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Conserved domains on  [gi|488284725|ref|WP_002355933|]
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MULTISPECIES: excinuclease ABC subunit UvrA [Bacillota]

Protein Classification

excinuclease ABC subunit UvrA( domain architecture ID 1000295)

excinuclease ABC subunit UvrA is a DNA-binding ATPase that recognizes DNA adducts in the nucleotide excision repair process catalyzed by the UvrABC excinuclease repair system

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UvrA super family cl33793
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-745 0e+00

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


The actual alignment was detected with superfamily member COG0178:

Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 784.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   1 MEWIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAE-SRR--ElndTFSSFVQNYLPKYGRPEVEKIE 77
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEgQRRyvE---SLSAYARQFLGQMDKPDVDSIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  78 NLPVAIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAG-----------------------------------SPFV-- 120
Cdd:COG0178   80 GLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGtphcpicgrpvekqtvdqivdrilalpegtrlqilAPVVrg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 121 ---------------GYS-----------------------------D-------------------------------- 124
Cdd:COG0178  160 rkgehkelleelrkqGFVrvrvdgevydldeepeldknkkhtievvvDrlvvkedirsrladsvetalklgdglvivevv 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 125 ---------------------------TFSFNHPDGKCPTCDGLGKITEINLHQLV-DYDKSLNEG---PIDFPTFtvgN 173
Cdd:COG0178  240 degeellfsekfacpdcgisfeeleprLFSFNSPYGACPTCDGLGRVLEFDPDLVIpDPSLSLAEGaiaPWSGPSS---S 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 174 WRWK---RYA-HSGlFDLDKKIKDYSPEELALFLYAPQQKLA----NPPKEWPHTALYEGIVPRMQRsiLHTDEGKRHQK 245
Cdd:COG0178  317 YYFQlleALAkHYG-FDLDTPWKDLPEEQRDLILYGSDEKIKfrykNRGRRRTYEKPFEGVIPFLER--RYRETYSEHVR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 246 -YLNHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS----LI-KNIQEELLVRLEALINIG 319
Cdd:COG0178  394 eELSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTereaEIaERILKEIRSRLGFLVDVG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 320 LSYLTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREA 399
Cdd:COG0178  474 LDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAA 553
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 400 DFIIDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKA-RKSLSIEHATLHNLNNLSVEVPLGVL 475
Cdd:COG0178  554 DYIIDIGPGAGEHGGEVVAQGTPEEILKNPdSLTGQYLsgRKRIPVPKKRRKGnGKFLTIKGARENNLKNVDVEIPLGVL 633
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 476 TVICGVAGSGKSSLAEEIYQKA------QADNQ--------------EIIHLSQKSI--TAnlRSTPMTYLNIFDKVRKL 533
Cdd:COG0178  634 TCVTGVSGSGKSTLVNDILYPAlarklnGAKEKpgphdsieglehidKVIDIDQSPIgrTP--RSNPATYTGVFDPIREL 711
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 534 FAEENHV-----SPALFSYNSKGA-CPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSVK 607
Cdd:COG0178  712 FAQTPEAkargyKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVE 791
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 608 DGYDFFKDQPfALS--LKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQ 682
Cdd:COG0178  792 EALEFFENIP-KIArkLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRstgKTLYILDEPTTGLHFHDIRKLLE 870
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 683 LFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:COG0178  871 VLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYL 933
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-745 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 784.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   1 MEWIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAE-SRR--ElndTFSSFVQNYLPKYGRPEVEKIE 77
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEgQRRyvE---SLSAYARQFLGQMDKPDVDSIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  78 NLPVAIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAG-----------------------------------SPFV-- 120
Cdd:COG0178   80 GLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGtphcpicgrpvekqtvdqivdrilalpegtrlqilAPVVrg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 121 ---------------GYS-----------------------------D-------------------------------- 124
Cdd:COG0178  160 rkgehkelleelrkqGFVrvrvdgevydldeepeldknkkhtievvvDrlvvkedirsrladsvetalklgdglvivevv 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 125 ---------------------------TFSFNHPDGKCPTCDGLGKITEINLHQLV-DYDKSLNEG---PIDFPTFtvgN 173
Cdd:COG0178  240 degeellfsekfacpdcgisfeeleprLFSFNSPYGACPTCDGLGRVLEFDPDLVIpDPSLSLAEGaiaPWSGPSS---S 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 174 WRWK---RYA-HSGlFDLDKKIKDYSPEELALFLYAPQQKLA----NPPKEWPHTALYEGIVPRMQRsiLHTDEGKRHQK 245
Cdd:COG0178  317 YYFQlleALAkHYG-FDLDTPWKDLPEEQRDLILYGSDEKIKfrykNRGRRRTYEKPFEGVIPFLER--RYRETYSEHVR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 246 -YLNHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS----LI-KNIQEELLVRLEALINIG 319
Cdd:COG0178  394 eELSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTereaEIaERILKEIRSRLGFLVDVG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 320 LSYLTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREA 399
Cdd:COG0178  474 LDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAA 553
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 400 DFIIDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKA-RKSLSIEHATLHNLNNLSVEVPLGVL 475
Cdd:COG0178  554 DYIIDIGPGAGEHGGEVVAQGTPEEILKNPdSLTGQYLsgRKRIPVPKKRRKGnGKFLTIKGARENNLKNVDVEIPLGVL 633
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 476 TVICGVAGSGKSSLAEEIYQKA------QADNQ--------------EIIHLSQKSI--TAnlRSTPMTYLNIFDKVRKL 533
Cdd:COG0178  634 TCVTGVSGSGKSTLVNDILYPAlarklnGAKEKpgphdsieglehidKVIDIDQSPIgrTP--RSNPATYTGVFDPIREL 711
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 534 FAEENHV-----SPALFSYNSKGA-CPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSVK 607
Cdd:COG0178  712 FAQTPEAkargyKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVE 791
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 608 DGYDFFKDQPfALS--LKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQ 682
Cdd:COG0178  792 EALEFFENIP-KIArkLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRstgKTLYILDEPTTGLHFHDIRKLLE 870
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 683 LFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:COG0178  871 VLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYL 933
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-745 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 684.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   1 MEWIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYLPKYGRPEVEKIENLP 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  81 VAIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAG-----------------------------------SPFV----- 120
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGkphcpncgrpieaqtvsqmvdrvlelpegtrlqilAPVVrgrkg 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 121 ------------GY-----------------------------------------------------SD----------- 124
Cdd:PRK00349 163 ehkkllenlrkqGFvrvrvdgevydldeppkldknkkhtievvvdrlvvkedirqrladsietalklSDglvvvevmddp 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 125 --------------------------TFSFNHPDGKCPTCDGLGKITEINLHQLV-DYDKSLNEGPIDFPTFTVGNWRWK 177
Cdd:PRK00349 243 eaeellfsekfacpvcgfsipeleprLFSFNSPYGACPTCDGLGVKLEFDPDLVVpDPELSLAEGAIAPWSRSSSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 178 RYA----HSGlFDLDKKIKDYSPEELALFLYAPQQK------LANPPKEWPHTALYEGIVPRMQRSILHTD-EGKRhqKY 246
Cdd:PRK00349 323 MLKslaeHYG-FDLDTPWKDLPEEVQDIILYGSGDEeiefryKNDRGRTRERKHPFEGVIPNLERRYRETEsEYVR--EE 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 247 LNHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS---------LIKNIQEellvRLEALIN 317
Cdd:PRK00349 400 LEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSeqeakiaepILKEIRE----RLKFLVD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 318 IGLSYLTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIR 397
Cdd:PRK00349 476 VGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIR 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 398 EADFIIDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKAR-KSLSIEHATLHNLNNLSVEVPLG 473
Cdd:PRK00349 556 AADYIVDIGPGAGVHGGEVVASGTPEEIMKNPnSLTGQYLsgKKKIEVPKERRKGNgKFLKLKGARENNLKNVDVEIPLG 635
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 474 VLTVICGVAGSGKSSLAEEIYQKAqADNQ---------------------EIIHLSQKSITANLRSTPMTYLNIFDKVRK 532
Cdd:PRK00349 636 KFTCVTGVSGSGKSTLINETLYKA-LARKlngakkvpgkhkeieglehldKVIDIDQSPIGRTPRSNPATYTGVFDPIRE 714
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 533 LFAE--ENHV---SPALFSYNSKGA-CPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSV 606
Cdd:PRK00349 715 LFAGtpEAKArgyKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTV 794
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 607 KDGYDFFKDQP-FALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQ 682
Cdd:PRK00349 795 EEALEFFEAIPkIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLHFEDIRKLLE 874
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 683 LFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK00349 875 VLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-730 0e+00

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: 684.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725    4 IEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYLPKYGRPEVEKIENLPVAI 83
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   84 VIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAGSPFV------------------------------------------- 120
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgefr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  121 ---------GYS-------------------------------------------------------------------- 123
Cdd:TIGR00630 162 klleklrkqGFArvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeeva 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  124 -------------------------DTFSFNHPDGKCPTCDGLGKITEINLHQLVDYDK-SLNEGPIDFPTFTVGNWRWK 177
Cdd:TIGR00630 242 eskeelfsekfacpecgfslpelepRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLlSLNGGAIVPFKKSTTSYYRQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  178 RY---AHSGLFDLDKKIKDYSPEELALFLYAPQQK------LANPPKEWPHTALYEGIVPRMQRSILHTD-EGKRhqKYL 247
Cdd:TIGR00630 322 MFaslAEHLGFDLDTPWKDLPEEAQKAILYGSGEEvivvkyRNGGGETFRYHKPFEGVIPELERRYLETEsESMR--EYL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  248 NHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS-----LIKNIQEELLVRLEALINIGLSY 322
Cdd:TIGR00630 400 EKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTpeekkIAEEVLKEIRERLGFLIDVGLDY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  323 LTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFI 402
Cdd:TIGR00630 480 LSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  403 IDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKA-RKSLSIEHATLHNLNNLSVEVPLGVLTVI 478
Cdd:TIGR00630 560 IDIGPGAGEHGGEVVASGTPEEILANPdSLTGQYLsgRKKIEVPAERRPGnGKFLTLKGARENNLKNITVSIPLGLFTCI 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  479 CGVAGSGKSSL---------AEEIYQ-KAQADNQE----------IIHLSQKSITANLRSTPMTYLNIFDKVRKLFAE-- 536
Cdd:TIGR00630 640 TGVSGSGKSTLindtlypalANRLNGaKTVPGRYTsieglehldkVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAEtp 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  537 ---ENHVSPALFSYNSK-GACPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDF 612
Cdd:TIGR00630 720 eakVRGYTPGRFSFNVKgGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEF 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  613 FKDQP-FALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQLFNRMV 688
Cdd:TIGR00630 800 FEAVPsISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|..
gi 488284725  689 EEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTP 730
Cdd:TIGR00630 880 DKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTP 921
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
453-730 5.46e-86

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: 272.18  E-value: 5.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 453 LSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLAEEIY----------QKAQADNQE----------IIHLSQKSI 512
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlKKEQPGNHDrieglehidkVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 513 TANLRSTPMTYLNIFDKVRKLFaeenhvspalfsynskgacptckgkgiivsdmsfmedvtsiCETCHGTRYKEEVLHYL 592
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------CEVCKGKRYNRETLEVR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 593 YNGKNIVEVLALSVKDGYDFFKDQP-FALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEP 668
Cdd:cd03271  120 YKGKSIADVLDMTVEEALEFFENIPkIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEP 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 669 TDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTP 730
Cdd:cd03271  200 TTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
625-713 8.43e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 61.87  E-value: 8.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI 704
Cdd:NF040873 104 LERVGLADL-AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182

                 ....*....
gi 488284725 705 KSADWLIEL 713
Cdd:NF040873 183 RRADPCVLL 191
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
463-669 1.56e-06

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: 48.41  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  463 LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIihlsqksitaNLRSTPMTYLNIfDKVRKlfaeenHVsp 542
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI----------LLDGQDLTDDER-KSLRK------EI-- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  543 alfsynskgacptckgkGIIVSDMSFMEDVTsicetchgtrykeevlhylyNGKNIVEVLALsvkdgYDFFKDQPFALSL 622
Cdd:pfam00005  62 -----------------GYVFQDPQLFPRLT--------------------VRENLRLGLLL-----KGLSKREKDARAE 99
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488284725  623 KNLLEVGLSYL---KLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPT 669
Cdd:pfam00005 100 EALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
 
Name Accession Description Interval E-value
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
1-745 0e+00

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 784.22  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   1 MEWIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAE-SRR--ElndTFSSFVQNYLPKYGRPEVEKIE 77
Cdd:COG0178    3 MDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAFDTIYAEgQRRyvE---SLSAYARQFLGQMDKPDVDSIE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  78 NLPVAIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAG-----------------------------------SPFV-- 120
Cdd:COG0178   80 GLSPAISIEQKTTSRNPRSTVGTVTEIYDYLRLLFARVGtphcpicgrpvekqtvdqivdrilalpegtrlqilAPVVrg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 121 ---------------GYS-----------------------------D-------------------------------- 124
Cdd:COG0178  160 rkgehkelleelrkqGFVrvrvdgevydldeepeldknkkhtievvvDrlvvkedirsrladsvetalklgdglvivevv 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 125 ---------------------------TFSFNHPDGKCPTCDGLGKITEINLHQLV-DYDKSLNEG---PIDFPTFtvgN 173
Cdd:COG0178  240 degeellfsekfacpdcgisfeeleprLFSFNSPYGACPTCDGLGRVLEFDPDLVIpDPSLSLAEGaiaPWSGPSS---S 316
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 174 WRWK---RYA-HSGlFDLDKKIKDYSPEELALFLYAPQQKLA----NPPKEWPHTALYEGIVPRMQRsiLHTDEGKRHQK 245
Cdd:COG0178  317 YYFQlleALAkHYG-FDLDTPWKDLPEEQRDLILYGSDEKIKfrykNRGRRRTYEKPFEGVIPFLER--RYRETYSEHVR 393
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 246 -YLNHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS----LI-KNIQEELLVRLEALINIG 319
Cdd:COG0178  394 eELSRYMSETPCPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFENLELTereaEIaERILKEIRSRLGFLVDVG 473
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 320 LSYLTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREA 399
Cdd:COG0178  474 LDYLTLDRSAGTLSGGEAQRIRLATQIGSGLVGVLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVEHDEDTIRAA 553
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 400 DFIIDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKA-RKSLSIEHATLHNLNNLSVEVPLGVL 475
Cdd:COG0178  554 DYIIDIGPGAGEHGGEVVAQGTPEEILKNPdSLTGQYLsgRKRIPVPKKRRKGnGKFLTIKGARENNLKNVDVEIPLGVL 633
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 476 TVICGVAGSGKSSLAEEIYQKA------QADNQ--------------EIIHLSQKSI--TAnlRSTPMTYLNIFDKVRKL 533
Cdd:COG0178  634 TCVTGVSGSGKSTLVNDILYPAlarklnGAKEKpgphdsieglehidKVIDIDQSPIgrTP--RSNPATYTGVFDPIREL 711
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 534 FAEENHV-----SPALFSYNSKGA-CPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSVK 607
Cdd:COG0178  712 FAQTPEAkargyKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVE 791
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 608 DGYDFFKDQPfALS--LKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQ 682
Cdd:COG0178  792 EALEFFENIP-KIArkLQTLQDVGLGYIKLGQPATTLSGGEAQRVKLASELSKRstgKTLYILDEPTTGLHFHDIRKLLE 870
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 683 LFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:COG0178  871 VLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKASYTGRYL 933
uvrA PRK00349
excinuclease ABC subunit UvrA;
1-745 0e+00

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 684.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   1 MEWIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYLPKYGRPEVEKIENLP 80
Cdd:PRK00349   3 MDKIIIRGAREHNLKNIDLDIPRDKLVVFTGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  81 VAIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAG-----------------------------------SPFV----- 120
Cdd:PRK00349  83 PAISIDQKTTSHNPRSTVGTVTEIYDYLRLLYARVGkphcpncgrpieaqtvsqmvdrvlelpegtrlqilAPVVrgrkg 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 121 ------------GY-----------------------------------------------------SD----------- 124
Cdd:PRK00349 163 ehkkllenlrkqGFvrvrvdgevydldeppkldknkkhtievvvdrlvvkedirqrladsietalklSDglvvvevmddp 242
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 125 --------------------------TFSFNHPDGKCPTCDGLGKITEINLHQLV-DYDKSLNEGPIDFPTFTVGNWRWK 177
Cdd:PRK00349 243 eaeellfsekfacpvcgfsipeleprLFSFNSPYGACPTCDGLGVKLEFDPDLVVpDPELSLAEGAIAPWSRSSSSYYFQ 322
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 178 RYA----HSGlFDLDKKIKDYSPEELALFLYAPQQK------LANPPKEWPHTALYEGIVPRMQRSILHTD-EGKRhqKY 246
Cdd:PRK00349 323 MLKslaeHYG-FDLDTPWKDLPEEVQDIILYGSGDEeiefryKNDRGRTRERKHPFEGVIPNLERRYRETEsEYVR--EE 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 247 LNHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS---------LIKNIQEellvRLEALIN 317
Cdd:PRK00349 400 LEKYMSERPCPSCKGKRLKPEALAVKVGGKNIGEVSELSIGEALEFFENLKLSeqeakiaepILKEIRE----RLKFLVD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 318 IGLSYLTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIR 397
Cdd:PRK00349 476 VGLDYLTLSRSAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNDRLIETLKHLRDLGNTLIVVEHDEDTIR 555
                        570       580       590       600       610       620       630       640
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 398 EADFIIDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKAR-KSLSIEHATLHNLNNLSVEVPLG 473
Cdd:PRK00349 556 AADYIVDIGPGAGVHGGEVVASGTPEEIMKNPnSLTGQYLsgKKKIEVPKERRKGNgKFLKLKGARENNLKNVDVEIPLG 635
                        650       660       670       680       690       700       710       720
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 474 VLTVICGVAGSGKSSLAEEIYQKAqADNQ---------------------EIIHLSQKSITANLRSTPMTYLNIFDKVRK 532
Cdd:PRK00349 636 KFTCVTGVSGSGKSTLINETLYKA-LARKlngakkvpgkhkeieglehldKVIDIDQSPIGRTPRSNPATYTGVFDPIRE 714
                        730       740       750       760       770       780       790       800
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 533 LFAE--ENHV---SPALFSYNSKGA-CPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSV 606
Cdd:PRK00349 715 LFAGtpEAKArgyKPGRFSFNVKGGrCEACQGDGVIKIEMHFLPDVYVPCDVCKGKRYNRETLEVKYKGKNIADVLDMTV 794
                        810       820       830       840       850       860       870       880
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 607 KDGYDFFKDQP-FALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQ 682
Cdd:PRK00349 795 EEALEFFEAIPkIARKLQTLVDVGLGYIKLGQPATTLSGGEAQRVKLAKELSKRstgKTLYILDEPTTGLHFEDIRKLLE 874
                        890       900       910       920       930       940
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 683 LFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK00349 875 VLHRLVDKGNTVVVIEHNLDVIKTADWIIDLGPEGGDGGGEIVATGTPEEVAKVEASYTGRYL 937
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
4-730 0e+00

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: 684.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725    4 IEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYLPKYGRPEVEKIENLPVAI 83
Cdd:TIGR00630   2 IIVRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGVMDKPDVDSIEGLSPAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   84 VIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAGSPFV------------------------------------------- 120
Cdd:TIGR00630  82 SIDQKTTSHNPRSTVGTITEIYDYLRLLFARVGTPYCptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgefr 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  121 ---------GYS-------------------------------------------------------------------- 123
Cdd:TIGR00630 162 klleklrkqGFArvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeeva 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  124 -------------------------DTFSFNHPDGKCPTCDGLGKITEINLHQLVDYDK-SLNEGPIDFPTFTVGNWRWK 177
Cdd:TIGR00630 242 eskeelfsekfacpecgfslpelepRLFSFNSPYGACPECSGLGIKQEFDPELIIPDPLlSLNGGAIVPFKKSTTSYYRQ 321
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  178 RY---AHSGLFDLDKKIKDYSPEELALFLYAPQQK------LANPPKEWPHTALYEGIVPRMQRSILHTD-EGKRhqKYL 247
Cdd:TIGR00630 322 MFaslAEHLGFDLDTPWKDLPEEAQKAILYGSGEEvivvkyRNGGGETFRYHKPFEGVIPELERRYLETEsESMR--EYL 399
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  248 NHFVTVKRCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLS-----LIKNIQEELLVRLEALINIGLSY 322
Cdd:TIGR00630 400 EKFMSERPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQLTLTpeekkIAEEVLKEIRERLGFLIDVGLDY 479
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  323 LTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFI 402
Cdd:TIGR00630 480 LSLSRAAGTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYV 559
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  403 IDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQAL--QEPLPLNDQPRKA-RKSLSIEHATLHNLNNLSVEVPLGVLTVI 478
Cdd:TIGR00630 560 IDIGPGAGEHGGEVVASGTPEEILANPdSLTGQYLsgRKKIEVPAERRPGnGKFLTLKGARENNLKNITVSIPLGLFTCI 639
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  479 CGVAGSGKSSL---------AEEIYQ-KAQADNQE----------IIHLSQKSITANLRSTPMTYLNIFDKVRKLFAE-- 536
Cdd:TIGR00630 640 TGVSGSGKSTLindtlypalANRLNGaKTVPGRYTsieglehldkVIHIDQSPIGRTPRSNPATYTGVFDEIRELFAEtp 719
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  537 ---ENHVSPALFSYNSK-GACPTCKGKGIIVSDMSFMEDVTSICETCHGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDF 612
Cdd:TIGR00630 720 eakVRGYTPGRFSFNVKgGRCEACQGDGVIKIEMHFLPDVYVPCEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEF 799
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  613 FKDQP-FALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEPTDGLHLIDIQQSLQLFNRMV 688
Cdd:TIGR00630 800 FEAVPsISRKLQTLCDVGLGYIRLGQPATTLSGGEAQRIKLAKELSKRstgRTLYILDEPTTGLHFDDIKKLLEVLQRLV 879
                         890       900       910       920
                  ....*....|....*....|....*....|....*....|..
gi 488284725  689 EEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTP 730
Cdd:TIGR00630 880 DKGNTVVVIEHNLDVIKTADYIIDLGPEGGDGGGTVVASGTP 921
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
10-734 1.54e-134

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 436.95  E-value: 1.54e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   10 TQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYLPKYGRPEVEKIENLPVAIVIDQKK 89
Cdd:PRK00635   12 TVRNLKNISIEFCPREIVLLTGVSGSGKSSLAFDTIYAAGRKRYLSTLPSFFATTLDSLPDPSVEKIEGLSPTIAVKQNH 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   90 VAGNSRSTVGTYTDIYTFLRLLFSRAG-----------------------------------SPFV-------------G 121
Cdd:PRK00635   92 FSQHSHATVGSTTELNSHLALLFSLEGqardpvtlhpltlyskekilstiaaipdgtqitllAPLPakdilaireclrqG 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  122 YS-----------------------------DTF---------------------------------------------- 126
Cdd:PRK00635  172 FTkvridgeispiykfltsgipedvpvdivvDTLiknesntarlkvslftaldighgecslhfdnqkrtfstqatipetq 251
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  127 ------------SFNHPDgKCPTCDGLGKITEINLHQLVDYDKSLNEGPIDFptftVGNWR-------WKRYAHSGLFDL 187
Cdd:PRK00635  252 qtytpltpqlfsPHSLED-RCPQCQGSGIFISIDDPSLIQQNLSIEENCCPF----AGNCStylyhtiYQSLADSLGFSL 326
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  188 DKKIKDYSPEELALFLYApQQKLANPPKEWPHTALYEGIVPRMQRSILHTDEGK-----RHQKYLNHFVTVKRCPDCLGS 262
Cdd:PRK00635  327 STPWKDLSPEIQNIFLYG-KEGLVLPVRLFDGTLGKKTLTHKVWRGVLNEIGEKvrysnKPSRYLPKGTSATSCPRCQGT 405
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  263 RVNERVRSCKINQKSIADAVDMPLTELHSFIRSMDLSL--IKNIQEELLVRLEALINIGLSYLTLGRATETLSGGEAQRI 340
Cdd:PRK00635  406 GLGDYANAATWHGKTFAEFQQMSLQELFIFLSQLPSKSlsIEEVLQGLKSRLSILIDLGLPYLTPERALATLSGGEQERT 485
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  341 KIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIGPFAGENGGHVQFSG 420
Cdd:PRK00635  486 ALAKHLGAELIGITYILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEHDEQMISLADRIIDIGPGAGIFGGEVLFNG 565
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  421 TYDAFLA-SKTLTSQALQEPL--PLNDQPRKARKSLSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSL-------- 489
Cdd:PRK00635  566 SPREFLAkSDSLTAKYLRQELtiPIPEKRTNSLGTLTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLindtlvpa 645
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  490 AEEIYQKAQADN--------QEIIHLSQKSITANLRSTPMTYLNIFDKVRKLFAEENHVSP-----ALFSYN-SKGACPT 555
Cdd:PRK00635  646 VEEFIEQGFCSNlsiqwgaiSRLVHITRDLPGRSQRSIPLTYIKAFDDLRELFAEQPRSKRlgltkSHFSFNtPLGACAE 725
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  556 CKGKGiivsDMSFMEDVTSI-CETCHGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDFFKDQP-FALSLKNLLEVGLSYL 633
Cdd:PRK00635  726 CQGLG----SITTTDNRTSIpCPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFFLDEPsIHEKIHALCSLGLDYL 801
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  634 KLNQSLSTLSGGELQRVKLADTL---HQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWL 710
Cdd:PRK00635  802 PLGRPLSSLSGGEIQRLKLAYELlapSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYV 881
                         890       900
                  ....*....|....*....|....
gi 488284725  711 IELGPEGGENGGQLLFTGTPANML 734
Cdd:PRK00635  882 LELGPEGGNLGGYLLASCSPEELI 905
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
4-745 1.90e-90

