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Conserved domains on  [gi|1184609190|ref|WP_085171193|]
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ATP-binding cassette domain-containing protein [Mycobacterium paraense]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
290-510 1.63e-67

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


:

Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 223.79  E-value: 1.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1131   158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAErLCDRVAIID-KGRIVADGTPDEL 218
3a01204 super family cl36780
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 302-777 2.32e-52

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


The actual alignment was detected with superfamily member TIGR00955:

Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 193.34  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTT---GSVTFEGHNIHTEygSLRTRIGMVPQDDVVHRQLT 378
Cdd:TIGR00955  38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPTLT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDT------RVDKLSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMApGGKTAYLGPPDQIggamgttnwAQIFAKVGAdp 530
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFELFDKIILMA-EGRVAYLGSPDQA---------VPFFSDLGH-- 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 531 deanrrflaqnkPPPPVESaPADL------GAPAHTS--------VRHQF--STIAR---RQVRLVVSDRAYFV------ 585
Cdd:TIGR00955 264 ------------PCPENYN-PADFyvqvlaVIPGSENesreriekICDSFavSDIGRdmlVNTNLWSGKAGGLVkdsenm 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 586 ------------FLALL----------PfVLGALSLTVPGNTGFGIASPTSGTPDESAQILTLTSVAAVFMgTALTIRDL 643
Cdd:TIGR00955 331 egigynaswwtqFYALLkrswlsvlrdP-LLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFL-TNMTFQNV 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 644 IG-------ERAIFRREQAVGL-STGAYLAAKLAVFCVFAVVQAAIVTVIVLvgkgaptqPAVLLgNPSFELFVTIAAMC 715
Cdd:TIGR00955 409 FPvinvftaELPVFLRETRSGLyRVSAYFLAKTIAELPLFIILPALFTSITY--------WMIGL-RSGATHFLTFLFLV 479

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 716 VASAV----LGLVLSSLARSSEQIMPLLVVSLMLQLVLAG-----GMVPVTGRiFLDQLSWLlpsRWGYAA 777
Cdd:TIGR00955 480 TLVANvatsFGYLISCAFSSTSMALTVGPPFVIPFLLFGGffinsDSIPVYFK-WLSYLSWF---RYGNEG 546
FHA super family cl00062
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 9-100 3.57e-26

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


The actual alignment was detected with superfamily member cd22694:

Pssm-ID: 469597 [Multi-domain]  Cd Length: 93  Bit Score: 102.79  E-value: 3.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190   9 LTVRSQRWEGNFAPGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVPAVDIQDGQSVNI 88
Cdd:cd22694     1 LTIRIPGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGTRVRL 80

                          90
                  ....*....|...
gi 1184609190  89 GKP-DGPLITFHV 100
Cdd:cd22694    81 GDPtDGPALTVVV 93
FHA_Rv1747-like_rpt2 super family cl41915
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 201-273 1.74e-22

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


The actual alignment was detected with superfamily member cd22737:

Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 1.74e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 201 GAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVFT 273
Cdd:cd22737    21 QAVRIGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTFVNGLRVDAALLHDGDVVTIGDIDFVFE 93
COG3456 super family cl34616
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 22-183 5.61e-05

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


The actual alignment was detected with superfamily member COG3456:

Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 46.29  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHP--LVARAHLLLRFDKGRWVAVDnHSLNGVFLNGQRVPA-----VDIQDGQSVNIgkpdGP 94
Cdd:COG3456    24 GRGGGTIGRSADCDWVLPDPdrSVSRRHAEIRFRDGAFCLTD-LSTNGTFLNGSDHPLgpgrpVRLRDGDRLRI----GD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  95 L-ITFHVGQHQGTVGLLP----------PTETLPTIVAPSGPLPVRPRGPAPRPPAPSRDETPRTDAIP--IIPP--GGP 159
Cdd:COG3456    99 YeIRVEISGEDEGADDPLaaapepavssPSNLSDTEAAPDAALAFSFSLDPLEALDEAATEAPATADDPpsLLPEdwLPS 178

                         170       180
                  ....*....|....*....|....
gi 1184609190 160 ASPAAQEENPPTQIGVSGEIAEFP 183
Cdd:COG3456   179 AAPVADEAAAQAIDQLPSAAAPAP 202
 
Name Accession Description Interval E-value
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
290-510 1.63e-67

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 223.79  E-value: 1.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1131   158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAErLCDRVAIID-KGRIVADGTPDEL 218
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 290-505 7.45e-63

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: 209.71  E-value: 7.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI------GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP--TTGSVTFEGHNIHTEygSLR 361
Cdd:cd03213     4 LSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR--SFR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQDDVVHRQLTVNQALGYAAELRlppdtskadraqvvaqvldelgltkhgdtrvdKLSGGQRKRASVALELLTG 441
Cdd:cd03213    82 KIIGYVPQDDILHPTLTVRETLMFAAKLR--------------------------------GLSGGERKRVSIALELVSN 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 442 PSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD--VCDQVLLMAPgGKTAYLG 505
Cdd:cd03213   130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQ-GRVIYFG 194
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 302-777 2.32e-52

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 193.34  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTT---GSVTFEGHNIHTEygSLRTRIGMVPQDDVVHRQLT 378
Cdd:TIGR00955  38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPTLT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDT------RVDKLSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMApGGKTAYLGPPDQIggamgttnwAQIFAKVGAdp 530
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFELFDKIILMA-EGRVAYLGSPDQA---------VPFFSDLGH-- 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 531 deanrrflaqnkPPPPVESaPADL------GAPAHTS--------VRHQF--STIAR---RQVRLVVSDRAYFV------ 585
Cdd:TIGR00955 264 ------------PCPENYN-PADFyvqvlaVIPGSENesreriekICDSFavSDIGRdmlVNTNLWSGKAGGLVkdsenm 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 586 ------------FLALL----------PfVLGALSLTVPGNTGFGIASPTSGTPDESAQILTLTSVAAVFMgTALTIRDL 643
Cdd:TIGR00955 331 egigynaswwtqFYALLkrswlsvlrdP-LLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFL-TNMTFQNV 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 644 IG-------ERAIFRREQAVGL-STGAYLAAKLAVFCVFAVVQAAIVTVIVLvgkgaptqPAVLLgNPSFELFVTIAAMC 715
Cdd:TIGR00955 409 FPvinvftaELPVFLRETRSGLyRVSAYFLAKTIAELPLFIILPALFTSITY--------WMIGL-RSGATHFLTFLFLV 479

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 716 VASAV----LGLVLSSLARSSEQIMPLLVVSLMLQLVLAG-----GMVPVTGRiFLDQLSWLlpsRWGYAA 777
Cdd:TIGR00955 480 TLVANvatsFGYLISCAFSSTSMALTVGPPFVIPFLLFGGffinsDSIPVYFK-WLSYLSWF---RYGNEG 546
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 294-534 9.37e-39

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 156.04  E-value: 9.37e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  294 EVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP---TTGSVTFEGHNIHTeygSLRTRIGMVPQD 370
Cdd:TIGR00956  768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS---SFQRSIGYVQQQ 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  371 DVVHRQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRV----DKLSGGQRKRASVALELLTGPSLLI 446
Cdd:TIGR00956  845 DLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLL 924

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  447 -LDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMAPGGKTAYLGPpdqIGgaMGTTNWAQIF 523
Cdd:TIGR00956  925 fLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEFDRLLLLQKGGQTVYFGD---LG--ENSHTIINYF 999

                          250
                   ....*....|...
gi 1184609190  524 AKVGAD--PDEAN 534
Cdd:TIGR00956 1000 EKHGAPkcPEDAN 1012
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 305-452 4.70e-38

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 138.93  E-value: 4.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH-TEYGSLRTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 384 GYAAELRLPPDTSKADRAQvvaQVLDELGLTKHGDTRVDK----LSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAE---EALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 290-509 1.06e-36

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 138.75  E-value: 1.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRIGMVP 368
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTVNQ--ALGyaaelRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVAlELLT------ 440
Cdd:PRK13548   83 QHSSLSFPFTVEEvvAMG-----RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA-RVLAqlwepd 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 441 -GPSLLILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSL----TYldvCDQVLLMApGGKTAYLGPPDQ 509
Cdd:PRK13548  157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLnlaaRY---ADRIVLLH-QGRLVADGTPAE 227
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
300-483 2.79e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 112.33  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHnihteygslrTRIGMVPQDDVVHRQL-- 377
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSLpl 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQ--ALGYAAELRLPPDTSKADRAqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:NF040873   73 TVRDlvAMGRWARRGLWRRLTRDDRA-AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                         170       180
                  ....*....|....*....|....*...
gi 1184609190 456 PALDLQVMTMLRQLADAGRVVLVVTHSL 483
Cdd:NF040873  152 AESRERIIALLAEEHARGATVVVVTHDL 179
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 9-100 3.57e-26

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 102.79  E-value: 3.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190   9 LTVRSQRWEGNFAPGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVPAVDIQDGQSVNI 88
Cdd:cd22694     1 LTIRIPGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGTRVRL 80

                          90
                  ....*....|...
gi 1184609190  89 GKP-DGPLITFHV 100
Cdd:cd22694    81 GDPtDGPALTVVV 93
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 201-273 1.74e-22

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 1.74e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 201 GAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVFT 273
Cdd:cd22737    21 QAVRIGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTFVNGLRVDAALLHDGDVVTIGDIDFVFE 93
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
303-498 1.29e-20

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 91.32  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 303 NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEYGSLRTR-IGMVPQDDVVHRQL 377
Cdd:NF038007   19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnlsYSQKIILRRElIGYIFQSFNLIPHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPA 457
Cdd:NF038007   99 SIFDNVALPLKYR---GVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSK 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1184609190 458 LDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:NF038007  176 NARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDG 216
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
205-272 1.82e-19

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 83.85  E-value: 1.82e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRV-GSAVLAEGDVVTIGNVDLVF 272
Cdd:COG1716    25 IGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVtEPAPLRDGDVIRLGKTELRF 93
YadH COG0842
ABC-type multidrug transport system, permease component [Defense mechanisms];
623-832 5.52e-15

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


Pssm-ID: 440604 [Multi-domain]  Cd Length: 200  Bit Score: 74.47  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 623 ILTLTSVAAVFMGTALTI-RDLigERAIFRREQAVGLSTGAYLAAKLAVFCVFAVVQAAIVTVIVLVGKGAPtqpavLLG 701
Cdd:COG0842     9 LLAMSLLFTALMLTALSIaRER--EQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVP-----LRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 702 NPSFELFVTIAAMCVASAVLGLVLSSLARSSEQIMPLLVVSLMLQLVLAGGMVPVTG-RIFLDQLSWLLPSRWGyaasas 780
Cdd:COG0842    82 LSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESlPGWLQAIAYLNPLTYF------ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 781 tvnVRLLVPGSLVQQDshwahtPAAWLLDMGMLVALSVLYAAIVRWRIRLRR 832
Cdd:COG0842   156 ---VEALRALFLGGAG------LADVWPSLLVLLAFAVVLLALALRLFRRRL 198
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
307-595 1.10e-14

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 78.24  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 307 RVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTVNQALGYA 386
Cdd:NF033858  284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELH 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 387 AEL-RLPPdtskADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTM 465
Cdd:NF033858  364 ARLfHLPA----AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 466 LRQLADAGRV-VLVVTHSLTYLDVCDQVLLM-ApgGKTAYLGPPDQIGGAMGTTNWAQIFAKVGADPDEAnrrflAQNKP 543
Cdd:NF033858  440 LIELSREDGVtIFISTHFMNEAERCDRISLMhA--GRVLASDTPAALVAARGAATLEEAFIAYLEEAAGA-----AAAPA 512

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 544 PPPVESAPADLGAPAHTSVRHQFS-----TIARRQVRLVVSD--RAYFVFL--ALLPFVLG 595
Cdd:NF033858  513 AAAAPAAAAAAPAAPAPAPRRRFSlrrllAYARREALELLRDpiRLTFALLgsVILMFVMG 573
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 205-265 1.94e-13

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 65.68  E-value: 1.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGT-EIRDAHSINGTFVNGIRVGS--AVLAEGDVVTI 265
Cdd:pfam00498   3 IGRSPDCDIVLDDPSVSRRHAEIRYDGGGRfYLEDLGSTNGTFVNGQRLGPepVRLKDGDVIRL 66
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
22-101 2.12e-13

