------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  92 nLFNSRTVFGNIAYPLrlaklpkneikervnellkfvgledkanyypeQLSGGQKQRVGIARALATSPDILICDEATSAL 171
Cdd:cd03215    89 -LVLDLSVAENIALSS--------------------------------LLSGGNQQKVVLARWLARDPRVLILDEPTRGV 135
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2050094043 172 DPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:cd03215   136 DVGAKAEIYRLIRELADA-GKAVLLISSELDELLGLCDRILVMYEGRI 182
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
1-244 2.91e-32

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 120.80  E-value: 2.91e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK-----DITSLSAK 75
Cdd:PRK11701    6 LLSVRGLTKLYGPR----KGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMRdgqlrDLYALSEA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  76 ELRKL-RQRIGMIFQsfnlfNSR-------TVFGNIAYPLrLAKLPKN--EIKERVNELLKFVGLE-DKANYYPEQLSGG 144
Cdd:PRK11701   82 ERRRLlRTEWGFVHQ-----HPRdglrmqvSAGGNIGERL-MAVGARHygDIRATAGDWLERVEIDaARIDDLPTTFSGG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 145 QKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGk 224
Cdd:PRK11701  156 MQQRLQIARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLVRELGLAVVIVTHDLAVARLLAHRLLVMKQGRVVESG- 234
                         250       260
                  ....*....|....*....|.
gi 2050094043 225 LFD-VFTQPKTKTTQNFVRSV 244
Cdd:PRK11701  235 LTDqVLDDPQHPYTQLLVSSV 255
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
2-219 3.68e-32

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: 119.88  E-value: 3.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESggQSVHAV-EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslSAKELRKL 80
Cdd:cd03248    12 VKFQNVTFAYPT--RPDTLVlQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPI---SQYEHKYL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFnSRTVFGNIAYPLrlAKLPKNEIKErvnellkfvgLEDKAN-----------YYPE------QLSG 143
Cdd:cd03248    87 HSKVSLVGQEPVLF-ARSLQDNIAYGL--QSCSFECVKE----------AAQKAHahsfiselasgYDTEvgekgsQLSG 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:cd03248   154 GQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQALYDWPE--RRTVLVIAHRLSTV-ERADQILVLDGGRI 226
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
2-214 1.05e-31

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: 124.32  E-value: 1.05e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlr 81
Cdd:TIGR02857 322 LEFSGVSVAYPGRRP---ALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLADADADSWRD-- 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qRIGMIFQSFNLFNsrtvfGNIAYPLRLAKL--PKNEIKE--RVNELLKFV-----GLEDKANYYPEQLSGGQKQRVGIA 152
Cdd:TIGR02857 397 -QIAWVPQHPFLFA-----GTIAENIRLARPdaSDAEIREalERAGLDEFVaalpqGLDTPIGEGGAGLSGGQAQRLALA 470
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVkEICHRVAVM 214
Cdd:TIGR02857 471 RAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ--GRTVLLVTHRLALA-ALADRIVVL 529
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
1-217 4.26e-31

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


Pssm-ID: 443809 [Multi-domain]  Cd Length: 229  Bit Score: 117.15  E-value: 4.26e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISK---VYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK----DITSLS 73
Cdd:COG4778     4 LLEVENLSKtftLHLQGGKRLPVLDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILVRHDggwvDLAQAS 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  74 AKELRKLRQR-IGMIFQsfnlF-------NSRTVfgnIAYPLRLAKLPKNEIKERVNELLKFVGL-EDKANYYPEQLSGG 144
Cdd:COG4778    84 PREILALRRRtIGYVSQ----FlrviprvSALDV---VAEPLLERGVDREEARARARELLARLNLpERLWDLPPATFSGG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 145 QKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKG 217
Cdd:COG4778   157 EQQRVNIARGFIADPPLLLLDEPTASLDAANRAVVVELIEEAKAR-GTAIIGIFHDEEVREAVADRVVDVTPF 228
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
2-223 6.81e-31

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: 115.97  E-value: 6.81e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:cd03369     7 IEVENLSVRYAPDLPPV--LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDISTI---PLEDLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFnSRTVFGNIAyplrlaklPKNEIKERvnELLKFVGLEDKANyypeQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03369    82 SSLTIIPQDPTLF-SGTIRSNLD--------PFDEYSDE--EIYGALRVSEGGL----NLSQGQRQLLCLARALLKRPRV 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 162 LICDEATSALDPETTTEIlnllKKVNRE--YNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:cd03369   147 LVLDEATASIDYATDALI----QKTIREefTNSTILTIAHRLRTIID-YDKILVMDAGEVKEYD 205
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
20-223 1.01e-30

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 122.93  E-value: 1.01e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTI-----SIDDKDITSlsakelrklRQRIGMIFQSFNLF 94
Cdd:NF033858  281 AVDHVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAwlfgqPVDAGDIAT---------RRRVGYMSQAFSLY 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:NF033858  352 GELTVRQNLELHARLFHLPAAEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPV 431
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:NF033858  432 ARDMFWRLLIELSREDGVTIFISTHFMNEA-ERCDRISLMHAGRVLASD 479
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
1-228 1.10e-30

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 121.43  E-value: 1.10e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK09700    5 YISMAGIGKSF--GP--VHALKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNINYNKLDHKLAAQL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFNSRTVFGNiaypLRLAKLPK-----------NEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRV 149
Cdd:PRK09700   81 --GIGIIYQELSVIDELTVLEN----LYIGRHLTkkvcgvniidwREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQML 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV 228
Cdd:PRK09700  155 EIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKE-GTAIVYISHKLAEIRRICDRYTVMKDGSSVCSGMVSDV 232
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
2-223 2.53e-30

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: 113.56  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelrkLR 81
Cdd:cd03247     1 LSINNVSFSYP--EQEQQVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKA----LS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSrTVFGNIAyplrlaklpkneikervnellkfvgledkanyypEQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03247    75 SLISVLNQRPYLFDT-TLRNNLG----------------------------------RRFSGGERQRLALARILLQDAPI 119
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:cd03247   120 VLLDEPTVGLDPITERQLLSLIFEVLK--DKTLIWITHHLTGIEHM-DKILFLENGKIIMQG 178
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
1-223 2.90e-30

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 115.88  E-value: 2.90e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGgQSVHAVEdvtLSVEKGEIFGIIGFSGAGKSTLLRLVNML---ERPTAGTISIDDKDITSLS--AK 75
Cdd:PRK09984    4 IIRVEKLAKTFNQH-QALHAVD---LNIHHGEMVALLGPSGSGKSTLLRHLSGLitgDKSAGSHIELLGRTVQREGrlAR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  76 ELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPlRLAKLP---------KNEIKERVNELLKFVGLEDKANYYPEQLSGGQK 146
Cdd:PRK09984   80 DIRKSRANTGYIFQQFNLVNRLSVLENVLIG-ALGSTPfwrtcfswfTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 147 QRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK09984  159 QRVAIARALMQQAKVILADEPIASLDPESARIVMDTLRDINQNDGITVVVTLHQVDYALRYCERIVALRQGHVFYDG 235
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
10-219 7.68e-30

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: 119.47  E-value: 7.68e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  10 VYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLeRPTAGTISIDDKDITSLSAKElrkLRQRIGMIF 88
Cdd:COG4618   337 TVVPPGSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARlLVGVW-PPTAGSVRLDGADLSQWDREE---LGRHIGYLP 412
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 QSFNLFNSrTVFGNIAyplRLAKLPKNEIKE-----RVNEL-LKF-------VGlEDKANyypeqLSGGQKQRVGIARAL 155
Cdd:COG4618   413 QDVELFDG-TIAENIA---RFGDADPEKVVAaaklaGVHEMiLRLpdgydtrIG-EGGAR-----LSGGQRQRIGLARAL 482
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVkEICHRVAVMEKGKV 219
Cdd:COG4618   483 YGDPRLVVLDEPNSNLDDEGEAALAAAIRAL-KARGATVVVITHRPSLL-AAVDKLLVLRDGRV 544
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
1-232 7.77e-30

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 117.64  E-value: 7.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISkvYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrkL 80
Cdd:PRK09536    3 MIDVSDLS--VEFGDTTV--LDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEALSARA---A 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQ----SFNlFNSRTV--FGNIAYPLRLAklPKNEIKER-VNELLKFVGLEDKANYYPEQLSGGQKQRVGIAR 153
Cdd:PRK09536   76 SRRVASVPQdtslSFE-FDVRQVveMGRTPHRSRFD--TWTETDRAaVERAMERTGVAQFADRPVTSLSGGERQRVLLAR 152
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK09536  153 ALAQATPVLLLDEPTASLDINHQVRTLELVRRL-VDDGKTAVAAIHDLDLAARYCDELVLLADGRVRAAGPPADVLTAD 230
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
14-247 9.65e-30

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 114.81  E-value: 9.65e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  14 GGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSA---KELRKLRQRIGMIFQS 90
Cdd:PRK14271   32 AGKTV--LDQVSMGFPARAVTSLMGPTGSGKTTFLRTLNRMNDKVSGYRYSGDVLLGGRSIfnyRDVLEFRRRVGMLFQR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  91 FNLFnSRTVFGNIAYPLRLAKL-PKNEIKERVNELLKFVGL----EDKANYYPEQLSGGQKQRVGIARALATSPDILICD 165
Cdd:PRK14271  110 PNPF-PMSIMDNVLAGVRAHKLvPRKEFRGVAQARLTEVGLwdavKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLD 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREynLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQNFVRSVI 245
Cdd:PRK14271  189 EPTSALDPTTTEKIEEFIRSLADR--LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAETARYVAGLS 266

                  ..
gi 2050094043 246 ND 247
Cdd:PRK14271  267 GD 268
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
2-223 1.98e-29

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 118.58  E-value: 1.98e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLR 81
Cdd:PRK11176  342 IEFRNVTFTYP--GKEVPALRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLRDY---TLASLR 416
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSrTVFGNIAYPlRLAKLPKNEIKE--RVNELLKFV-----GLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK11176  417 NQVALVSQNVHLFND-TIANNIAYA-RTEQYSREQIEEaaRMAYAMDFInkmdnGLDTVIGENGVLLSGGQRQRIAIARA 494
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 155 LATSPDILICDEATSALDPETTTEI---LNLLKKvnreyNLTILLITHEMHVVkEICHRVAVMEKGKVIEEG 223
Cdd:PRK11176  495 LLRDSPILILDEATSALDTESERAIqaaLDELQK-----NRTSLVIAHRLSTI-EKADEILVVEDGEIVERG 560
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
20-199 5.67e-29

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: 116.69  E-value: 5.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSFNLFNSrTV 99
Cdd:TIGR02868 350 VLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDEVRR---RVSVCAQDAHLFDT-TV 425
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 100 FGNiaypLRLAKlpKNEIKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:TIGR02868 426 REN----LRLAR--PDATDEELWAALERVGLADWLRALPDgldtvlgeggaRLSGGERQRLALARALLADAPILLLDEPT 499
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2050094043 169 SALDPETTTEILNLLKKVNREYnlTILLITH 199
Cdd:TIGR02868 500 EHLDAETADELLEDLLAALSGR--TVVLITH 528
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
1-231 5.78e-28

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 109.33  E-value: 5.78e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKl 80
Cdd:PRK11231    2 TLRTENLTVGY--GTKRI--LNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPISMLSSRQLAR- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFNSRTVFGNIAY---P-LRL-AKLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL 155
Cdd:PRK11231   77 --RLALLPQHHLTPEGITVRELVAYgrsPwLSLwGRLSAED-NARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVL 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 156 ATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK11231  154 AQDTPVVLLDEPTTYLDINHQVELMRLMRELNTQ-GKTVVTVLHDLNQASRYCDHLVVLANGHVMAQGTPEEVMTP 228
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
19-222 1.02e-27

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 112.80  E-value: 1.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIGMI---FQSFNLFN 95
Cdd:COG1129   266 GVVRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKPVRIRSPRD--AIRAGIAYVpedRKGEGLVL 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  96 SRTVFGNIAYPL--RLAK---LPKNEIKERVNEL-----LKFVGLEDKANyypeQLSGGQKQRVGIARALATSPDILICD 165
Cdd:COG1129   344 DLSIRENITLASldRLSRgglLDRRRERALAEEYikrlrIKTPSPEQPVG----NLSGGNQQKVVLAKWLATDPKVLILD 419
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 166 EATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:COG1129   420 EPTRGIDVGAKAEIYRLIRELAAE-GKAVIVISSELPELLGLSDRILVMREGRIVGE 475
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
11-209 2.79e-27

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 106.72  E-value: 2.79e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  11 YESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklrQRIGMIFQS 90
Cdd:PRK10247   15 YLAGDAKI--LNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTLKPEIYR---QQVSYCAQT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  91 FNLFNSrTVFGNIAYPLRLAKlPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK10247   90 PTLFGD-TVYDNLIFPWQIRN-QQPDPAIFLDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSA 167
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2050094043 171 LDPETTTEILNLLKKVNREYNLTILLITHEMHvvkEICH 209
Cdd:PRK10247  168 LDESNKHNVNEIIHRYVREQNIAVLWVTHDKD---EINH 203
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
3-221 1.22e-26

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 110.00  E-value: 1.22e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   3 SFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQ 82
Cdd:PRK11288    6 SFDGIGKTFPG----VKALDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMRFASTTA--ALAA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIGMIFQSFNLFNSRTVFGNI---AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK11288   80 GVAIIYQELHLVPEMTVAENLylgQLPHKGGIVNRRLLNYEAREQLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNA 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 160 DILICDEATSALdpeTTTEILNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:PRK11288  160 RVIAFDEPTSSL---SAREIEQLFRVIRelRAEGRVILYVSHRMEEIFALCDAITVFKDGRYVA 220
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
22-223 9.68e-26

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 103.91  E-value: 9.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSFNLFNSRTVFG 101
Cdd:PRK10253   24 ENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQHYASKEVAR---RIGLLAQNATTPGDITVQE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIA---YPLR-LAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK10253  101 LVArgrYPHQpLFTRWRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLDISHQI 180
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2050094043 178 EILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK10253  181 DLLELLSELNREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQG 226
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
15-223 1.24e-25