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 310.99  E-value: 1.90e-90
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725    4 IEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFV-QNYLPKYGRPEVEKIENLPVA 82
Cdd:PRK00635  941 ITIKNAYQHNLKHIDLSLPRNALTAVTGPSASGKHSLVFDILYAAGNIAYAELFPPYIrQALIKKTPLPSVDKVTGLSPV 1020
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   83 IVIDQKKVAGNSRSTVGTYTDIYTFLRLLFSRAGSPF------------------------------------------- 119
Cdd:PRK00635 1021 IAIEKTSASKNSNHSVASALEISNGLEKLFARLGHPYsplsgdalrkitpqtiaeellthytkgyvtitspipkeedlfi 1100
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725      --------------------------------------------------------------------------------
Cdd:PRK00635 1101 ylqeklkegflklyaneqfydldeplptslenpaiviqhtkiseknlssllssltlafslsssiclhieyagtslsltyr 1180
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  120 VGYSDTF------------SFNHPDGKCPTCDGLGKITEINLhqLVDYDKSLNEGPIDFPTFTVGNWRWKRyahsgLFDL 187
Cdd:PRK00635 1181 LGWQDSSgnlypnittpllSRDHEEGLCPLCHGKGFILKCSL--LPHKEKIAHYTPLSLFTLFFPNQDPKP-----VYPL 1253
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  188 DKKIKDYSPEELALFLYAPQQKLANPPKEWPHtalYEGIVprMQRSILHTDEgkrhqKYLNHFVTVKRCPDCLGSRVNER 267
Cdd:PRK00635 1254 LKELGIPSIALFQELDTLSFESLCLGTQQHPG---LNALL--MEAMLMESEE-----PLPPPLISKTPCNQCQGLGVYTY 1323
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  268 VRSCKINQKSIADAVDMPLTELHSFIRSMDLSLIKNIQEELLVRLEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVN 347
Cdd:PRK00635 1324 AHCVRIHNTSLSDIYQEDVTFLKKFLLTIHDDEEPSIIQDLLNRLTFIDKVGLSYITLGQEQDTLSDGEHYRLHLAKKIS 1403
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  348 SALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIGPFAGENGGHVqfsgtydafla 427
Cdd:PRK00635 1404 SNLTDIIYLLEDPLSGLHPQDAPTLLQLIKELVTNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGGYL----------- 1472
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  428 SKTLTSQALQEPLPlNDQPRKARKSLSIEhATLHNLNNLSVEVPLGVLTVICGVAGSGKSS-LAEEIYQKAQA--DN--- 501
Cdd:PRK00635 1473 LSTSALKQSQPDLH-NTRSSEETPTLSVS-LSIHTIQNLNVSAPLHSLVAISGVSGSGKTSlLLEGFYKQACAliEKgps 1550
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  502 --QEIIHLSQKSITANLRSTPMTYLNIFDKVRKLF-----AEENHVSPALFSYNSK-GACPTCKGKGIIVSDMSFMEDVT 573
Cdd:PRK00635 1551 vfSEIIFLDSHPQISSQRSDISTYFDIAPSLRNFYasltqAKALNISASMFSTNTKqGQCSDCWGLGYQWIDRAFYALEK 1630
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  574 SICETCHGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDFFkdqPF----ALSLKNLLEVGLSYLKLNQSLSTLSGGELQR 649
Cdd:PRK00635 1631 RPCPTCSGFRIQPLAQEVVYEGKHFGQLLQTPIEEVAETF---PFlkkiQKPLQALIDNGLGYLPLGQNLSSLSLSEKIA 1707
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  650 VKLADTLH---QKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLF 726
Cdd:PRK00635 1708 IKIAKFLYlppKHPTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGSGKTGGKILF 1787
                         890
                  ....*....|....*....
gi 488284725  727 TGTPANMLNSTHSITKGYL 745
Cdd:PRK00635 1788 SGPPKDISASKDSLLKTYM 1806
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
453-730 5.46e-86

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: 272.18  E-value: 5.46e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 453 LSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLAEEIY----------QKAQADNQE----------IIHLSQKSI 512
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLypalarrlhlKKEQPGNHDrieglehidkVIVIDQSPI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 513 TANLRSTPMTYLNIFDKVRKLFaeenhvspalfsynskgacptckgkgiivsdmsfmedvtsiCETCHGTRYKEEVLHYL 592
Cdd:cd03271   81 GRTPRSNPATYTGVFDEIRELF-----------------------------------------CEVCKGKRYNRETLEVR 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 593 YNGKNIVEVLALSVKDGYDFFKDQP-FALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK---KAIYLMDEP 668
Cdd:cd03271  120 YKGKSIADVLDMTVEEALEFFENIPkIARKLQTLCDVGLGYIKLGQPATTLSGGEAQRIKLAKELSKRstgKTLYILDEP 199
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 669 TDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGTP 730
Cdd:cd03271  200 TTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDLGPEGGDGGGQVVASGTP 261
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
4-420 1.96e-78

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: 251.02  E-value: 1.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   4 IEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYLPKYGRPEVEKIENLPVAI 83
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAFDTIYAEGQRRYVESLSAYARQFLGQMDKPDVDSIEGLSPAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  84 VIDQKKVAGNSRSTVGTYTDIYTFLRLLfsragspfvgysdtfsfnhpdgkcptcdglgkiteinlhqlvdydkslnegp 163
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLL---------------------------------------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 164 idfptftvgnwrwkrYAHSGlfdldkkikdyspeelalflyapqqklanppkewphtalyegivprmqrsilhtdegkrh 243
Cdd:cd03270  109 ---------------FARVG------------------------------------------------------------ 113
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 244 qkylnhfvtvkrcpdclgsrvnervrsckinqksiadavdmpltelhsfirsmdlslIKNiqeellvRLEALINIGLSYL 323
Cdd:cd03270  114 ---------------------------------------------------------IRE-------RLGFLVDVGLGYL 129
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 324 TLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFII 403
Cdd:cd03270  130 TLSRSAPTLSGGEAQRIRLATQIGSGLTGVLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVI 209
                        410
                 ....*....|....*..
gi 488284725 404 DIGPFAGENGGHVQFSG 420
Cdd:cd03270  210 DIGPGAGVHGGEIVAQG 226
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
3-438 3.77e-69

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 244.55  E-value: 3.77e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   3 WIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNdtfssfvqNYLPKYGRP-EVEKIENLPV 81
Cdd:COG0178  610 FLTIKGARENNLKNVDVEIPLGVLTCVTGVSGSGKSTLVNDILYPALARKLN--------GAKEKPGPHdSIEGLEHIDK 681
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  82 AIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFS-------RagspfvGYS-DTFSFNHPDGKCPTCDGLGKITeINLHQLV 153
Cdd:COG0178  682 VIDIDQSPIGRTPRSNPATYTGVFDPIRELFAqtpeakaR------GYKpGRFSFNVKGGRCEACQGDGVIK-IEMHFLP 754
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 154 DydkslnegpidfptftvgnwrwkryahsglfdldkkikdyspeelalfLYAPqqklanppkewphtalyegivprmqrs 233
Cdd:COG0178  755 D------------------------------------------------VYVP--------------------------- 759
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 234 ilhtdegkrhqkylnhfvtvkrCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIRSmdlslIKNIQEellvRLE 313
Cdd:COG0178  760 ----------------------CEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEALEFFEN-----IPKIAR----KLQ 808
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 314 ALINIGLSYLTLGRATETLSGGEAQRIKIAKY-VNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHN 392
Cdd:COG0178  809 TLQDVGLGYIKLGQPATTLSGGEAQRVKLASElSKRSTGKTLYILDEPTTGLHFHDIRKLLEVLHRLVDKGNTVVVIEHN 888
                        410       420       430       440
                 ....*....|....*....|....*....|....*....|....*..
gi 488284725 393 PQLIREADFIIDIGPFAGENGGHVQFSGTYDAFLASK-TLTSQALQE 438
Cdd:COG0178  889 LDVIKTADWIIDLGPEGGDGGGEIVAEGTPEEVAKVKaSYTGRYLKE 935
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
2-421 3.59e-62

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: 224.51  E-value: 3.59e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725    2 EWIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNdtfssfvQNYLPKYGRPEVEKIENLPV 81
Cdd:TIGR00630 612 KFLTLKGARENNLKNITVSIPLGLFTCITGVSGSGKSTLINDTLYPALANRLN-------GAKTVPGRYTSIEGLEHLDK 684
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   82 AIVIDQKKVAGNSRSTVGTYTDIYTFLRLLFsrAGSP---FVGYSDT-FSFNHPDGKCPTCDGLGKITeINLHQLVDydk 157
Cdd:TIGR00630 685 VIHIDQSPIGRTPRSNPATYTGVFDEIRELF--AETPeakVRGYTPGrFSFNVKGGRCEACQGDGVIK-IEMHFLPD--- 758
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  158 slnegpidfptftvgnwrwkryahsglfdldkkikdyspeelalfLYAPqqklanppkewphtalyegivprmqrsilht 237
Cdd:TIGR00630 759 ---------------------------------------------VYVP------------------------------- 762
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  238 degkrhqkylnhfvtvkrCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFirsmdLSLIKNIQeellVRLEALIN 317
Cdd:TIGR00630 763 ------------------CEVCKGKRYNRETLEVKYKGKNIADVLDMTVEEAYEF-----FEAVPSIS----RKLQTLCD 815
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  318 IGLSYLTLGRATETLSGGEAQRIKIAKYVNS-ALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLI 396
Cdd:TIGR00630 816 VGLGYIRLGQPATTLSGGEAQRIKLAKELSKrSTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVI 895
                         410       420
                  ....*....|....*....|....*
gi 488284725  397 READFIIDIGPFAGENGGHVQFSGT 421
Cdd:TIGR00630 896 KTADYIIDLGPEGGDGGGTVVASGT 920
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
3-729 5.87e-55

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 205.45  E-value: 5.87e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725    3 WIEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRelndtfssFVQNYLPKYGRPEVEKIENLpVA 82
Cdd:PRK00635  600 TLTLSKATKHNLKDLTISLPLGRLTVVTGVSGSGKSSLINDTLVPAVEE--------FIEQGFCSNLSIQWGAISRL-VH 670
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   83 IVIDqkkVAGNS-RSTVGTYTDIYTFLRLLFS-RAGSPFVGYSDT-FSFNHPDGKCPTCDGLGKITeinlhqLVDydksl 159
Cdd:PRK00635  671 ITRD---LPGRSqRSIPLTYIKAFDDLRELFAeQPRSKRLGLTKShFSFNTPLGACAECQGLGSIT------TTD----- 736
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  160 NEGPIDfptftvgnwrwkryahsglfdldkkikdyspeelalflyapqqklanppkewphtalyegivprmqrsilhtde 239
Cdd:PRK00635  737 NRTSIP-------------------------------------------------------------------------- 742
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  240 gkrhqkylnhfvtvkrCPDCLGSRVNERVRSCKINQKSIADAVDMPLTELHSFIrsMDLSLIKNiqeellvRLEALINIG 319
Cdd:PRK00635  743 ----------------CPSCLGKRFLPQVLEVRYKGKNIADILEMTAYEAEKFF--LDEPSIHE-------KIHALCSLG 797
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  320 LSYLTLGRATETLSGGEAQRIKIA-KYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE 398
Cdd:PRK00635  798 LDYLPLGRPLSSLSGGEIQRLKLAyELLAPSKKPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKV 877
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  399 ADFIIDIGPFAGENGGHVQFSGTYDAFLASKTLTSQALQ------EPLP-LNDQPRKARKS--LSIEHATLHNLNNLSVE 469
Cdd:PRK00635  878 ADYVLELGPEGGNLGGYLLASCSPEELIHLHTPTAKALRpylsspQELPyLPDPSPKPPVPadITIKNAYQHNLKHIDLS 957
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  470 VPLGVLTVICGVAGSGKSSLAEEIYQKA--------------QADNQE--------------IIHLSQKSITANLRSTPM 521
Cdd:PRK00635  958 LPRNALTAVTGPSASGKHSLVFDILYAAgniayaelfppyirQALIKKtplpsvdkvtglspVIAIEKTSASKNSNHSVA 1037
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  522 TYLNIFDKVRKLFA------------------------------------------------------------------ 535
Cdd:PRK00635 1038 SALEISNGLEKLFArlghpysplsgdalrkitpqtiaeellthytkgyvtitspipkeedlfiylqeklkegflklyane 1117
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  536 -------------------------EENHVS------------------------------------------------P 542
Cdd:PRK00635 1118 qfydldeplptslenpaiviqhtkiSEKNLSsllssltlafslsssiclhieyagtslsltyrlgwqdssgnlypnittP 1197
                         730       740       750       760       770       780       790       800
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  543 ALFSYNSKGACPTCKGKGIIvSDMSFME--------------------------------------------DVTSICET 578
Cdd:PRK00635 1198 LLSRDHEEGLCPLCHGKGFI-LKCSLLPhkekiahytplslftlffpnqdpkpvypllkelgipsialfqelDTLSFESL 1276
                         810       820       830       840       850       860       870       880
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  579 CHGTRY----------------KEEVLHYL--------------YNGKNIVEVLALSVKDGYD----FFKD--------- 615
Cdd:PRK00635 1277 CLGTQQhpglnallmeamlmesEEPLPPPLisktpcnqcqglgvYTYAHCVRIHNTSLSDIYQedvtFLKKflltihdde 1356
                         890       900       910       920       930       940       950       960
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  616 -QPFALSLKNLLE----VGLSYLKLNQSLSTLSGGELQRVKLADTLHQK--KAIYLMDEPTDGLHLIDIQQSLQLFNRMV 688
Cdd:PRK00635 1357 ePSIIQDLLNRLTfidkVGLSYITLGQEQDTLSDGEHYRLHLAKKISSNltDIIYLLEDPLSGLHPQDAPTLLQLIKELV 1436
                         970       980       990      1000
                  ....*....|....*....|....*....|....*....|.
gi 488284725  689 EEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTGT 729
Cdd:PRK00635 1437 TNNNTVIATDRSGSLAEHADHLIHLGPGSGPQGGYLLSTSA 1477
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
4-421 2.72e-53

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: 185.13  E-value: 2.72e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   4 IEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTfSSFVQNYlpkygrPEVEKIENLPVAI 83
Cdd:cd03271    1 LTLKGARENNLKNIDVDIPLGVLTCVTGVSGSGKSSLINDTLYPALARRLHLK-KEQPGNH------DRIEGLEHIDKVI 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  84 VIDQKKVAGNSRSTVGTYTDIYTFLRLLFsragspfvgysdtfsfnhpdgkCPTCDGlgkiteinlhqlvdydkslnegp 163
Cdd:cd03271   74 VIDQSPIGRTPRSNPATYTGVFDEIRELF----------------------CEVCKG----------------------- 108
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 164 idfptftvgnwrwkryahsglfdldkkiKDYSPEELALflyapqqklanppkewphtaLYEGivprmqrsilhtdegkrh 243
Cdd:cd03271  109 ----------------------------KRYNRETLEV--------------------RYKG------------------ 122
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 244 qkylnhfvtvkrcpdclgsrvnervrsckinqKSIADAVDMPLTELHSFIRSmdlslIKNIQEellvRLEALINIGLSYL 323
Cdd:cd03271  123 --------------------------------KSIADVLDMTVEEALEFFEN-----IPKIAR----KLQTLCDVGLGYI 161
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 324 TLGRATETLSGGEAQRIKIAK-YVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFI 402
Cdd:cd03271  162 KLGQPATTLSGGEAQRIKLAKeLSKRSTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWI 241
                        410
                 ....*....|....*....
gi 488284725 403 IDIGPFAGENGGHVQFSGT 421
Cdd:cd03271  242 IDLGPEGGDGGGQVVASGT 260
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
449-745 1.05e-43

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 169.82  E-value: 1.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 449 ARKSLSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLA-EEIY----------------------QKAQADNqeII 505
Cdd:COG0178    2 MMDKIRIRGAREHNLKNIDVDIPRNKLVVITGLSGSGKSSLAfDTIYaegqrryveslsayarqflgqmDKPDVDS--IE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 506 HLS------QKSITANLRST--PMT----YLN-------------------------IFDKV------------------ 530
Cdd:COG0178   80 GLSpaisieQKTTSRNPRSTvgTVTeiydYLRllfarvgtphcpicgrpvekqtvdqIVDRIlalpegtrlqilapvvrg 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 531 -----RKLFAE---------------------------ENHV-------------------------------------- 540
Cdd:COG0178  160 rkgehKELLEElrkqgfvrvrvdgevydldeepeldknKKHTievvvdrlvvkedirsrladsvetalklgdglvivevv 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 541 ------------------------SPALFSYNS-KGACPTCKGKGI--------IVSDMS-------------------- 567
Cdd:COG0178  240 degeellfsekfacpdcgisfeelEPRLFSFNSpYGACPTCDGLGRvlefdpdlVIPDPSlslaegaiapwsgpsssyyf 319
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 568 -------------------------------------------------------------------------------F 568
Cdd:COG0178  320 qllealakhygfdldtpwkdlpeeqrdlilygsdekikfryknrgrrrtyekpfegvipflerryretysehvreelsrY 399
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 569 MEDVTsiCETCHGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDFFKDqpFALS-----------------LKNLLEVGLS 631
Cdd:COG0178  400 MSETP--CPACKGARLKPEALAVKIGGKNIAELTALSIDEALEFFEN--LELTereaeiaerilkeirsrLGFLVDVGLD 475
                        490       500       510       520       530       540       550       560
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 632 YLKLNQSLSTLSGGELQRVKLA--------DTLhqkkaiYLMDEPTDGLH------LIDIQQSLQlfnrmvEEGNSLILL 697
Cdd:COG0178  476 YLTLDRSAGTLSGGEAQRIRLAtqigsglvGVL------YVLDEPSIGLHqrdndrLIETLKRLR------DLGNTVIVV 543
                        570       580       590       600
                 ....*....|....*....|....*....|....*....|....*...
gi 488284725 698 EHHIDVIKSADWLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:COG0178  544 EHDEDTIRAADYIIDIGPGAGEHGGEVVAQGTPEEILKNPDSLTGQYL 591
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
453-728 2.44e-41

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: 149.01  E-value: 2.44e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 453 LSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAqadnqeiihlsqksitanlrstpmtylnifdkvrk 532
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYAS----------------------------------- 45
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 533 lfaeenhvspalfsynskgacptckGKGIIVSDMSFMEDVTSIcetchgtrykeevlhylyngknivevlalsvkdgydf 612
Cdd:cd03238   46 -------------------------GKARLISFLPKFSRNKLI------------------------------------- 63
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 613 FKDQpfalsLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTL--HQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEE 690
Cdd:cd03238   64 FIDQ-----LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELfsEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDL 138
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 488284725 691 GNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTG 728
Cdd:cd03238  139 GNTVILIEHNLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
312-420 1.06e-39

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: 144.39  E-value: 1.06e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 312 LEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEH 391
Cdd:cd03238   68 LQFLIDVGLGYLTLGQKLSTLSGGELQRVKLASELFSEPPGTLFILDEPSTGLHQQDINQLLEVIKGLIDLGNTVILIEH 147
                         90       100
                 ....*....|....*....|....*....
gi 488284725 392 NPQLIREADFIIDIGPFAGENGGHVQFSG 420
Cdd:cd03238  148 NLDVLSSADWIIDFGPGSGKSGGKVVFSG 176
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
453-728 3.33e-39

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: 144.71  E-value: 3.33e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 453 LSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLA-EEIYQKAQ----------------------ADNQE----II 505
Cdd:cd03270    1 IIVRGAREHNLKNVDVDIPRNKLVVITGVSGSGKSSLAfDTIYAEGQrryveslsayarqflgqmdkpdVDSIEglspAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 506 HLSQKSITANLRSTPMTYLNIFDKVRKLFAEEnhvspalfsynskgacptckgkGIIvsdmsfmedvtsicetchgTRyk 585
Cdd:cd03270   81 AIDQKTTSRNPRSTVGTVTEIYDYLRLLFARV----------------------GIR-------------------ER-- 117
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 586 eevlhylyngknivevlalsvkdgydffkdqpfalsLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQK--KAIY 663
Cdd:cd03270  118 ------------------------------------LGFLVDVGLGYLTLSRSAPTLSGGEAQRIRLATQIGSGltGVLY 161
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 664 LMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENGGQLLFTG 728
Cdd:cd03270  162 VLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDEDTIRAADHVIDIGPGAGVHGGEIVAQG 226
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
455-745 1.24e-36

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: 148.24  E-value: 1.24e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  455 IEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLA-EEIYQKAQ--------------------ADNQEIIHLS----- 508
Cdd:TIGR00630   4 VRGAREHNLKNIDVEIPRDKLVVITGLSGSGKSSLAfDTIYAEGQrryveslsayarqflgvmdkPDVDSIEGLSpaisi 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  509 -QKSITANLRSTPMTYLNIFDKVRKLFA---------------------------------------------------- 535
Cdd:TIGR00630  84 dQKTTSHNPRSTVGTITEIYDYLRLLFArvgtpycptcgrpisrqtpsqivdqilalpegtrvillapivrgrkgefrkl 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725      --------------------------------------------------------------------------------
Cdd:TIGR00630 164 leklrkqgfarvrvdgevypledppkleknkkhtidvvidrltvknenrsrlaesvetalrlgdgllevefdddeevaes 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  536 -----EENHV-----------SPALFSYNS-KGACPTCKGKGI--------IV--------------------------- 563
Cdd:TIGR00630 244 keelfSEKFAcpecgfslpelEPRLFSFNSpYGACPECSGLGIkqefdpelIIpdpllslnggaivpfkksttsyyrqmf 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  564 ----------------------------------------------------------------------SDMSFMEDVT 573
Cdd:TIGR00630 324 aslaehlgfdldtpwkdlpeeaqkailygsgeevivvkyrngggetfryhkpfegvipelerryleteseSMREYLEKFM 403
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  574 S--ICETCHGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDFFKD---------------QPFALSLKNLLEVGLSYLKLN 636
Cdd:TIGR00630 404 SerPCPSCGGTRLKPEALAVTVGGKSIADVSELSIREAHEFFNQltltpeekkiaeevlKEIRERLGFLIDVGLDYLSLS 483
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  637 QSLSTLSGGELQRVKLADTLHQK--KAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELG 714
Cdd:TIGR00630 484 RAAGTLSGGEAQRIRLATQIGSGltGVLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIG 563
                         570       580       590
                  ....*....|....*....|....*....|.
gi 488284725  715 PEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:TIGR00630 564 PGAGEHGGEVVASGTPEEILANPDSLTGQYL 594
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
305-403 1.71e-14

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: 72.88  E-value: 1.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLEALINIGLSYLTLGRATETLSGGEAQRIKIAkyvnSALndIM----YILDEPSAGLHPKDIERISRALLNLK 380
Cdd:cd03225  108 EEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIA----GVL--AMdpdiLLLDEPTAGLDPAGRRELLELLKKLK 181
                         90       100
                 ....*....|....*....|....
gi 488284725 381 NKGNTVVLVEHNPQLIRE-ADFII 403
Cdd:cd03225  182 AEGKTIIIVTHDLDLLLElADRVI 205
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
4-65 6.38e-14

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: 70.43  E-value: 6.38e-14
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725   4 IEIKHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQNYL 65
Cdd:cd03238    1 LTVSGANVHNLQNLDVSIPLNVLVVVTGVSGSGKSTLVNEGLYASGKARLISFLPKFSRNKL 62
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
325-427 1.25e-13