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 66.52  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVP-AVDIQDGQSVNIGKpdgPLITFHV 100
Cdd:COG1716    19 DGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTePAPLRDGDVIRLGK---TELRFRL 95


                  .
gi 1184609190 101 G 101
Cdd:COG1716    96 S 96
ABC2_membrane pfam01061
ABC-2 type transporter;
569-777 1.86e-12

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 66.91  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 569 IARRQVRLVVSDRAYFVFLALLPFVLGALSLTVPGNTGFGIASPTSGtpdeSAQILTLTSVAAVFMGTALTIRDLigERA 648
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRP----GLLFFSILFNAFSALSGISPVFEK--ERG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 649 IFRREQAVGL-STGAYLAAKLAVFCVFAVVQAAIVTVIVLVGKGAPTQPAVLLgnpsFELFVTIAAMCVASAvLGLVLSS 727
Cdd:pfam01061  75 VLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFF----LFLLVLLLTALAASS-LGLFISA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 728 LARSSEQIMPLLVVSLMLQLVLAGGMVPVTgRI--FLDQLSWLLPSRWGYAA 777
Cdd:pfam01061 150 LAPSFEDASQLGPLVLLPLLLLSGFFIPID-SMpvWWQWIYYLNPLTYAIEA 200
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
289-515 1.37e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 67.07  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTlSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMvp 368
Cdd:NF000106   13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 qddvvHRQLTVNQALGYAAELRL-----PPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:NF000106   90 -----HRPVR*GRRESFSGRENLymigr*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQIGGAMG 515
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 26-88 1.56e-10

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 57.59  E-value: 1.56e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190  26 VVVGSDVRADLRVAHPLVARAHLLLRFDKG-RWVAVDNHSLNGVFLNGQRVP--AVDIQDGQSVNI 88
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGpePVRLKDGDVIRL 66
GguA NF040905
sugar ABC transporter ATP-binding protein;
301-498 1.25e-09

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 61.34  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG--YATPTTGSVTFEGHNIHTeygslRTrigmvpqddvVHRqlT 378
Cdd:NF040905  272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDV-----ST----------VSD--A 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAE------LRLPPD----TSKADRAQVV-AQVLDELGLTKHG--------------DTRVDKLSGG-QRKra 432
Cdd:NF040905  335 IDAGLAYVTEdrkgygLNLIDDikrnITLANLGKVSrRGVIDENEEIKVAeeyrkkmniktpsvFQKVGNLSGGnQQK-- 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 433 sVALE--LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:NF040905  413 -VVLSkwLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELpELLGMCDRIYVMNEG 480
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
291-456 3.29e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 60.52  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEygSLRTRIGM 366
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarHRR--AVCPRIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQddvvhrqltvnqALG---YaaelrlpPDTS---------------KADRAQVVAQVLDELGLTKHGDTRVDKLSGGQ 428
Cdd:NF033858   81 MPQ------------GLGknlY-------PTLSvfenldffgrlfgqdAAERRRRIDELLRATGLAPFADRPAGKLSGGM 141

                         170       180
                  ....*....|....*....|....*...
gi 1184609190 429 RKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:NF033858  142 KQKLGLCCALIHDPDLLILDEPTTGVDP 169
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 205-252 9.60e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 49.10  E-value: 9.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1184609190  205 IGR-SLDNDVVVHDVLASRHHAFLTATP-VGTEIRDAHSINGTFVNGIRV 252
Cdd:smart00240   3 IGRsSEDCDIQLDGPSISRRHAVIVYDGgGRFYLIDLGSTNGTFVNGKRI 52
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 26-75 2.01e-06

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 45.25  E-value: 2.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190   26 VVVG-SDVRADLRVAHPLVARAHLLLRFDKG-RWVAVDNHSLNGVFLNGQRV 75
Cdd:smart00240   1 VTIGrSSEDCDIQLDGPSISRRHAVIVYDGGgRFYLIDLGSTNGTFVNGKRI 52
GguA NF040905
sugar ABC transporter ATP-binding protein;
305-483 5.13e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG-YATPT-TGSVTFEGHniHTEYGSLRT--RIGMVpqddVVHRQLTVN 380
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYPHGSyEGEILFDGE--VCRFKDIRDseALGIV----IIHQELALI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGYAAELRLPPDTSKA---DRAQV---VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:NF040905   91 PYLSIAENIFLGNERAKRgviDWNETnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1184609190 455 ---DPA--LDLqvmtmLRQLADAGRVVLVVTHSL 483
Cdd:NF040905  171 neeDSAalLDL-----LLELKAQGITSIIISHKL 199
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 314-487 1.13e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  314 PGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVtfeghnihteygslrtrigmvpqddvvhrqltvnqalgyaaeLRLPP 393
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------IYIDG 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  394 DTSKADRAQVVAQVLdelgltkhgdTRVDKLSGGQRKRASVALELL--TGPSLLILDEPTSGLDPALDLQVM------TM 465
Cdd:smart00382  39 EDILEEVLDQLLLII----------VGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLlleelrLL 108

                          170       180
                   ....*....|....*....|..
gi 1184609190  466 LRQLADAGRVVLVVTHSLTYLD 487
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLG 130
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 22-183 5.61e-05

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 46.29  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHP--LVARAHLLLRFDKGRWVAVDnHSLNGVFLNGQRVPA-----VDIQDGQSVNIgkpdGP 94
Cdd:COG3456    24 GRGGGTIGRSADCDWVLPDPdrSVSRRHAEIRFRDGAFCLTD-LSTNGTFLNGSDHPLgpgrpVRLRDGDRLRI----GD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  95 L-ITFHVGQHQGTVGLLP----------PTETLPTIVAPSGPLPVRPRGPAPRPPAPSRDETPRTDAIP--IIPP--GGP 159
Cdd:COG3456    99 YeIRVEISGEDEGADDPLaaapepavssPSNLSDTEAAPDAALAFSFSLDPLEALDEAATEAPATADDPpsLLPEdwLPS 178

                         170       180
                  ....*....|....*....|....
gi 1184609190 160 ASPAAQEENPPTQIGVSGEIAEFP 183
Cdd:COG3456   179 AAPVADEAAAQAIDQLPSAAAPAP 202
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 205-281 5.73e-03

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 40.05  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 205 IGRSLDNDVVVHD--VLASRHHAFLTATPVGTEIRDaHSINGTFVNG----IRVG-SAVLAEGDVVTIGNVDL-VFTGGI 276
Cdd:TIGR03354  28 IGRSEDCDWVLPDpeRHVSGRHARIRYRDGAYLLTD-LSTNGVFLNGsgspLGRGnPVRLEQGDRLRLGDYEIrVSLGDP 106


                  ....*
gi 1184609190 277 LVRRQ 281
Cdd:TIGR03354 107 LVSRQ 111
 
Name Accession Description Interval E-value
CcmA COG1131
ABC-type multidrug transport system, ATPase component [Defense mechanisms];
290-510 1.63e-67

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


Pssm-ID: 440746 [Multi-domain]  Cd Length: 236  Bit Score: 223.79  E-value: 1.63e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:COG1131     1 IEVRGLTKRYGDKTALDGVSLTVEPGEIFGLLGPNGAGKTTTIRMLLGLLRPTSGEVRVLGEDVARDPAEVRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG1131    81 EPALYPDLTVRENLRFFARLY---GLPRKEARERIDELLELFGLTDAADRKVGTLSGGMKQRLGLALALLHDPELLILDE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1131   158 PTSGLDPEARRELWELLRELAAEGKTVLLSTHYLEEAErLCDRVAIID-KGRIVADGTPDEL 218
ABCG_EPDR cd03213
Eye pigment and drug resistance transporter subfamily G of the ATP-binding cassette ...
 290-505 7.45e-63

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: 209.71  E-value: 7.45e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI------GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP--TTGSVTFEGHNIHTEygSLR 361
Cdd:cd03213     4 LSFRNLTVTVksspskSGKQLLKNVSGKAKPGELTAIMGPSGAGKSTLLNALAGRRTGlgVSGEVLINGRPLDKR--SFR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQDDVVHRQLTVNQALGYAAELRlppdtskadraqvvaqvldelgltkhgdtrvdKLSGGQRKRASVALELLTG 441
Cdd:cd03213    82 KIIGYVPQDDILHPTLTVRETLMFAAKLR--------------------------------GLSGGERKRVSIALELVSN 129

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 442 PSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD--VCDQVLLMAPgGKTAYLG 505
Cdd:cd03213   130 PSLLFLDEPTSGLDSSSALQVMSLLRRLADTGRTIICSIHQPSSEIfeLFDKLLLLSQ-GRVIYFG 194
NatA COG4555
ABC-type Na+ transport system, ATPase component NatA [Energy production and conversion, ...
 290-523 1.97e-53

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: 185.45  E-value: 1.97e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:COG4555     2 IEVENLSKKYGKVPALKDVSFTAKDGEITGLLGPNGAGKTTLLRMLAGLLKPDSGSILIDGEDVRKEPREARRQIGVLPD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG4555    82 ERGLYDRLTVRENIRYFAELY---GLFDEELKKRIEELIELLGLEEFLDRRVGELSTGMKKKVALARALVHDPKVLLLDE 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMApGGKTAYLGPPDQIGGAMGTTNWAQIF 523
Cdd:COG4555   159 PTNGLDVMARRLLREILRALKKEGKTVLFSSHIMQEVeALCDRVVILH-KGKVVAQGSLDELREEIGEENLEDAF 232
3a01204 TIGR00955
The Eye Pigment Precursor Transporter (EPP) Family protein; [Transport and binding proteins, ...
 302-777 2.32e-52

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


Pssm-ID: 273361 [Multi-domain]  Cd Length: 617  Bit Score: 193.34  E-value: 2.32e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTT---GSVTFEGHNIHTEygSLRTRIGMVPQDDVVHRQLT 378
Cdd:TIGR00955  38 KHLLKNVSGVAKPGELLAVMGSSGAGKTTLMNALAFRSPKGVkgsGSVLLNGMPIDAK--EMRAISAYVQQDDLFIPTLT 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDT------RVDKLSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:TIGR00955 116 VREHLMFQAHLRMPRRVTKKEKRERVDEVLQALGLRKCANTrigvpgRVKGLSGGERKRLAFASELLTDPPLLFCDEPTS 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMApGGKTAYLGPPDQIggamgttnwAQIFAKVGAdp 530
Cdd:TIGR00955 196 GLDSFMAYSVVQVLKGLAQKGKTIICTIHqpSSELFELFDKIILMA-EGRVAYLGSPDQA---------VPFFSDLGH-- 263

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 531 deanrrflaqnkPPPPVESaPADL------GAPAHTS--------VRHQF--STIAR---RQVRLVVSDRAYFV------ 585
Cdd:TIGR00955 264 ------------PCPENYN-PADFyvqvlaVIPGSENesreriekICDSFavSDIGRdmlVNTNLWSGKAGGLVkdsenm 330

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 586 ------------FLALL----------PfVLGALSLTVPGNTGFGIASPTSGTPDESAQILTLTSVAAVFMgTALTIRDL 643
Cdd:TIGR00955 331 egigynaswwtqFYALLkrswlsvlrdP-LLLKVRLIQTMMTAILIGLIYLGQGLTQKGVQNINGALFLFL-TNMTFQNV 408

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 644 IG-------ERAIFRREQAVGL-STGAYLAAKLAVFCVFAVVQAAIVTVIVLvgkgaptqPAVLLgNPSFELFVTIAAMC 715
Cdd:TIGR00955 409 FPvinvftaELPVFLRETRSGLyRVSAYFLAKTIAELPLFIILPALFTSITY--------WMIGL-RSGATHFLTFLFLV 479

                         490       500       510       520       530       540       550
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 716 VASAV----LGLVLSSLARSSEQIMPLLVVSLMLQLVLAG-----GMVPVTGRiFLDQLSWLlpsRWGYAA 777
Cdd:TIGR00955 480 TLVANvatsFGYLISCAFSSTSMALTVGPPFVIPFLLFGGffinsDSIPVYFK-WLSYLSWF---RYGNEG 546
FepC COG1120
ABC-type cobalamin/Fe3+-siderophores transport system, ATPase component [Inorganic ion ...
 290-510 3.74e-50