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: 102.35  E-value: 1.24e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV-NMLERP--TAGTISIDDKDitsLSAKELRKlrqRIGMIFQSF 91
Cdd:cd03234    17 NKYARILNDVSLHVESGQVMAILGSSGSGKTTLLDAIsGRVEGGgtTSGQILFNGQP---RKPDQFQK---CVAYVRQDD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  92 NLFNSRTVFGNIAY--PLRLAKLPKNEIKERVNE--LLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEA 167
Cdd:cd03234    91 ILLPGLTVRETLTYtaILRLPRKSSDAIRKKRVEdvLLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEP 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 168 TSALDPETTTEILNLLKKVNREyNLTILLITH----EMHvvkEICHRVAVMEKGKVIEEG 223
Cdd:cd03234   171 TSGLDSFTALNLVSTLSQLARR-NRIVILTIHqprsDLF---RLFDRILLLSSGEIVYSG 226
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
2-223 1.35e-25

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: 107.52  E-value: 1.35e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRklr 81
Cdd:TIGR01193 474 IVINDVSYSY---GYGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLKDIDRHTLR--- 547
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNsrtvfGNIAYPLRLAKLPKNEIKErVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVG 150
Cdd:TIGR01193 548 QFINYLPQEPYIFS-----GSILENLLLGAKENVSQDE-IWAACEIAEIKDDIENMPLgyqtelseegsSISGGQKQRIA 621
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVNREynlTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:TIGR01193 622 LARALLTDSKVLILDESTSNLDTITEKKIVNNLLNLQDK---TIIFVAHRLSVAKQS-DKIIVLDHGKIIEQG 690
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
16-234 1.54e-25

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 103.16  E-value: 1.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  16 QSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItSLSAKELRKLRQRIGMIFQSFN--L 93
Cdd:PRK13638   12 QDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPL-DYSKRGLLALRQQVATVFQDPEqqI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSrTVFGNIAYPLRLAKLPKNEIKERVNELLKFVgledKANYYPEQ----LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK13638   91 FYT-DIDSDIAFSLRNLGVPEAEITRRVDEALTLV----DAQHFRHQpiqcLSHGQKKRVAIAGALVLQARYLLLDEPTA 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 170 ALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKT 234
Cdd:PRK13638  166 GLDPAGRTQMIAIIRRIVAQGN-HVIISSHDIDLIYEISDAVYVLRQGQILTHGAPGEVFACTEA 229
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
2-223 1.16e-24

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: 98.78  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNI-----SKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTA--GTISIDDKDItslsa 74
Cdd:cd03213     4 LSFRNLtvtvkSSPSKSGKQLLK---NVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGLGvsGEVLINGRPL----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  75 kELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLRLaklpkneikervnellkfvgledkanyypEQLSGGQKQRVGIARA 154
Cdd:cd03213    76 -DKRSFRKIIGYVPQDDILHPTLTVRETLMFAAKL-----------------------------RGLSGGERKRVSIALE 125
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITH----EMHvvkEICHRVAVMEKGKVIEEG 223
Cdd:cd03213   126 LVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADT-GRTIICSIHqpssEIF---ELFDKLLLLSQGRVIYFG 194
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
1-222 2.13e-24

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 99.57  E-value: 2.13e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesggQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKelRKL 80
Cdd:PRK11614    5 MLSFDKVSAHY----GKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDITDWQTA--KIM 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIK-ERVNELlkFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:PRK11614   79 REAVAIVPEGRRVFSRMTVEENLAMGGFFAERDQFQERiKWVYEL--FPRLHERRIQRAGTMSGGEQQMLAIGRALMSQP 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 160 DILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK11614  157 RLLLLDEPSLGLAPIIIQQIFDTIEQL-REQGMTIFLVEQNANQALKLADRGYVLENGHVVLE 218
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
24-223 2.60e-24

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 99.86  E-value: 2.60e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  24 VTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrqRIGMIFQSFNLFNSRTVFGNI 103
Cdd:PRK10575   30 LSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFAR---KVAYLPQQLPAAEGMTVRELV 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 104 A---YPLR--LAKLPKNEiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:PRK10575  107 AigrYPWHgaLGRFGAAD-REKVEEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALDIAHQVD 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2050094043 179 ILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:PRK10575  186 VLALVHRLSQERGLTVIAVLHDINMAARYCDYLVALRGGEMIAQG 230
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
18-222 3.91e-24

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 102.80  E-value: 3.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL--------RQRIGMIfQ 89
Cdd:COG3845   271 VPALKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRLDGEDITGLSPRERRRLgvayipedRLGRGLV-P 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  90 SFNLF-NsrTVFGNIAYPlRLAKLP---KNEIKERVNELL-----KFVGLEDKAnyypEQLSGGQKQRVGIARALATSPD 160
Cdd:COG3845   350 DMSVAeN--LILGRYRRP-PFSRGGfldRKAIRAFAEELIeefdvRTPGPDTPA----RSLSGGNQQKVILARELSRDPK 422
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:COG3845   423 LLIAAQPTRGLDVGAIEFIHQRLLEL-RDAGAAVLLISEDLDEILALSDRIAVMYEGRIVGE 483
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
2-223 5.31e-24

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: 103.17  E-value: 5.31e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    2 ISFNNISKVYESGGQSvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI-TSLSAkelrkL 80
Cdd:TIGR01257  929 VCVKNLVKIFEPSGRP--AVDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIeTNLDA-----V 1001
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   81 RQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:TIGR01257 1002 RQSLGMCPQHNILFHHLTVAEHILFYAQLKGRSWEEAQLEMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAK 1081
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043  161 ILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEG 223
Cdd:TIGR01257 1082 VVVLDEPTSGVDPYSRRSIWDLLLKYRS--GRTIIMSTHHMDEADLLGDRIAIISQGRLYCSG 1142
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
4-220 8.72e-24

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 101.68  E-value: 8.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   4 FNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIdDKDItslsakelrklrqR 83
Cdd:COG0488     1 LENLSKSF--GGRPL--LDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSI-PKGL-------------R 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  84 IGMIFQSFNLFNSRTVFGNI-------------------------AYPLRLAKLpKNEIKE--------RVNELLKFVGL 130
Cdd:COG0488    63 IGYLPQEPPLDDDLTVLDTVldgdaelraleaeleeleaklaepdEDLERLAEL-QEEFEAlggweaeaRAEEILSGLGF 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 131 EDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKvnreYNLTILLITHEMHVVKEICH 209
Cdd:COG0488   142 PEEDLDRPvSELSGGWRRRVALARALLSEPDLLLLDEPTNHLDLESIEWLEEFLKN----YPGTVLVVSHDRYFLDRVAT 217
                         250
                  ....*....|.
gi 2050094043 210 RVAVMEKGKVI 220
Cdd:COG0488   218 RILELDRGKLT 228
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
1-279 1.05e-22

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 98.58  E-value: 1.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYeSGgqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PRK15439   11 LLCARSISKQY-SG---VEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAHQL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFNSRTVFGNIAYplRLAKLPKNeiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:PRK15439   87 --GIYLVPQEPLLFPNLSVKENILF--GLPKRQAS--MQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMRDSR 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTeilNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVftqPKTKTTQ 238
Cdd:PRK15439  161 ILILDEPTASLTPAETE---RLFSRIRelLAQGVGIVFISHKLPEIRQLADRISVMRDGTIALSGKTADL---STDDIIQ 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 2050094043 239 NFVRSVINDHLPESvlakiqnggQIYRLTFTG----EETGQPVLS 279
Cdd:PRK15439  235 AITPAAREKSLSAS---------QKLWLELPGnrrqQAAGAPVLT 270
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
19-222 1.62e-22

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 93.87  E-value: 1.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSlsakelrklrqrigmifqsfnlfnS 96
Cdd:COG2401    44 YVLRDLNLEIEPGEIVLIVGASGSGKSTLLRLLagALKGTPVAGCVDVPDNQFGR------------------------E 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  97 RTVFGNIAyplrlaklPKNEIKERVnELLKFVGLEDKANYY--PEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:COG2401   100 ASLIDAIG--------RKGDFKDAV-ELLNAVGLSDAVLWLrrFKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQ 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREYNLTILLITHEMHVVKEIC-HRVAVMEKGKVIEE 222
Cdd:COG2401   171 TAKRVARNLQKLARRAGITLVVATHHYDVIDDLQpDLLIFVGYGGVPEE 219
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
15-223 7.24e-22

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 96.32  E-value: 7.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLsakELRKLRQRIGMIFQSFNLF 94
Cdd:PRK10789  325 QTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSLIQRHFDVSEGDIRFHDIPLTKL---QLDSWRSRLAVVSQTPFLF 401
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 nSRTVFGNIAyplrLAKlpKNEIKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK10789  402 -SDTVANNIA----LGR--PDATQQEIEHVARLASVHDDILRLPQgydtevgergvMLSGGQKQRISIARALLLNAEILI 474
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREYnlTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PRK10789  475 LDDALSAVDGRTEHQILHNLRQWGEGR--TVIISAHRLSALTE-ASEILVMQHGHIAQRG 531
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
21-223 7.61e-22

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: 91.43  E-value: 7.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSLSAKElrKLRQRIGMIFQsfnlfnsrt 98
Cdd:cd03217    16 LKGVNLTIKKGEVHALMGPNGSGKSTLAKTImgHPKYEVTEGEILFKGEDITDLPPEE--RARLGIFLAFQ--------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  99 vfgniaYPLRLAKLpkneikeRVNELLKFVGledkanyypEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTE 178
Cdd:cd03217    85 ------YPPEIPGV-------KNADFLRYVN---------EGFSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRL 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2050094043 179 ILNLLKKVnREYNLTILLITHEMHVVKEI-CHRVAVMEKGKVIEEG 223
Cdd:cd03217   143 VAEVINKL-REEGKSVLIITHYQRLLDYIkPDRVHVLYDGRIVKSG 187
NIL smart00930
This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine ...
260-334 9.34e-22

This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins; This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.


Pssm-ID: 197998 [Multi-domain]  Cd Length: 76  Bit Score: 87.57  E-value: 9.34e-22
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043  260 GGQIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKEIQKALQHLR-LQVQLKEV 334
Cdd:smart00930   1 DGRLVRLTFTGESADEPLISQLAREFGVDVNILHGNIERIQGGPFGSLVVELTGDEEDIEAALAYLReQGVEVEVL 76
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
2-218 2.19e-21

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: 88.66  E-value: 2.19e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrklr 81
Cdd:cd03221     1 IELENLSKTY--GGKLL--LKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTWGST-------------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGmifqsfnlfnsrtvfgniayplrlaklpkneikervnellkfvgledkanYYPeQLSGGQKQRVGIARALATSPDI 161
Cdd:cd03221    63 VKIG--------------------------------------------------YFE-QLSGGEKMRLALAKLLLENPNL 91
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 162 LICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:cd03221    92 LLLDEPTNHLDLESIEALEEALK----EYPGTVILVSHDRYFLDQVATKIIELEDGK 144
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
1-217 2.55e-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: 95.47  E-value: 2.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    1 MISFNNISKVYEsgGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDI-TSLSakelrK 79
Cdd:TIGR01257 1937 ILRLNELTKVYS--GTSSPAVDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSIlTNIS-----D 2009
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   80 LRQRIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSP 159
Cdd:TIGR01257 2010 VHQNMGYCPQFDAIDDLLTGREHLYLYARLRGVPAEEIEKVANWSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCP 2089
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043  160 DILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKG 217
Cdd:TIGR01257 2090 PLVLLDEPTTGMDPQARRMLWNTIVSIIRE-GRAVVLTSHSMEECEALCTRLAIMVKG 2146
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
5-220 7.01e-21

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 93.07  E-value: 7.01e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   5 NNISKVYesGGqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDDKDITSLSAKELRklR 81
Cdd:PRK13549    9 KNITKTF--GG--VKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGV-YPHGtyeGEIIFEGEELQASNIRDTE--R 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNSRTVFGNI---AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATS 158
Cdd:PRK13549   82 AGIAIIHQELALVKELSVLENIflgNEITPGGIMDYDAMYLRAQKLLAQLKLDINPATPVGNLGLGQQQLVEIAKALNKQ 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 159 PDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:PRK13549  162 ARLLILDEPTASLTESETAVLLDIIRDL-KAHGIACIYISHKLNEVKAISDTICVIRDGRHI 222
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
1-199 7.79e-21

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 93.33  E-value: 7.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISkVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI-DDKDITSLSakelrk 79
Cdd:COG4178   362 ALALEDLT-LRTPDGRPL--LEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARpAGARVLFLP------ 432
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 lrQRIGMIFQSFnlfnsRTVfgnIAYPLRLAKLPKneikERVNELLKFVGLEDKANYYPEQ------LSGGQKQRVGIAR 153
Cdd:COG4178   433 --QRPYLPLGTL-----REA---LLYPATAEAFSD----AELREALEAVGLGHLAERLDEEadwdqvLSLGEQQRLAFAR 498
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKvnREYNLTILLITH 199
Cdd:COG4178   499 LLLHKPDWLFLDEATSALDEENEAALYQLLRE--ELPGTTVISVGH 542
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
2-230 1.41e-20

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 89.56  E-value: 1.41e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHaveDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditsLSAKELRKLR 81
Cdd:PRK15056    7 IVVNDVTVTWRNGHTALR---DASFTVPGGSIAALVGVNGSGKSTLFKALMGFVRLASGKISI-------LGQPTRQALQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QR-IGMIFQS------FNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA 154
Cdd:PRK15056   77 KNlVAYVPQSeevdwsFPVLVEDVVMMGRYGHMGWLRRAKKRDRQIVTAALARVDMVEFRHRQIGELSGGQKKRVFLARA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 155 LATSPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHrVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK15056  157 IAQQGQVILLDEPFTGVDVKTEARIISLLREL-RDEGKTMLVSTHNLGSVTEFCD-YTVMVKGTVLASGPTETTFT 230
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
2-224 2.60e-20

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 91.70  E-value: 2.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGgQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAkelRKLR 81
Cdd:PRK10790  341 IDIDNVSFAYRDD-NLV--LQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSLSH---SVLR 414
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFnSRTVFGNIAyplrlakLPKNEIKERVNELLKFVGLEDKANYYP--------EQ---LSGGQKQRVG 150
Cdd:PRK10790  415 QGVAMVQQDPVVL-ADTFLANVT-------LGRDISEEQVWQALETVQLAELARSLPdglytplgEQgnnLSVGQKQLLA 486
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLKKVnREyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGK 224
Cdd:PRK10790  487 LARVLVQTPQILILDEATANIDSGTEQAIQQALAAV-RE-HTTLVVIAHRLSTIVE-ADTILVLHRGQAVEQGT 557
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
1-204 2.62e-20

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 88.63  E-value: 2.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesgGQSVhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakeLRKL 80
Cdd:PRK09544    4 LVSLENVSVSF---GQRR-VLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVI--------------KRNG 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLfnsrtvfgNIAYPL---RLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:PRK09544   66 KLRIGYVPQKLYL--------DTTLPLtvnRFLRLRPGTKKEDILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLN 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVV 204
Cdd:PRK09544  138 RPQLLVLDEPTQGVDVNGQVALYDLIDQLRRELDCAVLMVSHDLHLV 184
NIL pfam09383
NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in ...
262-326 2.79e-20

NIL domain; This domain is found at the C-terminus of ABC transporter proteins involved in D-methionine transport as well as a number of ferredoxin-like proteins. This domain is likely to act as a substrate binding domain. The domain has been named after a conserved sequence in some members of the family.