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: 70.54  E-value: 1.25e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 325 LGRATETLSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE-AD- 400
Cdd:cd03224  126 RKQLAGTLSGGEQQMLAIAR----ALmsRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADr 201
                         90       100
                 ....*....|....*....|....*...
gi 488284725 401 -FIIDigpfagenGGHVQFSGTYDAFLA 427
Cdd:cd03224  202 aYVLE--------RGRVVLEGTAAELLA 221
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
293-742 2.15e-13

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: 73.40  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 293 IRSMDLSLIKNIQEELL--VRLEALiniglsyltLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIE 370
Cdd:COG1123  111 NLGLSRAEARARVLELLeaVGLERR---------LDRYPHQLSGGQRQRVAIAMAL--ALDPDLLIADEPTTALDVTTQA 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 371 RISRALLNL-KNKGNTVVLVEHNPQLIRE-ADFIIDIgpfageNGGHVQFSGTYDAFLASktltSQALQEPLPLNDQPRK 448
Cdd:COG1123  180 EILDLLRELqRERGTTVLLITHDLGVVAEiADRVVVM------DDGRIVEDGPPEEILAA----PQALAAVPRLGAARGR 249
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 449 ARKS-------LSIEHAT----------LHNLNNLSVEVPLG-VLTVIcGVAGSGKSSLAEEI--YQKAQA-----DNQE 503
Cdd:COG1123  250 AAPAaaaaeplLEVRNLSkrypvrgkggVRAVDDVSLTLRRGeTLGLV-GESGSGKSTLARLLlgLLRPTSgsilfDGKD 328
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 504 IIHLSQKSITAnLRST-------PMTYLNIFDKVRKLFAEenhvspalfsynskgacptckgkGIIVsdmsfmedvtsic 576
Cdd:COG1123  329 LTKLSRRSLRE-LRRRvqmvfqdPYSSLNPRMTVGDIIAE-----------------------PLRL------------- 371
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 577 etcHGTRYKEEVLhylyngKNIVEVLALsvkdgydffkdqpfalslknlleVGLSYLKLNQSLSTLSGGELQRVKLADTL 656
Cdd:COG1123  372 ---HGLLSRAERR------ERVAELLER-----------------------VGLPPDLADRYPHELSGGQRQRVAIARAL 419
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 657 HQKKAIYLMDEPTDGLhliD--IQ-QSLQLFNRMVEEGN-SLILLEHHIDVIKS-ADWLIELgpeggeNGGQLLFTGTPA 731
Cdd:COG1123  420 ALEPKLLILDEPTSAL---DvsVQaQILNLLRDLQRELGlTYLFISHDLAVVRYiADRVAVM------YDGRIVEDGPTE 490
                        490
                 ....*....|..
gi 488284725 732 NML-NSTHSITK 742
Cdd:COG1123  491 EVFaNPQHPYTR 502
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
332-405 5.71e-13

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: 67.27  E-value: 5.71e-13
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREA-DFIIDI 405
Cdd:cd00267   81 LSGGQRQRVALARAL--LLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAELAaDRVIVL 153
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
332-407 1.35e-12

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: 66.23  E-value: 1.35e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284725 332 LSGGEAQRIKIAKYVNSAL--NDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIGP 407
Cdd:cd03227   78 LSGGEKELSALALILALASlkPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPELAELADKLIHIKK 155
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
332-429 2.24e-12

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: 70.17  E-value: 2.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKyvnsAL---NDImYILDEPSAGLhpkDIE---RISRALLNLKnKGNTVVLVEHNPQLIREADFIIDI 405
Cdd:COG4988  474 LSGGQAQRLALAR----ALlrdAPL-LLLDEPTAHL---DAEteaEILQALRRLA-KGRTVILITHRLALLAQADRILVL 544
                         90       100
                 ....*....|....*....|....
gi 488284725 406 gpfageNGGHVQFSGTYDAFLASK 429
Cdd:COG4988  545 ------DDGRIVEQGTHEELLAKN 562
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
642-713 2.88e-12

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: 64.96  E-value: 2.88e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI-KSADWLIEL 713
Cdd:cd00267   81 LSGGQRQRVALARALLLNPDLLLLDEPTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAeLAADRVIVL 153
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
622-713 2.95e-12

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: 66.34  E-value: 2.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 622 LKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHI 701
Cdd:cd03225  115 VEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDILLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDL 194
                         90
                 ....*....|...
gi 488284725 702 DVIKS-ADWLIEL 713
Cdd:cd03225  195 DLLLElADRVIVL 207
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
625-738 2.97e-12

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 67.04  E-value: 2.97e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGlhlIDI--QQSL-QLFNRMVEEGNSLILLEHHI 701
Cdd:COG1121  124 LERVGLEDLA-DRPIGELSGGQQQRVLLARALAQDPDLLLLDEPFAG---VDAatEEALyELLRELRREGKTILVVTHDL 199
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488284725 702 D-VIKSADWLIELgpeggenGGQLLFTGTPANMLNSTH 738
Cdd:COG1121  200 GaVREYFDRVLLL-------NRGLVAHGPPEEVLTPEN 230
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
625-734 2.30e-11

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: 64.28  E-value: 2.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID-V 703
Cdd:COG1122  119 LELVGLEHL-ADRPPHELSGGQKQRVAIAGVLAMEPEVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDlV 197
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 704 IKSADWLIELgpeggeNGGQLLFTGTPANML 734
Cdd:COG1122  198 AELADRVIVL------DDGRIVADGTPREVF 222
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
625-713 8.43e-11

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 61.87  E-value: 8.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI 704
Cdd:NF040873 104 LERVGLADL-AGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLDAESRERIIALLAEEHARGATVVVVTHDLELV 182

                 ....*....
gi 488284725 705 KSADWLIEL 713
Cdd:NF040873 183 RRADPCVLL 191
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
332-405 9.89e-11

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: 61.08  E-value: 9.89e-11
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284725 332 LSGGEAQRIKIAK--YVNSALndimYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDI 405
Cdd:cd03246   97 LSGGQRQRLGLARalYGNPRI----LVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
273-438 1.05e-10

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: 62.59  E-value: 1.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 273 INQKSIADAVDMPLTELHSFIRSMdLSLIKniQEELLVRLEALINIGLSYLTLGRATEtLSGGEAQRIKIAKyvnsALN- 351
Cdd:cd03256   90 IERLSVLENVLSGRLGRRSTWRSL-FGLFP--KEEKQRALAALERVGLLDKAYQRADQ-LSGGQQQRVAIAR----ALMq 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 352 --DIMyILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEHNPQLIRE-ADFIIdigpfaGENGGHVQFSGtydaflA 427
Cdd:cd03256  162 qpKLI-LADEPVASLDPASSRQVMDLLKRInREEGITVIVSLHQVDLAREyADRIV------GLKDGRIVFDG------P 228
                        170
                 ....*....|.
gi 488284725 428 SKTLTSQALQE 438
Cdd:cd03256  229 PAELTDEVLDE 239
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
604-704 1.06e-10

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: 62.77  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 604 LSVKDGYDFFKDQPFALSLKNLLEvglsylklnQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSL-- 681
Cdd:cd03236  111 LKKKDERGKLDELVDQLELRHVLD---------RNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYL---DIKQRLna 178
                         90       100
                 ....*....|....*....|....
gi 488284725 682 -QLFNRMVEEGNSLILLEHHIDVI 704
Cdd:cd03236  179 aRLIRELAEDDNYVLVVEHDLAVL 202
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
628-713 1.76e-10

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: 61.40  E-value: 1.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 628 VGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID-VIKS 706
Cdd:cd03235  120 VGLSELA-DRQIGELSGGQQQRVLLARALVQDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGlVLEY 198

                 ....*..
gi 488284725 707 ADWLIEL 713
Cdd:cd03235  199 FDRVLLL 205
BtuD COG4138
ABC-type cobalamin transport system, ATPase component BtuD [Coenzyme transport and metabolism]; ...
634-734 2.45e-10

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


Pssm-ID: 443313 [Multi-domain]  Cd Length: 248  Bit Score: 61.39  E-value: 2.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLA-------DTLHQKKAIYLMDEPTDGLhliDI-QQS--LQLFNRMVEEGNSLILLEH---- 699
Cdd:COG4138  119 KLSRPLTQLSGGEWQRVRLAavllqvwPTINPEGQLLLLDEPMNSL---DVaQQAalDRLLRELCQQGITVVMSSHdlnh 195
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488284725 700 ---HIDVIksadWLIelgpeggeNGGQLLFTGTPANML 734
Cdd:COG4138  196 tlrHADRV----WLL--------KQGKLVASGETAEVM 221
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
625-736 2.57e-10

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: 61.60  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL---HLIDIqqsLQLFNRMV-EEGNSLILLEHH 700
Cdd:COG1120  122 LERTGLEHLA-DRPVDELSGGERQRVLIARALAQEPPLLLLDEPTSHLdlaHQLEV---LELLRRLArERGRTVVMVLHD 197
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488284725 701 ID-VIKSADWLIELgpeggeNGGQLLFTGTPANMLNS 736
Cdd:COG1120  198 LNlAARYADRLVLL------KDGRIVAQGPPEEVLTP 228
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
325-704 2.98e-10

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: 63.65  E-value: 2.98e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 325 LGRATETLSGGEAQRIKIAkyvnSAL---NDImYILDEPSAGLhpkDI-ERI--SRALLNLKNKGNTVVLVEHNPQLIre 398
Cdd:COG1245  206 LDRDISELSGGELQRVAIA----AALlrdADF-YFFDEPSSYL---DIyQRLnvARLIRELAEEGKYVLVVEHDLAIL-- 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 399 aDFIID-IGPFAGENGGHVQFSGTY----------DAFLAS------------KTLTSQALQEPLPLNDQPRKARK---- 451
Cdd:COG1245  276 -DYLADyVHILYGEPGVYGVVSKPKsvrvginqylDGYLPEenvrirdepiefEVHAPRREKEEETLVEYPDLTKSyggf 354
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 452 SLSIEHATLHNlnnlsVEVpLGVLtvicGVAGSGKSS----LAEEIyqkaQADNQEI---IHLSQKS--ITANLRSTPMT 522
Cdd:COG1245  355 SLEVEGGEIRE-----GEV-LGIV----GPNGIGKTTfakiLAGVL----KPDEGEVdedLKISYKPqyISPDYDGTVEE 420
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 523 YLnifdkvrklfaeENHVSPALFSynskgacptckgkgiivsdmSFmedvtsicetchgtrYKEEVLhylyngknivevl 602
Cdd:COG1245  421 FL------------RSANTDDFGS--------------------SY---------------YKTEII------------- 440
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 603 alsvkdgydffkdQPfaLSLKNLLEvglsylklnQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTdgLHLiDIQQSLQ 682
Cdd:COG1245  441 -------------KP--LGLEKLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS--AHL-DVEQRLA 493
                        410       420
                 ....*....|....*....|....*.
gi 488284725 683 L---FNRMVEE-GNSLILLEHHIDVI 704
Cdd:COG1245  494 VakaIRRFAENrGKTAMVVDHDIYLI 519
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
306-407 4.55e-10

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 59.83  E-value: 4.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 306 EELLVRLealiniGLSYLTLGRATETLSGGEAQRIKIAkyvnSALN---DImYILDEPSAGLHPKDIERISRALLNL-KN 381
Cdd:COG4619  111 LELLERL------GLPPDILDKPVERLSGGERQRLALI----RALLlqpDV-LLLDEPTSALDPENTRRVEELLREYlAE 179
                         90       100
                 ....*....|....*....|....*..
gi 488284725 382 KGNTVVLVEHNPQLI-READFIIDIGP 407
Cdd:COG4619  180 EGRAVLWVSHDPEQIeRVADRVLTLEA 206
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
461-744 6.44e-10

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: 60.39  E-value: 6.44e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  461 HNLNNLSVEVPLGVLTVICGVAGSGKSSLAEEIyqkaqadNQeIIHLSQKSITANLRStpmtylnifdkVRKLFAEEnhv 540
Cdd:TIGR02315  16 QALKNINLNINPGEFVAIIGPSGAGKSTLLRCI-------NR-LVEPSSGSILLEGTD-----------ITKLRGKK--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  541 spaLFSYNSKgacptckgKGIIVSDMSFMEDVTSIcetchgtrykEEVLHYLYNGKNIVEVLalsvkdgYDFFKDQPFAL 620
Cdd:TIGR02315  74 ---LRKLRRR--------IGMIFQHYNLIERLTVL----------ENVLHGRLGYKPTWRSL-------LGRFSEEDKER 125
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  621 SLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRM-VEEGNSLILLEH 699
Cdd:TIGR02315 126 ALSALERVGLAD-KAYQRADQLSGGQQQRVAIARALAQQPDLILADEPIASLDPKTSKQVMDYLKRInKEDGITVIINLH 204
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 488284725  700 HIDVIKS-ADWLIELgpeggeNGGQLLFTGTPaNMLNsTHSITKGY 744
Cdd:TIGR02315 205 QVDLAKKyADRIVGL------KAGEIVFDGAP-SELD-DEVLRHIY 242
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
331-428 6.82e-10

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: 60.00  E-value: 6.82e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKyvnsAL---NDIMyILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE-AD--FIID 404
Cdd:COG0410  136 TLSGGEQQMLAIGR----ALmsrPKLL-LLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFALEiADraYVLE 210
                         90       100
                 ....*....|....*....|....
gi 488284725 405 igpfagenGGHVQFSGTYDAFLAS 428
Cdd:COG0410  211 --------RGRIVLEGTAAELLAD 226
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
332-403 9.23e-10

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: 58.16  E-value: 9.23e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 332 LSGGEAQRIKIAK--YVNSALndimYILDEPSAGLHPKDIERISRALLNLKnKGNTVVLVEHNPQLIREADFII 403
Cdd:cd03228   97 LSGGQRQRIAIARalLRDPPI----LILDEATSALDPETEALILEALRALA-KGKTVIVIAHRLSTIRDADRII 165
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
625-713 1.06e-09

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


Pssm-ID: 188353 [Multi-domain]  Cd Length: 206  Bit Score: 58.78  E-value: 1.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  625 LLEVGLsYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI 704
Cdd:TIGR03608 119 LEKVGL-NLKLKQKIYELSGGEQQRVALARAILKPPPLILADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVA 197

                  ....*....
gi 488284725  705 KSADWLIEL 713
Cdd:TIGR03608 198 KQADRVIEL 206
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
625-736 1.32e-09

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: 58.99  E-value: 1.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLE-VGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDV 703
Cdd:cd03219  127 LLErVGLAD-LADRPAGELSYGQQRRLEIARALATDPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDV 205
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488284725 704 IKS-ADWLIELgpeggeNGGQLLFTGTPANMLNS 736
Cdd:cd03219  206 VMSlADRVTVL------DQGRVIAEGTPDEVRNN 233
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
625-737 1.68e-09

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 58.92  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLE-VGLSYlKLNQSLSTLSGGELQRVKLADTL-HQKKaIYLMDEPTDGLhliDIQQS---LQLFNRMVEEGNSLILLEH 699
Cdd:COG1131  115 LLElFGLTD-AADRKVGTLSGGMKQRLGLALALlHDPE-LLILDEPTSGL---DPEARrelWELLRELAAEGKTVLLSTH 189
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488284725 700 HIDVI-KSADWLIELgpeggeNGGQLLFTGTPANMLNST 737
Cdd:COG1131  190 YLEEAeRLCDRVAII------DKGRIVADGTPDELKARL 222
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
627-702 1.72e-09

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: 57.83  E-value: 1.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 627 EVGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQS---LQLFNRMVEEGNSLILLE-HHID 702
Cdd:cd03214   84 LLGLAHLA-DRPFNELSGGERQRVLLARALAQEPPILLLDEPTSHL---DIAHQielLELLRRLARERGKTVVMVlHDLN 159
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
277-405 2.43e-09

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: 57.88  E-value: 2.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 277 SIADAVDMPLtelhsFIRSMDLSLIKNIQEELL--VRLEALINiglsyltlgRATETLSGGEAQRIKIAKyvnsAL-NDI 353
Cdd:cd03255   98 TALENVELPL-----LLAGVPKKERRERAEELLerVGLGDRLN---------HYPSELSGGQQQRVAIAR----ALaNDP 159
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488284725 354 MYIL-DEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEHNPQLIREADFIIDI 405
Cdd:cd03255  160 KIILaDEPTGNLDSETGKEVMELLRELnKEAGTTIVVVTHDPELAEYADRIIEL 213
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
331-399 2.54e-09

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: 57.93  E-value: 2.54e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284725 331 TLSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREA 399
Cdd:cd03235  132 ELSGGQQQRVLLAR----ALvqDPDLLLLDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLGLVLEY 198
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
612-732 5.19e-09

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: 57.58  E-value: 5.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 612 FFKDQPFALSLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRM-VEE 690
Cdd:cd03256  116 LFPKEEKQRALAALERVGLLD-KAYQRADQLSGGQQQRVAIARALMQQPKLILADEPVASLDPASSRQVMDLLKRInREE 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 488284725 691 GNSLILLEHHIDVIKS-ADWLIELgpeggeNGGQLLFTGTPAN 732
Cdd:cd03256  195 GITVIVSLHQVDLAREyADRIVGL------KDGRIVFDGPPAE 231
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
305-403 5.44e-09

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: 57.45  E-value: 5.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLEALIN-IGLSYLtLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKG 383
Cdd:cd03219  117 EREARERAEELLErVGLADL-ADRPAGELSYGQQRRLEIARAL--ATDPKLLLLDEPAAGLNPEETEELAELIRELRERG 193
                         90       100
                 ....*....|....*....|.
gi 488284725 384 NTVVLVEHNPQLIRE-ADFII 403
Cdd:cd03219  194 ITVLLVEHDMDVVMSlADRVT 214
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
595-736 1.01e-08

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: 58.38  E-value: 1.01e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 595 GKNIVEVLALSVKDgydffKDQPFALSLKNLLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHL 674
Cdd:COG1123  102 GDQIAEALENLGLS-----RAEARARVLELLEAVGLERR-LDRYPHQLSGGQRQRVAIAMALALDPDLLIADEPTTALDV 175
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 675 IDIQQSLQLFNRMVEE-GNSLILLEHHIDVI-KSADWLIELgpeggeNGGQLLFTGTPANMLNS 736
Cdd:COG1123  176 TTQAEILDLLRELQRErGTTVLLITHDLGVVaEIADRVVVM------DDGRIVEDGPPEEILAA 233
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
620-699 1.09e-08

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: 58.64  E-value: 1.09e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 620 LSLKNLLevglsylklNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSL---QLFNRMVEEGNSLIL 696
Cdd:COG1245  200 LGLENIL---------DRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYL---DIYQRLnvaRLIRELAEEGKYVLV 267

                 ...
gi 488284725 697 LEH 699
Cdd:COG1245  268 VEH 270
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
332-734 1.42e-08

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: 57.89  E-value: 1.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEHNPQLIRE-ADFIIDIgpfa 409
Cdd:TIGR03269 169 LSGGEKQRVVLARQL--AKEPFLFLADEPTGTLDPQTAKLVHNALEEAvKASGISMVLTSHWPEVIEDlSDKAIWL---- 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  410 gENGGHVQfSGTYDAFLASKTLTSQALQ--EPLPLNDQPRKAR----KSLSIEHATLHNLNNLSVEVPLGVLTVICGVAG 483
Cdd:TIGR03269 243 -ENGEIKE-EGTPDEVVAVFMEGVSEVEkeCEVEVGEPIIKVRnvskRYISVDRGVVKAVDNVSLEVKEGEIFGIVGTSG 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  484 SGKSSLAEEIYQKAQADNQEI--------IHLSQKSITANLRSTPmtYLNIFdkvrklfaeenHVSPALFSYNSkgacpt 555
Cdd:TIGR03269 321 AGKTTLSKIIAGVLEPTSGEVnvrvgdewVDMTKPGPDGRGRAKR--YIGIL-----------HQEYDLYPHRT------ 381
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  556 ckgkgiivsdmsfmedvtsicetchgtrykeeVLhylyngKNIVEVLALSVKDGYDFFKdqpfalSLKNLLEVGLSYLK- 634
Cdd:TIGR03269 382 --------------------------------VL------DNLTEAIGLELPDELARMK------AVITLKMVGFDEEKa 417
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  635 ---LNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPT---DGLHLIDIQQSlqLFNRMVEEGNSLILLEHHIDVIKSAD 708
Cdd:TIGR03269 418 eeiLDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTgtmDPITKVDVTHS--ILKAREEMEQTFIIVSHDMDFVLDVC 495
                         410       420
                  ....*....|....*....|....*.
gi 488284725  709 WLIELgpeggENGGQLLFTGTPANML 734
Cdd:TIGR03269 496 DRAAL-----MRDGKIVKIGDPEEIV 516
cbiO PRK13637
energy-coupling factor transporter ATPase;
305-421 1.72e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 56.59  E-value: 1.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLEALINI-GLSYLTL-GRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KN 381
Cdd:PRK13637 116 EEEIENRVKRAMNIvGLDYEDYkDKSPFELSGGQKRRVAIAGVV--AMEPKILILDEPTAGLDPKGRDEILNKIKELhKE 193
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 488284725 382 KGNTVVLVEHNPQLI-READFIIDIgpfageNGGHVQFSGT 421
Cdd:PRK13637 194 YNMTIILVSHSMEDVaKLADRIIVM------NKGKCELQGT 228
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
307-697 2.08e-08

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


Pssm-ID: 131681 [Multi-domain]  Cd Length: 500  Bit Score: 57.53  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  307 ELLVRLEALI-NIGLSYLTLGRATETLSGGEAQRIKIAKYVNSALNdiMYILDEPSAGLHPKDIERISRALLNLKNKGNT 385
Cdd:TIGR02633 116 AMYLRAKNLLrELQLDADNVTRPVGDYGGGQQQLVEIAKALNKQAR--LLILDEPSSSLTEKETEILLDIIRDLKAHGVA 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  386 VVLVEHNPQLIRE-ADFIIDIgpfagENGGHVqfsGTYDA----------FLASKTLTSQALQEPLPLNDQprkarkSLS 454
Cdd:TIGR02633 194 CVYISHKLNEVKAvCDTICVI-----RDGQHV---ATKDMstmseddiitMMVGREITSLYPHEPHEIGDV------ILE 259
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  455 IEHATLHN--------LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIIHLSQKSItaNLRstpmtylNI 526
Cdd:TIGR02633 260 ARNLTCWDvinphrkrVDDVSFSLRRGEILGVAGLVGAGRTELVQALFGAYPGKFEGNVFINGKPV--DIR-------NP 330
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  527 FDKVRKLFAeenhvspalfsynskgACPTCKGKGIIVSDMSFmedvtsicetchgtrykeevlhylynGKNIvevlALSV 606
Cdd:TIGR02633 331 AQAIRAGIA----------------MVPEDRKRHGIVPILGV--------------------------GKNI----TLSV 364
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  607 KDGYDFFKDQPFALSLKNLLEvGLSYLKLNQS-----LSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSL 681
Cdd:TIGR02633 365 LKSFCFKMRIDAAAELQIIGS-AIQRLKVKTAspflpIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGAKYEIY 443
                         410
                  ....*....|....*.
gi 488284725  682 QLFNRMVEEGNSLILL 697
Cdd:TIGR02633 444 KLINQLAQEGVAIIVV 459
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
325-405 2.23e-08

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: 57.30  E-value: 2.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  325 LGRATETLSGGEAQRIKIAKyvnsALNDI--MYILDEPSAGLHPKDIERISRALLNLKNkGNTVVLVEHNPQLIREADFI 402
Cdd:TIGR02857 452 IGEGGAGLSGGQAQRLALAR----AFLRDapLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRI 526

                  ...
gi 488284725  403 IDI 405
Cdd:TIGR02857 527 VVL 529
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
331-428 2.38e-08

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: 57.45  E-value: 2.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIgpf 408
Cdd:COG4618  467 RLSGGQRQRIGLAR----ALygDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVL--- 539
                         90       100
                 ....*....|....*....|
gi 488284725 409 ageNGGHVQFSGTYDAFLAS 428
Cdd:COG4618  540 ---RDGRVQAFGPRDEVLAR 556
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
642-728 2.58e-08

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: 54.24  E-value: 2.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEgNSLILLEHHIDVIKSADWLIELgpeggENg 721
Cdd:cd03247   99 FSGGERQRLALARILLQDAPIVLLDEPTVGLDPITERQLLSLIFEVLKD-KTLIWITHHLTGIEHMDKILFL-----EN- 171

                 ....*..
gi 488284725 722 GQLLFTG 728
Cdd:cd03247  172 GKIIMQG 178
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
640-736 2.69e-08

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: 57.08  E-value: 2.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVE--EGNSLILLEHHIDVIKSADWLIELgpeg 717
Cdd:COG4988  472 RGLSGGQAQRLALARALLRDAPLLLLDEPTAHL---DAETEAEILQALRRlaKGRTVILITHRLALLAQADRILVL---- 544
                         90
                 ....*....|....*....
gi 488284725 718 geNGGQLLFTGTPANMLNS 736
Cdd:COG4988  545 --DDGRIVEQGTHEELLAK 561
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
634-735 2.73e-08