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: 176.77  E-value: 3.74e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHtEYGS--LRTRIGMV 367
Cdd:COG1120     2 LEAENLSVGYGGRPVLDDVSLSLPPGEVTALLGPNGSGKSTLLRALAGLLKPSSGEVLLDGRDLA-SLSRreLARRIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDVVHRQLTVNQ--ALGYAAELRLPPDTSKADRAqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:COG1120    81 PQEPPAPFGLTVRElvALGRYPHLGLFGRPSAEDRE-AVEEALERTGLEHLADRPVDELSGGERQRVLIARALAQEPPLL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTY-LDVCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:COG1120   160 LLDEPTSHLDLAHQLEVLELLRRLArERGRTVVMVLHDLNLaARYADRLVLLKDGRIVAQ-GPPEEV 225
ZnuC COG1121
ABC-type Mn2+/Zn2+ transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 290-510 8.21e-50

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


Pssm-ID: 440738 [Multi-domain]  Cd Length: 245  Bit Score: 175.66  E-value: 8.21e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEygslRTRIGMVPQ 369
Cdd:COG1121     7 IELENLTVSYGGRPVLEDVSLTIPPGEFVAIVGPNGAGKSTLLKAILGLLPPTSGTVRLFGKPPRRA----RRRIGYVPQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQ--LTVNQ--ALGYAAELRLPPDTSKADRAQvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:COG1121    83 RAEVDWDfpITVRDvvLMGRYGRRGLFRRPSRADREA-VDEALERVGLEDLADRPIGELSGGQQQRVLLARALAQDPDLL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMApgGKTAYLGPPDQI 510
Cdd:COG1121   162 LLDEPFAGVDAATEEALYELLRELRREGKTILVVTHDLgAVREYFDRVLLLN--RGLVAHGPPEEV 225
EcfA2 COG1122
Energy-coupling factor transporter ATP-binding protein EcfA2 [Inorganic ion transport and ...
 290-510 1.58e-48

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: 171.36  E-value: 1.58e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI-GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS-LRTRIGMV 367
Cdd:COG1122     1 IELENLSFSYpGGTPALDDVSLSIEKGEFVAIIGPNGSGKSTLLRLLNGLLKPTSGEVLVDGKDITKKNLReLRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQD-DvvhRQL---TVNQALGYAAE-LRLPPDtskaDRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGP 442
Cdd:COG1122    81 FQNpD---DQLfapTVEEDVAFGPEnLGLPRE----EIRERVEEALELVGLEHLADRPPHELSGGQKQRVAIAGVLAMEP 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 443 SLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1122   154 EVLVLDEPTAGLDPRGRRELLELLKRLNKEGKTVIIVTHDLDLVaELADRVIVLD-DGRIVADGTPREV 221
ABC_cobalt_CbiO_domain1 cd03225
First domain of the ATP-binding cassette component of cobalt transport system; Domain I of the ...
 291-498 8.39e-48

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: 168.80  E-value: 8.39e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKN--LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRIGMV 367
Cdd:cd03225     1 ELKNLSFSYPDGArpALDDISLTIKKGEFVLIVGPNGSGKSTLLRLLNGLLGPTSGEVLVDGKDLtKLSLKELRRKVGLV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDdvVHRQL---TVNQALGYAAELRLppdTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:cd03225    81 FQN--PDDQFfgpTVEEEVAFGLENLG---LPEEEIEERVEEALELVGLEGLRDRSPFTLSGGQKQRVAIAGVLAMDPDI 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:cd03225   156 LLLDEPTAGLDPAGRRELLELLKKLKAEGKTIIIVTHDLDLLlELADRVIVLEDG 210
ABC_subfamily_A cd03263
ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily ...
 290-510 7.57e-47

ATP-binding cassette domain of the lipid transporters, subfamily A; The ABCA subfamily mediates the transport of a variety of lipid compounds. Mutations of members of ABCA subfamily are associated with human genetic diseases, such as, familial high-density lipoprotein (HDL) deficiency, neonatal surfactant deficiency, degenerative retinopathies, and congenital keratinization disorders. The ABCA1 protein is involved in disorders of cholesterol transport and high-density lipoprotein (HDL) biosynthesis. The ABCA4 (ABCR) protein transports vitamin A derivatives in the outer segments of photoreceptor cells, and therefore, performs a crucial step in the visual cycle. The ABCA genes are not present in yeast. However, evolutionary studies of ABCA genes indicate that they arose as transporters that subsequently duplicated and that certain sets of ABCA genes were lost in different eukaryotic lineages.


Pssm-ID: 213230 [Multi-domain]  Cd Length: 220  Bit Score: 166.53  E-value: 7.57e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVN--FSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMV 367
Cdd:cd03263     1 LQIRNLTktYKKGTKPAVDDLSLNVYKGEIFGLLGHNGAGKTTTLKMLTGELRPTSGTAYINGYSIRTDRKAARQSLGYC 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03263    81 PQFDALFDELTVREHLRFYARLK---GLPKSEIKEEVELLLRVLGLTDKANKRARTLSGGMKRKLSLAIALIGGPSVLLL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDV-CDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03263   158 DEPTSGLDPASRRAIWDLILEVR-KGRSIILTTHSMDEAEAlCDRIAIMS-DGKLRCIGSPQEL 219
ABC_Metallic_Cations cd03235
ATP-binding cassette domain of the metal-type transporters; This family includes transporters ...
 291-496 1.49e-46

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


Pssm-ID: 213202 [Multi-domain]  Cd Length: 213  Bit Score: 165.40  E-value: 1.49e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEygslRTRIGMVPQD 370
Cdd:cd03235     1 EVEDLTVSYGGHPVLEDVSFEVKPGEFLAIVGPNGAGKSTLLKAILGLLKPTSGSIRVFGKPLEKE----RKRIGYVPQR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 371 DVVHRQ--LTVNQ--ALGYAAELRLPPDTSKADRAqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLI 446
Cdd:cd03235    77 RSIDRDfpISVRDvvLMGLYGHKGLFRRLSKADKA-KVDEALERVGLSELADRQIGELSGGQQQRVLLARALVQDPDLLL 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMA 496
Cdd:cd03235   156 LDEPFAGVDPKTQEDIYELLRELRREGMTILVVTHDLgLVLEYFDRVLLLN 206
ABC_DR_subfamily_A cd03230
ATP-binding cassette domain of the drug resistance transporter and related proteins, subfamily ...
 290-498 9.93e-45

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: 158.71  E-value: 9.93e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:cd03230     1 IEVRNLSKRYGKKTALDDISLTVEKGEIYGLLGPNGAGKTTLIKIILGLLKPDSGEIKVLGKDIKKEPEEVKRRIGYLPE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALgyaaelrlppdtskadraqvvaqvldelgltkhgdtrvdKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03230    81 EPSLYENLTVRENL---------------------------------------KLSGGMKQRLALAQALLHDPELLILDE 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:cd03230   122 PTSGLDPESRREFWELLRELKKEGKTILLSSHILEEAeRLCDRVAILNNG 171
COG4559 COG4559
ABC-type hemin transport system, ATPase component [Inorganic ion transport and metabolism];
290-509 2.44e-44

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


Pssm-ID: 443620 [Multi-domain]  Cd Length: 258  Bit Score: 160.67  E-value: 2.44e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGMVP 368
Cdd:COG4559     2 LEAENLSVRLGGRTLLDDVSLTLRPGELTAIIGPNGAGKSTLLKLLTGELTPSSGEVRLNGRPLAAwSPWELARRRAVLP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTVNQ--ALGyaaelRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKR-------ASVALELL 439
Cdd:COG4559    82 QHSSLAFPFTVEEvvALG-----RAPHGSSAAQDRQIVREALALVGLAHLAGRSYQTLSGGEQQRvqlarvlAQLWEPVD 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLdVCDQVLLMApGGKTAYLGPPDQ 509
Cdd:COG4559   157 GGPRWLFLDEPTSALDLAHQHAVLRLARQLARRGGGVVAVLHdlNLAAQ-YADRILLLH-QGRLVAQGTPEE 226
ABCG_White cd03234
White pigment protein homolog of ABCG transporter subfamily; The White subfamily represents ...
 301-505 2.64e-44

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: 159.36  E-value: 2.64e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP---TTGSVTFEGHNIHTEygSLRTRIGMVPQDDVVHRQL 377
Cdd:cd03234    19 YARILNDVSLHVESGQVMAILGSSGSGKTTLLDAISGRVEGggtTSGQILFNGQPRKPD--QFQKCVAYVRQDDILLPGL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQALGYAAELRLPPDTSKADRAQVVAQV-LDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:cd03234    97 TVRETLTYTAILRLPRKSSDAIRKKRVEDVlLRDLALTRIGGNLVKGISGGERRRVSIAVQLLWDPKVLILDEPTSGLDS 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 457 ALDLQVMTMLRQLADAGRVVLVVTHSLT--YLDVCDQVLLMApGGKTAYLG 505
Cdd:cd03234   177 FTALNLVSTLSQLARRNRIVILTIHQPRsdLFRLFDRILLLS-SGEIVYSG 226
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 255-510 2.97e-44

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: 167.77  E-value: 2.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 255 AVLAEGDVVTIGNVDLVFTGG-------ILVRRQEVAARTGG-----LEVREVNFS-----IGDKNLLERVSLTARPGTL 317
Cdd:COG1123   214 VVMDDGRIVEDGPPEEILAAPqalaavpRLGAARGRAAPAAAaaeplLEVRNLSKRypvrgKGGVRAVDDVSLTLRRGET 293

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 318 TAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS----LRTRIGMVPQDdvVHRQL----TVNQALGYAaeL 389
Cdd:COG1123   294 LGLVGESGSGKSTLARLLLGLLRPTSGSILFDGKDLTKLSRRslreLRRRVQMVFQD--PYSSLnprmTVGDIIAEP--L 369

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 390 RLPPDTSKADRAQVVAQVLDELGL-TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQ 468
Cdd:COG1123   370 RLHGLLSRAERRERVAELLERVGLpPDLADRYPHELSGGQRQRVAIARALALEPKLLILDEPTSALDVSVQAQILNLLRD 449

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 469 LADA-GRVVLVVTHSL-TYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1123   450 LQRElGLTYLFISHDLaVVRYIADRVAVMY-DGRIVEDGPTEEV 492
ABC_Org_Solvent_Resistant cd03261
ATP-binding cassette transport system involved in resistance to organic solvents; ABC ...
 290-510 3.63e-44

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: 159.20  E-value: 3.63e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH----TEYGSLRTRIG 365
Cdd:cd03261     1 IELRGLTKSFGGRTVLKGVDLDVRRGEILAIIGPSGSGKSTLLRLIVGLLRPDSGEVLIDGEDISglseAELYRLRRRMG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQLTVNQALGYAaeLRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:cd03261    81 MLFQSGALFDSLTVFENVAFP--LREHTRLSEEEIREIVLEKLEAVGLRGAEDLYPAELSGGMKKRVALARALALDPELL 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSL-TYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03261   159 LYDEPTAGLDPIASGVIDDLIRSLKKElGLTSIMVTHDLdTAFAIADRIAVLY-DGKIVAEGTPEEL 224
CcmA COG4133
ABC-type transport system involved in cytochrome c biogenesis, ATPase component ...
 290-494 1.29e-43

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: 156.87  E-value: 1.29e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:COG4133     3 LEAENLSCRRGERLLFSGLSFTLAAGEALALTGPNGSGKTTLLRILAGLLPPSAGEVLWNGEPIRDAREDYRRRLAYLGH 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPdtskADRAQvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG4133    83 ADGLKPELTVRENLRFWAALYGLR----ADREA-IDEALEAVGLAGLADLPVRQLSAGQKRRVALARLLLSPAPLWLLDE 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLL 494
Cdd:COG4133   158 PFTALDAAGVALLAELIAAHLARGGAVLLTTHQPLELAAARVLDL 202
DppF COG1124
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 290-498 6.58e-43