Pssm-ID: 462781 [Multi-domain]  Cd Length: 73  Bit Score: 83.27  E-value: 2.79e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 262 QIYRLTFTGEETGQPVLSYIAKNYNVDVNVLYGNIIELQNVLFGNLLVELQGEQKEIQKALQHLR 326
Cdd:pfam09383   1 RLVRLTFPGESADEPVISRLAREFGVDVNILYGNIEEIQGTPFGSLILELPGDPEQIEAALAYLR 65
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
2-221 3.43e-20

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 91.19  E-value: 3.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKLR 81
Cdd:PRK10522  323 LELRNVTFAYQDNG---FSVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVT---AEQPEDYR 396
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSFNLFNsrtvfgniayplRLAKlPKNEIK--ERVNELLKFVGLEDKANYYPE-----QLSGGQKQRVGIARA 154
Cdd:PRK10522  397 KLFSAVFTDFHLFD------------QLLG-PEGKPAnpALVEKWLERLKMAHKLELEDGrisnlKLSKGQKKRLALLLA 463
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 155 LATSPDILICDEATSALDP----ETTTEILNLLkkvnREYNLTILLITHEMHVVkEICHRVAVMEKGKVIE 221
Cdd:PRK10522  464 LAEERDILLLDEWAADQDPhfrrEFYQVLLPLL----QEMGKTIFAISHDDHYF-IHADRLLEMRNGQLSE 529
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
1-221 3.69e-20

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 90.89  E-value: 3.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditslsAKELrkl 80
Cdd:COG0488   315 VLELEGLSKSY--GDKTL--LDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL---------GETV--- 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rqRIGMIFQSFNLFN-SRTVFGNIAyplRLAklpKNEIKERVNELLK---FVGleDKANYYPEQLSGGQKQRVGIARALA 156
Cdd:COG0488   379 --KIGYFDQHQEELDpDKTVLDELR---DGA---PGGTEQEVRGYLGrflFSG--DDAFKPVGVLSGGEKARLALAKLLL 448
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 157 TSPDILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:COG0488   449 SPPNVLLLDEPTNHLDIETLEALEEALD----DFPGTVLLVSHDRYFLDRVATRILEFEDGGVRE 509
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
2-218 1.12e-19

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: 85.60  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHAV-EDVTLSVEKGEIFGIIGFSGAGKSTLLR--LVNMleRPTAGTISIDDkditslsakelr 78
Cdd:cd03250     1 ISVEDASFTWDSGEQETSFTlKDINLEVPKGELVAIVGPVGSGKSSLLSalLGEL--EKLSGSVSVPG------------ 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  79 klrqRIGMIFQSFNLFNsRTVFGNIayplrLAKLPKNEikERVNELLKFVGLEDKANYYPEQ-----------LSGGQKQ 147
Cdd:cd03250    67 ----SIAYVSQEPWIQN-GTIRENI-----LFGKPFDE--ERYEKVIKACALEPDLEILPDGdlteigekginLSGGQKQ 134
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEI-----LNLLKKvNReynlTILLITHEMHVVKEiCHRVAVMEKGK 218
Cdd:cd03250   135 RISLARAVYSDADIYLLDDPLSAVDAHVGRHIfenciLGLLLN-NK----TRILVTHQLQLLPH-ADQIVVLDNGR 204
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
19-245 2.76e-19

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 88.57  E-value: 2.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  19 HAVEDVTLSVEKGEIFGIIGFSGAGKSTLL-----RLVNMLERptAGTISIDDKDItslsakELRKLRQRIGMIFQSFNL 93
Cdd:TIGR00955  39 HLLKNVSGVAKPGELLAVMGSSGAGKTTLMnalafRSPKGVKG--SGSVLLNGMPI------DAKEMRAISAYVQQDDLF 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSRTVFGNIAYPLRL---AKLPKNEIKERVNELLKFVGLEDKANY---YPEQ---LSGGQKQRVGIARALATSPDILIC 164
Cdd:TIGR00955 111 IPTLTVREHLMFQAHLrmpRRVTKKEKRERVDEVLQALGLRKCANTrigVPGRvkgLSGGERKRLAFASELLTDPPLLFC 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 165 DEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGK---LFDVFTQ-----PKTKT 236
Cdd:TIGR00955 191 DEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQPSSELFELFDKIILMAEGRVAYLGSpdqAVPFFSDlghpcPENYN 270

                  ....*....
gi 2050094043 237 TQNFVRSVI 245
Cdd:TIGR00955 271 PADFYVQVL 279
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
24-230 3.08e-19

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 85.28  E-value: 3.08e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  24 VTLSVEKGEIFGIIGFSGAGKSTLL-RLVNMLerPTAGTISIDDKDITSLSAKELRKLRqriGMIFQ----SFNLfnsrT 98
Cdd:COG4138    15 ISAQVNAGELIHLIGPNGAGKSTLLaRMAGLL--PGQGEILLNGRPLSDWSAAELARHR---AYLSQqqspPFAM----P 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  99 VFgniAYpLRL---AKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARAL-----ATSPD--ILICDEAT 168
Cdd:COG4138    86 VF---QY-LALhqpAGASSEAVEQLLAQLAEALGLEDKLSRPLTQLSGGEWQRVRLAAVLlqvwpTINPEgqLLLLDEPM 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 169 SALDPETTTEILNLLKKVnREYNLTILLITHEM-HVVKEiCHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:COG4138   162 NSLDVAQQAALDRLLREL-CQQGITVVMSSHDLnHTLRH-ADRVWLLKQGKLVASGETAEVMT 222
PLN03130 PLN03130
ABC transporter C family member; Provisional
24-221 4.93e-19

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 88.26  E-value: 4.93e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   24 VTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakeLRKLRQRIGMIFQSFNLFnSRTVFGNI 103
Cdd:PLN03130  1258 LSFEISPSEKVGIVGRTGAGKSSMLNALFRIVELERGRILIDGCDISKFG---LMDLRKVLGIIPQAPVLF-SGTVRFNL 1333
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  104 AyplrlaklPKNEIK--------ERVNelLKFV------GLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PLN03130  1334 D--------PFNEHNdadlweslERAH--LKDVirrnslGLDAEVSEAGENFSVGQRQLLSLARALLRRSKILVLDEATA 1403
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2050094043  170 ALDPETTTeilnLLKKVNRE--YNLTILLITHEMHVVKEiCHRVAVMEKGKVIE 221
Cdd:PLN03130  1404 AVDVRTDA----LIQKTIREefKSCTMLIIAHRLNTIID-CDRILVLDAGRVVE 1452
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
13-231 9.20e-19

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 86.87  E-value: 9.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  13 SGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditslsakelrklRQRIGMIFQSFN 92
Cdd:PRK13545   32 KDGEYHYALNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDI----------------KGSAALIAISSG 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  93 LFNSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALD 172
Cdd:PRK13545   96 LNGQLTGIENIELKGLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGD 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 173 PETTTEIlnlLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13545  176 QTFTKKC---LDKMNefKEQGKTIFFISHSLSQVKSFCTKALWLHYGQVKEYGDIKEVVDH 233
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
15-231 2.59e-18

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 83.33  E-value: 2.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrklrqrIGMIFQSFNLF 94
Cdd:PRK13546   34 NKTFFALDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNGE----------------VSVIAISAGLS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:PRK13546   98 GQLTGIENIEFKMLCMGFKRKEIKAMTPKIIEFSELGEFIYQPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQT 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 175 TTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK13546  178 FAQKCLDKIYEF-KEQNKTIFFVSHNLGQVRQFCTKIAWIEGGKLKDYGELDDVLPK 233
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
17-173 4.55e-18

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 85.18  E-value: 4.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslSAKELRKLRQRIGMIFQSF--NLF 94
Cdd:NF033858   13 KTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMA--DARHRRAVCPRIAYMPQGLgkNLY 90
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:NF033858   91 PTLSVFENLDFFGRLFGQDAAERRRRIDELLRATGLAPFADRPAGKLSGGMKQKLGLCCALIHDPDLLILDEPTTGVDP 169
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
1-220 6.46e-18

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 84.49  E-value: 6.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDDKDITSLSAKEL 77
Cdd:TIGR02633   1 LLEMKGIVKTFGG----VKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGV-YPHGtwdGEIYWSGSPLKASNIRDT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RklRQRIGMIFQSFNLFNSRTVFGNI----AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIA 152
Cdd:TIGR02633  76 E--RAGIVIIHQELTLVPELSVAENIflgnEITLPGGRMAYNAMYLRAKNLLRELQLDADNVTRPvGDYGGGQQQLVEIA 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 153 RALATSPDILICDEATSALDPETTTEILNLLKKVNReYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:TIGR02633 154 KALNKQARLLILDEPSSSLTEKETEILLDIIRDLKA-HGVACVYISHKLNEVKAVCDTICVIRDGQHV 220
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
2-231 7.08e-18

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: 85.00  E-value: 7.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL-LRLVNMLErPTAGTISIDDKDITSLSakeLRKL 80
Cdd:TIGR00957 1285 VEFRNYCLRYREDLDLV--LRHINVTIHGGEKVGIVGRTGAGKSSLtLGLFRINE-SAEGEIIIDGLNIAKIG---LHDL 1358
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   81 RQRIGMIFQSFNLFNSRtvfgniaypLRLAKLPKNEIKER-------VNELLKFV-GLEDKANYY----PEQLSGGQKQR 148
Cdd:TIGR00957 1359 RFKITIIPQDPVLFSGS---------LRMNLDPFSQYSDEevwwaleLAHLKTFVsALPDKLDHEcaegGENLSVGQRQL 1429
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  149 VGIARALATSPDILICDEATSALDPETTteilNLLKKVNREY--NLTILLITHEMHVVKEIChRVAVMEKGKVIEEGKLF 226
Cdd:TIGR00957 1430 VCLARALLRKTKILVLDEATAAVDLETD----NLIQSTIRTQfeDCTVLTIAHRLNTIMDYT-RVIVLDKGEVAEFGAPS 1504

                   ....*
gi 2050094043  227 DVFTQ 231
Cdd:TIGR00957 1505 NLLQQ 1509
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
18-222 8.92e-18

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 83.90  E-value: 8.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKlrQRIGMIFQSFNLFNSR 97
Cdd:PRK10762   17 VKALSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEVTFNGPKSSQE--AGIGIIHQELNLIPQL 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 TVFGNI----AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALdp 173
Cdd:PRK10762   95 TIAENIflgrEFVNRFGRIDWKKMYAEADKLLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDEPTDAL-- 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 174 eTTTEILNLLKKVN--REYNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK10762  173 -TDTETESLFRVIRelKSQGRGIVYISHRLKEIFEICDDVTVFRDGQFIAE 222
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
24-232 1.15e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 81.13  E-value: 1.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  24 VTLSVEKGEIFGIIGFSGAGKSTLL-RLVNMLerPTAGTISIDDKDITSLSAKELRklRQRIGMIFQSFNLFNSrTVFGN 102
Cdd:PRK03695   15 LSAEVRAGEILHLVGPNGAGKSTLLaRMAGLL--PGSGSIQFAGQPLEAWSAAELA--RHRAYLSQQQTPPFAM-PVFQY 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 103 IAypLRL-AKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARA-LATSPDI------LICDEATSALDPE 174
Cdd:PRK03695   90 LT--LHQpDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGEWQRVRLAAVvLQVWPDInpagqlLLLDEPMNSLDVA 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 175 TTTEILNLLKKVNREyNLTILLITHEM-HVVKEiCHRVAVMEKGKVIEEGKLFDVFTQP 232
Cdd:PRK03695  168 QQAALDRLLSELCQQ-GIAVVMSSHDLnHTLRH-ADRVWLLKQGKLLASGRRDEVLTPE 224
PLN03232 PLN03232
ABC transporter C family member; Provisional
1-277 1.19e-17