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 55.32  E-value: 2.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLA-------DTLHQKKAIYLMDEPTDGLhliDI-QQSL--QLFNRMVEEGNSLILLEHHID- 702
Cdd:PRK03695 119 KLGRSVNQLSGGEWQRVRLAavvlqvwPDINPAGQLLLLDEPMNSL---DVaQQAAldRLLSELCQQGIAVVMSSHDLNh 195
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488284725 703 VIKSAD--WLIelgpeggeNGGQLLFTGTPANMLN 735
Cdd:PRK03695 196 TLRHADrvWLL--------KQGKLLASGRRDEVLT 222
cbiO PRK13646
energy-coupling factor transporter ATPase;
614-745 2.97e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 55.94  E-value: 2.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 614 KDQPFALslknLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRM-VEEGN 692
Cdd:PRK13646 122 KNYAHRL----LMDLGFSRDVMSQSPFQMSGGQMRKIAIVSILAMNPDIIVLDEPTAGLDPQSKRQVMRLLKSLqTDENK 197
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488284725 693 SLILLEHHI-DVIKSADWLIELgpeggeNGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK13646 198 TIILVSHDMnEVARYADEVIVM------KEGSIVSQTSPKELFKDKKKLADWHI 245
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
599-704 3.05e-08

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 57.13  E-value: 3.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 599 VEVLALSVKDGYD--FFKD---QPfaLSLKNLLEvglsylklnQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTdgLH 673
Cdd:PRK13409 417 VEDLLRSITDDLGssYYKSeiiKP--LQLERLLD---------KNVKDLSGGELQRVAIAACLSRDADLYLLDEPS--AH 483
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488284725 674 LiDIQQSLQ---LFNRMVEE-GNSLILLEHHIDVI 704
Cdd:PRK13409 484 L-DVEQRLAvakAIRRIAEErEATALVVDHDIYMI 517
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
297-671 3.20e-08

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 56.98  E-value: 3.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 297 DLSLIKNI------QEELLVRLEALINIGLSYLTLGRATETLSGGEAQRIKIakyvnsaLNDIM-----YILDEPSAGLH 365
Cdd:PRK15439 100 NLSVKENIlfglpkRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEI-------LRGLMrdsriLILDEPTASLT 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 366 PKDIERISRALLNLKNKGNTVVLVEHNPQLIRE-ADFIIDIgpfageNGGHVQFSGTYDAF------------LASKTLT 432
Cdd:PRK15439 173 PAETERLFSRIRELLAQGVGIVFISHKLPEIRQlADRISVM------RDGTIALSGKTADLstddiiqaitpaAREKSLS 246
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 433 -SQALQEPLPLNdQPRKARKS--LSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLAEEIY--QKAQA-----DNQ 502
Cdd:PRK15439 247 aSQKLWLELPGN-RRQQAAGApvLTVEDLTGEGFRNISLEVRAGEILGLAGVVGAGRTELAETLYglRPARGgrimlNGK 325
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 503 EIIHLSqksiTANLRSTPMTYLNIFDKVRKLFAEenhvspALFSYNskgacpTCkgkGIIVSDMSFMEDVTSicETCHGT 582
Cdd:PRK15439 326 EINALS----TAQRLARGLVYLPEDRQSSGLYLD------APLAWN------VC---ALTHNRRGFWIKPAR--ENAVLE 384
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 583 RYKEevlhylyngknivevlALSVKdgydfFKDqpfalslknllevglsylkLNQSLSTLSGGELQRVKLADTLHQKKAI 662
Cdd:PRK15439 385 RYRR----------------ALNIK-----FNH-------------------AEQAARTLSGGNQQKVLIAKCLEASPQL 424

                 ....*....
gi 488284725 663 YLMDEPTDG 671
Cdd:PRK15439 425 LIVDEPTRG 433
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
332-403 3.50e-08

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: 53.59  E-value: 3.50e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 332 LSGGEAQRIKIAK--YVNSalnDIMyILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE-ADFII 403
Cdd:cd03216   83 LSVGERQMVEIARalARNA---RLL-ILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDEVFEiADRVT 153
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
635-721 4.05e-08

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: 54.72  E-value: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 635 LNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTdgLHLiDIQQSL---QLFNRMVEEGNSLILLEHHiDVIKS---AD 708
Cdd:cd03237  109 LDREVPELSGGELQRVAIAACLSKDADIYLLDEPS--AYL-DVEQRLmasKVIRRFAENNEKTAFVVEH-DIIMIdylAD 184
                         90
                 ....*....|...
gi 488284725 709 WLIELGPEGGENG 721
Cdd:cd03237  185 RLIVFEGEPSVNG 197
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
636-736 4.59e-08

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 56.00  E-value: 4.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 636 NQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDV-IKSADWLIELG 714
Cdd:PRK09536 134 DRPVTSLSGGERQRVLLARALAQATPVLLLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLA 213
                         90       100
                 ....*....|....*....|..
gi 488284725 715 peggenGGQLLFTGTPANMLNS 736
Cdd:PRK09536 214 ------DGRVRAAGPPADVLTA 229
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
298-433 6.97e-08

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: 54.09  E-value: 6.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 298 LSLIKNIQ----------EELLVRLEALI-NIGLSyLTLGRATETLSGGEAQRIKIAKyvnsAL---NDImYILDEPSAG 363
Cdd:COG4555   89 LTVRENIRyfaelyglfdEELKKRIEELIeLLGLE-EFLDRRVGELSTGMKKKVALAR----ALvhdPKV-LLLDEPTNG 162
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284725 364 LHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE-ADFIIDIgpfageNGGHVQFSGTYDAFLASKTLTS 433
Cdd:COG4555  163 LDVMARRLLREILRALKKEGKTVLFSSHIMQEVEAlCDRVVIL------HKGKVVAQGSLDELREEIGEEN 227
cbiO PRK13641
energy-coupling factor transporter ATPase;
621-745 9.65e-08

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 54.06  E-value: 9.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 621 SLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHH 700
Cdd:PRK13641 125 ALKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVMAYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTHN 204
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 488284725 701 I-DVIKSADWLIELgpeggeNGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK13641 205 MdDVAEYADDVLVL------EHGKLIKHASPKEIFSDKEWLKKHYL 244
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
315-439 1.08e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 54.47  E-value: 1.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 315 LINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQ 394
Cdd:PRK13631 160 LNKMGLDDSYLERSPFGLSGGQKRRVAIAGIL--AIQPEILIFDEPTAGLDPKGEHEMMQLILDAKANNKTVFVITHTME 237
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 488284725 395 LIRE-ADFIIDIgpfageNGGHVQFSGT-YDAFLASKTLTSQALQEP 439
Cdd:PRK13631 238 HVLEvADEVIVM------DKGKILKTGTpYEIFTDQHIINSTSIQVP 278
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
278-415 1.15e-07

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 55.20  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 278 IADAVDMPLTELHSFIRSM-DLSLIKNiqeELLVRLealiniGLSYLtLGRATETLSGGEAQRIKIAkyvnSALN---DI 353
Cdd:PRK13409 409 IKPDYDGTVEDLLRSITDDlGSSYYKS---EIIKPL------QLERL-LDKNVKDLSGGELQRVAIA----ACLSrdaDL 474
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 354 mYILDEPSAGLhpkDIE---RISRALLNL-KNKGNTVVLVEHNPQLIreaDFIID-IGPFAGENGGH 415
Cdd:PRK13409 475 -YLLDEPSAHL---DVEqrlAVAKAIRRIaEEREATALVVDHDIYMI---DYISDrLMVFEGEPGKH 534
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
605-697 1.25e-07

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 52.90  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 605 SVKD----GYDFFKDQPFALSLKNLLE-VGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQ 679
Cdd:COG4619   89 TVRDnlpfPFQLRERKFDRERALELLErLGLPPDILDKPVERLSGGERQRLALIRALLLQPDVLLLDEPTSAL---DPEN 165
                         90       100
                 ....*....|....*....|.
gi 488284725 680 S---LQLFNRMVEEGNSLILL 697
Cdd:COG4619  166 TrrvEELLREYLAEEGRAVLW 186
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
331-429 1.26e-07

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: 55.23  E-value: 1.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAK--YVNSALndimYILDEPSAGLHPKDIERISRALLNLKnKGNTVVLVEHNPQLIREADFIIDIgpf 408
Cdd:COG2274  611 NLSGGQRQRLAIARalLRNPRI----LILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVL--- 682
                         90       100
                 ....*....|....*....|.
gi 488284725 409 ageNGGHVQFSGTYDAFLASK 429
Cdd:COG2274  683 ---DKGRIVEDGTHEELLARK 700
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
332-428 1.28e-07

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: 53.27  E-value: 1.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKN-KGNTVVLVEHNPQLIRE-ADFIIDIGpfa 409
Cdd:cd03261  137 LSGGMKKRVALARAL--ALDPELLLYDEPTAGLDPIASGVIDDLIRSLKKeLGLTSIMVTHDLDTAFAiADRIAVLY--- 211
                         90
                 ....*....|....*....
gi 488284725 410 genGGHVQFSGTYDAFLAS 428
Cdd:cd03261  212 ---DGKIVAEGTPEELRAS 227
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
313-441 1.36e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 53.65  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 313 EALINIGLSYLtLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEH 391
Cdd:PRK13652 120 SALHMLGLEEL-RDRVPHHLSGGEKKRVAIAGVI--AMEPQVLVLDEPTAGLDPQGVKELIDFLNDLpETYGMTVIFSTH 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 488284725 392 NPQLIRE-ADFI--IDIGPFAGEngGHVQfsgtyDAFLASKTLTSQALQEP-LP 441
Cdd:PRK13652 197 QLDLVPEmADYIyvMDKGRIVAY--GTVE-----EIFLQPDLLARVHLDLPsLP 243
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
331-436 1.41e-07

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 52.96  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKYVNSALNdiMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNP-QLIREADfiidiGPFA 409
Cdd:PRK11614 137 TMSGGEQQMLAIGRALMSQPR--LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNAnQALKLAD-----RGYV 209
                         90       100
                 ....*....|....*....|....*..
gi 488284725 410 GENgGHVQFSGTYDAFLASKTLTSQAL 436
Cdd:PRK11614 210 LEN-GHVVLEDTGDALLANEAVRSAYL 235
cbiO PRK13643
energy-coupling factor transporter ATPase;
614-734 1.91e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 53.20  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 614 KDQPFALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNS 693
Cdd:PRK13643 117 KEKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQT 196
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488284725 694 LILLEHHI-DVIKSADWLIELgpeggeNGGQLLFTGTPANML 734
Cdd:PRK13643 197 VVLVTHLMdDVADYADYVYLL------EKGHIISCGTPSDVF 232
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
629-704 1.96e-07

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: 52.26  E-value: 1.96e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284725 629 GLSYLKLNQSLStLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI 704
Cdd:cd03226  115 DLYALKERHPLS-LSGGQKQRLAIAAALLSGKDLLIFDEPTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFL 189
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
298-429 2.08e-07

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: 52.55  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 298 LSLIKNIQEELLVRLEALIN-IGLSYLTLGRATeTLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRAL 376
Cdd:cd03218  100 LEIRGLSKKEREEKLEELLEeFHITHLRKSKAS-SLSGGERRRVEIARAL--ATNPKFLLLDEPFAGVDPIAVQDIQKII 176
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488284725 377 LNLKNKGNTVVLVEHNpqlIREADFIIDIGPFAGEngGHVQFSGTYDAFLASK 429
Cdd:cd03218  177 KILKDRGIGVLITDHN---VRETLSITDRAYIIYE--GKVLAEGTPEEIAANE 224
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
628-716 2.15e-07

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


Pssm-ID: 213194 [Multi-domain]  Cd Length: 162  Bit Score: 51.21  E-value: 2.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 628 VGLSYLKLNQSLSTLSGGELQRVKLADTLH----QKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDV 703
Cdd:cd03227   64 VAAVSAELIFTRLQLSGGEKELSALALILAlaslKPRPLYILDEIDRGLDPRDGQALAEAILEHLVKGAQVIVITHLPEL 143
                         90
                 ....*....|...
gi 488284725 704 IKSADWLIELGPE 716
Cdd:cd03227  144 AELADKLIHIKKV 156
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
332-405 2.32e-07

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 54.34  E-value: 2.32e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 332 LSGGEAQRIKIAKyvnSALNDIMYIL-DEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDI 405
Cdd:PRK10535 145 LSGGQQQRVSIAR---ALMNGGQVILaDEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
629-736 2.41e-07

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 52.68  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 629 GLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL---HLIDIQQSLQLFNRmvEEGNSLILLEHHID-VI 704
Cdd:PRK10253 132 GITHLA-DQSVDTLSGGQRQRAWIAMVLAQETAIMLLDEPTTWLdisHQIDLLELLSELNR--EKGYTLAAVLHDLNqAC 208
                         90       100       110
                 ....*....|....*....|....*....|..
gi 488284725 705 KSADWLIELgpeggeNGGQLLFTGTPANMLNS 736
Cdd:PRK10253 209 RYASHLIAL------REGKIVAQGAPKEIVTA 234
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
320-413 3.52e-07

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: 51.32  E-value: 3.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 320 LSYLTLGRATE------TLSGGEAQRIKIAK--YVNSalnDImYILDEPSAGLHPKDIERI-SRALLNLKNKGNTVVLVE 390
Cdd:cd03250  110 LEILPDGDLTEigekgiNLSGGQKQRISLARavYSDA---DI-YLLDDPLSAVDAHVGRHIfENCILGLLLNNKTRILVT 185
                         90       100
                 ....*....|....*....|...
gi 488284725 391 HNPQLIREADFIIDIgpfagENG 413
Cdd:cd03250  186 HQLQLLPHADQIVVL-----DNG 203
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
628-734 3.58e-07

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: 53.62  E-value: 3.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 628 VGLSYL--KLNQSLST--------LSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVE--EGNSLI 695
Cdd:COG4987  448 VGLGDWlaALPDGLDTwlgeggrrLSGGERRRLALARALLRDAPILLLDEPTEGL---DAATEQALLADLLEalAGRTVL 524
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488284725 696 LLEHHIDVIKSADWLIELGpeggenGGQLLFTGTPANML 734
Cdd:COG4987  525 LITHRLAGLERMDRILVLE------DGRIVEQGTHEELL 557
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
453-721 3.65e-07

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: 51.32  E-value: 3.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 453 LSIEHATLHN----------LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIIH------LSQKS--ITA 514
Cdd:cd03250    1 ISVEDASFTWdsgeqetsftLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVpgsiayVSQEPwiQNG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 515 NLRStpmtylNIfdkvrkLFAEEnhvspalfsYNSKgacptckgkgiivsdmsfmedvtsicetchgtRYKEevlhylyn 594
Cdd:cd03250   81 TIRE------NI------LFGKP---------FDEE--------------------------------RYEK-------- 99
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 595 gknIVEVLALsVKDgydfFKdqpfALSLKNLLEVGlsylklnQSLSTLSGGELQRVKLADTLHQKKAIYLMDEP---TD- 670
Cdd:cd03250  100 ---VIKACAL-EPD----LE----ILPDGDLTEIG-------EKGINLSGGQKQRISLARAVYSDADIYLLDDPlsaVDa 160
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488284725 671 --GLHLIDiqqslQLFNRMVEEGNSLILLEHHIDVIKSADWLIELgpeggENG 721
Cdd:cd03250  161 hvGRHIFE-----NCILGLLLNNKTRILVTHQLQLLPHADQIVVL-----DNG 203
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
440-700 3.69e-07

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: 51.89  E-value: 3.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 440 LPLNDQPRKARKslsiEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLAEeiyqkaqadnqeiihlsqkSITANLRST 519
Cdd:cd03234    4 LPWWDVGLKAKN----WNKYARILNDVSLHVESGQVMAILGSSGSGKTTLLD-------------------AISGRVEGG 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 520 PMTYLNIFdkvrkLFAEENhvSPALFSYNSkgacptckgkgiivsdmSFME--DVTSICETChgtrykEEVLHYlyngkn 597
Cdd:cd03234   61 GTTSGQIL-----FNGQPR--KPDQFQKCV-----------------AYVRqdDILLPGLTV------RETLTY------ 104
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 598 iVEVLALSVK--DGYDFFKDQPFALSLKNLLEVGLSYLKlnqslsTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhli 675
Cdd:cd03234  105 -TAILRLPRKssDAIRKKRVEDVLLRDLALTRIGGNLVK------GISGGERRRVSIAVQLLWDPKVLILDEPTSGL--- 174
                        250       260
                 ....*....|....*....|....*..
gi 488284725 676 DIQQSLQLFNRMVE--EGNSLILLEHH 700
Cdd:cd03234  175 DSFTALNLVSTLSQlaRRNRIVILTIH 201
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
463-735 3.73e-07

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: 51.85  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 463 LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQ-------KAQADNQEIIHLSQKSITANLRSTPMtylnifDKVrklfa 535
Cdd:cd03253   17 LKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRfydvssgSILIDGQDIREVTLDSLRRAIGVVPQ------DTV----- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 536 eenhvspaLFS----YNSKGACPTckgkgiiVSDmsfmEDVTSICETCHgtrykeevlhylyngknIVEVLaLSVKDGYD 611
Cdd:cd03253   86 --------LFNdtigYNIRYGRPD-------ATD----EEVIEAAKAAQ-----------------IHDKI-MRFPDGYD 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 612 ffkdqpfalslknlLEVGLSYLKLnqslstlSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRmVEEG 691
Cdd:cd03253  129 --------------TIVGERGLKL-------SGGEKQRVAIARAILKNPPILLLDEATSALDTHTEREIQAALRD-VSKG 186
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 488284725 692 NSLILLEHHIDVIKSADWLIELgpeggeNGGQLLFTGTPANMLN 735
Cdd:cd03253  187 RTTIVIAHRLSTIVNADKIIVL------KDGRIVERGTHEELLA 224
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
331-398 3.73e-07

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 51.59  E-value: 3.73e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284725 331 TLSGGEAQRIKIAKYVnsaLND-IMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE 398
Cdd:COG2884  137 ELSGGEQQRVAIARAL---VNRpELLLADEPTGNLDPETSWEIMELLEEINRRGTTVLIATHDLELVDR 202
cbiO PRK13649
energy-coupling factor transporter ATPase;
614-731 3.84e-07

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 52.44  E-value: 3.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 614 KDQPFALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNS 693
Cdd:PRK13649 118 QEEAEALAREKLALVGISESLFEKNPFELSGGQMRRVAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMT 197
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488284725 694 LILLEHHI-DVIKSADWLIELgpeggeNGGQLLFTGTPA 731
Cdd:PRK13649 198 IVLVTHLMdDVANYADFVYVL------EKGKLVLSGKPK 230
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
619-728 4.20e-07

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: 51.42  E-value: 4.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 619 ALSLKNLLEVGlsylklNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVEEG-NSLILL 697
Cdd:cd03264  114 VLELVNLGDRA------KKKIGSLSGGMRRRVGIAQALVGDPSILIVDEPTAGL---DPEERIRFRNLLSELGeDRIVIL 184
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488284725 698 EHHI--DVIKSADWLIELgpeggeNGGQLLFTG 728
Cdd:cd03264  185 STHIveDVESLCNQVAVL------NKGKLVFEG 211
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
610-742 4.60e-07

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 52.55  E-value: 4.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 610 YDFFKDQ--------PFALSLKN----------LLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDG 671
Cdd:PRK13631 127 YQLFKDTiekdimfgPVALGVKKseakklakfyLNKMGLDDSYLERSPFGLSGGQKRRVAIAGILAIQPEILIFDEPTAG 206
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 672 LHLIDIQQSLQLFNRMVEEGNSLILLEHHID-VIKSADWLIELgpeggeNGGQLLFTGTPANMLNSTHSITK 742
Cdd:PRK13631 207 LDPKGEHEMMQLILDAKANNKTVFVITHTMEhVLEVADEVIVM------DKGKILKTGTPYEIFTDQHIINS 272
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
641-705 4.68e-07

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: 51.34  E-value: 4.68e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284725 641 TLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRM-VEEGNSLILLEHHIDVIK 705
Cdd:cd03298  128 ELSGGERQRVALARVLVRDKPVLLLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAK 193
PTZ00243 PTZ00243
ABC transporter; Provisional
332-434 8.51e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 52.86  E-value: 8.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  332 LSGGEAQRIKIAKYVNSalNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIGpfage 411
Cdd:PTZ00243  783 LSGGQKARVSLARAVYA--NRDVYLLDDPLSALDAHVGERVVEECFLGALAGKTRVLATHQVHVVPRADYVVALG----- 855
                          90       100
                  ....*....|....*....|....*.
gi 488284725  412 nGGHVQFSGTYDAFLAS---KTLTSQ 434
Cdd:PTZ00243  856 -DGRVEFSGSSADFMRTslyATLAAE 880
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
325-407 9.91e-07

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 50.68  E-value: 9.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 325 LGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKnKGNTVVLVEHNP-QLIREADF-- 401
Cdd:PRK14247 140 LDAPAGKLSGGQQQRLCIARAL--AFQPEVLLADEPTANLDPENTAKIESLFLELK-KDMTIVLVTHFPqQAARISDYva 216
                         90
                 ....*....|..
gi 488284725 402 ------IIDIGP 407
Cdd:PRK14247 217 flykgqIVEWGP 228
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
635-731 1.00e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 51.17  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 635 LNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHHIDVIKSADWLIEL 713
Cdd:PRK13635 134 LNREPHRLSGGQKQRVAIAGVLALQPDIIILDEATSMLDPRGRREVLETVRQLKEQKGiTVLSITHDLDEAAQADRVIVM 213
                         90
                 ....*....|....*...
gi 488284725 714 gpeggeNGGQLLFTGTPA 731
Cdd:PRK13635 214 ------NKGEILEEGTPE 225
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
636-730 1.00e-06

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 50.78  E-value: 1.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 636 NQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVE---EGNSLILLEHHID-VIKSADWLI 711
Cdd:PRK11231 133 DRRLTDLSGGQRQRAFLAMVLAQDTPVVLLDEPTTYL---DINHQVELMRLMRElntQGKTVVTVLHDLNqASRYCDHLV 209
                         90
                 ....*....|....*....
gi 488284725 712 ELgpeggeNGGQLLFTGTP 730
Cdd:PRK11231 210 VL------ANGHVMAQGTP 222
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
628-737 1.05e-06

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 50.94  E-value: 1.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 628 VGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL---HLIDIqqsLQLFNRMVEE-GNSLILLEHHIDV 703
Cdd:PRK10575 135 VGLKPLA-HRLVDSLSGGERQRAWIAMLVAQDSRCLLLDEPTSALdiaHQVDV---LALVHRLSQErGLTVIAVLHDINM 210
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488284725 704 -IKSADWLIELgpeggeNGGQLLFTGTPANMLNST 737
Cdd:PRK10575 211 aARYCDYLVAL------RGGEMIAQGTPAELMRGE 239
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
314-403 1.22e-06

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: 49.36  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 314 ALINIGLSYLtLGRATETLSGGEAQRIKIAKyvnsALN---DIMyILDEPSAGLhpkDIeRISRALLNL-----KNKGNT 385
Cdd:cd03214   81 ALELLGLAHL-ADRPFNELSGGERQRVLLAR----ALAqepPIL-LLDEPTSHL---DI-AHQIELLELlrrlaRERGKT 150
                         90
                 ....*....|....*....
gi 488284725 386 VVLVEHNPQL-IREADFII 403
Cdd:cd03214  151 VVMVLHDLNLaARYADRVI 169
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
620-699 1.23e-06

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 51.73  E-value: 1.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 620 LSLKNLLevglsylklNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFN--RMVEEGNSLILL 697
Cdd:PRK13409 200 LGLENIL---------DRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYL---DIRQRLNVARliRELAEGKYVLVV 267

                 ..
gi 488284725 698 EH 699
Cdd:PRK13409 268 EH 269
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
642-739 1.30e-06

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: 50.38  E-value: 1.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEE-GNSLILLEHHID-VIKSADWLIELgpegge 719
Cdd:cd03295  136 LSGGQQQRVGVARALAADPPLLLMDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDeAFRLADRIAIM------ 209
                         90       100
                 ....*....|....*....|
gi 488284725 720 NGGQLLFTGTPANMLNSTHS 739
Cdd:cd03295  210 KNGEIVQVGTPDEILRSPAN 229
cbiO PRK13645
energy-coupling factor transporter ATPase;
327-403 1.31e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 50.78  E-value: 1.31e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284725 327 RATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEHN-PQLIREADFII 403
Cdd:PRK13645 146 RSPFELSGGQKRRVALAGII--AMDGNTLVLDEPTGGLDPKGEEDFINLFERLnKEYKKRIIMVTHNmDQVLRIADEVI 222
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
642-745 1.39e-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: 49.11  E-value: 1.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSL---QLFNRMVEEGN-SLILLEHHIDVIKS-ADWLIELGPE 716
Cdd:cd03222   72 LSGGELQRVAIAAALLRNATFYLFDEPSAYL---DIEQRLnaaRAIRRLSEEGKkTALVVEHDLAVLDYlSDRIHVFEGE 148
                         90       100
                 ....*....|....*....|....*....
gi 488284725 717 GGENGGQLlftgTPANMLNSTHSITKGYL 745
Cdd:cd03222  149 PGVYGIAS----QPKGTREGINRFLRGYL 173
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
332-407 1.50e-06