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


Pssm-ID: 440741 [Multi-domain]  Cd Length: 248  Bit Score: 156.12  E-value: 6.58e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN----LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRI 364
Cdd:COG1124     2 LEVRNLSVSYGQGGrrvpVLKDVSLEVAPGESFGLVGESGSGKSTLLRALAGLERPWSGEVTFDGRPVtRRRRKAFRRRV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQD--DVVHRQLTVNQALgyaAE-LRLppdTSKADRAQVVAQVLDELGLTKH-GDTRVDKLSGGQRKRASVALELLT 440
Cdd:COG1124    82 QMVFQDpyASLHPRHTVDRIL---AEpLRI---HGLPDREERIAELLEQVGLPPSfLDRYPHQLSGGQRQRVAIARALIL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:COG1124   156 EPELLLLDEPTSALDVSVQAEILNLLKDLrEERGLTYLFVSHDLAVVAhLCDRVAVMQNG 215
MlaF COG1127
ATPase subunit MlaF of the ABC-type intermembrane phospholipid transporter Mla [Cell wall ...
 290-510 2.89e-42

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: 154.37  E-value: 2.89e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSLRTRIG 365
Cdd:COG1127     6 IEVRNLTKSFGDRVVLDGVSLDVPRGEILAIIGGSGSGKSVLLKLIIGLLRPDSGEILVDGQDITGlsekELYELRRRIG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQ-----DDvvhrqLTV--NQALGyaaeLRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALEL 438
Cdd:COG1127    86 MLFQggalfDS-----LTVfeNVAFP----LREHTDLSEAEIRELVLEKLELVGLPGAADKMPSELSGGMRKRVALARAL 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYL-DVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1127   157 ALDPEILLYDEPTAGLDPITSAVIDELIRELRDElGLTSVVVTHDLDSAfAIADRVAVLA-DGKIIAEGTPEEL 229
ABC_NikE_OppD_transporters cd03257
ATP-binding cassette domain of nickel/oligopeptides specific transporters; The ABC transporter ...
 290-495 8.73e-42

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: 152.27  E-value: 8.73e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL----LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSL----R 361
Cdd:cd03257     2 LEVKNLSVSFPTGGGsvkaLDDVSFSIKKGETLGLVGESGSGKSTLARAILGLLKPTSGSIIFDGKDLLKLSRRLrkirR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQD--DVVHRQLTVNQALGYAAELRLPPDtSKADRAQVVAQVLDELGLTKhgdTRVDK----LSGGQRKRASVA 435
Cdd:cd03257    82 KEIQMVFQDpmSSLNPRMTIGEQIAEPLRIHGKLS-KKEARKEAVLLLLVGVGLPE---EVLNRypheLSGGQRQRVAIA 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 436 LELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYL-DVCDQVLLM 495
Cdd:cd03257   158 RALALNPKLLIADEPTSALDVSVQAQILDLLKKLQEElGLTLLFITHDLGVVaKIADRVAVM 219
ABC_cobalt_CbiO_domain2 cd03226
Second domain of the ATP-binding cassette component of cobalt transport system; Domain II of ...
 291-498 1.11e-41

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: 151.26  E-value: 1.11e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKN-LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteYGSLRTRIGMVPQ 369
Cdd:cd03226     1 RIENISFSYKKGTeILDDLSLDLYAGEIIALTGKNGAGKTTLAKILAGLIKESSGSILLNGKPIK--AKERRKSIGYVMQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DdvVHRQLTVNQAlgyAAELRLPPDtSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03226    79 D--VDYQLFTDSV---REELLLGLK-ELDAGNEQAETVLKDLDLYALKERHPLSLSGGQKQRLAIAAALLSGKDLLIFDE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:cd03226   153 PTSGLDYKNMERVGELIRELAAQGKAVIVITHDYEFLaKVCDRVLLLANG 202
ABC_drug_resistance_like cd03264
ABC-type multidrug transport system, ATPase component; The biological function of this family ...
 290-505 1.23e-41

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: 151.19  E-value: 1.23e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGtLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:cd03264     1 LQLENLTKRYGKKRALDGVSLTLGPG-MYGLLGPNGAGKTTLMRILATLTPPSSGTIRIDGQDVLKQPQKLRRRIGYLPQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPDtSKADRAqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03264    80 EFGVYPNFTVREFLDYIAWLKGIPS-KEVKAR--VDEVLELVNLGDRAKKKIGSLSGGMRRRVGIAQALVGDPSILIVDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTylDV---CDQVLLMApGGKTAYLG 505
Cdd:cd03264   157 PTAGLDPEERIRFRNLLSELG-EDRIVILSTHIVE--DVeslCNQVAVLN-KGKLVFEG 211
ABC_Carb_Solutes_like cd03259
ATP-binding cassette domain of the carbohydrate and solute transporters-like; This family is ...
 290-498 1.72e-41

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: 151.13  E-value: 1.72e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTRIGMVPQ 369
Cdd:cd03259     1 LELKGLSKTYGSVRALDDLSLTVEPGEFLALLGPSGCGKTTLLRLIAGLERPDSGEILIDGRDV-TGVPPERRNIGMVFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03259    80 DYALFPHLTVAENIAFGLKLRGVP---KAEIRARVRELLELVGLEGLLNRYPHELSGGQQQRVALARALAREPSLLLLDE 156

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 450 PTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLT-YLDVCDQVLLMAPG 498
Cdd:cd03259   157 PLSALDAKLREELREELKELqRELGITTIYVTHDQEeALALADRIAVMNEG 207
PhnC COG3638
ABC-type phosphate/phosphonate transport system, ATPase component [Inorganic ion transport and ...
 290-514 3.95e-41

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


Pssm-ID: 442855 [Multi-domain]  Cd Length: 249  Bit Score: 151.36  E-value: 3.95e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFS-IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS----LRTRI 364
Cdd:COG3638     3 LELRNLSKRyPGGTPALDDVSLEIERGEFVALIGPSGAGKSTLLRCLNGLVEPTSGEILVDGQDVTALRGRalrrLRRRI 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQD-DVVHRqLTVNQ-----ALGYAAELR-LPPDTSKADRAQVvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALE 437
Cdd:COG3638    83 GMIFQQfNLVPR-LSVLTnvlagRLGRTSTWRsLLGLFPPEDRERA-LEALERVGLADKAYQRADQLSGGQQQRVAIARA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQIGGAM 514
Cdd:COG3638   161 LVQEPKLILADEPVASLDPKTARQVMDLLRRIAREdGITVVVNLHQVDLaRRYADRIIGLR-DGRVVFDGPPAELTDAV 238
LolD COG1136
ABC-type lipoprotein export system, ATPase component [Cell wall/membrane/envelope biogenesis];
290-498 8.79e-41

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


Pssm-ID: 440751 [Multi-domain]  Cd Length: 227  Bit Score: 149.42  E-value: 8.79e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL----LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR-- 363
Cdd:COG1136     5 LELRNLTKSYGTGEGevtaLRGVSLSIEAGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVLIDGQDISSLSERELARlr 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 ---IGMVPQDdvvHR---QLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALE 437
Cdd:COG1136    85 rrhIGFVFQF---FNllpELTALENVALPLLLA---GVSRKERRERARELLERVGLGDRLDHRPSQLSGGQQQRVAIARA 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:COG1136   159 LVNRPKLILADEPTGNLDSKTGEEVLELLRELNRElGTTIVMVTHDPELAARADRVIRLRDG 220
ABC_ATPase cd00267
ATP-binding cassette transporter nucleotide-binding domain; ABC transporters are a large ...
 291-498 1.99e-40

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


Pssm-ID: 213179 [Multi-domain]  Cd Length: 157  Bit Score: 145.85  E-value: 1.99e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGMVPQ 369
Cdd:cd00267     1 EIENLSFRYGGRTALDNVSLTLKAGEIVALVGPNGSGKSTLLRAIAGLLKPTSGEILIDGKDIAKlPLEELRRRIGYVPQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 ddvvhrqltvnqalgyaaelrlppdtskadraqvvaqvldelgltkhgdtrvdkLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd00267    81 ------------------------------------------------------LSGGQRQRVALARALLLNPDLLLLDE 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:cd00267   107 PTSGLDPASRERLLELLRELAEEGRTVIIVTHDPELAElAADRVIVLKDG 156
ABCC_MRP_Like cd03228
ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP ...
 290-498 8.13e-40

ATP-binding cassette domain of multidrug resistance protein-like transporters; The MRP (Multidrug Resistance Protein)-like transporters are involved in drug, peptide, and lipid export. They belong to the subfamily C of the ATP-binding cassette (ABC) superfamily of transport proteins. The ABCC subfamily contains transporters with a diverse functional spectrum that includes ion transport, cell surface receptor, and toxin secretion activities. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains, each composed of six transmembrane (TM) helices, and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213195 [Multi-domain]  Cd Length: 171  Bit Score: 144.83  E-value: 8.13e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN--LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGM 366
Cdd:cd03228     1 IEFKNVSFSYPGRPkpVLKDVSLTIKPGEKVAIVGPSGSGKSTLLKLLLRLYDPTSGEILIDGVDLRDlDLESLRKNIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVvhrqltvnqalgyaaelrLPPDTskadraqvvaqVLDELgltkhgdtrvdkLSGGQRKRASVALELLTGPSLLI 446
Cdd:cd03228    81 VPQDPF------------------LFSGT-----------IRENI------------LSGGQRQRIAIARALLRDPPILI 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03228   120 LDEATSALDPETEALILEALRALAK-GKTVIVIAHRLSTIRDADRIIVLDDG 170
ABC_PhnC_transporter cd03256
ATP-binding cassette domain of the binding protein-dependent phosphonate transport system; ...
 300-510 2.71e-39

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: 145.79  E-value: 2.71e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYG----SLRTRIGMVPQDDVVHR 375
Cdd:cd03256    12 NGKKALKDVSLSINPGEFVALIGPSGAGKSTLLRCLNGLVEPTSGSVLIDGTDINKLKGkalrQLRRQIGMIFQQFNLIE 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 376 QLTVNQ-----ALGYAAELR-LPPDTSKADRaQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03256    92 RLSVLEnvlsgRLGRRSTWRsLFGLFPKEEK-QRALAALERVGLLDKAYQRADQLSGGQQQRVAIARALMQQPKLILADE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03256   171 PVASLDPASSRQVMDLLKRINREeGITVIVSLHQVDLaREYADRIVGLK-DGRIVFDGPPAEL 232
ABC_Iron-Siderophores_B12_Hemin cd03214
ATP-binding component of iron-siderophores, vitamin B12 and hemin transporters and related ...
 291-503 5.33e-39

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: 142.57  E-value: 5.33e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTeygslrtrigmvpqd 370
Cdd:cd03214     1 EVENLSVGYGGRTVLDDLSLSIEAGEIVGILGPNGAGKSTLLKTLAGLLKPSSGEILLDGKDLAS--------------- 65

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 371 dvvhrqltvnqalgyaaelrlppdTSKADRAQ---VVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03214    66 ------------------------LSPKELARkiaYVPQALELLGLAHLADRPFNELSGGERQRVLLARALAQEPPILLL 121

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTY-LDVCDQVLLMAPGGKTAY 503
Cdd:cd03214   122 DEPTSHLDIAHQIELLELLRRLARErGKTVVMVLHDLNLaARYADRVILLKDGRIVAQ 179
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 294-534 9.37e-39

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 156.04  E-value: 9.37e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  294 EVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP---TTGSVTFEGHNIHTeygSLRTRIGMVPQD 370
Cdd:TIGR00956  768 EVKIKKEKRVILNNVDGWVKPGTLTALMGASGAGKTTLLNVLAERVTTgviTGGDRLVNGRPLDS---SFQRSIGYVQQQ 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  371 DVVHRQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRV----DKLSGGQRKRASVALELLTGPSLLI 446
Cdd:TIGR00956  845 DLHLPTSTVRESLRFSAYLRQPKSVSKSEKMEYVEEVIKLLEMESYADAVVgvpgEGLNVEQRKRLTIGVELVAKPKLLL 924

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  447 -LDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMAPGGKTAYLGPpdqIGgaMGTTNWAQIF 523
Cdd:TIGR00956  925 fLDEPTSGLDSQTAWSICKLMRKLADHGQAILCTIHqpSAILFEEFDRLLLLQKGGQTVYFGD---LG--ENSHTIINYF 999

                          250
                   ....*....|...
gi 1184609190  524 AKVGAD--PDEAN 534
Cdd:TIGR00956 1000 EKHGAPkcPEDAN 1012
SunT COG2274
ABC-type bacteriocin/lantibiotic exporters, contain an N-terminal double-glycine peptidase ...
 288-510 9.46e-39