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 84.26  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    1 MISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKELRKL 80
Cdd:PLN03232  1234 SIKFEDVHLRYRPGLPPV--LHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDVAKFGLTDLRRV 1311
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   81 rqrIGMIFQSFNLFnSRTVFGNIAyPLR-------LAKLPKNEIKERVNEllKFVGLEDKANYYPEQLSGGQKQRVGIAR 153
Cdd:PLN03232  1312 ---LSIIPQSPVLF-SGTVRFNID-PFSehndadlWEALERAHIKDVIDR--NPFGLDAEVSEGGENFSVGQRQLLSLAR 1384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  154 ALATSPDILICDEATSALDPETTTeilnLLKKVNRE--YNLTILLITHEMHVVKEiCHRVAVMEKGKVIEegklFDVFTQ 231
Cdd:PLN03232  1385 ALLRRSKILVLDEATASVDVRTDS----LIQRTIREefKSCTMLVIAHRLNTIID-CDKILVLSSGQVLE----YDSPQE 1455
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 2050094043  232 PKTKTTQNFVRsVINDHLPEsvlakiqNGGQIYRLTFTGEETGQPV 277
Cdd:PLN03232  1456 LLSRDTSAFFR-MVHSTGPA-------NAQYLSNLVFERRENGMSL 1493
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
6-220 1.81e-17

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 82.85  E-value: 1.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYESggqsVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIG 85
Cdd:PRK10982    3 NISKSFPG----VKALDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKEIDFKSSKE--ALENGIS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  86 MIFQSFNLFNSRTVFGNI---AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDIL 162
Cdd:PRK10982   77 MVHQELNLVLQRSVMDNMwlgRYPTKGMFVDQDKMYRDTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIV 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:PRK10982  157 IMDEPTSSLTEKEVNHLFTIIRKL-KERGCGIVYISHKMEEIFQLCDEITILRDGQWI 213
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
20-174 2.37e-17

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: 78.94  E-value: 2.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakELRKLRQR-IGMIFQSFNLFNSRT 98
Cdd:TIGR01189  15 LFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLA-----EQRDEPHEnILYLGHLPGLKPELS 89
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043  99 VFGNIAYPLRLAKLPKNEIkervNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:TIGR01189  90 ALENLHFWAAIHGGAQRTI----EDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDEPTTALDKA 161
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
22-199 2.38e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 79.15  E-value: 2.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakELRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:PRK13539   19 SGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDI------DDPDVAEACHYLGHRNAMKPALTVAE 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAYPLRLaklpKNEIKERVNELLKFVGLED----KANYypeqLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK13539   93 NLEFWAAF----LGGEELDIAAALEAVGLAPlahlPFGY----LSAGQKRRVALARLLVSNRPIWILDEPTAALDAAAVA 164
                         170       180
                  ....*....|....*....|..
gi 2050094043 178 EILNLLkKVNREYNLTILLITH 199
Cdd:PRK13539  165 LFAELI-RAHLAQGGIVIAATH 185
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
2-205 3.00e-17

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 83.15  E-value: 3.00e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    2 ISFNNISKVYESGgQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDitSLSAKELRKLR 81
Cdd:PTZ00265   383 IQFKNVRFHYDTR-KDVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIINDSH--NLKDINLKWWR 459
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   82 QRIGMIFQSFNLFnSRTVFGNIAYPLRLAK---LPKNEIKER------------------------------VNELL--- 125
Cdd:PTZ00265   460 SKIGVVSQDPLLF-SNSIKNNIKYSLYSLKdleALSNYYNEDgndsqenknkrnscrakcagdlndmsnttdSNELIemr 538
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  126 ---------------KFVGLEDKANYYPE-----------QLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEI 179
Cdd:PTZ00265   539 knyqtikdsevvdvsKKVLIHDFVSALPDkyetlvgsnasKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLV 618
                          250       260
                   ....*....|....*....|....*.
gi 2050094043  180 LNLLKKVNREYNLTILLITHEMHVVK 205
Cdd:PTZ00265   619 QKTINNLKGNENRITIIIAHRLSTIR 644
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
24-223 3.58e-17

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 82.20  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  24 VTLSVEKGEIFGIIGFSGAGKSTLLrlvNMLE--RPTAGTISIDDKDITSLsakELRKLRQRIGMIFQSFNLFNSrTVFG 101
Cdd:PRK11174  369 LNFTLPAGQRIALVGPSGAGKTSLL---NALLgfLPYQGSLKINGIELREL---DPESWRKHLSWVGQNPQLPHG-TLRD 441
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAyplrLAKLPKNEikERVNELLK------FVGLEDKANYYP--EQ---LSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK11174  442 NVL----LGNPDASD--EQLQQALEnawvseFLPLLPQGLDTPigDQaagLSVGQAQRLALARALLQPCQLLLLDEPTAS 515
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2050094043 171 LDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PRK11174  516 LDAHSEQLVMQALNAASR--RQTTLMVTHQLEDLAQ-WDQIWVMQDGQIVQQG 565
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
23-219 3.73e-17

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 82.02  E-value: 3.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKElrklRQRIGMIF-----QSFNLF--- 94
Cdd:PRK15439  281 NISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQ----RLARGLVYlpedrQSSGLYlda 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 -----NSRTVFGNIAYPLRLAKlpKNEIKERVNELL--KFVGLEDKAnyypEQLSGGQKQRVGIARALATSPDILICDEA 167
Cdd:PRK15439  357 plawnVCALTHNRRGFWIKPAR--ENAVLERYRRALniKFNHAEQAA----RTLSGGNQQKVLIAKCLEASPQLLIVDEP 430
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 168 TSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK15439  431 TRGVDVSARNDIYQLIRSIAAQ-NVAVLFISSDLEEIEQMADRVLVMHQGEI 481
GguA NF040905
sugar ABC transporter ATP-binding protein;
18-221 5.68e-17

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 81.37  E-value: 5.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLeRPTA---GTISIDD-----KDItslSAKElrklRQRIGMIFQ 89
Cdd:NF040905   14 VKALDDVNLSVREGEIHALCGENGAGKSTLMKVLSGV-YPHGsyeGEILFDGevcrfKDI---RDSE----ALGIVIIHQ 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  90 SF----------NLF--NSRTVFGNIAYplrlaklpkNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:NF040905   86 ELalipylsiaeNIFlgNERAKRGVIDW---------NETNRRARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSK 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:NF040905  157 DVKLLILDEPTAALNEEDSAALLDLLLEL-KAQGITSIIISHKLNEIRRVADSITVLRDGRTIE 219
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
2-221 7.19e-17

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: 81.38  E-value: 7.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYES-GGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsAKELRKL 80
Cdd:COG4615   328 LELRGVTYRYPGeDGDEGFTLGPIDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQPVT---ADNREAY 404
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNsrtvfgniayplRLAKLPKNEIKERVNELLKFVGLEDKANYypE-------QLSGGQKQRVGIAR 153
Cdd:COG4615   405 RQLFSAVFSDFHLFD------------RLLGLDGEADPARARELLERLELDHKVSV--EdgrfsttDLSQGQRKRLALLV 470
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 154 ALATSPDILICDEATSALDPET----TTEILNLLKKVNReynlTILLITHE---MHVvkeiCHRVAVMEKGKVIE 221
Cdd:COG4615   471 ALLEDRPILVFDEWAADQDPEFrrvfYTELLPELKARGK----TVIAISHDdryFDL----ADRVLKMDYGKLVE 537
hmuV PRK13547
heme ABC transporter ATP-binding protein;
21-230 1.21e-16

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 78.72  E-value: 1.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERPTA-------GTISIDDKDITSLSAKELRKLRQRIGMIFQSFN 92
Cdd:PRK13547   17 LRDLSLRIEPGRVTALLGRNGAGKSTLLKaLAGDLTGGGAprgarvtGDVTLNGEPLAAIDAPRLARLRAVLPQAAQPAF 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  93 LFNSRTVFGNIAYP-LRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALA---------TSPDIL 162
Cdd:PRK13547   97 AFSAREIVLLGRYPhARRAGALTHRDGEIAWQALALAGATALVGRDVTTLSGGELARVQFARVLAqlwpphdaaQPPRYL 176
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 163 ICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFT 230
Cdd:PRK13547  177 LLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLAIVHDPNLAARHADRIAMLADGAIVAHGAPADVLT 244
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
18-238 1.75e-16

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 79.39  E-value: 1.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  18 VHAVEDVTLSVEKGEIFGIIGFSGAGKSTLlRLVNMLERPTAGTisiDDKDITSLSAKElRKLRQRIG----MIFQSFNL 93
Cdd:NF000106   26 VKAVDGVDLDVREGTVLGVLGP*GAA**RG-ALPAHV*GPDAGR---RPWRF*TWCANR-RALRRTIG*hrpVR*GRRES 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  94 FNSRTvfgNIAYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:NF000106  101 FSGRE---NLYMIGR*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPAVLYLDEPTTGLDP 177
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 174 ETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQPKTKTTQ 238
Cdd:NF000106  178 RTRNEVWDEVRSMVRD-GATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVGGRTLQ 241
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
2-219 6.12e-16

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: 76.82  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL----LRLVNmlerpTAGTISIDDKDITSLSakeL 77
Cdd:cd03289     3 MTVKDLTAKYTEGGNAV--LENISFSISPGQRVGLLGRTGSGKSTLlsafLRLLN-----TEGDIQIDGVSWNSVP---L 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKLRQRIGMIFQSFNLFNSrtvfgniayPLRLAKLPKNEIKERvnELLKF---VGLEDKANYYPEQL-----------SG 143
Cdd:cd03289    73 QKWRKAFGVIPQKVFIFSG---------TFRKNLDPYGKWSDE--EIWKVaeeVGLKSVIEQFPGQLdfvlvdggcvlSH 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKV 219
Cdd:cd03289   142 GHKQLMCLARSVLSKAKILLLDEPSAHLDPITYQVIRKTLKQAFA--DCTVILSEHRIEAMLE-CQRFLVIEENKV 214
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
2-175 7.60e-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: 78.44  E-value: 7.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrklr 81
Cdd:TIGR03719 323 IEAENLTKAF--GDKLL--IDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTIEIGET-------------- 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 QRIGMIFQSF-NLFNSRTVFGNIAYPLRLAKLPKNEIKERV---------NELLKFVGledkanyypeQLSGGQKQRVGI 151
Cdd:TIGR03719 385 VKLAYVDQSRdALDPNKTVWEEISGGLDIIKLGKREIPSRAyvgrfnfkgSDQQKKVG----------QLSGGERNRVHL 454
                         170       180
                  ....*....|....*....|....
gi 2050094043 152 ARALATSPDILICDEATSALDPET 175
Cdd:TIGR03719 455 AKTLKSGGNVLLLDEPTNDLDVET 478
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
21-242 9.94e-16

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 77.90  E-value: 9.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakELRKLRQRIGMIFQS---FNLFNSR 97
Cdd:PRK09700  279 VRDISFSVCRGEILGFAGLVGSGRTELMNCLFGVDKRAGGEIRLNGKDISPRS--PLDAVKKGMAYITESrrdNGFFPNF 356
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 TVFGNIAYP--LRLAKL--------PKNEIK--ERVNELL--KFVGLEDKANyypeQLSGGQKQRVGIARALATSPDILI 163
Cdd:PRK09700  357 SIAQNMAISrsLKDGGYkgamglfhEVDEQRtaENQRELLalKCHSVNQNIT----ELSGGNQQKVLISKWLCCCPEVII 432
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMekgkviEEGKLFDVFTQPKTKTTQNFVR 242
Cdd:PRK09700  433 FDEPTRGIDVGAKAEIYKVMRQLADD-GKVILMVSSELPEIITVCDRIAVF------CEGRLTQILTNRDDMSEEEIMA 504
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
5-219 1.11e-15

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: 78.41  E-value: 1.11e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    5 NNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLL----RLVNmlerpTAGTISIDDKDITSLSakeLRKL 80
Cdd:TIGR01271 1221 QGLTAKYTEAGRAV--LQDLSFSVEGGQRVGLLGRTGSGKSTLLsallRLLS-----TEGEIQIDGVSWNSVT---LQTW 1290
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   81 RQRIGMIFQSFNLFnSRTVFGNIAyplRLAKLPKNEIKERVNEllkfVGLEDKANYYPEQL-----------SGGQKQRV 149
Cdd:TIGR01271 1291 RKAFGVIPQKVFIF-SGTFRKNLD---PYEQWSDEEIWKVAEE----VGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLM 1362
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  150 GIARALATSPDILICDEATSALDPETTTEILNLLKKVNReyNLTILLITHEMHVVKEiCHRVAVMEKGKV 219
Cdd:TIGR01271 1363 CLARSILSKAKILLLDEPSAHLDPVTLQIIRKTLKQSFS--NCTVILSEHRVEALLE-CQQFLVIEGSSV 1429
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
21-219 1.57e-15

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 77.35  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKE--------LRKLRQRIGMIF---- 88
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQDglangivyISEDRKRDGLVLgmsv 347
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 -QSFNLfNSRTVFGNIAYPLRLAklpkneikERVNELLKFVGLEDKANYYPEQ----LSGGQKQRVGIARALATSPDILI 163
Cdd:PRK10762  348 kENMSL-TALRYFSRAGGSLKHA--------DEQQAVSDFIRLFNIKTPSMEQaiglLSGGNQQKVAIARGLMTRPKVLI 418
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 164 CDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10762  419 LDEPTRGVDVGAKKEIYQLINQFKAE-GLSIILVSSEMPEVLGMSDRILVMHEGRI 473
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
2-199 2.10e-15

ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding cassette transporter (Pat) is involved in the import of very long-chain fatty acids (VLCFA) into the peroxisome. The peroxisomal membrane forms a permeability barrier for a wide variety of metabolites required for and formed during fatty acid beta-oxidation. To communicate with the cytoplasm and mitochondria, peroxisomes need dedicated proteins to transport such hydrophilic molecules across their membranes. X-linked adrenoleukodystrophy (X-ALD) is caused by mutations in the ALD gene, which encodes ALDP (adrenoleukodystrophy protein ), a peroxisomal integral membrane protein that is a member of the ATP-binding cassette (ABC) transporter protein family. The disease is characterized by a striking and unpredictable variation in phenotypic expression. Phenotypes include the rapidly progressive childhood cerebral form (CCALD), the milder adult form, adrenomyeloneuropathy (AMN), and variants without neurologic involvement (i.e. asymptomatic).