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 50.23  E-value: 1.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKgNTVVLVEHNP-QLIREADF--------I 402
Cdd:PRK14267 150 LSGGQRQRLVIARAL--AMKPKILLMDEPTANIDPVGTAKIEELLFELKKE-YTIVLVTHSPaQAARVSDYvaflylgkL 226

                 ....*
gi 488284725 403 IDIGP 407
Cdd:PRK14267 227 IEVGP 231
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
622-719 1.53e-06

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 49.71  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 622 LKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLIL-LEHH 700
Cdd:PRK10247 118 LDDLERFALPDTILTKNIAELSGGEKQRISLIRNLQFMPKVLLLDEITSALDESNKHNVNEIIHRYVREQNIAVLwVTHD 197
                         90
                 ....*....|....*....
gi 488284725 701 IDVIKSADWLIELGPEGGE 719
Cdd:PRK10247 198 KDEINHADKVITLQPHAGE 216
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
463-669 1.56e-06

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: 48.41  E-value: 1.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  463 LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIihlsqksitaNLRSTPMTYLNIfDKVRKlfaeenHVsp 542
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTI----------LLDGQDLTDDER-KSLRK------EI-- 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  543 alfsynskgacptckgkGIIVSDMSFMEDVTsicetchgtrykeevlhylyNGKNIVEVLALsvkdgYDFFKDQPFALSL 622
Cdd:pfam00005  62 -----------------GYVFQDPQLFPRLT--------------------VRENLRLGLLL-----KGLSKREKDARAE 99
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 488284725  623 KNLLEVGLSYL---KLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPT 669
Cdd:pfam00005 100 EALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARALLTKPKLLLLDEPT 149
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
313-403 1.56e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 50.40  E-value: 1.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 313 EALINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEH 391
Cdd:PRK13634 127 EMIELVGLPEELLARSPFELSGGQMRRVAIAGVL--AMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLhKEKGLTTVLVTH 204
                         90
                 ....*....|...
gi 488284725 392 NPQ-LIREADFII 403
Cdd:PRK13634 205 SMEdAARYADQIV 217
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
304-415 1.71e-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: 51.32  E-value: 1.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 304 IQEELLVRLealiniGLSYLtLGRATETLSGGEAQRIKIAkyvnSALN---DImYILDEPSAGLhpkDIE---RISRALL 377
Cdd:COG1245  435 YKTEIIKPL------GLEKL-LDKNVKDLSGGELQRVAIA----ACLSrdaDL-YLLDEPSAHL---DVEqrlAVAKAIR 499
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 488284725 378 NL-KNKGNTVVLVEHNPQLIreaDFIID-IGPFAGENGGH 415
Cdd:COG1245  500 RFaENRGKTAMVVDHDIYLI---DYISDrLMVFEGEPGVH 536
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
641-718 2.08e-06

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: 48.30  E-value: 2.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284725 641 TLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGG 718
Cdd:cd03223   91 VLSGGEQQRLAFARLLLHKPKFVFLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
628-702 2.25e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 50.08  E-value: 2.25e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 628 VGL--SYLKlnQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID 702
Cdd:PRK13651 152 VGLdeSYLQ--RSPFELSGGQKRRVALAGILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDLD 226
cbiO PRK13641
energy-coupling factor transporter ATPase;
312-441 2.38e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 49.83  E-value: 2.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 312 LEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEH 391
Cdd:PRK13641 126 LKWLKKVGLSEDLISKSPFELSGGQMRRVAIAGVM--AYEPEILCLDEPAAGLDPEGRKEMMQLFKDYQKAGHTVILVTH 203
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 488284725 392 NPQLIreADFIIDIgpFAGENGGHVQFSGTYDAFLASKTLTSQALQEPLP 441
Cdd:PRK13641 204 NMDDV--AEYADDV--LVLEHGKLIKHASPKEIFSDKEWLKKHYLDEPAT 249
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
276-403 2.47e-06

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: 49.10  E-value: 2.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 276 KSIADAVDMPLTelhsfirsmdLSLIKNIQE-ELLVRlEALINIGLSYLTLGRATET-LSGGEAQRIKIAKYVnsALNDI 353
Cdd:cd03260   95 GSIYDNVAYGLR----------LHGIKLKEElDERVE-EALRKAALWDEVKDRLHALgLSGGQQQRLCLARAL--ANEPE 161
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488284725 354 MYILDEPSAGLHPKDIERISRALLNLKNKgNTVVLVEHNP-QLIREADFII 403
Cdd:cd03260  162 VLLLDEPTSALDPISTAKIEELIAELKKE-YTIVIVTHNMqQAARVADRTA 211
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
330-398 2.54e-06

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: 48.82  E-value: 2.54e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGEAQRIKiakYVNSALNDI-MYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE 398
Cdd:cd03269  127 EELSKGNQQKVQ---FIAAVIHDPeLLILDEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVEE 193
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
330-491 2.65e-06

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 50.80  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGEAQRIKIAKyvnsAL---NDIMyILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNpqlIRE----ADFI 402
Cdd:COG3845  140 EDLSVGEQQRVEILK----ALyrgARIL-ILDEPTAVLTPQEADELFEILRRLAAEGKSIIFITHK---LREvmaiADRV 211
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 403 IDIgpfageNGGHVqfSGTYDAflasKTLTSQALQE-------PLPLNDQPRKARKS-LSIEHATLHN------LNNLSV 468
Cdd:COG3845  212 TVL------RRGKV--VGTVDT----AETSEEELAElmvgrevLLRVEKAPAEPGEVvLEVENLSVRDdrgvpaLKDVSL 279
                        170       180
                 ....*....|....*....|....*..
gi 488284725 469 EVP----LGvltvICGVAGSGKSSLAE 491
Cdd:COG3845  280 EVRageiLG----IAGVAGNGQSELAE 302
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
623-730 3.01e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 49.63  E-value: 3.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 623 KNLLE-VGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHH 700
Cdd:PRK13634 126 REMIElVGLPEELLARSPFELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDPKGRKEMMEMFYKLHKEKGlTTVLVTHS 205
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 701 I-DVIKSADWLIELgpeggeNGGQLLFTGTP 730
Cdd:PRK13634 206 MeDAARYADQIVVM------HKGTVFLQGTP 230
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
636-745 3.09e-06

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 49.62  E-value: 3.09e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 636 NQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI-KSADWLIELg 714
Cdd:PRK13638 131 HQPIQCLSHGQKKRVAIAGALVLQARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVL- 209
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 715 peggeNGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK13638 210 -----RQGQILTHGAPGEVFACTEAMEQAGL 235
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
276-431 3.78e-06

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 50.06  E-value: 3.78e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 276 KSIADAVDMPLTELHSFIRSMDLSLIK--------NIQEELLVRLEA-------------LINIGLSYLTLGRATETLSG 334
Cdd:COG0488   76 LTVLDTVLDGDAELRALEAELEELEAKlaepdedlERLAELQEEFEAlggweaearaeeiLSGLGFPEEDLDRPVSELSG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 335 GEAQRIKIAKyvnsAL---NDIMyILDEPSAGLhpkDIERISRaLLN-LKNKGNTVVLVEHNPQLIRE-ADFIIDIgpfa 409
Cdd:COG0488  156 GWRRRVALAR----ALlsePDLL-LLDEPTNHL---DLESIEW-LEEfLKNYPGTVLVVSHDRYFLDRvATRILEL---- 222
                        170       180
                 ....*....|....*....|..
gi 488284725 410 gENGGHVQFSGTYDAFLASKTL 431
Cdd:COG0488  223 -DRGKLTLYPGNYSAYLEQRAE 243
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
623-713 3.82e-06

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: 48.64  E-value: 3.82e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 623 KNLLE-VGLSyLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQS---LQLFNRMVEE-GNSLILL 697
Cdd:cd03255  122 EELLErVGLG-DRLNHYPSELSGGQQQRVAIARALANDPKIILADEPTGNL---DSETGkevMELLRELNKEaGTTIVVV 197
                         90
                 ....*....|....*.
gi 488284725 698 EHHIDVIKSADWLIEL 713
Cdd:cd03255  198 THDPELAEYADRIIEL 213
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
625-733 3.88e-06

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 48.90  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLE-VGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDI---QQSLQLFNRMVEE-GNSLILLEH 699
Cdd:COG3638  130 ALErVGLAD-KAYQRADQLSGGQQQRVAIARALVQEPKLILADEPVASL---DPktaRQVMDLLRRIAREdGITVVVNLH 205
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488284725 700 HIDVIKS-ADWLIelgpegGENGGQLLFTGTPANM 733
Cdd:COG3638  206 QVDLARRyADRII------GLRDGRVVFDGPPAEL 234
UvrA_DNA-bind pfam17755
UvrA DNA-binding domain;
154-232 4.06e-06

UvrA DNA-binding domain;


Pssm-ID: 465484 [Multi-domain]  Cd Length: 110  Bit Score: 46.31  E-value: 4.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  154 DYDKSLNEGPIDFPTFTVGNWRWKRYA----HSGlFDLDKKIKDYSPEELALFLYAPQQKL-----ANPPKEWPHTALYE 224
Cdd:pfam17755   8 DPSLSLAEGAIAPWGKKRSSYYFQLLEalakHYG-FDLDTPFKDLPEEQQDIILYGSGEEIivfyySRGGRTRTYTKPFE 86

                  ....*...
gi 488284725  225 GIVPRMQR 232
Cdd:pfam17755  87 GVIPNLER 94
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
332-396 4.56e-06

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 48.92  E-value: 4.56e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLI 396
Cdd:PRK13639 138 LSGGQKKRVAIAGIL--AMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLV 200
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
330-402 5.15e-06

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: 47.91  E-value: 5.15e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 330 ETLSGGEAQRIKIAKYvnSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIR--EADFI 402
Cdd:cd03217  103 EGFSGGEKKRNEILQL--LLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHYQRLLDyiKPDRV 175
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
331-393 5.89e-06

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: 49.67  E-value: 5.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284725  331 TLSGGEAQRIKIAKyvnsAL---NDIMyILDEPSAGLHPKDIERISRALLNlKNKGNTVVLVEHNP 393
Cdd:TIGR02868 471 RLSGGERQRLALAR----ALladAPIL-LLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
305-403 6.31e-06

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: 47.89  E-value: 6.31e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALN-DIMyILDEPSAGLHPKDIERISRALLNLKNK- 382
Cdd:cd03257  119 EARKEAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARAL--ALNpKLL-IADEPTSALDVSVQAQILDLLKKLQEEl 195
                         90       100
                 ....*....|....*....|..
gi 488284725 383 GNTVVLVEHNPQLIRE-ADFII 403
Cdd:cd03257  196 GLTLLFITHDLGVVAKiADRVA 217
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
332-458 6.74e-06

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 49.57  E-value: 6.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsaLND--IMyILDEPSAGLHPKDIERISRALLNLKnKGNTVVLVEHNPQLIREADFIIDIgpfa 409
Cdd:PRK13657 472 LSGGERQRLAIARAL---LKDppIL-ILDEATSALDVETEAKVKAALDELM-KGRTTFIIAHRLSTVRNADRILVF---- 542
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 488284725 410 gENgGHVQFSGTYDAFLASKTLTSQALQEPLPLNDQPRkaRKSLSIEHA 458
Cdd:PRK13657 543 -DN-GRVVESGSFDELVARGGRFAALLRAQGMLQEDER--RKQPAAEGA 587
cbiO PRK13643
energy-coupling factor transporter ATPase;
305-469 6.88e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 48.58  E-value: 6.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGN 384
Cdd:PRK13643 118 EKAEKIAAEKLEMVGLADEFWEKSPFELSGGQMRRVAIAGIL--AMEPEVLVLDEPTAGLDPKARIEMMQLFESIHQSGQ 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 385 TVVLVEHNPQLIRE-ADFIIDIgpfageNGGHVQFSGT-YDAFLASKTLTSQALQEPLPLN--DQPRKAR----KSLSIE 456
Cdd:PRK13643 196 TVVLVTHLMDDVADyADYVYLL------EKGHIISCGTpSDVFQEVDFLKAHELGVPKATHfaDQLQKTGavtfEKLPIT 269
                        170
                 ....*....|....
gi 488284725 457 HATLHN-LNNLSVE 469
Cdd:PRK13643 270 RAELVTlLTSLSVN 283
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
642-713 7.08e-06

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: 46.83  E-value: 7.08e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIEL 713
Cdd:cd03246   97 LSGGQRQRLGLARALYGNPRILVLDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVL 168
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
313-396 8.20e-06

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: 47.40  E-value: 8.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 313 EALINIGLSYLTLGRATEtLSGGEAQRIKIAKYVNSalNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHN 392
Cdd:cd03292  119 AALELVGLSHKHRALPAE-LSGGEQQRVAIARAIVN--SPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATHA 195

                 ....
gi 488284725 393 PQLI 396
Cdd:cd03292  196 KELV 199
cbiO PRK13644
energy-coupling factor transporter ATPase;
310-493 8.30e-06

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 48.06  E-value: 8.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 310 VRLEALINIGLSYLTLG----RATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNT 385
Cdd:PRK13644 111 IEIRKRVDRALAEIGLEkyrhRSPKTLSGGQGQCVALAGIL--TMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKT 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 386 VVLVEHNPQLIREADFIIDIgpfageNGGHVQFSGTYDAFLASKTLTSQALQEPlplndqprkarkSLsIEHAtlHNLNN 465
Cdd:PRK13644 189 IVYITHNLEELHDADRIIVM------DRGKIVLEGEPENVLSDVSLQTLGLTPP------------SL-IELA--ENLKM 247
                        170       180
                 ....*....|....*....|....*...
gi 488284725 466 LSVEVPLGvltvicgvAGSGKSSLAEEI 493
Cdd:PRK13644 248 HGVVIPWE--------NTSSPSSFAEEI 267
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
628-735 8.75e-06

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 47.44  E-value: 8.75e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 628 VGLSYLKlnQSL-STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDI---QQSLQLFNRMVEE-GNSLILLEHHI- 701
Cdd:COG3840  117 VGLAGLL--DRLpGQLSGGQRQRVALARCLVRKRPILLLDEPFSAL---DPalrQEMLDLVDELCRErGLTVLMVTHDPe 191
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488284725 702 DVIKSADWLIELgpeggeNGGQLLFTGTPANMLN 735
Cdd:COG3840  192 DAARIADRVLLV------ADGRIAADGPTAALLD 219
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
640-735 9.15e-06

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: 49.06  E-value: 9.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliD------IQQSLQLFNRmveeGNSLILLEHHIDVIKSADWLIEL 713
Cdd:COG2274  610 SNLSGGQRQRLAIARALLRNPRILILDEATSAL---DaeteaiILENLRRLLK----GRTVIIIAHRLSTIRLADRIIVL 682
                         90       100
                 ....*....|....*....|..
gi 488284725 714 gpeggeNGGQLLFTGTPANMLN 735
Cdd:COG2274  683 ------DKGRIVEDGTHEELLA 698
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
332-426 9.17e-06

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 47.85  E-value: 9.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKgNTVVLVEHNPQlirEADFIIDIGPFAgE 411
Cdd:PRK14239 149 LSGGQQQRVCIARVL--ATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSMQ---QASRISDRTGFF-L 221
                         90
                 ....*....|....*
gi 488284725 412 NGGHVQFSGTYDAFL 426
Cdd:PRK14239 222 DGDLIEYNDTKQMFM 236
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
331-429 9.49e-06

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 49.01  E-value: 9.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAK--YVNSALndimYILDEPSAGLhpkDIE---RISRALLNLKnKGNTVVLVEHNPQLIREADFIIDI 405
Cdd:COG1132  476 NLSGGQRQRIAIARalLKDPPI----LILDEATSAL---DTEteaLIQEALERLM-KGRTTIVIAHRLSTIRNADRILVL 547
                         90       100
                 ....*....|....*....|....
gi 488284725 406 gpfageNGGHVQFSGTYDAFLASK 429
Cdd:COG1132  548 ------DDGRIVEQGTHEELLARG 565
cbiO PRK13645
energy-coupling factor transporter ATPase;
608-742 1.01e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 48.08  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 608 DGYDFFKDQPFALSLKNLLEvglSYLKlnQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRM 687
Cdd:PRK13645 122 NKQEAYKKVPELLKLVQLPE---DYVK--RSPFELSGGQKRRVALAGIIAMDGNTLVLDEPTGGLDPKGEEDFINLFERL 196
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 688 -VEEGNSLILLEHHID-VIKSADWLIELgpeggeNGGQLLFTGTPANMLNSTHSITK 742
Cdd:PRK13645 197 nKEYKKRIIMVTHNMDqVLRIADEVIVM------HEGKVISIGSPFEIFSNQELLTK 247
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
299-405 1.04e-05

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: 45.90  E-value: 1.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 299 SLIKNIQEELLV---RLEALINIGLSYLtlgratETLSGGEAQRIKIAKYVNSALNdiMYILDEPSAGLhpkDIEriSRA 375
Cdd:cd03221   41 TLLKLIAGELEPdegIVTWGSTVKIGYF------EQLSGGEKMRLALAKLLLENPN--LLLLDEPTNHL---DLE--SIE 107
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488284725 376 LLN--LKNKGNTVVLVEHNPQLIRE-ADFIIDI 405
Cdd:cd03221  108 ALEeaLKEYPGTVILVSHDRYFLDQvATKIIEL 140
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
306-429 1.05e-05

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 48.67  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 306 EELLvrlEALINIGLSYLT---------LGRATETLSGGEAQRIKIAKYVnsaLND--IMyILDEPSAGLHpKDIERISR 374
Cdd:PRK11160 444 EALI---EVLQQVGLEKLLeddkglnawLGEGGRQLSGGEQRRLGIARAL---LHDapLL-LLDEPTEGLD-AETERQIL 515
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 375 ALLNLKNKGNTVVLVEHNPQLIREADFIIDIgpfageNGGHVQFSGTYDAFLASK 429
Cdd:PRK11160 516 ELLAEHAQNKTVLMITHRLTGLEQFDRICVM------DNGQIIEQGTHQELLAQQ 564
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
294-392 1.07e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 48.16  E-value: 1.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 294 RSMDLSliKNIQEELLVRLEALINIGLSYLTlgRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERIS 373
Cdd:PRK13651 132 VSMGVS--KEEAKKRAAKYIELVGLDESYLQ--RSPFELSGGQKRRVALAGIL--AMEPDFLVFDEPTAGLDPQGVKEIL 205
                         90
                 ....*....|....*....
gi 488284725 374 RALLNLKNKGNTVVLVEHN 392
Cdd:PRK13651 206 EIFDNLNKQGKTIILVTHD 224
cbiO PRK13649
energy-coupling factor transporter ATPase;
307-391 1.28e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 47.82  E-value: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 307 ELLVRlEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTV 386
Cdd:PRK13649 122 EALAR-EKLALVGISESLFEKNPFELSGGQMRRVAIAGIL--AMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTI 198

                 ....*
gi 488284725 387 VLVEH 391
Cdd:PRK13649 199 VLVTH 203
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
637-727 1.35e-05

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 47.18  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 637 QSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID-VIKSAD--WLIEL 713
Cdd:PRK11614 133 QRAGTMSGGEQQMLAIGRALMSQPRLLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLVEQNANqALKLADrgYVLEN 212
                         90
                 ....*....|....
gi 488284725 714 GPEGGENGGQLLFT 727
Cdd:PRK11614 213 GHVVLEDTGDALLA 226
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
301-402 1.53e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 47.35  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 301 IKNIQEELLVRLEALINIGL---SYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALL 377
Cdd:PRK14246 120 IKEKREIKKIVEECLRKVGLwkeVYDRLNSPASQLSGGQQQRLTIARAL--ALKPKVLLMDEPTSMIDIVNSQAIEKLIT 197
                         90       100
                 ....*....|....*....|....*.
gi 488284725 378 NLKNKgNTVVLVEHNPQLI-READFI 402
Cdd:PRK14246 198 ELKNE-IAIVIVSHNPQQVaRVADYV 222
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
599-702 1.59e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 47.27  E-value: 1.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 599 VEVLALSvkdgydffKDQPFALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQ 678
Cdd:PRK10619 118 IQVLGLS--------KQEARERAVKYLAKVGIDERAQGKYPVHLSGGQQQRVSIARALAMEPEVLLFDEPTSALDPELVG 189
                         90       100
                 ....*....|....*....|....
gi 488284725 679 QSLQLFNRMVEEGNSLILLEHHID 702
Cdd:PRK10619 190 EVLRIMQQLAEEGKTMVVVTHEMG 213
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
332-429 1.65e-05

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: 46.90  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsALN-DIMyILDEPSAGLHPKDIERISRALLNLKNK-GNTVVLVEHNPQLIRE-ADFIIDIGpf 408
Cdd:COG1127  142 LSGGMRKRVALARAL--ALDpEIL-LYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAFAiADRVAVLA-- 216
                         90       100
                 ....*....|....*....|.
gi 488284725 409 agenGGHVQFSGTYDAFLASK 429
Cdd:COG1127  217 ----DGKIIAEGTPEELLASD 233
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
330-442 1.71e-05

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 46.81  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNpqlIREADFIIDIGPFA 409
Cdd:PRK10895 136 QSLSGGERRRVEIARAL--AANPKFILLDEPFAGVDPISVIDIKRIIEHLRDSGLGVLITDHN---VRETLAVCERAYIV 210
                         90       100       110
                 ....*....|....*....|....*....|...
gi 488284725 410 GEngGHVQFSGTYDAFLASKTLTSQALQEPLPL 442
Cdd:PRK10895 211 SQ--GHLIAHGTPTEILQDEHVKRVYLGEDFRL 241
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
463-699 1.85e-05

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: 46.63  E-value: 1.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 463 LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIIHLSQKsiTANLRSTPMTYLNifdkvRKLfaeenhvsp 542
Cdd:cd03292   17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQD--VSDLRGRAIPYLR-----RKI--------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 543 alfsynskgacptckgkGIIVSDMSFMEDVTSIcetchgtrykeevlhylyngKNIVEVLALSVKDGYDFFKDQPFALSL 622
Cdd:cd03292   81 -----------------GVVFQDFRLLPDRNVY--------------------ENVAFALEVTGVPPREIRKRVPAALEL 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 623 knlleVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEH 699
Cdd:cd03292  124 -----VGLSH-KHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTWEIMNLLKKINKAGTTVVVATH 194
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
634-735 2.18e-05

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: 46.27  E-value: 2.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKS-AD--WL 710
Cdd:cd03224  125 RRKQLAGTLSGGEQQMLAIARALMSRPKLLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFALEiADraYV 204
                         90       100
                 ....*....|....*....|....*
gi 488284725 711 IElgpeggenGGQLLFTGTPANMLN 735
Cdd:cd03224  205 LE--------RGRVVLEGTAAELLA 221
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
308-696 2.19e-05

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 47.69  E-value: 2.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 308 LLVRLealiniGLSYLTLGRATEtLSGGEAQRIKIAKYVNSALNDImyILDEPSAGLHPKDIERISRALLNLKNKGNTVV 387
Cdd:PRK10762 125 LLARL------NLRFSSDKLVGE-LSIGEQQMVEIAKVLSFESKVI--IMDEPTDALTDTETESLFRVIRELKSQGRGIV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 388 LVEHNPQLIREadfIIDI------GPFAGENgghvqfsgtydaflASKTLTSQALQEPL---PLNDQ-PRKAR----KSL 453
Cdd:PRK10762 196 YISHRLKEIFE---ICDDvtvfrdGQFIAER--------------EVADLTEDSLIEMMvgrKLEDQyPRLDKapgeVRL 258
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 454 SIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYqKAQADNQEIIHLSQKSITANlrsTPMTYLNifdkvrkl 533
Cdd:PRK10762 259 KVDNLSGPGVNDVSFTLRKGEILGVSGLMGAGRTELMKVLY-GALPRTSGYVTLDGHEVVTR---SPQDGLA-------- 326
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 534 faeenhvspALFSYNSKGAcptcKGKGIIVsDMSFMEDVtSICetchgtrykeeVLHYLYNG----KNIVEVLALSvkdg 609
Cdd:PRK10762 327 ---------NGIVYISEDR----KRDGLVL-GMSVKENM-SLT-----------ALRYFSRAggslKHADEQQAVS---- 376
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 610 yDFFKdqpfALSLKNLlevglsylKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVE 689
Cdd:PRK10762 377 -DFIR----LFNIKTP--------SMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVDVGAKKEIYQLINQFKA 443