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: 154.22  E-value: 9.46e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFS--IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRI 364
Cdd:COG2274   472 GDIELENVSFRypGDSPPVLDNISLTIKPGERVAIVGRSGSGKSTLLKLLLGLYEPTSGRILIDGIDLRQiDPASLRRQI 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQDDvvhrQL---TV--NQALGyaaelRLPPDTSKADRAQVVAQVLDELGLTKHG-DTRV----DKLSGGQRKRASV 434
Cdd:COG2274   552 GVVLQDV----FLfsgTIreNITLG-----DPDATDEEIIEAARLAGLHDFIEALPMGyDTVVgeggSNLSGGQRQRLAI 622

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 435 ALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG2274   623 ARALLRNPRILILDEATSALDAETEAIILENLRRLL-KGRTVIIIAHRLSTIRLADRIIVLD-KGRIVEDGTHEEL 696
TauB COG1116
ABC-type nitrate/sulfonate/bicarbonate transport system, ATPase component [Inorganic ion ...
 284-498 1.43e-38

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


Pssm-ID: 440733 [Multi-domain]  Cd Length: 260  Bit Score: 144.46  E-value: 1.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 284 AARTGGLEVREVNFS----IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteygS 359
Cdd:COG1116     2 SAAAPALELRGVSKRfptgGGGVTALDDVSLTVAAGEFVALVGPSGCGKSTLLRLIAGLEKPTSGEVLVDGKPVT----G 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELL 439
Cdd:COG1116    78 PGPDRGVVFQEPALLPWLTVLDNVALGLELR---GVPKAERRERARELLELVGLAGFEDAYPHQLSGGMRQRVAIARALA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 440 TGPSLLILDEPTSGLDP--ALDLQVMtMLRQLADAGRVVLVVTHSLT---YLdvCDQVLLMAPG 498
Cdd:COG1116   155 NDPEVLLMDEPFGALDAltRERLQDE-LLRLWQETGKTVLFVTHDVDeavFL--ADRVVVLSAR 215
ABC_Mj1267_LivG_branched cd03219
ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ...
 290-510 2.97e-38

ATP-binding cassette component of branched chain amino acids transport system; The Mj1267/LivG ABC transporter subfamily is involved in the transport of the hydrophobic amino acids leucine, isoleucine and valine. MJ1267 is a branched-chain amino acid transporter with 29% similarity to both the LivF and LivG components of the E. coli branched-chain amino acid transporter. MJ1267 contains an insertion from residues 114 to 123 characteristic of LivG (Leucine-Isoleucine-Valine) homologs. The branched-chain amino acid transporter from E. coli comprises a heterodimer of ABCs (LivF and LivG), a heterodimer of six-helix TM domains (LivM and LivH), and one of two alternative soluble periplasmic substrate binding proteins (LivK or LivJ).


Pssm-ID: 213186 [Multi-domain]  Cd Length: 236  Bit Score: 142.58  E-value: 2.97e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVP- 368
Cdd:cd03219     1 LEVRGLTKRFGGLVALDDVSFSVRPGEIHGLIGPNGAGKTTLFNLISGFLRPTSGSVLFDGEDITGLPPHEIARLGIGRt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 -QDDVVHRQLTVNQALGYAAELRLPPDTSKADRAQV-------VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLT 440
Cdd:cd03219    81 fQIPRLFPELTVLENVMVAAQARTGSGLLLARARREerearerAEELLERVGLADLADRPAGELSYGQQRRLEIARALAT 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMAPGGKTAyLGPPDQI 510
Cdd:cd03219   161 DPKLLLLDEPAAGLNPEETEELAELIRELRERGITVLLVEHDMDVvMSLADRVTVLDQGRVIA-EGTPDEV 230
ABC_putative_ATPase cd03269
ATP-binding cassette domain of an uncharacterized transporter; This subgroup is related to the ...
 290-503 3.31e-38

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: 141.65  E-value: 3.31e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEygsLRTRIGMVPQ 369
Cdd:cd03269     1 LEVENVTKRFGRVTALDDISFSVEKGEIFGLLGPNGAGKTTTIRMILGIILPDSGEVLFDGKPLDIA---ARNRIGYLPE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03269    78 ERGLYPKMKVIDQLVYLAQLK---GLKKEEARRRIDEWLERLELSEYANKRVEELSKGNQQKVQFIAAVIHDPELLILDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPGGKTAY 503
Cdd:cd03269   155 PFSGLDPVNVELLKDVIRELARAGKTVILSTHQMELVeELCDRVLLLNKGRAVLY 209
ABC_tran pfam00005
ABC transporter; ABC transporters for a large family of proteins responsible for translocation ...
 305-452 4.70e-38

ABC transporter; ABC transporters for a large family of proteins responsible for translocation of a variety of compounds across biological membranes. ABC transporters are the largest family of proteins in many completely sequenced bacteria. ABC transporters are composed of two copies of this domain and two copies of a transmembrane domain pfam00664. These four domains may belong to a single polypeptide or belong in different polypeptide chains.


Pssm-ID: 394964 [Multi-domain]  Cd Length: 150  Bit Score: 138.93  E-value: 4.70e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH-TEYGSLRTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:pfam00005   1 LKNVSLTLNPGEILALVGPNGAGKSTLLKLIAGLLSPTEGTILLDGQDLTdDERKSLRKEIGYVFQDPQLFPRLTVRENL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 384 GYAAELRLPPDTSKADRAQvvaQVLDELGLTKHGDTRVDK----LSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:pfam00005  81 RLGLLLKGLSKREKDARAE---EALEKLGLGDLADRPVGErpgtLSGGQRQRVAIARALLTKPKLLLLDEPTA 150
ThiQ COG3840
ABC-type thiamine transport system, ATPase component ThiQ [Coenzyme transport and metabolism];
290-510 4.72e-38

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


Pssm-ID: 443051 [Multi-domain]  Cd Length: 232  Bit Score: 141.82  E-value: 4.72e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLleRVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNiHTEYGSLRTRIGMVPQ 369
Cdd:COG3840     2 LRLDDLTYRYGDFPL--RFDLTIAAGERVAILGPSGAGKSTLLNLIAGFLPPDSGRILWNGQD-LTALPPAERPVSMLFQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTV--NQALGYAAELRLppdtSKADRAQvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:COG3840    79 ENNLFPHLTVaqNIGLGLRPGLKL----TAEQRAQ-VEQALERVGLAGLLDRLPGQLSGGQRQRVALARCLVRKRPILLL 153

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLT-YLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG3840   154 DEPFSALDPALRQEMLDLVDELCRErGLTVLMVTHDPEdAARIADRVLLVA-DGRIAADGPTAAL 217
ABC_MJ0796_LolCDE_FtsE cd03255
ATP-binding cassette domain of the transporters involved in export of lipoprotein and ...
 290-495 7.13e-38

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: 140.70  E-value: 7.13e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL----LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS-----L 360
Cdd:cd03255     1 IELKNLSKTYGGGGEkvqaLKGVSLSIEKGEFVAIVGPSGSGKSTLLNILGGLDRPTSGEVRVDGTDISKLSEKelaafR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 361 RTRIGMVPQDDVVHRQLTVNQALGYAAELRLPPDTSKADRAqvvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLT 440
Cdd:cd03255    81 RRHIGFVFQSFNLLPDLTALENVELPLLLAGVPKKERRERA---EELLERVGLGDRLNHYPSELSGGQQQRVAIARALAN 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTYLDVCDQVLLM 495
Cdd:cd03255   158 DPKIILADEPTGNLDSETGKEVMELLRELNkEAGTTIVVVTHDPELAEYADRIIEL 213
FetA COG4619
ABC-type iron transporter FetAB, ATPase component [Inorganic ion transport and metabolism];
290-498 7.35e-38

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


Pssm-ID: 443661 [Multi-domain]  Cd Length: 209  Bit Score: 140.34  E-value: 7.35e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYG--SLRTRIGMV 367
Cdd:COG4619     1 LELEGLSFRVGGKPILSPVSLTLEAGECVAITGPSGSGKSTLLRALADLDPPTSGEIYLDGKPL-SAMPppEWRRQVAYV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQ-----DDvvhrqlTVNQALGYAAELR-LPPDTSKADRAqvvaqvLDELGLTKHG-DTRVDKLSGGQRKRASVALELLT 440
Cdd:COG4619    80 PQepalwGG------TVRDNLPFPFQLReRKFDRERALEL------LERLGLPPDIlDKPVERLSGGERQRLALIRALLL 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:COG4619   148 QPDVLLLDEPTSALDPENTRRVEELLREYlAEEGRAVLWVSHDPEQIErVADRVLTLEAG 207
YhaQ COG4152
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 290-519 1.24e-37

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


Pssm-ID: 443322 [Multi-domain]  Cd Length: 298  Bit Score: 142.94  E-value: 1.24e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEygsLRTRIGMVPQ 369
Cdd:COG4152     2 LELKGLTKRFGDKTAVDDVSFTVPKGEIFGLLGPNGAGKTTTIRIILGILAPDSGEVLWDGEPLDPE---DRRRIGYLPE 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG4152    79 ERGLYPKMKVGEQLVYLARLK---GLSKAEAKRRADEWLERLGLGDRANKKVEELSKGNQQKVQLIAALLHDPELLILDE 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDP-ALDLqVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMApGGKTAYLGPPDQIGGAMGTTNW 519
Cdd:COG4152   156 PFSGLDPvNVEL-LKDVIRELAAKGTTVIFSSHQMELVEeLCDRIVIIN-KGRKVLSGSVDEIRRQFGRNTL 225
hmuV PRK13548
hemin importer ATP-binding subunit; Provisional
 290-509 1.06e-36

hemin importer ATP-binding subunit; Provisional


Pssm-ID: 237422 [Multi-domain]  Cd Length: 258  Bit Score: 138.75  E-value: 1.06e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRIGMVP 368
Cdd:PRK13548    3 LEARNLSVRLGGRTLLDDVSLTLRPGEVVAILGPNGAGKSTLLRALSGELSPDSGEVRLNGRPLaDWSPAELARRRAVLP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTVNQ--ALGyaaelRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVAlELLT------ 440
Cdd:PRK13548   83 QHSSLSFPFTVEEvvAMG-----RAPHGLSRAEDDALVAAALAQVDLAHLAGRDYPQLSGGEQQRVQLA-RVLAqlwepd 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 441 -GPSLLILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSL----TYldvCDQVLLMApGGKTAYLGPPDQ 509
Cdd:PRK13548  157 gPPRWLLLDEPTSALDLAHQHHVLRLARQLAhERGLAVIVVLHDLnlaaRY---ADRIVLLH-QGRLVADGTPAE 227
CysA COG1118
ABC-type sulfate/molybdate transport systems, ATPase component [Inorganic ion transport and ...
 289-510 2.25e-36

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


Pssm-ID: 440735 [Multi-domain]  Cd Length: 348  Bit Score: 140.67  E-value: 2.25e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVP 368
Cdd:COG1118     2 SIEVRNISKRFGSFTLLDDVSLEIASGELVALLGPSGSGKTTLLRIIAGLETPDSGRIVLNGRDLFTNLPPRERRVGFVF 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTVNQALGYAAELRLPpdtSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRasVALE--LLTGPSLLI 446
Cdd:COG1118    82 QHYALFPHMTVAENIAFGLRVRPP---SKAEIRARVEELLELVQLEGLADRYPSQLSGGQRQR--VALAraLAVEPEVLL 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLT-YLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1118   157 LDEPFGALDAKVRKELRRWLRRLHDElGGTTVFVTHDQEeALELADRVVVMN-QGRIEQVGTPDEV 221
ABC_phnC TIGR02315
phosphonate ABC transporter, ATP-binding protein; Phosphonates are a class of ...
 300-510 3.80e-36

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: 136.66  E-value: 3.80e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYG----SLRTRIGMVPQD-DVVH 374
Cdd:TIGR02315  13 NGKQALKNINLNINPGEFVAIIGPSGAGKSTLLRCINRLVEPSSGSILLEGTDITKLRGkklrKLRRRIGMIFQHyNLIE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RqLTVNQ-----ALGYAAELR-LPPDTSKADRaQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILD 448
Cdd:TIGR02315  93 R-LTVLEnvlhgRLGYKPTWRsLLGRFSEEDK-ERALSALERVGLADKAYQRADQLSGGQQQRVAIARALAQQPDLILAD 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 449 EPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR02315 171 EPIASLDPKTSKQVMDYLKRINkEDGITVIINLHQVDLaKKYADRIVGLK-AGEIVFDGAPSEL 233
MdlB COG1132
ABC-type multidrug transport system, ATPase and permease component [Defense mechanisms];
281-495 5.20e-36