Pssm-ID: 213190 [Multi-domain]  Cd Length: 166  Bit Score: 72.96  E-value: 2.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISkVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISI-DDKDITSLSakelrkl 80
Cdd:cd03223     1 IELENLS-LATPDGRVL--LKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRIGMpEGEDLLFLP------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rQRIGMIFQSFnlfnsRTVfgnIAYPLRlaklpkneikervnellkfvgledkanyypEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03223    71 -QRPYLPLGTL-----REQ---LIYPWD------------------------------DVLSGGEQQRLAFARLLLHKPK 111
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITH 199
Cdd:cd03223   112 FVFLDEATSALDEESEDRLYQLLK----ELGITVISVGH 146
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
22-222 2.93e-15

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 76.49  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakeLRKLRQRI--GMIF-----QSFNLF 94
Cdd:PRK11288  270 EPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPID------IRSPRDAIraGIMLcpedrKAEGII 343
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 NSRTVFGNIAYPLRLAKLPK----NEIKERVNELLKFVGLEDKANyYPEQ----LSGGQKQRVGIARALATSPDILICDE 166
Cdd:PRK11288  344 PVHSVADNINISARRHHLRAgcliNNRWEAENADRFIRSLNIKTP-SREQlimnLSGGNQQKAILGRWLSEDMKVILLDE 422
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 167 ATSALDPETTTEILNLLkkvnreYNL-----TILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:PRK11288  423 PTRGIDVGAKHEIYNVI------YELaaqgvAVLFVSSDLPEVLGVADRIVVMREGRIAGE 477
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
23-215 9.60e-15

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: 72.83  E-value: 9.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKG-----EIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDIT----SLSAKE---LRKLRQRIGMIFQS 90
Cdd:cd03237    12 EFTLEVEGGsisesEVIGILGPNGIGKTTFIKMLAGVLKPDEGDIEIELDTVSykpqYIKADYegtVRDLLSSITKDFYT 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  91 FNLFNSrtvfgNIAYPLRLAKLPKNEIKErvnellkfvgledkanyypeqLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:cd03237    92 HPYFKT-----EIAKPLQIEQILDREVPE---------------------LSGGELQRVAIAACLSKDADIYLLDEPSAY 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2050094043 171 LDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVME 215
Cdd:cd03237   146 LDVEQRLMASKVIRRFAENNEKTAFVVEHDIIMIDYLADRLIVFE 190
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
3-200 1.03e-14

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


Pssm-ID: 274744 [Multi-domain]  Cd Length: 552  Bit Score: 74.97  E-value: 1.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   3 SFNNISKVYESGGqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVnmlerptAGTisidDKDItslSAKELRKLRQ 82
Cdd:TIGR03719   6 TMNRVSKVVPPKK---EILKDISLSFFPGAKIGVLGLNGAGKSTLLRIM-------AGV----DKDF---NGEARPQPGI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIGMIFQSFNLFNSRTVFGNIAYPLR-----LAKLpkNEIKER-------VNELLKFVG-LEDK---------------- 133
Cdd:TIGR03719  69 KVGYLPQEPQLDPTKTVRENVEEGVAeikdaLDRF--NEISAKyaepdadFDKLAAEQAeLQEIidaadawdldsqleia 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 134 --ANYYP------EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHE 200
Cdd:TIGR03719 147 mdALRCPpwdadvTKLSGGERRRVALCRLLLSKPDMLLLDEPTNHLDAESVAWLERHLQ----EYPGTVVAVTHD 217
PTZ00243 PTZ00243
ABC transporter; Provisional
24-223 1.62e-14

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 74.82  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   24 VTLSVEKGEIFGIIGFSGAGKST-LLRLVNMLErPTAGTISIDDKDITSLSakeLRKLRQRIGMIFQSFNLFNSrTVFGN 102
Cdd:PTZ00243  1329 VSFRIAPREKVGIVGRTGSGKSTlLLTFMRMVE-VCGGEIRVNGREIGAYG---LRELRRQFSMIPQDPVLFDG-TVRQN 1403
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  103 I-----AYPLRL-AKLPKNEIKERV---NELLKFVGLEDKANYypeqlSGGQKQRVGIARALAT--SPDILIcDEATSAL 171
Cdd:PTZ00243  1404 VdpfleASSAEVwAALELVGLRERVaseSEGIDSRVLEGGSNY-----SVGQRQLMCMARALLKkgSGFILM-DEATANI 1477
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2050094043  172 DPETTTEILNLLKKVNREYnlTILLITHEMHVVKEiCHRVAVMEKGKVIEEG 223
Cdd:PTZ00243  1478 DPALDRQIQATVMSAFSAY--TVITIAHRLHTVAQ-YDKIIVMDHGAVAEMG 1526
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
59-205 2.86e-14

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 73.91  E-value: 2.86e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   59 AGTISIDDKDITSLSAKELRKLrqrIGMIFQSFNLFNsRTVFGNIAYPlrlaklPKNEIKERVNELLKFVGLEDKANYYP 138
Cdd:PTZ00265  1276 SGKILLDGVDICDYNLKDLRNL---FSIVSQEPMLFN-MSIYENIKFG------KEDATREDVKRACKFAAIDEFIESLP 1345
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043  139 EQ-----------LSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVK 205
Cdd:PTZ00265  1346 NKydtnvgpygksLSGGQKQRIAIARALLREPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADKTIITIAHRIASIK 1423
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
2-243 2.94e-14

ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The sulfonylurea receptor SUR is an ATP binding cassette (ABC) protein of the ABCC/MRP family. Unlike other ABC proteins, it has no intrinsic transport function, neither active nor passive, but associates with the potassium channel proteins Kir6.1 or Kir6.2 to form the ATP-sensitive potassium (K(ATP)) channel. Within the channel complex, SUR serves as a regulatory subunit that fine-tunes the gating of Kir6.x in response to alterations in cellular metabolism. It constitutes a major pharmaceutical target as it binds numerous drugs, K(ATP) channel openers and blockers, capable of up- or down-regulating channel activity.


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 71.48  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTL----LRLVNMLErptaGTISIDDKDITSLSakeL 77
Cdd:cd03288    20 IKIHDLCVRYENNLKPV--LKHVKAYIKPGQKVGICGRTGSGKSSLslafFRMVDIFD----GKIVIDGIDISKLP---L 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKLRQRIGMIFQSFNLFNSRTVFG----------NIAYPLRLAKLpKNEIKERVNellkfvGLEDKANYYPEQLSGGQKQ 147
Cdd:cd03288    91 HTLRSRLSIILQDPILFSGSIRFNldpeckctddRLWEALEIAQL-KNMVKSLPG------GLDAVVTEGGENFSVGQRQ 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTteilNLLKKV--NREYNLTILLITHEMHVVKEiCHRVAVMEKGKVIEEGKL 225
Cdd:cd03288   164 LFCLARAFVRKSSILIMDEATASIDMATE----NILQKVvmTAFADRTVVTIAHRVSTILD-ADLVLVLSRGILVECDTP 238
                         250
                  ....*....|....*...
gi 2050094043 226 FDVFTQpKTKTTQNFVRS 243
Cdd:cd03288   239 ENLLAQ-EDGVFASLVRT 255
ycf16 CHL00131
sulfate ABC transporter protein; Validated
21-223 1.59e-13

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 69.29  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV------NMLErptaGTISIDDKDITSLSAKElrklRQRIGmIFQSFN-- 92
Cdd:CHL00131   23 LKGLNLSINKGEIHAIMGPNGSGKSTLSKVIaghpayKILE----GDILFKGESILDLEPEE----RAHLG-IFLAFQyp 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  93 -----LFNSRtvFGNIAYPLRLAKLPKNEIK-----ERVNELLKFVGLEDK--ANYYPEQLSGGQKQRVGIARALATSPD 160
Cdd:CHL00131   94 ieipgVSNAD--FLRLAYNSKRKFQGLPELDpleflEIINEKLKLVGMDPSflSRNVNEGFSGGEKKRNEILQMALLDSE 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKEIC-HRVAVMEKGKVIEEG 223
Cdd:CHL00131  172 LAILDETDSGLDIDALKIIAEGINKLMTSEN-SIILITHYQRLLDYIKpDYVHVMQNGKIIKTG 234
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
21-219 3.73e-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: 69.85  E-value: 3.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERPTAGTISIDDKDITSLSAkeLRKLRQRIGMIFQSFNLFNSRTV 99
Cdd:TIGR02633 276 VDDVSFSLRRGEILGVAGLVGAGRTELVQaLFGAYPGKFEGNVFINGKPVDIRNP--AQAIRAGIAMVPEDRKRHGIVPI 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 100 FGnIAYPLRLAKLPKNEIKERVNEL---------LKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:TIGR02633 354 LG-VGKNITLSVLKSFCFKMRIDAAaelqiigsaIQRLKVKTASPFLPiGRLSGGNQQKAVLAKMLLTNPRVLILDEPTR 432
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2050094043 170 ALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:TIGR02633 433 GVDVGAKYEIYKLINQLAQE-GVAIIVVSSELAEVLGLSDRVLVIGEGKL 481
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
2-224 4.51e-13

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 69.81  E-value: 4.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYEsggqsvhaveDVTLSVE-----KGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDK--------- 67
Cdd:COG1245   342 VEYPDLTKSYG----------GFSLEVEggeirEGEVLGIVGPNGIGKTTFAKILAGVLKPDEGEVDEDLKisykpqyis 411
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  68 DITSLSAKELrkLRQRIGMIFQSfNLFNSRtvfgnIAYPLRLAKLPKNEIKErvnellkfvgledkanyypeqLSGGQKQ 147
Cdd:COG1245   412 PDYDGTVEEF--LRSANTDDFGS-SYYKTE-----IIKPLGLEKLLDKNVKD---------------------LSGGELQ 462
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 148 RVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEkGKVIEEGK 224
Cdd:COG1245   463 RVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRFAENRGKTAMVVDHDIYLIDYISDRLMVFE-GEPGVHGH 538
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
2-175 7.09e-13

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 69.38  E-value: 7.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDkditslSAKelrklr 81
Cdd:PRK11819  325 IEAENLSKSF--GDRLL--IDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTIKIGE------TVK------ 388
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  82 qrIGMIFQSF-NLFNSRTVFGNIAYPLRLAKLPKNEIKERV---------NELLKFVGledkanyypeQLSGGQKQRVGI 151
Cdd:PRK11819  389 --LAYVDQSRdALDPNKTVWEEISGGLDIIKVGNREIPSRAyvgrfnfkgGDQQKKVG----------VLSGGERNRLHL 456
                         170       180
                  ....*....|....*....|....
gi 2050094043 152 ARALATSPDILICDEATSALDPET 175
Cdd:PRK11819  457 AKTLKQGGNVLLLDEPTNDLDVET 480
PLN03211 PLN03211
ABC transporter G-25; Provisional
24-227 7.69e-13

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 69.14  E-value: 7.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  24 VTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITslsakelRKLRQRIGMIFQSFNLFNSRTVFG 101
Cdd:PLN03211   87 VTGMASPGEILAVLGPSGSGKSTLLNALagRIQGNNFTGTILANNRKPT-------KQILKRTGFVTQDDILYPHLTVRE 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAY------PLRLAKLPKNEIKERVNELLKFVGLEDK--ANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDP 173
Cdd:PLN03211  160 TLVFcsllrlPKSLTKQEKILVAESVISELGLTKCENTiiGNSFIRGISGGERKRVSIAHEMLINPSLLILDEPTSGLDA 239
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 174 ETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFD 227
Cdd:PLN03211  240 TAAYRLVLTLGSLAQKGKTIVTSMHQPSSRVYQMFDSVLVLSEGRCLFFGKGSD 293
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
2-220 3.92e-12

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: 64.59  E-value: 3.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLE---RPTaGTISIDDKDitslSAKEL 77
Cdd:cd03233     4 LSWRNISFTTGKGRSKIPILKDFSGVVKPGEMVLVLGRPGSGCSTLLKaLANRTEgnvSVE-GDIHYNGIP----YKEFA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 RKLRQRIGMIFQSFNLFNSRTVFgniayplrlaklpkneikervnELLKFVgLEDKANYYPEQLSGGQKQRVGIARALAT 157
Cdd:cd03233    79 EKYPGEIIYVSEEDVHFPTLTVR----------------------ETLDFA-LRCKGNEFVRGISGGERKRVSIAEALVS 135
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 158 SPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHvvKEICH---RVAVMEKGKVI 220
Cdd:cd03233   136 RASVLCWDNSTRGLDSSTALEILKCIRTMADVLKTTTFVSLYQAS--DEIYDlfdKVLVLYEGRQI 199
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
12-172 4.88e-12

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: 64.05  E-value: 4.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  12 ESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsAKELRKLRQRIGMIFQSF 91
Cdd:cd03231     9 ERDGRAL--FSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPL----DFQRDSIARGLLYLGHAP 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  92 NLFNSRTVFGNIAYPLRLAKlpkneiKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSAL 171
Cdd:cd03231    83 GIKTTLSVLENLRFWHADHS------DEQVEEALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDEPTTAL 156

                  .
gi 2050094043 172 D 172
Cdd:cd03231   157 D 157
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
2-200 5.95e-12