                 ....*..
gi 488284725 690 EGNSLIL 696
Cdd:PRK10762 444 EGLSIIL 450
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
332-401 2.23e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 46.57  E-value: 2.23e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGN-TVVLVEHN-PQLIREADF 401
Cdd:PRK14258 151 LSGGQQQRLCIARAL--AVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSElTMVIVSHNlHQVSRLSDF 220
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
642-713 2.27e-05

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: 46.17  E-value: 2.27e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGL--HLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIEL 713
Cdd:cd03290  141 LSGGQRQRICVARALYQNTNIVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWIIAM 214
cbiO PRK13637
energy-coupling factor transporter ATPase;
628-735 2.32e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 46.96  E-value: 2.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 628 VGLSYLKL-NQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHI--DVI 704
Cdd:PRK13637 130 VGLDYEDYkDKSPFELSGGQKRRVAIAGVVAMEPKILILDEPTAGLDPKGRDEILNKIKELHKEYNMTIILVSHSmeDVA 209
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 705 KSADWLIELgpeggeNGGQLLFTGTPANMLN 735
Cdd:PRK13637 210 KLADRIIVM------NKGKCELQGTPREVFK 234
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
330-427 2.54e-05

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 47.37  E-value: 2.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGEAQRIKIAKYVNSALNdiMYILDEPSAGLhpkDIEriSRALLN--LKN-KGnTVVLVEHNPQLIRE-ADFIIDI 405
Cdd:COG0488  431 GVLSGGEKARLALAKLLLSPPN--VLLLDEPTNHL---DIE--TLEALEeaLDDfPG-TVLLVSHDRYFLDRvATRILEF 502
                         90       100
                 ....*....|....*....|..
gi 488284725 406 gpfagENGGHVQFSGTYDAFLA 427
Cdd:COG0488  503 -----EDGGVREYPGGYDDYLE 519
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
642-713 2.55e-05

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: 45.45  E-value: 2.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVE--EGNSLILLEHHIDVIKSADWLIEL 713
Cdd:cd03228   97 LSGGQRQRIAIARALLRDPPILILDEATSAL---DPETEALILEALRAlaKGKTVIVIAHRLSTIRDADRIIVL 167
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
642-745 3.01e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 46.61  E-value: 3.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID-VIKSADWLIELgpeggeN 720
Cdd:PRK13639 138 LSGGQKKRVAIAGILAMKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDlVPVYADKVYVM------S 211
                         90       100
                 ....*....|....*....|....*
gi 488284725 721 GGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK13639 212 DGKIIKEGTPKEVFSDIETIRKANL 236
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
614-701 3.07e-05

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 46.24  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 614 KDQPFALSLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNS 693
Cdd:PRK09493 110 KEEAEKQARELLAKVGLAE-RAHHYPSELSGGQQQRVAIARALAVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMT 188

                 ....*...
gi 488284725 694 LILLEHHI 701
Cdd:PRK09493 189 MVIVTHEI 196
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
614-711 3.75e-05

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: 45.60  E-value: 3.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 614 KDQPFALSLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliD---IQQSLQLFNRMVEE 690
Cdd:cd03262  109 KAEAEERALELLEKVGLAD-KADAYPAQLSGGQQQRVAIARALAMNPKVMLFDEPTSAL---DpelVGEVLDVMKDLAEE 184
                         90       100
                 ....*....|....*....|..
gi 488284725 691 GNSLILLEHHIDVIKS-ADWLI 711
Cdd:cd03262  185 GMTMVVVTHEMGFAREvADRVI 206
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
642-713 4.02e-05

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: 44.70  E-value: 4.02e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 642 LSGGELQRVKLADTL-HQKKaIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKS-ADWLIEL 713
Cdd:cd03230   96 LSGGMKQRLALAQALlHDPE-LLILDEPTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAERlCDRVAIL 168
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
642-704 4.09e-05

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: 44.87  E-value: 4.09e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEE-GNSLILLEHHIDVI 704
Cdd:cd03229  101 LSGGQQQRVALARALAMDPDVLLLDEPTSALDPITRREVRALLKSLQAQlGITVVLVTHDLDEA 164
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
298-397 4.24e-05

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 45.73  E-value: 4.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 298 LSLIKNIQEELLVRLeaLINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALL 377
Cdd:PRK10619 121 LGLSKQEARERAVKY--LAKVGIDERAQGKYPVHLSGGQQQRVSIARAL--AMEPEVLLFDEPTSALDPELVGEVLRIMQ 196
                         90       100
                 ....*....|....*....|
gi 488284725 378 NLKNKGNTVVLVEHNPQLIR 397
Cdd:PRK10619 197 QLAEEGKTMVVVTHEMGFAR 216
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
331-429 4.45e-05

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: 45.61  E-value: 4.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDIERISRALLNLKnKGNTVVLVEHNPQLIREADFIIDIGpf 408
Cdd:cd03249  139 QLSGGQKQRIAIAR----ALlrNPKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIAVLQ-- 211
                         90       100
                 ....*....|....*....|.
gi 488284725 409 agenGGHVQFSGTYDAFLASK 429
Cdd:cd03249  212 ----NGQVVEQGTHDELMAQK 228
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
305-405 4.51e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 45.88  E-value: 4.51e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLEALINIGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGN 384
Cdd:PRK13647 112 KDEVERRVEEALKAVRMWDFRDKPPYHLSYGQKKRVAIAGVL--AMDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGK 189
                         90       100
                 ....*....|....*....|..
gi 488284725 385 TVVLVEHNPQLIRE-ADFIIDI 405
Cdd:PRK13647 190 TVIVATHDVDLAAEwADQVIVL 211
cbiO PRK13646
energy-coupling factor transporter ATPase;
296-392 4.58e-05

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 45.93  E-value: 4.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 296 MDLSLIKNIQEELLVRLealiniGLSYLTLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRA 375
Cdd:PRK13646 116 MNLDEVKNYAHRLLMDL------GFSRDVMSQSPFQMSGGQMRKIAIVSIL--AMNPDIIVLDEPTAGLDPQSKRQVMRL 187
                         90
                 ....*....|....*...
gi 488284725 376 LLNLKNKGN-TVVLVEHN 392
Cdd:PRK13646 188 LKSLQTDENkTIILVSHD 205
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
306-696 5.17e-05

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 46.46  E-value: 5.17e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 306 EELLVRLEALINIGLSYLTLGratetlsGGEAQRIKIAKYVNSalNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNT 385
Cdd:PRK13549 125 QKLLAQLKLDINPATPVGNLG-------LGQQQLVEIAKALNK--QARLLILDEPTASLTESETAVLLDIIRDLKAHGIA 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 386 VVLVEHNPQLIRE-ADFIIDIgpfagENGGHVqfsGTYDA----------FLASKTLTSQALQEPLPLNDQPRKARKsLS 454
Cdd:PRK13549 196 CIYISHKLNEVKAiSDTICVI-----RDGRHI---GTRPAagmteddiitMMVGRELTALYPREPHTIGEVILEVRN-LT 266
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 455 IEHATLHN---LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIIHLSQKSITANlrstpmtylNIFDKVR 531
Cdd:PRK13549 267 AWDPVNPHikrVDDVSFSLRRGEILGIAGLVGAGRTELVQCLFGAYPGRWEGEIFIDGKPVKIR---------NPQQAIA 337
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 532 klfaeenhvspalfsynsKGAC--PTCKGKGIIVSDMSFmedvtsicetchgtrykeevlhylynGKNIvevlALSVKDG 609
Cdd:PRK13549 338 ------------------QGIAmvPEDRKRDGIVPVMGV--------------------------GKNI----TLAALDR 369
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 610 YDFFKDQPFALSLKNLLEvGLSYLKLN-----QSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGlhlIDI---QQSL 681
Cdd:PRK13549 370 FTGGSRIDDAAELKTILE-SIQRLKVKtaspeLAIARLSGGNQQKAVLAKCLLLNPKILILDEPTRG---IDVgakYEIY 445
                        410
                 ....*....|....*
gi 488284725 682 QLFNRMVEEGNSLIL 696
Cdd:PRK13549 446 KLINQLVQQGVAIIV 460
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
312-425 5.19e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 45.77  E-value: 5.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 312 LEALINIGLSYLTLGRATeTLSGGEAQRIKIAKYVNSALNDIMyiLDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVE 390
Cdd:PRK09984 134 LQALTRVGMVHFAHQRVS-TLSGGQQQRVAIARALMQQAKVIL--ADEPIASLDPESARIVMDTLRDInQNDGITVVVTL 210
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488284725 391 HNPQL-IREADFIIDIgpfageNGGHVQFSGTYDAF 425
Cdd:PRK09984 211 HQVDYaLRYCERIVAL------RQGHVFYDGSSQQF 240
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
625-704 5.48e-05

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: 45.56  E-value: 5.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIdIQ-QSLQLFNRMVEE-GNSLILLEHHID 702
Cdd:COG1124  122 LEQVGLPPSFLDRYPHQLSGGQRQRVAIARALILEPELLLLDEPTSALDVS-VQaEILNLLKDLREErGLTYLFVSHDLA 200

                 ..
gi 488284725 703 VI 704
Cdd:COG1124  201 VV 202
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
331-403 6.29e-05

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: 44.83  E-value: 6.29e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 331 TLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIRE-ADFII 403
Cdd:cd03262  135 QLSGGQQQRVAIARAL--AMNPKVMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFAREvADRVI 206
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
621-702 6.32e-05

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 45.39  E-value: 6.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 621 SLKNLLEVGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLH----------LIDIQQSlqlfnrmveE 690
Cdd:PRK09984 133 ALQALTRVGMVHFA-HQRVSTLSGGQQQRVAIARALMQQAKVILADEPIASLDpesarivmdtLRDINQN---------D 202
                         90
                 ....*....|..
gi 488284725 691 GNSLILLEHHID 702
Cdd:PRK09984 203 GITVVVTLHQVD 214
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
642-738 7.03e-05

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 45.18  E-value: 7.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEE-GNSLILLEHHIDVIKS-ADWLIELgpegge 719
Cdd:PRK13652 138 LSGGEKKRVAIAGVIAMEPQVLVLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVPEmADYIYVM------ 211
                         90       100
                 ....*....|....*....|....*
gi 488284725 720 NGGQLLFTGTPA------NMLNSTH 738
Cdd:PRK13652 212 DKGRIVAYGTVEeiflqpDLLARVH 236
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
595-705 7.04e-05

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: 44.80  E-value: 7.04e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 595 GKNIVEVL-ALSVKDGYDFFKdqpfALSLKNLLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLH 673
Cdd:cd03257  102 GEQIAEPLrIHGKLSKKEARK----EAVLLLLVGVGLPEEVLNRYPHELSGGQRQRVAIARALALNPKLLIADEPTSALD 177
                         90       100       110
                 ....*....|....*....|....*....|....
gi 488284725 674 lIDIQ-QSLQLFNRMVEE-GNSLILLEHHIDVIK 705
Cdd:cd03257  178 -VSVQaQILDLLKKLQEElGLTLLFITHDLGVVA 210
PLN03211 PLN03211
ABC transporter G-25; Provisional
332-393 7.07e-05

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 46.41  E-value: 7.07e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNP 393
Cdd:PLN03211 207 ISGGERKRVSIAHEM--LINPSLLILDEPTSGLDATAAYRLVLTLGSLAQKGKTIVTSMHQP 266
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
592-742 7.36e-05

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 45.04  E-value: 7.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 592 LYNGKNIVEVLALSVKD--GYDFFKDQPF---------ALSLKN----------------LLEVGL---SYLKLNQSLST 641
Cdd:PRK14246  74 LYFGKDIFQIDAIKLRKevGMVFQQPNPFphlsiydniAYPLKShgikekreikkiveecLRKVGLwkeVYDRLNSPASQ 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLI-----ELGPE 716
Cdd:PRK14246 154 LSGGQQQRLTIARALALKPKVLLMDEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAflyngELVEW 233
                        170       180
                 ....*....|....*....|....*.
gi 488284725 717 GGENGgqlLFTgTPANMLNSTHSITK 742
Cdd:PRK14246 234 GSSNE---IFT-SPKNELTEKYVIGR 255
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
14-40 7.59e-05

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: 44.38  E-value: 7.59e-05
                         10        20
                 ....*....|....*....|....*..
gi 488284725  14 LKNVSVNIPKKQLTVVTGLSGSGKSSL 40
Cdd:cd03250   21 LKDINLEVPKGELVAIVGPVGSGKSSL 47
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
332-393 7.75e-05

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 46.19  E-value: 7.75e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725  332 LSGGEAQRIKIAkyvNSALND-IMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNP 393
Cdd:TIGR00955 167 LSGGERKRLAFA---SELLTDpPLLFCDEPTSGLDSFMAYSVVQVLKGLAQKGKTIICTIHQP 226
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
642-708 8.15e-05

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: 43.57  E-value: 8.15e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID-VIKSAD 708
Cdd:cd03216   83 LSVGERQMVEIARALARNARLLILDEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLDeVFEIAD 150
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
625-691 8.18e-05

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 45.11  E-value: 8.18e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 625 LLEVGLSYLKlNQSLSTLSGGELQRVKLADTLHQ-------KKAIYLMDEPTDGLhliDI---QQSLQLFNRMVEEG 691
Cdd:COG4559  118 LALVGLAHLA-GRSYQTLSGGEQQRVQLARVLAQlwepvdgGPRWLFLDEPTSAL---DLahqHAVLRLARQLARRG 190
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
642-744 8.36e-05

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: 44.80  E-value: 8.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLI---DIQQSLQLFNRmvEEGNSLILLEHHIDVIKS-ADWLIELGpeg 717
Cdd:cd03261  137 LSGGMKKRVALARALALDPELLLYDEPTAGLDPIasgVIDDLIRSLKK--ELGLTSIMVTHDLDTAFAiADRIAVLY--- 211
                         90       100
                 ....*....|....*....|....*..
gi 488284725 718 genGGQLLFTGTPANMLNSTHSITKGY 744
Cdd:cd03261  212 ---DGKIVAEGTPEELRASDDPLVRQF 235
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
628-702 8.43e-05

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: 44.59  E-value: 8.43e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284725 628 VGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHHID 702
Cdd:cd03297  119 LGLDHL-LNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPELKQIKKNLNiPVIFVTHDLS 193
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
625-715 9.18e-05

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: 44.39  E-value: 9.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDiQQSLQLFNRMVEE---GNSLILLEHHI 701
Cdd:COG4133  116 LEAVGLAGL-ADLPVRQLSAGQKRRVALARLLLSPAPLWLLDEPFTAL---D-AAGVALLAELIAAhlaRGGAVLLTTHQ 190
                         90
                 ....*....|....
gi 488284725 702 DVIKSADWLIELGP 715
Cdd:COG4133  191 PLELAAARVLDLGD 204
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
331-424 9.40e-05

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 44.77  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKgNTVVLVEHN-PQLIREADFIIDIGPFA 409
Cdd:PRK14243 151 SLSGGQQQRLCIARAI--AVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNmQQAARVSDMTAFFNVEL 227
                         90
                 ....*....|....*
gi 488284725 410 GENGGHVQFSGTYDA 424
Cdd:PRK14243 228 TEGGGRYGYLVEFDR 242
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
302-392 9.49e-05

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: 44.66  E-value: 9.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 302 KNIQEELLVRLEaLINIglsyltLGRATETLSGGEAQRIKIAkyVNSALNDIMYILDEPSAGLhpkDI-ERISRALL--N 378
Cdd:cd03236  117 RGKLDELVDQLE-LRHV------LDRNIDQLSGGELQRVAIA--AALARDADFYFFDEPSSYL---DIkQRLNAARLirE 184
                         90
                 ....*....|....
gi 488284725 379 LKNKGNTVVLVEHN 392
Cdd:cd03236  185 LAEDDNYVLVVEHD 198
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
460-705 9.87e-05

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 45.55  E-value: 9.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 460 LHNLNNLSVEVPLGVLTVICGVAGSGKSSLAE---EIYQKaqadnqeiihlSQKSITANLRstpmtylnifdkvrklfaE 536
Cdd:PRK09700  18 VHALKSVNLTVYPGEIHALLGENGAGKSTLMKvlsGIHEP-----------TKGTITINNI------------------N 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 537 ENHVSPALFSYNskgacptckGKGIIVSDMSFMEDVTsicetchgtrykeeVLHYLYNGKNIV-EVLALSVKDgYDFFKD 615
Cdd:PRK09700  69 YNKLDHKLAAQL---------GIGIIYQELSVIDELT--------------VLENLYIGRHLTkKVCGVNIID-WREMRV 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 616 QPFALslknLLEVGLSyLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLI 695
Cdd:PRK09700 125 RAAMM----LLRVGLK-VDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEPTSSLTNKEVDYLFLIMNQLRKEGTAIV 199
                        250
                 ....*....|
gi 488284725 696 LLEHHIDVIK 705
Cdd:PRK09700 200 YISHKLAEIR 209
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
625-685 1.02e-04

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 44.76  E-value: 1.02e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 625 LLEVGLSYLKlNQSLSTLSGGELQRVKLADTLHQ------KKAIYLMDEPTDGLhliDIQQSLQLFN 685
Cdd:PRK13548 119 LAQVDLAHLA-GRDYPQLSGGEQQRVQLARVLAQlwepdgPPRWLLLDEPTSAL---DLAHQHHVLR 181
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
332-413 1.08e-04

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: 43.46  E-value: 1.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsaLNDI-MYILDEPSAGLHPKDIERISRALLN-LKNKgnTVVLVEHNPQLIREADFIIDIgpfa 409
Cdd:cd03247   99 FSGGERQRLALARIL---LQDApIVLLDEPTVGLDPITERQLLSLIFEvLKDK--TLIWITHHLTGIEHMDKILFL---- 169

                 ....
gi 488284725 410 gENG 413
Cdd:cd03247  170 -ENG 172
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
629-672 1.12e-04

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: 44.25  E-value: 1.12e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488284725 629 GLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL 672
Cdd:cd03299  118 GIDHL-LNRKPETLSGGEQQRVAIARALVVNPKILLLDEPFSAL 160
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
332-437 1.22e-04

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: 44.40  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLhpkDIERISRALLNLKN--KGNTVVLVEHNPQLIREADFIIDIgp 407
Cdd:cd03252  139 LSGGQRQRIAIAR----ALihNPRILIFDEATSAL---DYESEHAIMRNMHDicAGRTVIIIAHRLSTVKNADRIIVM-- 209
                         90       100       110
                 ....*....|....*....|....*....|
gi 488284725 408 fageNGGHVQFSGTYDAFLASKTLTSQALQ 437
Cdd:cd03252  210 ----EKGRIVEQGSHDELLAENGLYAYLYQ 235
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
332-395 1.22e-04

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 44.00  E-value: 1.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 332 LSGGEAQRIKIAKYVNSAlNDIMYIlDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEHNPQL 395
Cdd:PRK10584 147 LSGGEQQRVALARAFNGR-PDVLFA-DEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQL 209
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
639-717 1.43e-04

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: 42.44  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 639 LSTLSGGELQRVKLADTLHQKKAIYLMDEPTDglHLiDIQQSLQLFNRMVEEGNSLILLEHHIDVIKS-ADWLIELGPEG 717
Cdd:cd03221   68 FEQLSGGEKMRLALAKLLLENPNLLLLDEPTN--HL-DLESIEALEEALKEYPGTVILVSHDRYFLDQvATKIIELEDGK 144
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
325-429 1.49e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 44.21  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 325 LGRATETLSGGEAQRIKIAKYVnsALN-DIMyILDEPSAGLHPKDIERISRALLNLKNKGN-TVVLVEHNPQLIREADFI 402
Cdd:PRK13632 136 LDKEPQNLSGGQKQRVAIASVL--ALNpEII-IFDESTSMLDPKGKREIKKIMVDLRKTRKkTLISITHDMDEAILADKV 212
                         90       100
                 ....*....|....*....|....*..
gi 488284725 403 IDIgpfageNGGHVQFSGTYDAFLASK 429
Cdd:PRK13632 213 IVF------SEGKLIAQGKPKEILNNK 233
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
332-429 1.49e-04

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 44.88  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVNSALNdiMYILDEPSAGLhpkDIERISRALLNLKNKGNTVVLVEHNpqliRE-----ADFIIDIG 406
Cdd:PRK15064 439 LSGGEKGRMLFGKLMMQKPN--VLVMDEPTNHM---DMESIESLNMALEKYEGTLIFVSHD----REfvsslATRIIEIT 509
                         90       100
                 ....*....|....*....|...
gi 488284725 407 PfagenGGHVQFSGTYDAFLASK 429
Cdd:PRK15064 510 P-----DGVVDFSGTYEEYLRSQ 527
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
625-731 1.56e-04

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: 44.34  E-value: 1.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  625 LLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL------HLIDIQQSLqlfNRmvEEGNSLILLE 698
Cdd:TIGR04520 121 LKLVGMEDF-RDREPHLLSGGQKQRVAIAGVLAMRPDIIILDEATSMLdpkgrkEVLETIRKL---NK--EEGITVISIT 194
                          90       100       110
                  ....*....|....*....|....*....|...
gi 488284725  699 HHIDVIKSADWLIELgpeggeNGGQLLFTGTPA 731
Cdd:TIGR04520 195 HDMEEAVLADRVIVM------NKGKIVAEGTPR 221
cbiO PRK13640
energy-coupling factor transporter ATPase;
640-737 1.63e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 44.41  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHHIDVIKSADWLIELgpegg 718
Cdd:PRK13640 142 ANLSGGQKQRVAIAGILAVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVLVL----- 216
                         90
                 ....*....|....*....
gi 488284725 719 eNGGQLLFTGTPANMLNST 737
Cdd:PRK13640 217 -DDGKLLAQGSPVEIFSKV 234
FtsE TIGR02673
cell division ATP-binding protein FtsE; This model describes FtsE, a member of the ABC ...
625-704 1.83e-04

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


Pssm-ID: 131721 [Multi-domain]  Cd Length: 214  Bit Score: 43.39  E-value: 1.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  625 LLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI 704
Cdd:TIGR02673 122 LRQVGLEH-KADAFPEQLSGGEQQRVAIARAIVNSPPLLLADEPTGNLDPDLSERILDLLKRLNKRGTTVIVATHDLSLV 200
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
331-429 1.84e-04

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: 43.76  E-value: 1.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKYVnsaLND--IMyILDEPSAGLHPKDIERISRALLNLKnKGNTVVLVEHNPQLIREADFIIDIgpf 408
Cdd:cd03251  138 KLSGGQRQRIAIARAL---LKDppIL-ILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVVL--- 209
                         90       100
                 ....*....|....*....|.
gi 488284725 409 agENGGHVQfSGTYDAFLASK 429
Cdd:cd03251  210 --EDGKIVE-RGTHEELLAQG 227
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
642-713 1.96e-04

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: 44.58  E-value: 1.96e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725  642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDiQQSLQLFNRMVEE---GNSLILLEHHIDVIKSADWLIEL 713
Cdd:TIGR02857 459 LSGGQAQRLALARAFLRDAPLLLLDEPTAHL---D-AETEAEVLEALRAlaqGRTVLLVTHRLALAALADRIVVL 529
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
625-699 1.97e-04

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 44.82  E-value: 1.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYL-KLNQSLST--------LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFnRMVEEGNSLI 695
Cdd:PRK11160 450 LQQVGLEKLlEDDKGLNAwlgeggrqLSGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELL-AEHAQNKTVL 528

                 ....
gi 488284725 696 LLEH 699
Cdd:PRK11160 529 MITH 532
cbiO PRK13644
energy-coupling factor transporter ATPase;
625-735 2.19e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 43.82  E-value: 2.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYLKlNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVI 704
Cdd:PRK13644 121 LAEIGLEKYR-HRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDPDSGIAVLERIKKLHEKGKTIVYITHNLEEL 199
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 705 KSADWLIELgpeggeNGGQLLFTGTPANMLN 735
Cdd:PRK13644 200 HDADRIIVM------DRGKIVLEGEPENVLS 224
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
305-429 2.20e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 43.68  E-value: 2.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRLE-ALINIGLSYLTlGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KNK 382
Cdd:PRK13636 115 EDEVRKRVDnALKRTGIEHLK-DKPTHCLSFGQKKRVAIAGVL--VMEPKVLVLDEPTAGLDPMGVSEIMKLLVEMqKEL 191
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 488284725 383 GNTVVLVEHNpqlireadfiIDIGPFAGENG-----GHVQFSGTYDAFLASK 429
Cdd:PRK13636 192 GLTIIIATHD----------IDIVPLYCDNVfvmkeGRVILQGNPKEVFAEK 233
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
298-392 2.28e-04