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


Pssm-ID: 440747 [Multi-domain]  Cd Length: 579  Bit Score: 144.15  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 281 QEVAARTGGLEVREVNFS-IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYG 358
Cdd:COG1132   331 VPLPPVRGEIEFENVSFSyPGDRPVLKDISLTIPPGETVALVGPSGSGKSTLVNLLLRFYDPTSGRILIDGVDIRDlTLE 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 359 SLRTRIGMVPQDDVV-HRqlTVNQALGYAAElrlppdtsKADRAQVV-----AQVLDELGLTKHG-DTRVD----KLSGG 427
Cdd:COG1132   411 SLRRQIGVVPQDTFLfSG--TIRENIRYGRP--------DATDEEVEeaakaAQAHEFIEALPDGyDTVVGergvNLSGG 480

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 428 QRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLM 495
Cdd:COG1132   481 QRQRIAIARALLKDPPILILDEATSALDTETEALIQEALERLM-KGRTTIVIAHRLSTIRNADRILVL 547
ABC_NrtD_SsuB_transporters cd03293
ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ...
 290-497 5.29e-36

ATP-binding cassette domain of the nitrate and sulfonate transporters; NrtD and SsuB are the ATP-binding subunits of the bacterial ABC-type nitrate and sulfonate transport systems, respectively. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213260 [Multi-domain]  Cd Length: 220  Bit Score: 135.68  E-value: 5.29e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL----LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteygSLRTRIG 365
Cdd:cd03293     1 LEVRNVSKTYGGGGGavtaLEDISLSVEEGEFVALVGPSGCGKSTLLRIIAGLERPTSGEVLVDGEPVT----GPGPDRG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:cd03293    77 YVFQQDALLPWLTVLDNVALGLELQ---GVPKAEARERAEELLELVGLSGFENAYPHQLSGGMRQRVALARALAVDPDVL 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 446 ILDEPTSGLDP--ALDLQVmTMLRQLADAGRVVLVVTHSLT---YLdvCDQVLLMAP 497
Cdd:cd03293   154 LLDEPFSALDAltREQLQE-ELLDIWRETGKTVLLVTHDIDeavFL--ADRVVVLSA 207
ABC_BcrA_bacitracin_resist cd03268
ATP-binding cassette domain of the bacitracin-resistance transporter; The BcrA subfamily ...
 290-498 1.38e-35

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


Pssm-ID: 213235 [Multi-domain]  Cd Length: 208  Bit Score: 133.88  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRtRIGMVPQ 369
Cdd:cd03268     1 LKTNDLTKTYGKKRVLDDISLHVKKGEIYGFLGPNGAGKTTTMKIILGLIKPDSGEITFDGKSYQKNIEALR-RIGALIE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPDtskadraQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03268    80 APGFYPNLTARENLRLLARLLGIRK-------KRIDEVLDVVGLKDSAKKKVKGFSLGMKQRLGIALALLGNPDLLILDE 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:cd03268   153 PTNGLDPDGIKELRELILSLRDQGITVLISSHLLSEIQkVADRIGIINKG 202
GsiA COG1123
ABC-type glutathione transport system ATPase component, contains duplicated ATPase domain ...
 290-510 1.56e-35

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: 141.96  E-value: 1.56e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI--GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPT---TGSVTFEGHNIHTEYGSLR-TR 363
Cdd:COG1123     5 LEVRDLSVRYpgGDVPAVDGVSLTIAPGETVALVGESGSGKSTLALALMGLLPHGgriSGEVLLDGRDLLELSEALRgRR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQD-DVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGP 442
Cdd:COG1123    85 IGMVFQDpMTQLNPVTVGDQIAEALENL---GLSRAEARARVLELLEAVGLERRLDRYPHQLSGGQRQRVAIAMALALDP 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 443 SLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1123   162 DLLIADEPTTALDVTTQAEILDLLRELqRERGTTVLLITHDLGVvAEIADRVVVMD-DGRIVEDGPPEEI 230
FtsE COG2884
Cell division ATPase FtsE [Cell cycle control, cell division, chromosome partitioning];
300-481 1.67e-35

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


Pssm-ID: 442130 [Multi-domain]  Cd Length: 223  Bit Score: 134.41  E-value: 1.67e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSLRTRIGMVPQDdvvHR 375
Cdd:COG2884    13 GGREALSDVSLEIEKGEFVFLTGPSGAGKSTLLKLLYGEERPTSGQVLVNGQDLSRlkrrEIPYLRRRIGVVFQD---FR 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 376 ---QLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:COG2884    90 llpDRTVYENVALPLRVT---GKSRKEIRRRVREVLDLVGLSDKAKALPHELSGGEQQRVAIARALVNRPELLLADEPTG 166

                         170       180
                  ....*....|....*....|....*....
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:COG2884   167 NLDPETSWEIMELLEEINRRGTTVLIATH 195
CydD COG4988
ABC-type transport system involved in cytochrome bd biosynthesis, ATPase and permease ...
 284-498 1.89e-35

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: 142.59  E-value: 1.89e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 284 AARTGGLEVREVNFS-IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLR 361
Cdd:COG4988   331 AAGPPSIELEDVSFSyPGGRPALDGLSLTIPPGERVALVGPSGAGKSTLLNLLLGFLPPYSGSILINGVDLSDlDPASWR 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQDDVVHrQLTVnqalgyAAELRLP-PDTSKADRAQVVAQV-LDEL------GLtkhgDTRVD----KLSGGQR 429
Cdd:COG4988   411 RQIAWVPQNPYLF-AGTI------RENLRLGrPDASDEELEAALEAAgLDEFvaalpdGL----DTPLGeggrGLSGGQA 479

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 430 KRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:COG4988   480 QRLALARALLRDAPLLLLDEPTAHLDAETEAEILQALRRLA-KGRTVILITHRLALLAQADRILVLDDG 547
PotA COG3842
ABC-type Fe3+/spermidine/putrescine transport systems, ATPase component [Amino acid transport ...
 290-510 2.12e-35

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


Pssm-ID: 443052 [Multi-domain]  Cd Length: 353  Bit Score: 137.92  E-value: 2.12e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteygSL---RTRIGM 366
Cdd:COG3842     6 LELENVSKRYGDVTALDDVSLSIEPGEFVALLGPSGCGKTTLLRMIAGFETPDSGRILLDGRDVT----GLppeKRNVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVV--HrqLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRasVAL--ELLTGP 442
Cdd:COG3842    82 VFQDYALfpH--LTVAENVAFGLRMR---GVPKAEIRARVAELLELVGLEGLADRYPHQLSGGQQQR--VALarALAPEP 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 443 SLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHS----LTyldVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG3842   155 RVLLLDEPLSALDAKLREEMREELRRLqRELGITFIYVTHDqeeaLA---LADRIAVMN-DGRIEQVGTPEEI 223
ABC_TM1139_LivF_branched cd03224
ATP-binding cassette domain of branched-chain amino acid transporter; LivF (TM1139) is part of ...
 290-510 2.14e-35

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: 134.10  E-value: 2.14e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR--IGMV 367
Cdd:cd03224     1 LEVENLNAGYGKSQILFGVSLTVPEGEIVALLGRNGAGKTTLLKTIMGLLPPRSGSIRFDGRDITGLPPHERARagIGYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDVVHRQLTV--NQALGyaaELRLPPDTSKADRAQVVAQ--VLDELGLTKHGDtrvdkLSGGQRKRASVALELLTGPS 443
Cdd:cd03224    81 PEGRRIFPELTVeeNLLLG---AYARRRAKRKARLERVYELfpRLKERRKQLAGT-----LSGGEQQMLAIARALMSRPK 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03224   153 LLLLDEPSEGLAPKIVEEIFEAIRELRDEGVTILLVEQNARFaLEIADRAYVLE-RGRVVLEGTAAEL 219
ABC_DrrA cd03265
Daunorubicin/doxorubicin resistance ATP-binding protein; DrrA is the ATP-binding protein ...
 290-510 8.44e-35

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


Pssm-ID: 213232 [Multi-domain]  Cd Length: 220  Bit Score: 132.11  E-value: 8.44e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:cd03265     1 IEVENLVKKYGDFEAVRGVSFRVRRGEIFGLLGPNGAGKTTTIKMLTTLLKPTSGRATVAGHDVVREPREVRRRIGIVFQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03265    81 DLSVDDELTGWENLYIHARLYGVP---GAERRERIDELLDFVGLLEAADRLVKTYSGGMRRRLEIARSLVHRPEVLFLDE 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 450 PTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHsltYLD----VCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03265   158 PTIGLDPQTRAHVWEYIEKLkEEFGMTILLTTH---YMEeaeqLCDRVAIID-HGRIIAEGTPEEL 219
ABCG_PDR_domain2 cd03232
Second domain of the pleiotropic drug resistance-like (PDR) subfamily G of ATP-binding ...
 294-505 1.05e-34

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


Pssm-ID: 213199 [Multi-domain]  Cd Length: 192  Bit Score: 130.83  E-value: 1.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 294 EVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP--TTGSVTFEGHNIHTEYgslRTRIGMVPQDD 371
Cdd:cd03232    12 TVPVKGGKRQLLNNISGYVKPGTLTALMGESGAGKTTLLDVLAGRKTAgvITGEILINGRPLDKNF---QRSTGYVEQQD 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 372 VVHRQLTVNQALGYAAELRlppdtskadraqvvaqvldelgltkhgdtrvdKLSGGQRKRASVALELLTGPSLLILDEPT 451
Cdd:cd03232    89 VHSPNLTVREALRFSALLR--------------------------------GLSVEQRKRLTIGVELAAKPSILFLDEPT 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 452 SGLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMAPGGKTAYLG 505
Cdd:cd03232   137 SGLDSQAAYNIVRFLKKLADSGQAILCTIHqpSASIFEKFDRLLLLKRGGKTVYFG 192
ABC_HisP_GlnQ cd03262
ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ...
 290-498 1.23e-34

ATP-binding cassette domain of the histidine and glutamine transporters; HisP and GlnQ are the ATP-binding components of the bacterial periplasmic histidine and glutamine permeases, respectively. Histidine permease is a multi-subunit complex containing the HisQ and HisM integral membrane subunits and two copies of HisP. HisP has properties intermediate between those of integral and peripheral membrane proteins and is accessible from both sides of the membrane, presumably by its interaction with HisQ and HisM. The two HisP subunits form a homodimer within the complex. The domain structure of the amino acid uptake systems is typical for prokaryotic extracellular solute binding protein-dependent uptake systems. All of the amino acid uptake systems also have at least one, and in a few cases, two extracellular solute binding proteins located in the periplasm of Gram-negative bacteria, or attached to the cell membrane of Gram-positive bacteria. The best-studied member of the PAAT (polar amino acid transport) family is the HisJQMP system of S. typhimurium, where HisJ is the extracellular solute binding proteins and HisP is the ABC protein.