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 63.80  E-value: 5.95e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   2 ISFNNISKVYESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNmlERPTAGTISiddKDITsLSAKELRK-L 80
Cdd:cd03232     4 LTWKNLNYTVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLA--GRKTAGVIT---GEIL-INGRPLDKnF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 RQRIGMIFQSFNLFNSRTVfgniayplrlaklpkneikervNELLKFvgledKANYypEQLSGGQKQRVGIARALATSPD 160
Cdd:cd03232    78 QRSTGYVEQQDVHSPNLTV----------------------REALRF-----SALL--RGLSVEQRKRLTIGVELAAKPS 128
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2050094043 161 ILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHE 200
Cdd:cd03232   129 ILFLDEPTSGLDSQAAYNIVRFLKKLADS-GQAILCTIHQ 167
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
20-219 7.93e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 65.91  E-value: 7.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  20 AVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSAKE-------LRKLRQRIGMIFQSFN 92
Cdd:PRK10982  263 SIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKINNHNANEainhgfaLVTEERRSTGIYAYLD 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  93 L-FNSrtVFGNI-AYPLRLAKLPKNEIKERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:PRK10982  343 IgFNS--LISNIrNYKNKVGLLDNSRMKSDTQWVIDSMRVKTPGHRTQiGSLSGGNQQKVIIGRWLLTQPEILMLDEPTR 420
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2050094043 170 ALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK10982  421 GIDVGAKFEIYQLIAELAKK-DKGIIIISSEMPELLGITDRILVMSNGLV 469
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
1-215 2.73e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 64.44  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYEsggqsvhaveDVTLSVE-----KGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISID---------- 65
Cdd:PRK13409  340 LVEYPDLTKKLG----------DFSLEVEggeiyEGEVIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPElkisykpqyi 409
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  66 --DKDITslsakeLRKLRQRIGMIFQSfNLFNSrtvfgNIAYPLRLAKLPKNEIKErvnellkfvgledkanyypeqLSG 143
Cdd:PRK13409  410 kpDYDGT------VEDLLRSITDDLGS-SYYKS-----EIIKPLQLERLLDKNVKD---------------------LSG 456
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 144 GQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKVNREYNLTILLITHEMHVVKEICHRVAVME 215
Cdd:PRK13409  457 GELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVAKAIRRIAEEREATALVVDHDIYMIDYISDRLMVFE 528
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
3-199 8.34e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 62.83  E-value: 8.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   3 SFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLvnMlerptAGTisidDKDIT-----SLSAKel 77
Cdd:PRK11819    8 TMNRVSKVVPPKKQ---ILKDISLSFFPGAKIGVLGLNGAGKSTLLRI--M-----AGV----DKEFEgearpAPGIK-- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  78 rklrqrIGMIFQSFNLFNSRTVFGNIAYPLR--LAKLPK-NEIKER-------VNELLKFVG-LEDK---ANYY------ 137
Cdd:PRK11819   72 ------VGYLPQEPQLDPEKTVRENVEEGVAevKAALDRfNEIYAAyaepdadFDALAAEQGeLQEIidaADAWdldsql 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2050094043 138 ---------P------EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTteilNLLKKVNREYNLTILLITH 199
Cdd:PRK11819  146 eiamdalrcPpwdakvTKLSGGERRRVALCRLLLEKPDMLLLDEPTNHLDAESV----AWLEQFLHDYPGTVVAVTH 218
PLN03232 PLN03232
ABC transporter C family member; Provisional
23-229 1.09e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 63.07  E-value: 1.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLvnML-ERPTAGTISIDdkditslsakelrkLRQRIGMIFQSFNLFNSrTVFG 101
Cdd:PLN03232   635 DINLEIPVGSLVAIVGGTGEGKTSLISA--MLgELSHAETSSVV--------------IRGSVAYVPQVSWIFNA-TVRE 697
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  102 NIAYPLRLAKlpkneikERVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PLN03232   698 NILFGSDFES-------ERYWRAIDVTALQHDLDLLPGRdlteigergvnISGGQKQRVSMARAVYSNSDIYIFDDPLSA 770
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043  171 LDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEGKLFDVF 229
Cdd:PLN03232   771 LDAHVAHQVFDSCMKDELK-GKTRVLVTNQLHFLPLM-DRIILVSEGMIKEEGTFAELS 827
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
22-172 1.58e-10

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 59.82  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  22 EDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDItslsakelRKLRQRigmiFQSfNLF------- 94
Cdd:PRK13538   18 SGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPI--------RRQRDE----YHQ-DLLylghqpg 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 -NSR-TVFGNIAYPLRLAKLPKNeikERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALD 172
Cdd:PRK13538   85 iKTElTALENLRFYQRLHGPGDD---EALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWILDEPFTAID 161
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
28-185 2.00e-10

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 62.05  E-value: 2.00e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   28 VEKGEIFGIIGFSGAGKSTLLrlvNML-ERPTAGTISIDDKDItslSAKELRKLRQR-IGMIFQSFNLFNSRTVFGNIAY 105
Cdd:TIGR00956  786 VKPGTLTALMGASGAGKTTLL---NVLaERVTTGVITGGDRLV---NGRPLDSSFQRsIGYVQQQDLHLPTSTVRESLRF 859
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  106 PLRL---AKLPKNEIKERVNELLKFVGLEDKANYY----PEQLSGGQKQRVGIARALATSPDILI-CDEATSALDPETTT 177
Cdd:TIGR00956  860 SAYLrqpKSVSKSEKMEYVEEVIKLLEMESYADAVvgvpGEGLNVEQRKRLTIGVELVAKPKLLLfLDEPTSGLDSQTAW 939

                   ....*...
gi 2050094043  178 EILNLLKK 185
Cdd:TIGR00956  940 SICKLMRK 947
3a01203 TIGR00954
Peroxysomal Fatty Acyl CoA Transporter (FAT) Family protein; [Transport and binding proteins, ...
1-199 2.45e-10

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: 61.69  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYESGGQsvhAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKditslsakelrkl 80
Cdd:TIGR00954 451 GIKFENIPLVTPNGDV---LIESLSFEVPSGNNLLICGPNGCGKSSLFRILGELWPVYGGRLTKPAK------------- 514
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  81 rQRIGMIFQSfNLFNSRTVFGNIAYPLRLAKLPKNEIKERV-NELLKFVGLE---------DKANYYPEQLSGGQKQRVG 150
Cdd:TIGR00954 515 -GKLFYVPQR-PYMTLGTLRDQIIYPDSSEDMKRRGLSDKDlEQILDNVQLThilereggwSAVQDWMDVLSGGEKQRIA 592
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTEILNLLkkvnREYNLTILLITH 199
Cdd:TIGR00954 593 MARLFYHKPQFAILDECTSAVSVDVEGYMYRLC----REFGITLFSVSH 637
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
21-219 3.12e-10

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 61.10  E-value: 3.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLERPTAGTISIDDKDITSLSAKElrKLRQRIGMIFQSFNLFNSRTV 99
Cdd:PRK13549  278 VDDVSFSLRRGEILGIAGLVGAGRTELVQcLFGAYPGRWEGEIFIDGKPVKIRNPQQ--AIAQGIAMVPEDRKRDGIVPV 355
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 100 FGnIAYPLRLAKLPKNEIKERVNELLKFVGLED-------KANYyPEQ----LSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:PRK13549  356 MG-VGKNITLAALDRFTGGSRIDDAAELKTILEsiqrlkvKTAS-PELaiarLSGGNQQKAVLAKCLLLNPKILILDEPT 433
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 169 SALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PRK13549  434 RGIDVGAKYEIYKLINQLVQQ-GVAIIVISSELPEVLGLSDRVLVMHEGKL 483
PTZ00243 PTZ00243
ABC transporter; Provisional
23-219 3.57e-10

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 61.33  E-value: 3.57e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   23 DVTLSVEKGEIFGIIGFSGAGKSTLLRlvnmlerptagtisiddkdiTSLSAKELRKLR----QRIGMIFQSFNLFNSrT 98
Cdd:PTZ00243   678 DVSVSVPRGKLTVVLGATGSGKSTLLQ--------------------SLLSQFEISEGRvwaeRSIAYVPQQAWIMNA-T 736
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   99 VFGNIAY-----PLRLAKLPkneikeRVNELLKFV-----GLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:PTZ00243   737 VRGNILFfdeedAARLADAV------RVSQLEADLaqlggGLETEIGEKGVNLSGGQKARVSLARAVYANRDVYLLDDPL 810
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043  169 SALDP---ETTTE--ILNLLKKVNReynltiLLITHEMHVVKEICHRVAvMEKGKV 219
Cdd:PTZ00243   811 SALDAhvgERVVEecFLGALAGKTR------VLATHQVHVVPRADYVVA-LGDGRV 859
PLN03130 PLN03130
ABC transporter C family member; Provisional
2-223 6.65e-10

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 60.52  E-value: 6.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043    2 ISFNNISKVYESGGQSvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIddkditslsakelrkLR 81
Cdd:PLN03130   615 ISIKNGYFSWDSKAER-PTLSNINLDVPVGSLVAIVGSTGEGKTSLISAMLGELPPRSDASVV---------------IR 678
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   82 QRIGMIFQSFNLFNSrTVFGNIAY-----PLR-------------LAKLP---KNEIKER-VNellkfvgledkanyype 139
Cdd:PLN03130   679 GTVAYVPQVSWIFNA-TVRDNILFgspfdPERyeraidvtalqhdLDLLPggdLTEIGERgVN----------------- 740
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  140 qLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNllKKVNREY-NLTILLITHEMHVVKEIcHRVAVMEKGK 218
Cdd:PLN03130   741 -ISGGQKQRVSMARAVYSNSDVYIFDDPLSALDAHVGRQVFD--KCIKDELrGKTRVLVTNQLHFLSQV-DRIILVHEGM 816

                   ....*
gi 2050094043  219 VIEEG 223
Cdd:PLN03130   817 IKEEG 821
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
11-202 8.42e-10

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: 58.11  E-value: 8.42e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  11 YESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLrLVNMLERPT-AGTISIDDKDITSLSAKELRKL-RQRIGMIF 88
Cdd:cd03290     7 YFSWGSGLATLSNINIRIPTGQLTMIVGQVGCGKSSLL-LAILGEMQTlEGKVHWSNKNESEPSFEATRSRnRYSVAYAA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 QSFNLFNSrTVFGNIAYplrlaKLPKNeiKERVNELLKFVGLEDKANYYPE-----------QLSGGQKQRVGIARALAT 157
Cdd:cd03290    86 QKPWLLNA-TVEENITF-----GSPFN--KQRYKAVTDACSLQPDIDLLPFgdqteigergiNLSGGQRQRICVARALYQ 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2050094043 158 SPDILICDEATSALDPETTTE-----ILNLLKKVNReynlTILLITHEMH 202
Cdd:cd03290   158 NTNIVFLDDPFSALDIHLSDHlmqegILKFLQDDKR----TLVLVTHKLQ 203
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
30-206 1.50e-09

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 55.84  E-value: 1.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   30 KGEIFGIIGFSGAGKSTLLR-LVNMLERPTAGTISIDDKDITSLSAKELRKLRQRIGmifqsfnlfnsrtvfgniayplr 108
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARaLARELGPPGGGVIYIDGEDILEEVLDQLLLIIVGGK----------------------- 57
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  109 laklpkneikervnellkfvgledkanyyPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL-----NLL 183
Cdd:smart00382  58 -----------------------------KASGSGELRLRLALALARKLKPDVLILDEITSLLDAEQEALLLlleelRLL 108
                          170       180
                   ....*....|....*....|...
gi 2050094043  184 KKVNREYNLTILLITHEMHVVKE 206
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLGP 131
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
1-218 2.21e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 58.36  E-value: 2.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   1 MISFNNISKVYesGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLErPTAGTISIDDKDitslsakELRK 79
Cdd:PRK15064    1 MLSTANITMQF--GAKPL--FENISVKFGGGNRYGLIGANGCGKSTFMKiLGGDLE-PSAGNVSLDPNE-------RLGK 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRiGMIFQSFNLFNsrTV-FGNI-------------AYP-------LRLAKLpknEIK----------ERVNELLKFV 128
Cdd:PRK15064   69 LRQD-QFAFEEFTVLD--TViMGHTelwevkqerdriyALPemseedgMKVADL---EVKfaemdgytaeARAGELLLGV 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 129 GLEDKANYYP-EQLSGGQKQRVGIARALATSPDILICDEATSALDPETtteiLNLLKKVNREYNLTILLITHEMHVVKEI 207
Cdd:PRK15064  143 GIPEEQHYGLmSEVAPGWKLRVLLAQALFSNPDILLLDEPTNNLDINT----IRWLEDVLNERNSTMIIISHDRHFLNSV 218
                         250
                  ....*....|.
gi 2050094043 208 CHRVAVMEKGK 218
Cdd:PRK15064  219 CTHMADLDYGE 229
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
28-246 2.61e-09

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 58.58  E-value: 2.61e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   28 VEKGEIFGIIGFSGAGKSTLLRLV----NMLERPTAGTISIDdkditSLSAKELRK-LRQRIGMIFQSFNLFNSRTVFGN 102
Cdd:TIGR00956   84 IKPGELTVVLGRPGSGCSTLLKTIasntDGFHIGVEGVITYD-----GITPEEIKKhYRGDVVYNAETDVHFPHLTVGET 158
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  103 IAYPLRLaKLPKNEIK-----ERVNELLKFV----GLEDK-----ANYYPEQLSGGQKQRVGIARALATSPDILICDEAT 168
Cdd:TIGR00956  159 LDFAARC-KTPQNRPDgvsreEYAKHIADVYmatyGLSHTrntkvGNDFVRGVSGGERKRVSIAEASLGGAKIQCWDNAT 237
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  169 SALDPETTTEILNLLKKVNREYNLTILL-ITHEMHVVKEICHRVAVMEKGKVIEEGKLFDV--------FTQPKTKTTQN 239
Cdd:TIGR00956  238 RGLDSATALEFIRALKTSANILDTTPLVaIYQCSQDAYELFDKVIVLYEGYQIYFGPADKAkqyfekmgFKCPDRQTTAD 317

                   ....*..
gi 2050094043  240 FVRSVIN 246
Cdd:TIGR00956  318 FLTSLTS 324
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
28-177 2.87e-09

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 56.40  E-value: 2.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  28 VEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLS-AKELRKLRQRIGMIFQSFNLFNSRtvFGNIAYP 106
Cdd:PRK13543   34 VDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTATRGDrSRFMAYLGHLPGLKADLSTLENLH--FLCGLHG 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 107 LRLAKLPKNEikervnelLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTT 177
Cdd:PRK13543  112 RRAKQMPGSA--------LAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPLWLLDEPYANLDLEGIT 174
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
26-220 4.20e-09