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: 43.48  E-value: 2.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 298 LSLIKNIQEELLVRLEALINI-----------GLSYLtLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHP 366
Cdd:cd03299   86 MTVYKNIAYGLKKRKVDKKEIerkvleiaemlGIDHL-LNRKPETLSGGEQQRVAIARAL--VVNPKILLLDEPFSALDV 162
                         90       100
                 ....*....|....*....|....*..
gi 488284725 367 KDIERISRALLNLKNKGNTVVL-VEHN 392
Cdd:cd03299  163 RTKEKLREELKKIRKEFGVTVLhVTHD 189
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
308-403 2.32e-04

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: 42.56  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 308 LLVRLEALINIGLSyltlgratetLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLK-NKGNTV 386
Cdd:cd03229   87 LFPHLTVLENIALG----------LSGGQQQRVALARAL--AMDPDVLLLDEPTSALDPITRREVRALLKSLQaQLGITV 154
                         90
                 ....*....|....*...
gi 488284725 387 VLVEHNP-QLIREADFII 403
Cdd:cd03229  155 VLVTHDLdEAARLADRVV 172
LPS_export_lptB TIGR04406
LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ...
597-736 2.32e-04

LPS export ABC transporter ATP-binding protein; Members of this fmaily are LptB, the ATP-binding cassette protein of an ABC transporter involved in lipopolysaccharide export. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides, Transport and binding proteins, Other]


Pssm-ID: 275199 [Multi-domain]  Cd Length: 239  Bit Score: 43.42  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  597 NIVEVLALSvkdgYDFFKDQpFALSLKNLL-EVGLSYLKLNQSLStLSGGELQRVKLADTLHQKKAIYLMDEP---TDGL 672
Cdd:TIGR04406  96 NIMAVLEIR----KDLDRAE-REERLEALLeEFQISHLRDNKAMS-LSGGERRRVEIARALATNPKFILLDEPfagVDPI 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284725  673 HLIDIQqslQLFNRMVEEGNSLILLEHHI----DVIKSAdWLIelgpeggeNGGQLLFTGTPANMLNS 736
Cdd:TIGR04406 170 AVGDIK---KIIKHLKERGIGVLITDHNVretlDICDRA-YII--------SDGKVLAEGTPAEIVAN 225
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
325-429 2.36e-04

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 44.63  E-value: 2.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  325 LGRATETLSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDIERISRALLNLKNKGN-TVVLVEHNPQLIREADF 401
Cdd:PTZ00265 1352 VGPYGKSLSGGQKQRIAIAR----ALlrEPKILLLDEATSSLDSNSEKLIEKTIVDIKDKADkTIITIAHRIASIKRSDK 1427
                          90       100
                  ....*....|....*....|....*...
gi 488284725  402 IIdIGPFAGENGGHVQFSGTYDAFLASK 429
Cdd:PTZ00265 1428 IV-VFNNPDRTGSFVQAHGTHEELLSVQ 1454
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
330-442 2.51e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 43.59  E-value: 2.51e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLK-NKGNTVVLVEHNPQLIREADFIIDIgpf 408
Cdd:PRK13648 141 NALSGGQKQRVAIAGVL--ALNPSVIILDEATSMLDPDARQNLLDLVRKVKsEHNITIISITHDLSEAMEADHVIVM--- 215
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 488284725 409 ageNGGHVQFSGT-YDAFLASKTLTSQALQEPLPL 442
Cdd:PRK13648 216 ---NKGTVYKEGTpTEIFDHAEELTRIGLDLPFPI 247
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
7-40 2.53e-04

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: 42.23  E-value: 2.53e-04
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488284725   7 KHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSL 40
Cdd:cd00267    8 RYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTL 41
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
634-745 2.58e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 43.49  E-value: 2.58e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL---------HLIdiqQSLQLFNRMveegnSLILLEHHI-DV 703
Cdd:PRK14258 143 KIHKSALDLSGGQQQRLCIARALAVKPKVLLMDEPCFGLdpiasmkveSLI---QSLRLRSEL-----TMVIVSHNLhQV 214
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 488284725 704 IKSADWLIELgpEGGENG-GQLLFTGTPANMLNSTH-SITKGYL 745
Cdd:PRK14258 215 SRLSDFTAFF--KGNENRiGQLVEFGLTKKIFNSPHdSRTREYV 256
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
332-431 2.63e-04

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: 43.37  E-value: 2.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVNSalNDIMYILDEPSAGLhpkDI--ERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIgpfa 409
Cdd:cd03253  138 LSGGEKQRVAIARAILK--NPPILLLDEATSAL---DThtEREIQAALRDVSKGRTTIVIAHRLSTIVNADKIIVL---- 208
                         90       100
                 ....*....|....*....|..
gi 488284725 410 geNGGHVQFSGTYDAFLASKTL 431
Cdd:cd03253  209 --KDGRIVERGTHEELLAKGGL 228
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
330-407 2.66e-04

ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ATP-binding cassette of ABC transporters, but are not associated with membrane-spanning domains. The conserved ATP-binding motifs common to Rad50 and the ABC transporter family include the Walker A and Walker B motifs, the Q loop, a histidine residue in the switch region, a D-loop, and a conserved LSGG sequence. This conserved sequence, LSGG, is the most specific and characteristic motif of this family and is thus known as the ABC signature sequence.


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 42.98  E-value: 2.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGE------AQRIKIAKYVNSALNdiMYILDEPSAGLhpkDIERISRALLNL-----KNKGNTVVLVEHNPQLIRE 398
Cdd:cd03240  114 GRCSGGEkvlaslIIRLALAETFGSNCG--ILALDEPTTNL---DEENIEESLAEIieerkSQKNFQLIVITHDEELVDA 188

                 ....*....
gi 488284725 399 ADFIIDIGP 407
Cdd:cd03240  189 ADHIYRVEK 197
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
640-700 2.76e-04

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: 44.27  E-value: 2.76e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725  640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRM--VEEGNSLILLEHH 700
Cdd:TIGR02868 470 ARLSGGERQRLALARALLADAPILLLDEPTEHL---DAETADELLEDLlaALSGRTVVLITHH 529
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
327-396 2.78e-04

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 43.44  E-value: 2.78e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284725 327 RATETLSGGEAQRIKIAKYVNSALNDIMyiLDEPSAGLHPKDIERISRALLNLKNK-GNTVVLVEHNPQLI 396
Cdd:PRK11300 149 RQAGNLAYGQQRRLEIARCMVTQPEILM--LDEPAAGLNPKETKELDELIAELRNEhNVTVLLIEHDMKLV 217
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
584-672 2.96e-04

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: 42.63  E-value: 2.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 584 YKEEVLHY----LYNGKNIVEVLALSVKDGYDFfkdqpfALSLKNllevglsylklNQSLSTLSGGELQRVKLADTLHQK 659
Cdd:cd03233   74 YKEFAEKYpgeiIYVSEEDVHFPTLTVRETLDF------ALRCKG-----------NEFVRGISGGERKRVSIAEALVSR 136
                         90
                 ....*....|...
gi 488284725 660 KAIYLMDEPTDGL 672
Cdd:cd03233  137 ASVLCWDNSTRGL 149
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
331-404 2.97e-04

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: 43.17  E-value: 2.97e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488284725 331 TLSGGEAQRIKIAKYVnSALNDImYILDEPSAGLhpkDIE---RISRALLNL-KNKGNTVVLVEHNpqlIREADFIID 404
Cdd:cd03237  115 ELSGGELQRVAIAACL-SKDADI-YLLDEPSAYL---DVEqrlMASKVIRRFaENNEKTAFVVEHD---IIMIDYLAD 184
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
451-669 3.16e-04

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: 42.94  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 451 KSLSIEHATLHNLNNLSVEVPLGVLTVICGVAGSGKSSL------AEEIYQKAQADNQeiIHLSQKsitaNLRSTPMTYL 524
Cdd:cd03260    4 RDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLlrllnrLNDLIPGAPDEGE--VLLDGK----DIYDLDVDVL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 525 NIFDKVRKLFAEenhvsPALFsynskgacptckgkgiivsDMSFMEDVtSICETCHGTRYKEEVlhylyngKNIVEVlAL 604
Cdd:cd03260   78 ELRRRVGMVFQK-----PNPF-------------------PGSIYDNV-AYGLRLHGIKLKEEL-------DERVEE-AL 124
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 605 SVKDGYDFFKDQPFALSLknllevglsylklnqslstlSGGELQRVKLADTLHQKKAIYLMDEPT 669
Cdd:cd03260  125 RKAALWDEVKDRLHALGL--------------------SGGQQQRLCLARALANEPEVLLLDEPT 169
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
625-668 3.38e-04

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: 42.51  E-value: 3.38e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 488284725 625 LLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEP 668
Cdd:cd03259  115 LELVGLEGL-LNRYPHELSGGQQQRVALARALAREPSLLLLDEP 157
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
634-745 3.42e-04

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 43.23  E-value: 3.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEgNSLILLEHHIDVI-----KSAD 708
Cdd:PRK14243 144 KLKQSGLSLSGGQQQRLCIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQ-YTIIIVTHNMQQAarvsdMTAF 222
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 488284725 709 WLIELGPEGGENGGQLLFTGTPANMLNSTHSITKGYL 745
Cdd:PRK14243 223 FNVELTEGGGRYGYLVEFDRTEKIFNSPQQQATRDYV 259
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
642-723 3.87e-04

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 42.55  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIELGPEGGENG 721
Cdd:PRK10908 138 LSGGEQQRVGIARAVVNKPAVLLADEPTGNLDDALSEGILRLFEEFNRVGVTVLMATHDIGLISRRSYRMLTLSDGHLHG 217

                 ..
gi 488284725 722 GQ 723
Cdd:PRK10908 218 GV 219
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
332-419 4.23e-04

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: 41.79  E-value: 4.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVNSalNDIMYILDEPSAGLHPKDIERISRALLNLKNKGN-TVVLVEHNpqlIREADFIID-IGPFA 409
Cdd:cd03222   72 LSGGELQRVAIAAALLR--NATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGKkTALVVEHD---LAVLDYLSDrIHVFE 146
                         90
                 ....*....|
gi 488284725 410 GENGGHVQFS 419
Cdd:cd03222  147 GEPGVYGIAS 156
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
306-696 4.30e-04

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 43.47  E-value: 4.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 306 EELLVRLEALINiglsyltLGRATETLSGGEAQRIKIAKyvnsALN---DIMyILDEPSAGLHPKDIERISRALLNLKNK 382
Cdd:COG1129  122 RELLARLGLDID-------PDTPVGDLSVAQQQLVEIAR----ALSrdaRVL-ILDEPTASLTEREVERLFRIIRRLKAQ 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 383 GNTVVLVEHN-PQLIREADFII---DigpfagenGGHVqfsGTYDAflasKTLTSQAL------QEplpLNDQ-PRKARK 451
Cdd:COG1129  190 GVAIIYISHRlDEVFEIADRVTvlrD--------GRLV---GTGPV----AELTEDELvrlmvgRE---LEDLfPKRAAA 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 452 S----LSIEHAT----LHNLNnLSV---EVpLGvltvICGVAGSGKSSLAEEIYQKAQADNQEIIhlsqksitanLRSTP 520
Cdd:COG1129  252 PgevvLEVEGLSvggvVRDVS-FSVragEI-LG----IAGLVGAGRTELARALFGADPADSGEIR----------LDGKP 315
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 521 MTYLNIFDKVRK---LFAEENhvspalfsynskgacptcKGKGIIVsDMSFMEdvtsicetchgtrykeevlhylyngkN 597
Cdd:COG1129  316 VRIRSPRDAIRAgiaYVPEDR------------------KGEGLVL-DLSIRE--------------------------N 350
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 598 IVevLALSVKDGYDFFkdqpfaLSLKNLLEVGLSYLK--------LNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPT 669
Cdd:COG1129  351 IT--LASLDRLSRGGL------LDRRRERALAEEYIKrlriktpsPEQPVGNLSGGNQQKVVLAKWLATDPKVLILDEPT 422
                        410       420       430
                 ....*....|....*....|....*....|
gi 488284725 670 DGlhlIDI---QQSLQLFNRMVEEGNSLIL 696
Cdd:COG1129  423 RG---IDVgakAEIYRLIRELAAEGKAVIV 449
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
313-362 4.48e-04

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: 41.09  E-value: 4.48e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488284725  313 EALINIGLSYL---TLGRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSA 362
Cdd:pfam00005 100 EALEKLGLGDLadrPVGERPGTLSGGQRQRVAIARAL--LTKPKLLLLDEPTA 150
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
331-420 4.56e-04

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: 42.18  E-value: 4.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKyvnSALND--IMyILDEPSAGLHPKdiERIS-RALLNLKNKGNTVVLVEHnpqlIREadfiiDIGP 407
Cdd:cd03264  130 SLSGGMRRRVGIAQ---ALVGDpsIL-IVDEPTAGLDPE--ERIRfRNLLSELGEDRIVILSTH----IVE-----DVES 194
                         90
                 ....*....|....*..
gi 488284725 408 FAGE----NGGHVQFSG 420
Cdd:cd03264  195 LCNQvavlNKGKLVFEG 211
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
332-403 4.76e-04

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 42.77  E-value: 4.76e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVEHNPQLIREADFII 403
Cdd:PRK13633 145 LSGGQKQRVAIAGIL--AMRPECIIFDEPTAMLDPSGRREVVNTIKELnKKYGITIILITHYMEEAVEADRII 215
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
625-677 4.96e-04

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 43.52  E-value: 4.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 488284725 625 LLEVGLSYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDglHLiDI 677
Cdd:COG0488  136 LSGLGFPEEDLDRPVSELSGGWRRRVALARALLSEPDLLLLDEPTN--HL-DL 185
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
615-714 5.08e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 43.29  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 615 DQPFALSLKNLLEVGLSYLKLNQSlSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVeEGNSL 694
Cdd:PRK11174 460 ENAWVSEFLPLLPQGLDTPIGDQA-AGLSVGQAQRLALARALLQPCQLLLLDEPTASLDAHSEQLVMQALNAAS-RRQTT 537
                         90       100
                 ....*....|....*....|..
gi 488284725 695 ILLEHHIDVIKSAD--WLIELG 714
Cdd:PRK11174 538 LMVTHQLEDLAQWDqiWVMQDG 559
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
355-397 5.29e-04

AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being of the abortive phage resistance system, in which case the family would be acting as the toxin for a type IV toxin-antitoxin resistance system.


Pssm-ID: 433102 [Multi-domain]  Cd Length: 303  Bit Score: 42.76  E-value: 5.29e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 488284725  355 YILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIR 397
Cdd:pfam13304 261 LLIDEPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
314-397 5.55e-04

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: 42.10  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 314 ALINIGLSYLTLgRATETLSGGEAQRIKIAKYVnsaLND--IMyILDEPSAGLHPKDIERISRALLNL-KNKGNTVVLVE 390
Cdd:cd03298  112 ALARVGLAGLEK-RLPGELSGGERQRVALARVL---VRDkpVL-LLDEPFAALDPALRAEMLDLVLDLhAETKMTVLMVT 186

                 ....*..
gi 488284725 391 HNPQLIR 397
Cdd:cd03298  187 HQPEDAK 193
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
463-741 5.56e-04

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 42.43  E-value: 5.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 463 LNNLSVEVPLGVLTVICGVAGSGKSSLAEEIYQKAQADNQEIIHLSQKSITANLRstpmtylnifdKVRKlfaeenHVSP 542
Cdd:PRK13648  25 LKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDNFE-----------KLRK------HIGI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 543 ALFSynskgacPTCKGKGIIVS-DMSF-MEDvtsicetcHGTRYKEEvlhylyngKNIVEVlALSVKDGYDFFKDQPFAL 620
Cdd:PRK13648  88 VFQN-------PDNQFVGSIVKyDVAFgLEN--------HAVPYDEM--------HRRVSE-ALKQVDMLERADYEPNAL 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 621 SlknllevglsylklnqslstlsGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEH 699
Cdd:PRK13648 144 S----------------------GGQKQRVAIAGVLALNPSVIILDEATSMLDPDARQNLLDLVRKVKSEHNiTIISITH 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 488284725 700 HIDVIKSADWLIELgpeggeNGGQLLFTGTPANMLNSTHSIT 741
Cdd:PRK13648 202 DLSEAMEADHVIVM------NKGTVYKEGTPTEIFDHAEELT 237
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
325-427 5.83e-04

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: 43.40  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   325 LGRATETLSGGEAQRIKIAKYVNSalNDIMYILDEPSAGLHPKDIERISRALLNLKN--KGNTVVLVEHNPQLIREADFI 402
Cdd:TIGR00957  754 IGEKGVNLSGGQKQRVSLARAVYS--NADIYLFDDPLSAVDAHVGKHIFEHVIGPEGvlKNKTRILVTHGISYLPQVDVI 831
                           90       100
                   ....*....|....*....|....*
gi 488284725   403 IDIgpfageNGGHVQFSGTYDAFLA 427
Cdd:TIGR00957  832 IVM------SGGKISEMGSYQELLQ 850
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
634-715 5.83e-04

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 42.14  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADW---- 709
Cdd:PRK14267 142 RLNDYPSNLSGGQRQRLVIARALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVLVTHSPAQAARVSDYvafl 221
                         90
                 ....*....|
gi 488284725 710 ----LIELGP 715
Cdd:PRK14267 222 ylgkLIEVGP 231
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
319-438 6.24e-04

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 43.29  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 319 GLSYlTLGRATETLSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDIERISRALLNLKNkGNTVVLVEHNPQLI 396
Cdd:PRK11174 474 GLDT-PIGDQAAGLSVGQAQRLALAR----ALlqPCQLLLLDEPTASLDAHSEQLVMQALNAASR-RQTTLMVTHQLEDL 547
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488284725 397 READFIIDIgpfagENGGHVQfSGTYDAFLASKTLTSQALQE 438
Cdd:PRK11174 548 AQWDQIWVM-----QDGQIVQ-QGDYAELSQAGGLFATLLAH 583
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
630-715 6.42e-04

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: 42.04  E-value: 6.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 630 LSYLKLNQSL-----STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDiQQSLQLFNRMVEE----GNSLILLEHH 700
Cdd:COG4778  136 LARLNLPERLwdlppATFSGGEQQRVNIARGFIADPPLLLLDEPTASL---D-AANRAVVVELIEEakarGTAIIGIFHD 211
                         90
                 ....*....|....*.
gi 488284725 701 IDVIKS-ADWLIELGP 715
Cdd:COG4778  212 EEVREAvADRVVDVTP 227
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
14-41 6.97e-04

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: 41.21  E-value: 6.97e-04
                         10        20
                 ....*....|....*....|....*...
gi 488284725  14 LKNVSVNIPKKQLTVVTGLSGSGKSSLV 41
Cdd:cd03228   18 LKDVSLTIKPGEKVAIVGPSGSGKSTLL 45
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
325-428 7.89e-04

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: 41.90  E-value: 7.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 325 LGRATETLSGGEAQRIKIAKyvnsAL-NDIMYIL-DEPSAGLHPKDIERISRALLNLKNK-GNTVVLVEHNPQ-LIREAD 400
Cdd:cd03295  129 ADRYPHELSGGQQQRVGVAR----ALaADPPLLLmDEPFGALDPITRDQLQEEFKRLQQElGKTIVFVTHDIDeAFRLAD 204
                         90       100
                 ....*....|....*....|....*...
gi 488284725 401 FIIDIGpfageNGGHVQFsGTYDAFLAS 428
Cdd:cd03295  205 RIAIMK-----NGEIVQV-GTPDEILRS 226
PTZ00243 PTZ00243
ABC transporter; Provisional
14-41 9.46e-04

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 42.84  E-value: 9.46e-04
                          10        20
                  ....*....|....*....|....*...
gi 488284725   14 LKNVSVNIPKKQLTVVTGLSGSGKSSLV 41
Cdd:PTZ00243  676 LRDVSVSVPRGKLTVVLGATGSGKSTLL 703
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
625-706 9.66e-04

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: 41.41  E-value: 9.66e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLE-VGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLH----------LIDIQQSLQLfnrmveegnS 693
Cdd:cd03258  124 LLElVGLED-KADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDpettqsilalLRDINRELGL---------T 193
                         90
                 ....*....|...
gi 488284725 694 LILLEHHIDVIKS 706
Cdd:cd03258  194 IVLITHEMEVVKR 206
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
332-434 9.67e-04

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 42.40  E-value: 9.67e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  332 LSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLhpkDIErISRALLNLKN-KGNTVVLVEHNPQLIREADFIIDIgpf 408
Cdd:TIGR00958 618 LSGGQKQRIAIAR----ALvrKPRVLILDEATSAL---DAE-CEQLLQESRSrASRTVLLIAHRLSTVERADQILVL--- 686
                          90       100
                  ....*....|....*....|....*.
gi 488284725  409 ageNGGHVQFSGTYDAFLASKTLTSQ 434
Cdd:TIGR00958 687 ---KKGSVVEMGTHKQLMEDQGCYKH 709
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
7-41 1.03e-03

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: 41.30  E-value: 1.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 488284725   7 KHATQNNLKNVSVNIPKKQLTVVTGLSGSGKSSLV 41
Cdd:cd03225   10 PDGARPALDDISLTIKKGEFVLIVGPNGSGKSTLL 44
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
306-421 1.03e-03

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 41.54  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 306 EELLVRL-EALINIGL-SYLTlgRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKG 383
Cdd:PRK13635 115 EEMVERVdQALRQVGMeDFLN--REPHRLSGGQKQRVAIAGVL--ALQPDIIILDEATSMLDPRGRREVLETVRQLKEQK 190
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 488284725 384 N-TVVLVEHNPQLIREADFIIDIgpfageNGGHVQFSGT 421
Cdd:PRK13635 191 GiTVLSITHDLDEAAQADRVIVM------NKGEILEEGT 223
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
642-735 1.08e-03

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: 42.10  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHlidiQQSLQLFNRMVEEGN-----SLILLEHHIDVI-KSADWLIELgp 715
Cdd:TIGR03269 169 LSGGEKQRVVLARQLAKEPFLFLADEPTGTLD----PQTAKLVHNALEEAVkasgiSMVLTSHWPEVIeDLSDKAIWL-- 242
                          90       100
                  ....*....|....*....|
gi 488284725  716 eggENgGQLLFTGTPANMLN 735
Cdd:TIGR03269 243 ---EN-GEIKEEGTPDEVVA 258
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
642-705 1.12e-03

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 42.38  E-value: 1.12e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHHIDVIK 705
Cdd:PRK15134 157 LSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELQQELNmGLLFITHNLSIVR 221
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
332-391 1.15e-03

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 41.23  E-value: 1.15e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEH 391
Cdd:PRK09493 137 LSGGQQQRVAIARAL--AVKPKLMLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTH 194
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
635-700 1.19e-03

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 41.25  E-value: 1.19e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488284725 635 LNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGlhlIDIQQSLQLF---NRMVEEGNSLILLEHH 700
Cdd:PRK09544 114 IDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQG---VDVNGQVALYdliDQLRRELDCAVLMVSH 179
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
322-402 1.20e-03

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 42.32  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  322 YLTL-GRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLK-NKGNTVVLVEHNPQLIREA 399
Cdd:PTZ00265  569 YETLvGSNASKLSGGQKQRISIARAI--IRNPKILILDEATSSLDNKSEYLVQKTINNLKgNENRITIIIAHRLSTIRYA 646

                  ...
gi 488284725  400 DFI 402
Cdd:PTZ00265  647 NTI 649
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
640-713 1.27e-03

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 42.02  E-value: 1.27e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHIDVIKSADWLIEL 713
Cdd:PRK10535 143 SQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSGEEVMAILHQLRDRGHTVIIVTHDPQVAAQAERVIEI 216
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
625-699 1.36e-03

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 40.92  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL------HLIDIQQSLqlfNRmvEEGNSLILLE 698
Cdd:PRK10584 131 LEQLGLGK-RLDHLPAQLSGGEQQRVALARAFNGRPDVLFADEPTGNLdrqtgdKIADLLFSL---NR--EHGTTLILVT 204

                 .
gi 488284725 699 H 699
Cdd:PRK10584 205 H 205
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
330-410 1.39e-03

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: 40.21  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 330 ETLSGGEAQRIKIA-------KYVnsalndimyILDEPSAGLhpkDIERISRALLNLKNKGNTVVLVEHNPQLIREADFI 402
Cdd:cd03223   90 DVLSGGEQQRLAFArlllhkpKFV---------FLDEATSAL---DEESEDRLYQLLKELGITVISVGHRPSLWKFHDRV 157

                 ....*...
gi 488284725 403 IDIGPFAG 410
Cdd:cd03223  158 LDLDGEGG 165
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
642-697 1.48e-03