Pssm-ID: 213229 [Multi-domain]  Cd Length: 213  Bit Score: 131.50  E-value: 1.23e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI---HTEYGSLRTRIGM 366
Cdd:cd03262     1 IEIKNLHKSFGDFHVLKGIDLTVKKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTIIIDGLKLtddKKNINELRQKVGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQALGYAaelrlPPDTSKADRAQVVA---QVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:cd03262    81 VFQQFNLFPHLTVLENITLA-----PIKVKGMSKAEAEEralELLEKVGLADKADAYPAQLSGGQQQRVAIARALAMNPK 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMAPG 498
Cdd:cd03262   156 VMLFDEPTSALDPELVGEVLDVMKDLAEEGMTMVVVTHEMGFaREVADRVIFMDDG 211
GlnQ COG1126
ABC-type polar amino acid transport system, ATPase component [Amino acid transport and ...
 290-510 2.05e-34

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


Pssm-ID: 440743 [Multi-domain]  Cd Length: 239  Bit Score: 131.65  E-value: 2.05e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH---TEYGSLRTRIGM 366
Cdd:COG1126     2 IEIENLHKSFGDLEVLKGISLDVEKGEVVVIIGPSGSGKSTLLRCINLLEEPDSGTITVDGEDLTdskKDINKLRRKVGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQddvvHRQL----TV--NQALGYAAELRLPPDTSKAdRAQvvaQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLT 440
Cdd:COG1126    82 VFQ----QFNLfphlTVleNVTLAPIKVKKMSKAEAEE-RAM---ELLERVGLADKADAYPAQLSGGQQQRVAIARALAM 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 441 GPSLLILDEPTSGLDPALD---LQVMtmlRQLADAGRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1126   154 EPKVMLFDEPTSALDPELVgevLDVM---RDLAKEGMTMVVVTHEMGFaREVADRVVFMD-GGRIVEEGPPEEF 223
ABC_Class3 cd03229
ATP-binding cassette domain of the binding protein-dependent transport systems; This class is ...
 290-498 3.33e-34

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: 128.84  E-value: 3.33e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS---LRTRIGM 366
Cdd:cd03229     1 LELKNVSKRYGQKTVLNDVSLNIEAGEIVALLGPSGSGKSTLLRCIAGLEEPDSGSILIDGEDLTDLEDElppLRRRIGM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQALGYAaelrlppdtskadraqvvaqvldelgltkhgdtrvdkLSGGQRKRASVALELLTGPSLLI 446
Cdd:cd03229    81 VFQDFALFPHLTVLENIALG-------------------------------------LSGGQQQRVALARALAMDPDVLL 123

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLAD-AGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:cd03229   124 LDEPTSALDPITRREVRALLKSLQAqLGITVVLVTHDLDEAArLADRVVVLRDG 177
YnjD COG4136
ABC-type uncharacterized transport system YnjBCD, ATPase component [General function ...
 289-481 6.10e-34

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


Pssm-ID: 443311 [Multi-domain]  Cd Length: 211  Bit Score: 129.52  E-value: 6.10e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP---TTGSVTFEGHNIhTEYGSLRTRIG 365
Cdd:COG4136     1 MLSLENLTITLGGRPLLAPLSLTVAPGEILTLMGPSGSGKSTLLAAIAGTLSPafsASGEVLLNGRRL-TALPAEQRRIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQLTVNQALGYAaelrLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:COG4136    80 ILFQDDLLFPHLSVGENLAFA----LPPTIGRAQRRARVEQALEEAGLAGFADRDPATLSGGQRARVALLRALLAEPRAL 155

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLR-QLADAGRVVLVVTH 481
Cdd:COG4136   156 LLDEPFSKLDAALRAQFREFVFeQIRQRGIPALLVTH 192
ModF COG1119
ABC-type molybdenum transport system, ATPase component ModF/photorepair protein PhrA ...
 290-510 1.75e-33

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: 129.43  E-value: 1.75e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSV------TFEGHNIHTeygsLRTR 363
Cdd:COG1119     4 LELRNVTVRRGGKTILDDISWTVKPGEHWAILGPNGAGKSTLLSLITGDLPPTYGNDvrlfgeRRGGEDVWE----LRKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQD--DVVHRQLTVNQAL--GYAAELRLPPDTSKADRAQVvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELL 439
Cdd:COG1119    80 IGLVSPAlqLRFPRDETVLDVVlsGFFDSIGLYREPTDEQRERA-RELLELLGLAHLADRPFGTLSQGEQRRVLIARALV 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLV-VTHSLTYLDVC-DQVLLMAPgGKTAYLGPPDQI 510
Cdd:COG1119   159 KDPELLILDEPTAGLDLGARELLLALLDKLAAEGAPTLVlVTHHVEEIPPGiTHVLLLKD-GRVVAAGPKEEV 230
LivG COG0411
ABC-type branched-chain amino acid transport system, ATPase component LivG [Amino acid ...
 305-510 2.23e-33

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


Pssm-ID: 440180 [Multi-domain]  Cd Length: 257  Bit Score: 129.39  E-value: 2.23e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMV-----PQddvVHRQLTV 379
Cdd:COG0411    20 VDDVSLEVERGEIVGLIGPNGAGKTTLFNLITGFYRPTSGRILFDGRDITGLPPHRIARLGIArtfqnPR---LFPELTV 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 --NQALGYAAELR-------LPPDTSKADRAQVVAQV---LDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:COG0411    97 leNVLVAAHARLGrgllaalLRLPRARREEREARERAeelLERVGLADRADEPAGNLSYGQQRRLEIARALATEPKLLLL 176

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYL-DVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG0411   177 DEPAAGLNPEETEELAELIRRLRDErGITILLIEHDMDLVmGLADRIVVLD-FGRVIAEGTPAEV 240
ABC_PstB_phosphate_transporter cd03260
ATP-binding cassette domain of the phosphate transport system; Phosphate uptake is of ...
 290-510 2.52e-33

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: 128.07  E-value: 2.52e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG-----YATPTTGSVTFEGHNIHTEYG---SLR 361
Cdd:cd03260     1 IELRDLNVYYGDKHALKDISLDIPKGEITALIGPSGCGKSTLLRLLNRlndliPGAPDEGEVLLDGKDIYDLDVdvlELR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQDDVVHRqLTV--NQALGyaaeLRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVD--KLSGGQRKRASVALE 437
Cdd:cd03260    81 RRVGMVFQKPNPFP-GSIydNVAYG----LRLHGIKLKEELDERVEEALRKAALWDEVKDRLHalGLSGGQQQRLCLARA 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLvVTHSLTY-LDVCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:cd03260   156 LANEPEVLLLDEPTSALDPISTAKIEELIAELKKEYTIVI-VTHNMQQaARVADRTAFLLNGRLVEF-GPTEQI 227
ABC_MetN_methionine_transporter cd03258
ATP-binding cassette domain of methionine transporter; MetN (also known as YusC) is an ...
 305-498 3.69e-33

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: 127.70  E-value: 3.69e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS----LRTRIGMVPQddvvHRQL--- 377
Cdd:cd03258    21 LKDVSLSVPKGEIFGIIGRSGAGKSTLIRCINGLERPTSGSVLVDGTDLTLLSGKelrkARRRIGMIFQ----HFNLlss 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 -TVNQALGYAAELrlpPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:cd03258    97 rTVFENVALPLEI---AGVPKAEIEERVLELLELVGLEDKADAYPAQLSGGQKQRVGIARALANNPKVLLCDEATSALDP 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 457 ALDLQVMTMLRQL-ADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:cd03258   174 ETTQSILALLRDInRELGLTIVLITHEMeVVKRICDRVAVMEKG 217
CydC COG4987
ABC-type transport system involved in cytochrome bd biosynthesis, fused ATPase and permease ...
 281-498 6.46e-33

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: 134.89  E-value: 6.46e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 281 QEVAARTGGLEVREVNFSI--GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYG 358
Cdd:COG4987   325 PAPAPGGPSLELEDVSFRYpgAGRPVLDGLSLTLPPGERVAIVGPSGSGKSTLLALLLRFLDPQSGSITLGGVDLRDLDE 404

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 359 -SLRTRIGMVPQDDVVHRQlTVNQALGYAAelrlpPDTSKADRAQVVAQV-LDEL------GLtkhgDTRVD----KLSG 426
Cdd:COG4987   405 dDLRRRIAVVPQRPHLFDT-TLRENLRLAR-----PDATDEELWAALERVgLGDWlaalpdGL----DTWLGeggrRLSG 474

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 427 GQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:COG4987   475 GERRRLALARALLRDAPILLLDEPTEGLDAATEQALLADLLEAL-AGRTVLLITHRLAGLERMDRILVLEDG 545
ABC_NatA_sodium_exporter cd03266
ATP-binding cassette domain of the Na+ transporter; NatA is the ATPase component of a ...
 305-505 2.19e-32

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


Pssm-ID: 213233 [Multi-domain]  Cd Length: 218  Bit Score: 125.17  E-value: 2.19e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTVNQALG 384
Cdd:cd03266    21 VDGVSFTVKPGEVTGLLGPNGAGKTTTLRMLAGLLEPDAGFATVDGFDVVKEPAEARRRLGFVSDSTGLYDRLTARENLE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 385 YAAELR-LPPDTSKAdRAQVVAQVLDelgLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:cd03266   101 YFAGLYgLKGDELTA-RLEELADRLG---MEELLDRRVGGFSTGMRQKVAIARALVHDPPVLLLDEPTTGLDVMATRALR 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1184609190 464 TMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPgGKTAYLG 505
Cdd:cd03266   177 EFIRQLRALGKCILFSTHIMQEVErLCDRVVVLHR-GRVVYEG 218
PRK13536 PRK13536
nodulation factor ABC transporter ATP-binding protein NodI;
290-532 2.49e-32

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237419 [Multi-domain]  Cd Length: 340  Bit Score: 128.80  E-value: 2.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:PRK13536   42 IDLAGVSKSYGDKAVVNGLSFTVASGECFGLLGPNGAGKSTIARMILGMTSPDAGKITVLGVPVPARARLARARIGVVPQ 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQAL-GYAAELRLPPDTSKAdraqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILD 448
Cdd:PRK13536  122 FDNLDLEFTVRENLlVFGRYFGMSTREIEA----VIPSLLEFARLESKADARVSDLSGGMKRRLTLARALINDPQLLILD 197

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 449 EPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPGGKTAYLGPPDQIGGAMGttnwAQIFAKVG 527
Cdd:PRK13536  198 EPTTGLDPHARHLIWERLRSLLARGKTILLTTHFMEEAErLCDRLCVLEAGRKIAEGRPHALIDEHIG----CQVIEIYG 273


                  ....*
gi 1184609190 528 ADPDE 532
Cdd:PRK13536  274 GDPHE 278
ABCC_ATM1_transporter cd03253
ATP-binding cassette domain of iron-sulfur clusters transporter, subfamily C; ATM1 is an ABC ...
 290-509 2.67e-32

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: 125.42  E-value: 2.67e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN-LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEY--GSLRTRIGM 366
Cdd:cd03253     1 IEFENVTFAYDPGRpVLKDVSFTIPAGKKVAIVGPSGSGKSTILRLLFRFYDVSSGSILIDGQDI-REVtlDSLRRAIGV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQlTVNQALGYAAelrlpPDTSKAD--RAQVVAQVLDE-LGLTKHGDTRVD----KLSGGQRKRASVALELL 439
Cdd:cd03253    80 VPQDTVLFND-TIGYNIRYGR-----PDATDEEviEAAKAAQIHDKiMRFPDGYDTIVGerglKLSGGEKQRVAIARAIL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQ 509
Cdd:cd03253   154 KNPPILLLDEATSALDTHTEREIQAALRDVS-KGRTTIVIAHRLSTIVNADKIIVLK-DGRIVERGTHEE 221
PLN03211 PLN03211
ABC transporter G-25; Provisional
 298-498 6.15e-32

ABC transporter G-25; Provisional


Pssm-ID: 215634 [Multi-domain]  Cd Length: 659  Bit Score: 132.70  E-value: 6.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 298 SIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG--YATPTTGSVTFEGHNIHTEygsLRTRIGMVPQDDVVHR 375
Cdd:PLN03211   77 QIQERTILNGVTGMASPGEILAVLGPSGSGKSTLLNALAGriQGNNFTGTILANNRKPTKQ---ILKRTGFVTQDDILYP 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 376 QLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDK-----LSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:PLN03211  154 HLTVRETLVFCSLLRLPKSLTKQEKILVAESVISELGLTKCENTIIGNsfirgISGGERKRVSIAHEMLINPSLLILDEP 233

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 451 TSGLDPALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMAPG 498
Cdd:PLN03211  234 TSGLDATAAYRLVLTLGSLAQKGKTIVTSMHqpSSRVYQMFDSVLVLSEG 283
PLN03140 PLN03140
ABC transporter G family member; Provisional
 304-506 6.76e-32

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 134.20  E-value: 6.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP--TTGSVTFEGHNIHTEYGSlrtRI-GMVPQDDVVHRQLTVN 380
Cdd:PLN03140   895 LLREVTGAFRPGVLTALMGVSGAGKTTLMDVLAGRKTGgyIEGDIRISGFPKKQETFA---RIsGYCEQNDIHSPQVTVR 971

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  381 QALGYAAELRLPPDTSKADRAQVVAQV-----LDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:PLN03140   972 ESLIYSAFLRLPKEVSKEEKMMFVDEVmelveLDNLKDAIVGLPGVTGLSTEQRKRLTIAVELVANPSIIFMDEPTSGLD 1051