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 57.65  E-value: 4.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  26 LSVEKGEIFGIIGFSGAGKSTLLRLVnmlerptAGTISIDDKDItslsakelrklrqrigmIFQSfNLFNSR-------- 97
Cdd:PRK11147   24 LHIEDNERVCLVGRNGAGKSTLMKIL-------NGEVLLDDGRI-----------------IYEQ-DLIVARlqqdpprn 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  98 ---TVFGNIAYPL---------------------------RLAKLpkNEIKE---------RVNELLKFVGLEdkANYYP 138
Cdd:PRK11147   79 vegTVYDFVAEGIeeqaeylkryhdishlvetdpseknlnELAKL--QEQLDhhnlwqlenRINEVLAQLGLD--PDAAL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 139 EQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKkvnrEYNLTILLITHEMHVVKEICHRVAVMEKGK 218
Cdd:PRK11147  155 SSLSGGWLRKAALGRALVSNPDVLLLDEPTNHLDIETIEWLEGFLK----TFQGSIIFISHDRSFIRNMATRIVDLDRGK 230

                  ..
gi 2050094043 219 VI 220
Cdd:PRK11147  231 LV 232
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
21-200 4.44e-09

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 55.73  E-value: 4.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsaKELRKLRQRIGMIFQSFNLFNSRTVF 100
Cdd:PRK13540   17 LQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIK----KDLCTYQKQLCFVGHRSGINPYLTLR 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAklpknEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEIL 180
Cdd:PRK13540   93 ENCLYDIHFS-----PGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDEPLVALDELSLLTII 167
                         170       180
                  ....*....|....*....|
gi 2050094043 181 NLLKKvNREYNLTILLITHE 200
Cdd:PRK13540  168 TKIQE-HRAKGGAVLLTSHQ 186
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
27-249 6.62e-08

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: 52.75  E-value: 6.62e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  27 SVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGtiSIDDKD-----ITSLSAKELR----KLRQ---RIGMIFQSFNLF 94
Cdd:cd03236    22 VPREGQVLGLVGPNGIGKSTALKILAGKLKPNLG--KFDDPPdwdeiLDEFRGSELQnyftKLLEgdvKVIVKPQYVDLI 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  95 nSRTVFGNIayplrLAKLPKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPE 174
Cdd:cd03236   100 -PKAVKGKV-----GELLKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIK 173
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2050094043 175 TTTEILNLLKKVNREYNlTILLITHEMHVVKEICHRVAVMekgkvIEEGKLFDVFTQPKTkttqnfVRSVINDHL 249
Cdd:cd03236   174 QRLNAARLIRELAEDDN-YVLVVEHDLAVLDYLSDYIHCL-----YGEPGAYGVVTLPKS------VREGINEFL 236
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
21-206 1.17e-07

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 53.38  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakelrKLRQRIGMIFQsFNLFNSRTVF 100
Cdd:TIGR01271  442 LKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKI----------------KHSGRISFSPQ-TSWIMPGTIK 504
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  101 GNIAYPLRLAKLpkneikeRVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:TIGR01271  505 DNIIFGLSYDEY-------RYTSVIKACQLEEDIALFPEKdktvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFT 577
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2050094043  170 ALDPETTTEILN--LLKKVNreyNLTILLITHEMHVVKE 206
Cdd:TIGR01271  578 HLDVVTEKEIFEscLCKLMS---NKTRILVTSKLEHLKK 613
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
24-223 1.97e-07

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: 52.64  E-value: 1.97e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   24 VTLSVEKGEIFGIIGFSGAGKSTLLrlvnmlerptagtisiddkdiTSLSAkELRKLRQRIGMIfqsfnlfnsrtvfGNI 103
Cdd:TIGR00957  657 ITFSIPEGALVAVVGQVGCGKSSLL---------------------SALLA-EMDKVEGHVHMK-------------GSV 701
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  104 AYPLRLAKLPKNEIKERVnellkFVGLEDKANYYPE---------------------------QLSGGQKQRVGIARALA 156
Cdd:TIGR00957  702 AYVPQQAWIQNDSLRENI-----LFGKALNEKYYQQvleacallpdleilpsgdrteigekgvNLSGGQKQRVSLARAVY 776
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043  157 TSPDILICDEATSALDPETTTEIL-NLLKKVNREYNLTILLITHEMHVVKEIcHRVAVMEKGKVIEEG 223
Cdd:TIGR00957  777 SNADIYLFDDPLSAVDAHVGKHIFeHVIGPEGVLKNKTRILVTHGISYLPQV-DVIIVMSGGKISEMG 843
GguA NF040905
sugar ABC transporter ATP-binding protein;
21-222 2.57e-07

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 52.10  E-value: 2.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLV--NMLERPTAGTISIDDKDITSLS-----------AKELRKlrqRIGMi 87
Cdd:NF040905  276 VDDVSLNVRRGEIVGIAGLMGAGRTELAMSVfgRSYGRNISGTVFKDGKEVDVSTvsdaidaglayVTEDRK---GYGL- 351
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  88 fqsfNLFNsrTVFGNIAyplrLAKLPK-------NEIKE-RVNE------LLKFVGLEDKAnyypEQLSGGQKQRVGIAR 153
Cdd:NF040905  352 ----NLID--DIKRNIT----LANLGKvsrrgviDENEEiKVAEeyrkkmNIKTPSVFQKV----GNLSGGNQQKVVLSK 417
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 154 ALATSPDILICDEATSALDPETTTEILNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEE 222
Cdd:NF040905  418 WLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAE-GKGVIVISSELPELLGMCDRIYVMNEGRITGE 485
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
21-179 4.86e-07

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: 50.63  E-value: 4.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakelrKLRQRIGMIFQsFNLFNSRTVF 100
Cdd:cd03291    53 LKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKI----------------KHSGRISFSSQ-FSWIMPGTIK 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 101 GNIAYPLRLAKLpkneikeRVNELLKFVGLEDKANYYPEQ-----------LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:cd03291   116 ENIIFGVSYDEY-------RYKSVVKACQLEEDITKFPEKdntvlgeggitLSGGQRARISLARAVYKDADLYLLDSPFG 188
                         170
                  ....*....|
gi 2050094043 170 ALDPETTTEI 179
Cdd:cd03291   189 YLDVFTEKEI 198
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
26-231 6.15e-07

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 50.78  E-value: 6.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  26 LSVEKGEIFGIIGFSGAGKSTLLR-LVNMLErPTAGTISIDDKDITSLSakeLRKLRQRIGMIFQSFN---LFNSRTVFG 101
Cdd:PRK10938   24 LTLNAGDSWAFVGANGSGKSALARaLAGELP-LLSGERQSQFSHITRLS---FEQLQKLVSDEWQRNNtdmLSPGEDDTG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 102 NIAyplrlAKLPKNEIK--ERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEI 179
Cdd:PRK10938  100 RTT-----AEIIQDEVKdpARCEQLAQQFGITALLDRRFKYLSTGETRKTLLCQALMSEPDLLILDEPFDGLDVASRQQL 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 180 LNLLKKVNREyNLTILLITHEMHVVKEICHRVAVMEKGKVIEEGKLFDVFTQ 231
Cdd:PRK10938  175 AELLASLHQS-GITLVLVLNRFDEIPDFVQFAGVLADCTLAETGEREEILQQ 225
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
11-206 9.14e-07

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: 48.47  E-value: 9.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  11 YESGGQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR--LVNMLERPTAGTISIDDKDITsLSAKELRKLrqrigmif 88
Cdd:cd03238     1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNegLYASGKARLISFLPKFSRNKL-IFIDQLQFL-------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 qsfnlfnsrtvfgniayplrlaklpkneikerVNELLKFVGLEDKANyypeQLSGGQKQRVGIARALATSPD--ILICDE 166
Cdd:cd03238    72 --------------------------------IDVGLGYLTLGQKLS----TLSGGELQRVKLASELFSEPPgtLFILDE 115
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2050094043 167 ATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVKE 206
Cdd:cd03238   116 PSTGLHQQDINQLLEVIKGLIDLGN-TVILIEHNLDVLSS 154
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
28-249 9.34e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 50.19  E-value: 9.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  28 VEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAG-TISIDDKD--------------ITSLSAKELRKLR--QRIGMIfqs 90
Cdd:PRK13409   96 PKEGKVTGILGPNGIGKTTAVKILSGELIPNLGdYEEEPSWDevlkrfrgtelqnyFKKLYNGEIKVVHkpQYVDLI--- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  91 fnlfnSRTVFGNIAYPLRlaklpKNEIKERVNELLKFVGLEDKANYYPEQLSGGQKQRVGIARALATSPDILICDEATSA 170
Cdd:PRK13409  173 -----PKVFKGKVRELLK-----KVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSY 242
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 171 LDpetTTEILNLLKKVnREY--NLTILLITHEMHVVKEICHRVAVM--EKGkvieegkLFDVFTQPKTkttqnfVRSVIN 246
Cdd:PRK13409  243 LD---IRQRLNVARLI-RELaeGKYVLVVEHDLAVLDYLADNVHIAygEPG-------AYGVVSKPKG------VRVGIN 305

                  ...
gi 2050094043 247 DHL 249
Cdd:PRK13409  306 EYL 308
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
29-172 1.26e-06

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 49.78  E-value: 1.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  29 EKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISID-DKDitslsaKELRKLRqriGMIFQSF--NLFNsrtvfGNI-- 103
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDEEpSWD------EVLKRFR---GTELQDYfkKLAN-----GEIkv 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 104 AY-PLRLAKLPKnEIKERVNELLKFVGLEDKANYYPEQ-------------LSGGQKQRVGIARALATSPDILICDEATS 169
Cdd:COG1245   163 AHkPQYVDLIPK-VFKGTVRELLEKVDERGKLDELAEKlglenildrdiseLSGGELQRVAIAAALLRDADFYFFDEPSS 241

                  ...
gi 2050094043 170 ALD 172
Cdd:COG1245   242 YLD 244
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
6-220 1.30e-06

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 49.89  E-value: 1.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   6 NISKVYESGgqsvHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR-LVNMLErPTAGTISIDDKditslsakelrklrQRI 84
Cdd:PRK15064  324 NLTKGFDNG----PLFKNLNLLLEAGERLAIIGENGVGKTTLLRtLVGELE-PDSGTVKWSEN--------------ANI 384
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  85 GMIFQ--SFNLFNSRTVFGNIAYpLRLAKLPKNEIKERVNELLkFVGleDKANYYPEQLSGGQKQRVGIARALATSPDIL 162
Cdd:PRK15064  385 GYYAQdhAYDFENDLTLFDWMSQ-WRQEGDDEQAVRGTLGRLL-FSQ--DDIKKSVKVLSGGEKGRMLFGKLMMQKPNVL 460
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 163 ICDEATSALDPEtTTEILNL-LKKvnreYNLTILLITHEMHVVKEICHRVAVMEKGKVI 220
Cdd:PRK15064  461 VMDEPTNHMDME-SIESLNMaLEK----YEGTLIFVSHDREFVSSLATRIIEITPDGVV 514
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
23-173 1.39e-06

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 49.63  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  23 DVTLSVEKGEIFGIIGFSGAGKSTLLRLV---------NML-----ERPTAGTISiddkDItslsakelrklRQRIGMIF 88
Cdd:PRK10938  278 NLSWQVNPGEHWQIVGPNGAGKSTLLSLItgdhpqgysNDLtlfgrRRGSGETIW----DI-----------KKHIGYVS 342
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 QSFNL-----FNSRTV-----FGNI----AYPLRLAKLpkneikerVNELLKFVGLEDKANYYPEQ-LSGGQKQRVGIAR 153
Cdd:PRK10938  343 SSLHLdyrvsTSVRNVilsgfFDSIgiyqAVSDRQQKL--------AQQWLDILGIDKRTADAPFHsLSWGQQRLALIVR 414
                         170       180
                  ....*....|....*....|
gi 2050094043 154 ALATSPDILICDEATSALDP 173
Cdd:PRK10938  415 ALVKHPTLLILDEPLQGLDP 434
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
15-206 1.43e-06

ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair in eubacteria is a process that repairs DNA damage by the removal of a 12-13-mer oligonucleotide containing the lesion. Recognition and cleavage of the damaged DNA is a multistep ATP-dependent reaction that requires the UvrA, UvrB, and UvrC proteins. Both UvrA and UvrB are ATPases, with UvrA having two ATP binding sites, which have the characteristic signature of the family of ABC proteins, and UvrB having one ATP binding site that is structurally related to that of helicases.