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: 40.11  E-value: 1.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGlhlIDI---QQSLQLFNRMVEEGNSLILL 697
Cdd:cd03215  105 LSGGNQQKVVLARWLARDPRVLILDEPTRG---VDVgakAEIYRLIRELADAGKAVLLI 160
PRK14291 PRK14291
chaperone protein DnaJ; Provisional
553-611 1.50e-03

chaperone protein DnaJ; Provisional


Pssm-ID: 237661 [Multi-domain]  Cd Length: 382  Bit Score: 41.68  E-value: 1.50e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 553 CPTCKGKGIIVSDMSFMEdVTSICETCHGTRYKEEVLHYLyNGKNIV---EVLALSVKDGYD 611
Cdd:PRK14291 176 CPTCGGSGEIYQRGGFFR-ISQTCPTCGGEGVLREPCSKC-NGRGLVikkETIKVRIPPGVD 235
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
306-396 1.51e-03

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: 40.84  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 306 EELLVRLealiniGLSYLtLGRATETLSGGEAQRIKIAKyvnsAL-ND--IMyILDEPSAGLHPKDIERISRALLNLKNK 382
Cdd:COG1119  124 RELLELL------GLAHL-ADRPFGTLSQGEQRRVLIAR----ALvKDpeLL-ILDEPTAGLDLGARELLLALLDKLAAE 191
                         90
                 ....*....|....*
gi 488284725 383 GN-TVVLVEHNPQLI 396
Cdd:COG1119  192 GApTLVLVTHHVEEI 206
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
619-674 1.52e-03

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: 41.84  E-value: 1.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 488284725  619 ALSLKNLLEVGLSYLKL---NQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDglHL 674
Cdd:TIGR03719 136 AWDLDSQLEIAMDALRCppwDADVTKLSGGERRRVALCRLLLSKPDMLLLDEPTN--HL 192
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
615-699 1.58e-03

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: 40.88  E-value: 1.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 615 DQPFALSLKNLLEVGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGL------HLIDIqqslqLFNRMV 688
Cdd:COG4181  121 RDARARARALLERVGLGHR-LDHYPAQLSGGEQQRVALARAFATEPAILFADEPTGNLdaatgeQIIDL-----LFELNR 194
                         90
                 ....*....|.
gi 488284725 689 EEGNSLILLEH 699
Cdd:COG4181  195 ERGTTLVLVTH 205
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
309-393 1.61e-03

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: 40.58  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 309 LVRLEALiniglsyltLGRATETLSGGEAQRIKIAKyvnsAL---NDIMyILDEPSAGLHPKDIERISRALLNL-KNKGN 384
Cdd:cd03259  117 LVGLEGL---------LNRYPHELSGGQQQRVALAR----ALarePSLL-LLDEPLSALDAKLREELREELKELqRELGI 182

                 ....*....
gi 488284725 385 TVVLVEHNP 393
Cdd:cd03259  183 TTIYVTHDQ 191
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
14-109 1.62e-03

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 40.71  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  14 LKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFsSFVQNYLPkygrPEVEKIENLPVAIVIDQKKVAGN 93
Cdd:COG2401   46 LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVAGCV-DVPDNQFG----REASLIDAIGRKGDFKDAVELLN 120
                         90
                 ....*....|....*.
gi 488284725  94 SrstVGtYTDIYTFLR 109
Cdd:COG2401  121 A---VG-LSDAVLWLR 132
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
614-699 1.70e-03

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 40.89  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 614 KDQPFALSLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNS 693
Cdd:PRK11264 118 KEEATARARELLAKVGLAG-KETSYPRRLSGGQQQRVAIARALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRT 196

                 ....*.
gi 488284725 694 LILLEH 699
Cdd:PRK11264 197 MVIVTH 202
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
554-701 1.70e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 40.85  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 554 PTCKGKGIIVSDMSFMEDVTSicetchGTRYKEEVLHYLYNGKNIVEVLALSVKDGYDFFKDQPFALSLKN--------- 624
Cdd:PRK14271  55 PTGSGKTTFLRTLNRMNDKVS------GYRYSGDVLLGGRSIFNYRDVLEFRRRVGMLFQRPNPFPMSIMDnvlagvrah 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 ---------------LLEVGL---SYLKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQsLQLFNR 686
Cdd:PRK14271 129 klvprkefrgvaqarLTEVGLwdaVKDRLSDSPFRLSGGQQQLLCLARTLAVNPEVLLLDEPTSALDPTTTEK-IEEFIR 207
                        170
                 ....*....|....*
gi 488284725 687 MVEEGNSLILLEHHI 701
Cdd:PRK14271 208 SLADRLTVIIVTHNL 222
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
640-719 1.81e-03

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: 40.53  E-value: 1.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFnRMVEEGNSLILLEHHIDVIKSADWLIELgpEGGE 719
Cdd:cd03248  149 SQLSGGQKQRVAIARALIRNPQVLILDEATSALDAESEQQVQQAL-YDWPERRTVLVIAHRLSTVERADQILVL--DGGR 225
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
331-409 1.82e-03

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: 40.50  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 331 TLSGGEAQRIKIAKyvnsAL---NDIMyILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQlIRE--ADFIIDI 405
Cdd:COG4778  152 TFSGGEQQRVNIAR----GFiadPPLL-LLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEE-VREavADRVVDV 225

                 ....
gi 488284725 406 GPFA 409
Cdd:COG4778  226 TPFS 229
YbjD COG3593
Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM ...
276-401 2.09e-03

Predicted ATP-dependent endonuclease of the OLD family, contains P-loop ATPase and TOPRIM domains [Replication, recombination and repair];


Pssm-ID: 442812 [Multi-domain]  Cd Length: 359  Bit Score: 41.14  E-value: 2.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 276 KSIADAVDMPLTELHSFIRSMDLSLIKNIQEELLVRLEALINIgLSYLTLGRATET------LSGGEAQRIKIA-----K 344
Cdd:COG3593  102 EELNEELKEALKALNELLSEYLKELLDGLDLELELSLDELEDL-LKSLSLRIEDGKelpldrLGSGFQRLILLAllsalA 180
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 488284725 345 YVNSALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADF 401
Cdd:COG3593  181 ELKRAPANPILLIEEPEAHLHPQAQRRLLKLLKELSEKPNQVIITTHSPHLLSEVPL 237
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
12-62 2.12e-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: 39.65  E-value: 2.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 488284725  12 NNLKNVSVNIPKKQLTVVTGLSGSGKSSLVFDTLAAESRRELNDTFSSFVQ 62
Cdd:cd03227    9 SYFVPNDVTFGEGSLTIITGPNGSGKSTILDAIGLALGGAQSATRRRSGVK 59
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
625-713 2.14e-03

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 40.41  E-value: 2.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 625 LLE-VGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQS---LQLFNRMVEE-GNSLILLEH 699
Cdd:COG1136  128 LLErVGLGD-RLDHRPSQLSGGQQQRVAIARALVNRPKLILADEPTGNL---DSKTGeevLELLRELNRElGTTIVMVTH 203
                         90
                 ....*....|....
gi 488284725 700 HIDVIKSADWLIEL 713
Cdd:COG1136  204 DPELAARADRVIRL 217
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
622-736 2.27e-03

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: 40.22  E-value: 2.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 622 LKNLL-EVGLSYLKLNQSlSTLSGGELQRVKLADTLHQKKAIYLMDEP---TDGLHLIDIQqslQLFNRMVEEGNSLILL 697
Cdd:cd03218  114 LEELLeEFHITHLRKSKA-SSLSGGERRRVEIARALATNPKFLLLDEPfagVDPIAVQDIQ---KIIKILKDRGIGVLIT 189
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488284725 698 EHHI-DVIKSAD--WLIelgpeggeNGGQLLFTGTPANMLNS 736
Cdd:cd03218  190 DHNVrETLSITDraYII--------YEGKVLAEGTPEEIAAN 223
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
332-441 2.33e-03

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 40.88  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGN-TVVLVEHNPQLIREADFIIdIGPFAG 410
Cdd:PRK11022 154 LSGGMSQRVMIAMAI--ACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENmALVLITHDLALVAEAAHKI-IVMYAG 230
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 411 ENgghVQFSGTYDAFLASKTLTSQALQEPLP 441
Cdd:PRK11022 231 QV---VETGKAHDIFRAPRHPYTQALLRALP 258
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
332-403 2.40e-03

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: 40.01  E-value: 2.40e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488284725 332 LSGGEAQRIKIAKYVNSALNdiMYILDEPSAGL--HPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFII 403
Cdd:cd03290  141 LSGGQRQRICVARALYQNTN--IVFLDDPFSALdiHLSDHLMQEGILKFLQDDKRTLVLVTHKLQYLPHADWII 212
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
621-717 2.47e-03

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 40.43  E-value: 2.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 621 SLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEP---TDGLHLIDIQqslQLFNRMVEEGNSLILL 697
Cdd:PRK11247 114 ALQALAAVGLAD-RANEWPAALSGGQKQRVALARALIHRPGLLLLDEPlgaLDALTRIEMQ---DLIESLWQQHGFTVLL 189
                         90       100
                 ....*....|....*....|....*
gi 488284725 698 EHHiDV---IKSAD--WLIELGPEG 717
Cdd:PRK11247 190 VTH-DVseaVAMADrvLLIEEGKIG 213
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
622-731 2.52e-03

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 40.95  E-value: 2.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 622 LKNLLE-VGLSYL--KLNQSLS---TLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVEE--GNS 693
Cdd:COG4178  460 LREALEaVGLGHLaeRLDEEADwdqVLSLGEQQRLAFARLLLHKPDWLFLDEATSAL---DEENEAALYQLLREElpGTT 536
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 488284725 694 LILLEHHIDVIKSADWLIELGPEGgenGGQLLFTGTPA 731
Cdd:COG4178  537 VISVGHRSTLAAFHDRVLELTGDG---SWQLLPAEAPA 571
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
642-700 2.66e-03

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: 39.82  E-value: 2.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHH 700
Cdd:cd03217  105 FSGGEKKRNEILQLLLLEPDLAILDEPDSGLDIDALRLVAEVINKLREEGKSVLIITHY 163
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
634-702 2.86e-03

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: 39.96  E-value: 2.86e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 634 KLNQSLSTLSGGELQRVKLADT-LHQKKAIYLmDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHHID 702
Cdd:cd03269  121 YANKRVEELSKGNQQKVQFIAAvIHDPELLIL-DEPFSGLDPVNVELLKDVIRELARAGKTVILSTHQME 189
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
629-736 2.87e-03

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: 40.48  E-value: 2.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  629 GLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHHID-VIKS 706
Cdd:TIGR02142 120 GIGHL-LGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEILPYLERLHAEFGiPILYVSHSLQeVLRL 198
                          90       100       110
                  ....*....|....*....|....*....|
gi 488284725  707 ADWLIELgpeggeNGGQLLFTGTPANMLNS 736
Cdd:TIGR02142 199 ADRVVVL------EDGRVAAAGPIAEVWAS 222
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
304-404 3.11e-03

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 40.58  E-value: 3.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 304 IQEELLV----------RLEALINIGLSYLTLGRATET----LSGGEAQRIKIAKyvnSALNDI-MYILDEPSAGLHPKD 368
Cdd:PRK13536 131 VRENLLVfgryfgmstrEIEAVIPSLLEFARLESKADArvsdLSGGMKRRLTLAR---ALINDPqLLILDEPTTGLDPHA 207
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 488284725 369 IERISRALLNLKNKGNTVVLVEHnpqLIREADFIID 404
Cdd:PRK13536 208 RHLIWERLRSLLARGKTILLTTH---FMEEAERLCD 240
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
635-668 3.45e-03

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: 39.55  E-value: 3.45e-03
                         10        20        30
                 ....*....|....*....|....*....|....
gi 488284725 635 LNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEP 668
Cdd:cd03301  124 LDRKPKQLSGGQRQRVALGRAIVREPKVFLMDEP 157
hmuV PRK13547
heme ABC transporter ATP-binding protein;
639-738 3.50e-03

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 40.20  E-value: 3.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 639 LSTLSGGELQRVKLADTLHQ--------KKAIY-LMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLIL-LEHHIDV-IKSA 707
Cdd:PRK13547 143 VTTLSGGELARVQFARVLAQlwpphdaaQPPRYlLLDEPTAALDLAHQHRLLDTVRRLARDWNLGVLaIVHDPNLaARHA 222
                         90       100       110
                 ....*....|....*....|....*....|.
gi 488284725 708 DWLIELGpeggenGGQLLFTGTPANMLNSTH 738
Cdd:PRK13547 223 DRIAMLA------DGAIVAHGAPADVLTPAH 247
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
642-711 3.54e-03

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: 39.50  E-value: 3.54e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRMVE--EGNSLILLEHHIDVIKSADWLI 711
Cdd:cd03245  141 LSGGQRQAVALARALLNDPPILLLDEPTSAM---DMNSEERLKERLRQllGDKTLIIITHRPSLLDLVDRII 209
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
14-40 3.54e-03

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: 38.78  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*..
gi 488284725   14 LKNVSVNIPKKQLTVVTGLSGSGKSSL 40
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTL 27
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
4-41 3.67e-03

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: 40.59  E-value: 3.67e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 488284725   4 IEIKHAT-------QNNLKNVSVNIPKKQLTVVTGLSGSGKSSLV 41
Cdd:COG2274  474 IELENVSfrypgdsPPVLDNISLTIKPGERVAIVGRSGSGKSTLL 518
DnaJ_zf cd10719
Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of ...
553-582 3.87e-03

Zinc finger domain of DnaJ and HSP40; Central/middle or CxxCxGxG-motif containing domain of DnaJ/Hsp40 (heat shock protein 40). DnaJ proteins are highly conserved and play crucial roles in protein translation, folding, unfolding, translocation, and degradation. They act primarily by stimulating the ATPase activity of Hsp70s, an important chaperonin family. Hsp40 proteins are characterized by the presence of an N-terminal J domain, which mediates the interaction with Hsp70. This central domain contains four repeats of a CxxCxGxG motif and binds to two Zinc ions. It has been implicated in substrate binding.


Pssm-ID: 199908 [Multi-domain]  Cd Length: 65  Bit Score: 36.46  E-value: 3.87e-03
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 488284725 553 CPTCKGKGIIVS-----DMSFMedVTSICETCHGT 582
Cdd:cd10719   18 CPTCGGSGQVRQvqgtgFGFFQ--TQTTCPTCGGT 50
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
642-705 3.97e-03

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 39.61  E-value: 3.97e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGL------HLIDIQQSLQlfnrmvEEGNSLILLEHHIDVIK 705
Cdd:PRK11124 142 LSGGQQQRVAIARALMMEPQVLLFDEPTAALdpeitaQIVSIIRELA------ETGITQVIVTHEVEVAR 205
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
642-715 4.29e-03

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: 40.70  E-value: 4.29e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725   642 LSGGELQRVKLADTLHQKKAIYLMDEPtdgLHLIDIQQSLQLFNRMVE-----EGNSLILLEHHIDVIKSADWLI----- 711
Cdd:TIGR00957  761 LSGGQKQRVSLARAVYSNADIYLFDDP---LSAVDAHVGKHIFEHVIGpegvlKNKTRILVTHGISYLPQVDVIIvmsgg 837

                   ....*..
gi 488284725   712 ---ELGP 715
Cdd:TIGR00957  838 kisEMGS 844
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
14-40 4.32e-03

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 39.27  E-value: 4.32e-03
                         10        20
                 ....*....|....*....|....*..
gi 488284725  14 LKNVSVNIPKKQLTVVTGLSGSGKSSL 40
Cdd:COG2884   18 LSDVSLEIEKGEFVFLTGPSGAGKSTL 44
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
298-410 4.39e-03

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 39.09  E-value: 4.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 298 LSLIKNIQ-------EELLVRLEALINIGLSYLTlGRATETLSGGEAQRIKIAKY--VNSALndimYILDEPSAGLHPKD 368
Cdd:PRK13539  88 LTVAENLEfwaaflgGEELDIAAALEAVGLAPLA-HLPFGYLSAGQKRRVALARLlvSNRPI----WILDEPTAALDAAA 162
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 488284725 369 IERISRALLNLKNKGNTVVLVEHNPQLIREADfIIDIGPFAG 410
Cdd:PRK13539 163 VALFAELIRAHLAQGGIVIAATHIPLGLPGAR-ELDLGPFAA 203
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
312-393 4.47e-03

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: 39.01  E-value: 4.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 312 LEALINIGLSYLTlGRATETLSGGEAQRIKIAK-YVNSAlndIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVE 390
Cdd:cd03231  107 EEALARVGLNGFE-DRPVAQLSAGQQRRVALARlLLSGR---PLWILDEPTTALDKAGVARFAEAMAGHCARGGMVVLTT 182

                 ...
gi 488284725 391 HNP 393
Cdd:cd03231  183 HQD 185
PLN03232 PLN03232
ABC transporter C family member; Provisional
325-457 4.64e-03

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 40.73  E-value: 4.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  325 LGRATETLSGGEAQRIKIAKYVNSalNDIMYILDEPSAGLHPKDIERISRALLNLKNKGNTVVLVEHNPQLIREADFIID 404
Cdd:PLN03232  734 IGERGVNISGGQKQRVSMARAVYS--NSDIYIFDDPLSALDAHVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIIL 811
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488284725  405 IGPfagengGHVQFSGTYDAFLASKTLTSQALQEPLPLNDQPRKARKSLSIEH 457
Cdd:PLN03232  812 VSE------GMIKEEGTFAELSKSGSLFKKLMENAGKMDATQEVNTNDENILK 858
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
628-702 4.93e-03

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 39.18  E-value: 4.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488284725 628 VGLSYLkLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGN-SLILLEHHID 702
Cdd:PRK10771 117 MGIEDL-LARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLTLVSQVCQERQlTLLMVSHSLE 191
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
332-434 4.95e-03

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 40.39  E-value: 4.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 332 LSGGEAQRIKIAKyvnsAL--NDIMYILDEPSAGLHPKDiERISRALLNLKNKGNTVVLVEHNPQLIREADFIIDIgpfa 409
Cdd:PRK11176 481 LSGGQRQRIAIAR----ALlrDSPILILDEATSALDTES-ERAIQAALDELQKNRTSLVIAHRLSTIEKADEILVV---- 551
                         90       100
                 ....*....|....*....|....*
gi 488284725 410 gENGGHVQfSGTYDAFLASKTLTSQ 434
Cdd:PRK11176 552 -EDGEIVE-RGTHAELLAQNGVYAQ 574
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
14-41 4.97e-03

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: 39.47  E-value: 4.97e-03
                         10        20
                 ....*....|....*....|....*...
gi 488284725  14 LKNVSVNIPKKQLTVVTGLSGSGKSSLV 41
Cdd:cd03256   17 LKDVSLSINPGEFVALIGPSGAGKSTLL 44
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
553-582 5.03e-03

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 36.00  E-value: 5.03e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 488284725  553 CPTCKGKGIIV----SDMSFMEdVTSICETCHGT 582
Cdd:pfam00684  18 CPTCGGTGQVRrvqqTGPGFFQ-MQSTCPTCGGT 50
cbiO PRK13640
energy-coupling factor transporter ATPase;
332-403 5.34e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 39.40  E-value: 5.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKGN-TVVLVEHNPQLIREADFII 403
Cdd:PRK13640 144 LSGGQKQRVAIAGIL--AVEPKIIILDESTSMLDPAGKEQILKLIRKLKKKNNlTVISITHDIDEANMADQVL 214
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
621-713 5.48e-03

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 39.03  E-value: 5.48e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 621 SLKNLLEVGLSYlKLNQSLSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRM-VEEGNSLILLEH 699
Cdd:PRK11629 126 ALEMLAAVGLEH-RANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNLDARNADSIFQLLGELnRLQGTAFLVVTH 204
                         90
                 ....*....|....
gi 488284725 700 HIDVIKSADWLIEL 713
Cdd:PRK11629 205 DLQLAKRMSRQLEM 218
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
332-392 5.64e-03

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 39.31  E-value: 5.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488284725 332 LSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNKgNTVVLVEHN 392
Cdd:PRK14271 164 LSGGQQQLLCLARTL--AVNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHN 221
PTZ00243 PTZ00243
ABC transporter; Provisional
642-736 5.76e-03

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 40.15  E-value: 5.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  642 LSGGELQRVKLADTLHQKKAIYLMDEPTDGLhlidiqqSLQLFNRMVEE-------GNSLILLEHHIDVIKSADWLIELG 714
Cdd:PTZ00243  783 LSGGQKARVSLARAVYANRDVYLLDDPLSAL-------DAHVGERVVEEcflgalaGKTRVLATHQVHVVPRADYVVALG 855
                          90       100
                  ....*....|....*....|..
gi 488284725  715 peggenGGQLLFTGTPANMLNS 736
Cdd:PTZ00243  856 ------DGRVEFSGSSADFMRT 871
DnaJ_CXXCXGXG pfam00684
DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four ...
553-583 6.13e-03

DnaJ central domain; The central cysteine-rich (CR) domain of DnaJ proteins contains four repeats of the motif CXXCXGXG where X is any amino acid. The isolated cysteine rich domain folds in zinc dependent fashion. Each set of two repeats binds one unit of zinc. Although this domain has been implicated in substrate binding, no evidence of specific interaction between the isolated DNAJ cysteine rich domain and various hydrophobic peptides has been found.


Pssm-ID: 459904 [Multi-domain]  Cd Length: 65  Bit Score: 36.00  E-value: 6.13e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 488284725  553 CPTCKGKGIIVSDMsfmedvtsiCETCHGTR 583
Cdd:pfam00684  44 CPTCGGTGKIIKDP---------CKKCKGKG 65
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
639-728 6.93e-03

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: 38.30  E-value: 6.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 639 LSTLSGGELQRVKLADTLHQKKAIYLMDEPTDGLHLIDIQQSLQLFNRMVEEGNSLILLEHH--IDVIKSADWLIELGPe 716
Cdd:cd03213  109 LRGLSGGERKRVSIALELVSNPSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQpsSEIFELFDKLLLLSQ- 187
                         90
                 ....*....|..
gi 488284725 717 ggengGQLLFTG 728
Cdd:cd03213  188 -----GRVIYFG 194
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
640-719 7.20e-03

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: 39.01  E-value: 7.20e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 640 STLSGGELQRVKLADTLHQKKAIYLMDEPTDGLhliDIQQSLQLFNRM--VEEGNSLILLEHHIDVIKSADWLIELgpEG 717
Cdd:cd03252  137 AGLSGGQRQRIAIARALIHNPRILIFDEATSAL---DYESEHAIMRNMhdICAGRTVIIIAHRLSTVKNADRIIVM--EK 211

                 ..
gi 488284725 718 GE 719
Cdd:cd03252  212 GR 213
cbiO PRK13642
energy-coupling factor transporter ATPase;
305-403 7.74e-03

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 38.92  E-value: 7.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 305 QEELLVRL-EALINIG-LSYLTlgRATETLSGGEAQRIKIAKYVnsALNDIMYILDEPSAGLHPKDIERISRALLNLKNK 382
Cdd:PRK13642 114 REEMIKRVdEALLAVNmLDFKT--REPARLSGGQKQRVAVAGII--ALRPEIIILDESTSMLDPTGRQEIMRVIHEIKEK 189
                         90       100
                 ....*....|....*....|..
gi 488284725 383 GN-TVVLVEHNPQLIREADFII 403
Cdd:PRK13642 190 YQlTVLSITHDLDEAASSDRIL 211
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
305-429 8.08e-03

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: 39.72  E-value: 8.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725  305 QEELLVRLE-ALINIGLSYLTLGRATE------TLSGGEAQRIKIAKYVNSALNdiMYILDEPSAGLHPKDIERISRALL 377
Cdd:TIGR01193 578 QDEIWAACEiAEIKDDIENMPLGYQTElseegsSISGGQKQRIALARALLTDSK--VLILDESTSNLDTITEKKIVNNLL 655
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 488284725  378 NLKNKgnTVVLVEHNPQLIREADFIIDIgpfageNGGHVQFSGTYDAFLASK 429
Cdd:TIGR01193 656 NLQDK--TIIFVAHRLSVAKQSDKIIVL------DHGKIIEQGSHDELLDRN 699
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
627-745 9.23e-03

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 38.34  E-value: 9.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488284725 627 EVGLSYLK--LNQSLStlsGGELQRVKLADTLHQKKAIYLMDEP---TDGLHLIDIQQSLQlfnRMVEEGNSLILLEHHI 701
Cdd:PRK10895 124 EFHIEHLRdsMGQSLS---GGERRRVEIARALAANPKFILLDEPfagVDPISVIDIKRIIE---HLRDSGLGVLITDHNV 197
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 488284725 702 ----DVIKSAdWLIelgpeggeNGGQLLFTGTPANMLNSTHsITKGYL 745
Cdd:PRK10895 198 retlAVCERA-YIV--------SQGHLIAHGTPTEILQDEH-VKRVYL 235
 
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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