Pssm-ID: 213237 [Multi-domain]  Cd Length: 226  Bit Score: 48.41  E-value: 1.43e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  15 GQSVHAVEDVTLSVEKGEIFGIIGFSGAGKSTL----------LRLVN-----------MLERPT-------AGTISIDD 66
Cdd:cd03270     5 GAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLafdtiyaegqRRYVEslsayarqflgQMDKPDvdsieglSPAIAIDQ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  67 KDITslsakelRKLRQRIGMIFQSFNLFnsRTVFGNIAyplrlaklpkneIKERVNELLKfVGLE----DKANyypEQLS 142
Cdd:cd03270    85 KTTS-------RNPRSTVGTVTEIYDYL--RLLFARVG------------IRERLGFLVD-VGLGyltlSRSA---PTLS 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2050094043 143 GGQKQRVGIARALATSPD--ILICDEATSALDPETTTEILNLLKKVnREYNLTILLITHEMHVVKE 206
Cdd:cd03270   140 GGEAQRIRLATQIGSGLTgvLYVLDEPSIGLHPRDNDRLIETLKRL-RDLGNTVLVVEHDEDTIRA 204
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
7-200 1.58e-06

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: 47.99  E-value: 1.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   7 ISKVYESGGQSVHAVEDVTLsveKGEIFGIIGFSGAGKSTLLRLVNM----LERPTAGTISIDDKDITSLSAK---ELRk 79
Cdd:cd03240     1 IDKLSIRNIRSFHERSEIEF---FSPLTLIVGQNGAGKTTIIEALKYaltgELPPNSKGGAHDPKLIREGEVRaqvKLA- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  80 LRQRIG---MIFQSFNLFnsrtvfgniayplrlaklpKNEIKERVNELLKFVGLEdkanyyPEQLSGGQKQ------RVG 150
Cdd:cd03240    77 FENANGkkyTITRSLAIL-------------------ENVIFCHQGESNWPLLDM------RGRCSGGEKVlasliiRLA 131
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2050094043 151 IARALATSPDILICDEATSALDPETTTE-ILNLLKKVNREYNLTILLITHE 200
Cdd:cd03240   132 LAETFGSNCGILALDEPTTNLDEENIEEsLAEIIEERKSQKNFQLIVITHD 182
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
11-200 2.00e-06

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 49.56  E-value: 2.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  11 YESGGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLvnMLE--RPTAGTISIDdkdiTSLSAKELRKLRQrigmif 88
Cdd:PRK11147  327 YQIDGKQL--VKDFSAQVQRGDKIALIGPNGCGKTTLLKL--MLGqlQADSGRIHCG----TKLEVAYFDQHRA------ 392
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  89 qsfNLFNSRTVFGNIAYPlrlaklpKNEIKerVNELLKFV--GLED------------KAnyypeqLSGGQKQRVGIARA 154
Cdd:PRK11147  393 ---ELDPEKTVMDNLAEG-------KQEVM--VNGRPRHVlgYLQDflfhpkramtpvKA------LSGGERNRLLLARL 454
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2050094043 155 LATSPDILICDEATSALDPETtteiLNLLKKVNREYNLTILLITHE 200
Cdd:PRK11147  455 FLKPSNLLILDEPTNDLDVET----LELLEELLDSYQGTVLLVSHD 496
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
26-223 4.08e-06

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 47.48  E-value: 4.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  26 LSVEKGEIFGIIGFSGAGKSTLLRLVNMLE--RPTAGTISIDDKDITSLSAKElrKLRQRIGMIFQ--------SFNLFN 95
Cdd:PRK09580   22 LEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPED--RAGEGIFMAFQypveipgvSNQFFL 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  96 SRTVFGNIAY----PL-------------RLAKLPKNEIKERVNellkfVGLedkanyypeqlSGGQKQRVGIARALATS 158
Cdd:PRK09580  100 QTALNAVRSYrgqePLdrfdfqdlmeekiALLKMPEDLLTRSVN-----VGF-----------SGGEKKRNDILQMAVLE 163
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 159 PDILICDEATSALDPE---TTTEILNLLKKVNREYnltiLLITHEMHVVKEI-CHRVAVMEKGKVIEEG 223
Cdd:PRK09580  164 PELCILDESDSGLDIDalkIVADGVNSLRDGKRSF----IIVTHYQRILDYIkPDYVHVLYQGRIVKSG 228
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
27-199 5.04e-06

ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are implicated in the metabolism of DNA ends. They cleave ends sealed by hairpin structures and are thought to play a role in removing protein bound to DNA termini.


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 46.88  E-value: 5.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  27 SVEKGEIFGIIGFSGAGKSTLLRLVNML---ERPTAGTiSIDDKDITSLSAKELR-----KLRQRIGMIFQSFNLfNSRT 98
Cdd:cd03279    24 GLDNNGLFLICGPTGAGKSTILDAITYAlygKTPRYGR-QENLRSVFAPGEDTAEvsftfQLGGKKYRVERSRGL-DYDQ 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  99 vFGNIAYplrlakLPKNEIKERvneLLKFVgledkanyypEQLSGGQKQRVGIARALATSP----------DILICDEAT 168
Cdd:cd03279   102 -FTRIVL------LPQGEFDRF---LARPV----------STLSGGETFLASLSLALALSEvlqnrggarlEALFIDEGF 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2050094043 169 SALDPETTTEILNLLKKVNREyNLTILLITH 199
Cdd:cd03279   162 GTLDPEALEAVATALELIRTE-NRMVGVISH 191
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
28-233 8.87e-06

ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins, and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains, which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213189 [Multi-domain]  Cd Length: 177  Bit Score: 45.64  E-value: 8.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  28 VEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITslsakelrklrqrigmifqsfnlfnsrtvfgniaypl 107
Cdd:cd03222    22 VKEGEVIGIVGPNGTGKTTAVKILAGQLIPNGDNDEWDGITPV------------------------------------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 108 rlaklpkneikervnellkfvgledkanYYPE--QLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKK 185
Cdd:cd03222    65 ----------------------------YKPQyiDLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRR 116
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2050094043 186 VNREYNLTILLITHEMHVVKEICHRVAVMEKgkvieEGKLFDVFTQPK 233
Cdd:cd03222   117 LSEEGKKTALVVEHDLAVLDYLSDRIHVFEG-----EPGVYGIASQPK 159
PLN03073 PLN03073
ABC transporter F family; Provisional
14-172 9.16e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 47.55  E-value: 9.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  14 GGQSVhaVEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNM--------------LERPTAGTisiddkDITSL-----SA 74
Cdd:PLN03073  188 GGRDL--IVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMhaidgipkncqilhVEQEVVGD------DTTALqcvlnTD 259
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  75 KELRKLRQRIGMIFQSFNLFNSRTVFGNIAYPLRlAKLPKNEIKERVNELLKFVGL------EDKA-------NYYPE-- 139
Cdd:PLN03073  260 IERTQLLEEEAQLVAQQRELEFETETGKGKGANK-DGVDKDAVSQRLEEIYKRLELidaytaEARAasilaglSFTPEmq 338
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2050094043 140 -----QLSGGQKQRVGIARALATSPDILICDEATSALD 172
Cdd:PLN03073  339 vkatkTFSGGWRMRIALARALFIEPDLLLLDEPTNHLD 376
PLN03073 PLN03073
ABC transporter F family; Provisional
36-219 3.22e-05

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 45.62  E-value: 3.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  36 IIGFSGAGKSTLLRLVNMLERPTAGTIsiddkditslsakeLRKLRQRIGMIFQ----SFNLFNSRTVFGNIAYPlrlaK 111
Cdd:PLN03073  540 MVGPNGIGKSTILKLISGELQPSSGTV--------------FRSAKVRMAVFSQhhvdGLDLSSNPLLYMMRCFP----G 601
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043 112 LPKNEIKERVNELLKFVGLEDKANYypeQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLLKKvnreYN 191
Cdd:PLN03073  602 VPEQKLRAHLGSFGVTGNLALQPMY---TLSGGQKSRVAFAKITFKKPHILLLDEPSNHLDLDAVEALIQGLVL----FQ 674
                         170       180
                  ....*....|....*....|....*...
gi 2050094043 192 LTILLITHEMHVVKEICHRVAVMEKGKV 219
Cdd:PLN03073  675 GGVLMVSHDEHLISGSVDELWVVSEGKV 702
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
36-183 5.24e-05

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 43.71  E-value: 5.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  36 IIGFSGAGKSTLLRLVNMLERPTAGTISIDDKDITSLSakelrklRQRIGMIFQSFNLFNSRTVFGNIAYplrlaklpKN 115
Cdd:PRK13541   31 IKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIA-------KPYCTYIGHNLGLKLEMTVFENLKF--------WS 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 116 EIKERVNEL------LKFVGLEDKANYypeQLSGGQKQRVGIARALATSPDILICDEATSALDPETTTEILNLL 183
Cdd:PRK13541   96 EIYNSAETLyaaihyFKLHDLLDEKCY---SLSSGMQKIVAIARLIACQSDLWLLDEVETNLSKENRDLLNNLI 166
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
21-221 5.46e-05

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 44.78  E-value: 5.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  21 VEDVTLSVEKGEIFGIIGFSGAGKSTLLRLVNMLERPTAGTISID--------DKDITSLSA----------KELRKLRQ 82
Cdd:PRK10636   17 LDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPgnwqlawvNQETPALPQpaleyvidgdREYRQLEA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIgmifQSFNLFNSrtvfGNIAYPL--RLAKLPKNEIKERVNELLKFVGLEDKANYYP-EQLSGGQKQRVGIARALATSP 159
Cdd:PRK10636   97 QL----HDANERND----GHAIATIhgKLDAIDAWTIRSRAASLLHGLGFSNEQLERPvSDFSGGWRMRLNLAQALICRS 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2050094043 160 DILICDEATSALDPETTTeilnLLKKVNREYNLTILLITHEMHVVKEICHRVAVMEKGKVIE 221
Cdd:PRK10636  169 DLLLLDEPTNHLDLDAVI----WLEKWLKSYQGTLILISHDRDFLDPIVDKIIHIEQQSLFE 226
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
141-205 7.68e-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: 43.76  E-value: 7.68e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 141 LSGGQKQRVGIARAL---ATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVK 205
Cdd:cd03271   170 LSGGEAQRIKLAKELskrSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 236
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
141-205 7.82e-05

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: 44.62  E-value: 7.82e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2050094043 141 LSGGQKQRVGIARAL---ATSPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVK 205
Cdd:TIGR00630 830 LSGGEAQRIKLAKELskrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGN-TVVVIEHNLDVIK 896
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
33-199 8.08e-05

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 440188 [Multi-domain]  Cd Length: 204  Bit Score: 43.08  E-value: 8.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  33 IFGIIGFSGAGKSTLLRLV----------------NMLERPTAGT--------------ISIDDKDITSLSAKELRKLRQ 82
Cdd:COG0419    25 LNLIVGPNGAGKSTILEAIryalygkarsrsklrsDLINVGSEEAsvelefehggkryrIERRQGEFAEFLEAKPSERKE 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  83 RIGMIFQSFNLFNSRTVFGNIAYPLRLAKLPKNEIKERVNELL-KFVGLEDkanyyPEQLSGGQKQRVGIARALAtspdi 161
Cdd:COG0419   105 ALKRLLGLEIYEELKERLKELEEALESALEELAELQKLKQEILaQLSGLDP-----IETLSGGERLRLALADLLS----- 174
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2050094043 162 LICDeaTSALDPETTTEILNLLKKvnreynltILLITH 199
Cdd:COG0419   175 LILD--FGSLDEERLERLLDALEE--------LAIITH 202
SbcC_Walker_B pfam13558
SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from ...
140-185 1.58e-04

SbcC/RAD50-like, Walker B motif; This entry represents the Walker B domain of RAD50 from eukaryotes and the prokaryotic homolog SbcCD complex subunit C. RAD50-ATPase forms a complex with Mre11-nuclease that detects and processes diverse and obstructed DNA ends. This domain is separated of the Walker A domain by a long coiled-coil domain and forms the nucleotide-binding domain (NBD) when the coiled coils fold back on themselves and bring together Walker A and B domains. Two RAD50-NBDs forms heterotetramers with a Mre11 nuclease dimer that assemble as catalytic head module that binds and cleaves DNA in an ATP-dependent reaction. Through secondary structural analysis, it has been suggested that there is a wide structural conservation in the Rad50/SMC protein family as seen in structural similarities between RAD50's hook and ABC-ATPase MukB's elbow region.


Pssm-ID: 463921 [Multi-domain]  Cd Length: 90  Bit Score: 39.91  E-value: 1.58e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2050094043 140 QLSGGQKQ-------------RVGIARALATSPDILICDEATSALDPETTTEILNLLKK 185
Cdd:pfam13558  32 GLSGGEKQllaylplaaalaaQYGSAEGRPPAPRLVFLDEAFAKLDEENIRTALELLRA 90
Udk COG0572
Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway ...
33-76 6.71e-04

Uridine kinase [Nucleotide transport and metabolism]; Uridine kinase is part of the Pathway/BioSystem: Pyrimidine salvage


Pssm-ID: 440337 [Multi-domain]  Cd Length: 206  Bit Score: 40.21  E-value: 6.71e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2050094043  33 IFGIIGFSGAGKSTLL-RLVNMLERPTAGTISIDD--KDITSLSAKE 76
Cdd:COG0572     9 IIGIAGPSGSGKTTFArRLAEQLGADKVVVISLDDyyKDREHLPLDE 55
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
17-205 3.04e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.43  E-value: 3.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   17 SVHAVEDVTLSVEKGEIFGIIGFSGAGKSTLLR--LVNMLERPTAG----TISIDDKDITSL------------------ 72
Cdd:PRK00635   607 TKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINdtLVPAVEEFIEQgfcsNLSIQWGAISRLvhitrdlpgrsqrsiplt 686
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043   73 ---SAKELRKL------RQRIGMI---FqSFNL----------FNSRTVFGN---IAYPLRLAKLPKNEIKE------RV 121
Cdd:PRK00635   687 yikAFDDLRELfaeqprSKRLGLTkshF-SFNTplgacaecqgLGSITTTDNrtsIPCPSCLGKRFLPQVLEvrykgkNI 765
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2050094043  122 NELLKFVGLEDKA--------------------NYYP-----EQLSGGQKQRVGIARAL---ATSPDILICDEATSALDP 173
Cdd:PRK00635   766 ADILEMTAYEAEKffldepsihekihalcslglDYLPlgrplSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHT 845
                          250       260       270
                   ....*....|....*....|....*....|..
gi 2050094043  174 ETTTEILNLLKKVNREYNlTILLITHEMHVVK 205
Cdd:PRK00635   846 HDIKALIYVLQSLTHQGH-TVVIIEHNMHVVK 876
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
140-199 4.13e-03

ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems involved in cellular processes other than transport. These families are characterized by the fact that the ABC subunit is made up of duplicated, fused ABC modules (ABC2). No known transmembrane proteins or domains are associated with these proteins.


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 37.34  E-value: 4.13e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2050094043 140 QLSGGQKQRVGIARALA---TSPDILIC-DEATSALDPETTTEILNLLKKvNREYNLTILLITH 199
Cdd:cd03227    77 QLSGGEKELSALALILAlasLKPRPLYIlDEIDRGLDPRDGQALAEAILE-HLVKGAQVIVITH 139
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
141-211 4.65e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 39.04  E-value: 4.65e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2050094043  141 LSGGQKQRVGIARALAT--SPDILICDEATSALDPETTTEILNLLKKVNREYNlTILLITHEMHVVkEICHRV 211
Cdd:PRK00635   477 LSGGEQERTALAKHLGAelIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGN-TVLLVEHDEQMI-SLADRI 547
 
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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