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1184609190  456 PALDLQVMTMLRQLADAGRVVLVVTH--SLTYLDVCDQVLLMAPGGKTAYLGP 506
Cdd:PLN03140  1052 ARAAAIVMRTVRNTVDTGRTVVCTIHqpSIDIFEAFDELLLMKRGGQVIYSGP 1104
ABCC_bacteriocin_exporters cd03245
ATP-binding cassette domain of bacteriocin exporters, subfamily C; Many non-lantibiotic ...
 288-498 7.99e-32

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: 123.47  E-value: 7.99e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSI-GDKNL-LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRI 364
Cdd:cd03245     1 GRIEFRNVSFSYpNQEIPaLDNVSLTIRAGEKVAIIGRVGSGKSTLLKLLAGLYKPTSGSVLLDGTDIRQlDPADLRRNI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQDDV-VHRQLTVNQALGyaaelRLPPDTSKADRAQVVAQVLDELGLTKHG-DTRV----DKLSGGQRKRASVALEL 438
Cdd:cd03245    81 GYVPQDVTlFYGTLRDNITLG-----APLADDERILRAAELAGVTDFVNKHPNGlDLQIgergRGLSGGQRQAVALARAL 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03245   156 LNDPPILLLDEPTSAMDMNSEERLKERLRQLL-GDKTLIIITHRPSLLDLVDRIIVMDSG 214
AbcC COG1135
ABC-type methionine transport system, ATPase component [Amino acid transport and metabolism];
305-582 1.35e-31

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


Pssm-ID: 440750 [Multi-domain]  Cd Length: 339  Bit Score: 126.35  E-value: 1.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS----LRTRIGMVPQddvvH----RQ 376
Cdd:COG1135    21 LDDVSLTIEKGEIFGIIGYSGAGKSTLIRCINLLERPTSGSVLVDGVDLTALSERelraARRKIGMIFQ----HfnllSS 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 377 LTV--NQALGyaaeLRLPpDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:COG1135    97 RTVaeNVALP----LEIA-GVPKAEIRKRVAELLELVGLSDKADAYPSQLSGGQKQRVGIARALANNPKVLLCDEATSAL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 455 DPALDLQVMTMLRQL-ADAGRVVLVVTHSltyLDV----CDQVLLMApGGKTAylgppdqiggAMGTTnwAQIFakvgAD 529
Cdd:COG1135   172 DPETTRSILDLLKDInRELGLTIVLITHE---MDVvrriCDRVAVLE-NGRIV----------EQGPV--LDVF----AN 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 530 PD-EANRRFLAQnkppppvesaPADLGAPAHTSVRHQFSTIARRQVRLVVSDRA 582
Cdd:COG1135   232 PQsELTRRFLPT----------VLNDELPEELLARLREAAGGGRLVRLTFVGES 275
CeuD COG4604
ABC-type enterochelin transport system, ATPase component [Inorganic ion transport and ...
 291-510 1.85e-31

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


Pssm-ID: 443654 [Multi-domain]  Cd Length: 252  Bit Score: 123.65  E-value: 1.85e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRIGMVPQ 369
Cdd:COG4604     3 EIKNVSKRYGGKVVLDDVSLTIPKGGITALIGPNGAGKSTLLSMISRLLPPDSGEVLVDGLDVaTTPSRELAKRLAILRQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAaelRLP-----PdtSKADRAqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:COG4604    83 ENHINSRLTVRELVAFG---RFPyskgrL--TAEDRE-IIDEAIAYLDLEDLADRYLDELSGGQRQRAFIAMVLAQDTDY 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLAD-AGRVVLVVTHSLTYLDV-CDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG4604   157 VLLDEPLNNLDMKHSVQMMKLLRRLADeLGKTVVIVLHDINFASCyADHIVAMK-DGRVVAQGTPEEI 223
ABC_ModC_molybdenum_transporter cd03297
ATP-binding cassette domain of the molybdenum transport system; ModC is an ABC-type ...
 314-498 2.19e-31

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: 122.02  E-value: 2.19e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 314 PGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEG-------HNIHTEygSLRTRIGMVPQDDVVHRQLTVNQALGYA 386
Cdd:cd03297    22 NEEVTGIFGASGAGKSTLLRCIAGLEKPDGGTIVLNGtvlfdsrKKINLP--PQQRKIGLVFQQYALFPHLNVRENLAFG 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 387 aelrLPPDTSKADRAQVvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTML 466
Cdd:cd03297   100 ----LKRKRNREDRISV-DELLDLLGLDHLLNRYPAQLSGGEKQRVALARALAAQPELLLLDEPFSALDRALRLQLLPEL 174

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1184609190 467 RQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:cd03297   175 KQIkKNLNIPVIFVTHDLSEAEyLADRIVVMEDG 208
LptB COG1137
ABC-type lipopolysaccharide export system, ATPase component [Cell wall/membrane/envelope ...
 288-510 8.46e-31

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


Pssm-ID: 440752 [Multi-domain]  Cd Length: 240  Bit Score: 121.29  E-value: 8.46e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR--IG 365
Cdd:COG1137     2 MTLEAENLVKSYGKRTVVKDVSLEVNQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGRIFLDGEDITHLPMHKRARlgIG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:COG1137    82 YLPQEASIFRKLTVEDNILAVLELR---KLSKKEREERLEELLEEFGITHLRKSKAYSLSGGERRRVEIARALATNPKFI 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 446 ILDEPTSGLDP--ALDLQvmTMLRQLADAGRVVLVVTHSL--TyLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1137   159 LLDEPFAGVDPiaVADIQ--KIIRHLKERGIGVLITDHNVreT-LGICDRAYIIS-EGKVLAEGTPEEI 223
fecE PRK11231
Fe(3+) dicitrate ABC transporter ATP-binding protein FecE;
290-510 1.25e-30

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


Pssm-ID: 183044 [Multi-domain]  Cd Length: 255  Bit Score: 121.27  E-value: 1.25e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGS--LRTRIGMV 367
Cdd:PRK11231    3 LRTENLTVGYGTKRILNDLSLSLPTGKITALIGPNGCGKSTLLKCFARLLTPQSGTVFLGDKPI-SMLSSrqLARRLALL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDVVHRQLTVNQALGYAAE--LRLPPDTSKADRaQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:PRK11231   82 PQHHLTPEGITVRELVAYGRSpwLSLWGRLSAEDN-ARVNQAMEQTRINHLADRRLTDLSGGQRQRAFLAMVLAQDTPVV 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLT----YldvCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:PRK11231  161 LLDEPTTYLDINHQVELMRLMRELNTQGKTVVTVLHDLNqasrY---CDHLVVLANGHVMAQ-GTPEEV 225
LivF COG0410
ABC-type branched-chain amino acid transport system, ATPase component LivF [Amino acid ...
 290-510 1.55e-30

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: 120.47  E-value: 1.55e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteygSLRTR------ 363
Cdd:COG0410     4 LEVENLHAGYGGIHVLHGVSLEVEEGEIVALLGRNGAGKTTLLKAISGLLPPRSGSIRFDGEDIT----GLPPHriarlg 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQDDVVHRQLTVNQALGYAAELRLPPDTSKADRAQVVAQ--VLDELgLTKHGDTrvdkLSGGQRK-----RAsval 436
Cdd:COG0410    80 IGYVPEGRRIFPSLTVEENLLLGAYARRDRAEVRADLERVYELfpRLKER-RRQRAGT----LSGGEQQmlaigRA---- 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 437 eLLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG0410   151 -LMSRPKLLLLDEPSLGLAPLIVEEIFEIIRRLNREGVTILLVEQNARFaLEIADRAYVLE-RGRIVLEGTAAEL 223
L_ocin_972_ABC TIGR03608
putative bacteriocin export ABC transporter, lactococcin 972 group; A gene pair with a fairly ...
 292-493 2.93e-30

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: 118.49  E-value: 2.93e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 292 VREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS-----LRTRIGM 366
Cdd:TIGR03608   1 LKNISKKFGDKVILDDLNLTIEKGKMYAIIGESGSGKSTLLNIIGLLEKFDSGQVYLNGQETPPLNSKkaskfRREKLGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLI 446
Cdd:TIGR03608  81 LFQNFALIENETVEENLDLGLKYK---KLSKKEKREKKKEALEKVGLNLKLKQKIYELSGGEQQRVALARAILKPPPLIL 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVL 493
Cdd:TIGR03608 158 ADEPTGSLDPKNRDEVLDLLLELNDEGKTIIIVTHDPEVAKQADRVI 204
drrA TIGR01188
daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin ...
 300-498 3.77e-30

daunorubicin resistance ABC transporter ATP-binding subunit; This model describes daunorubicin resistance ABC transporter, ATP binding subunit in bacteria and archaea. This model is restricted in its scope to preferentially recognize the ATP binding subunit associated with effux of the drug, daunorubicin. This transport system belong to the larger ATP-Binding Cassette (ABC) transporter superfamily. The characteristic feature of these transporter is the obligatory coupling of ATP hydrolysis to substrate translocation. The minimal configuration of bacterial ABC transport system: an ATPase or ATP binding subunit; An integral membrane protein; a hydrophilic polypetpide, which likely functions as substrate binding protein. In eukaryotes proteins of similar function include p-gyco proteins, multidrug resistance protein etc. [Transport and binding proteins, Other]


Pssm-ID: 130256 [Multi-domain]  Cd Length: 302  Bit Score: 121.34  E-value: 3.77e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTV 379
Cdd:TIGR01188   4 GDFKAVDGVNFKVREGEVFGFLGPNGAGKTTTIRMLTTLLRPTSGTARVAGYDVVREPRKVRRSIGIVPQYASVDEDLTG 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:TIGR01188  84 RENLEMMGRLY---GLPKDEAEERAEELLELFELGEAADRPVGTYSGGMRRRLDIAASLIHQPDVLFLDEPTTGLDPRTR 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1184609190 460 LQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:TIGR01188 161 RAIWDYIRALKEEGVTILLTTHYMEEADkLCDRIAIIDHG 200
ECF_ATPase_1 TIGR04520
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 290-510 5.91e-30

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: 119.84  E-value: 5.91e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFS--IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE--YGSLRTRIG 365
Cdd:TIGR04520   1 IEVENVSFSypESEKPALKNVSLSIEKGEFVAIIGHNGSGKSTLAKLLNGLLLPTSGKVTVDGLDTLDEenLWEIRKKVG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQD-DvvhrqltvNQALGYAAE---------LRLPPDTSKadraQVVAQVLDELGLTKHGDTRVDKLSGGQRKR---A 432
Cdd:TIGR04520  81 MVFQNpD--------NQFVGATVEddvafglenLGVPREEMR----KRVDEALKLVGMEDFRDREPHLLSGGQKQRvaiA 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 433 SV-ALElltgPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR04520 149 GVlAMR----PDIIILDEATSMLDPKGRKEVLETIRKLnKEEGITVISITHDMEEAVLADRVIVMN-KGKIVAEGTPREI 223
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 290-505 8.20e-30

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 124.79  E-value: 8.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFeGHNIhteygslrtRIGMVPQ 369
Cdd:COG0488   316 LELEGLSKSYGDKTLLDDLSLRIDRGDRIGLIGPNGAGKSTLLKLLAGELEPDSGTVKL-GETV---------KIGYFDQ 385

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 D-DVVHRQLTVNQALGYAAElrlppdtskADRAQVVAQVLDELGLTkhGD---TRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:COG0488   386 HqEELDPDKTVLDELRDGAP---------GGTEQEVRGYLGRFLFS--GDdafKPVGVLSGGEKARLALAKLLLSPPNVL 454

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 446 ILDEPTSGLDpaldlqvMTMLRQLADA-----GrVVLVVTHSLTYLD-VCDQVLLMAPGGKTAYLG 505
Cdd:COG0488   455 LLDEPTNHLD-------IETLEALEEAlddfpG-TVLLVSHDRYFLDrVATRILEFEDGGVREYPG 512
ABC_CysA_sulfate_importer cd03296
ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex ...
 289-510 8.74e-30

ATP-binding cassette domain of the sulfate transporter; Part of the ABC transporter complex cysAWTP involved in sulfate import. Responsible for energy coupling to the transport system. The complex is composed of two ATP-binding proteins (cysA), two transmembrane proteins (cysT and cysW), and a solute-binding protein (cysP). ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213263 [Multi-domain]  Cd Length: 239  Bit Score: 118.21  E-value: 8.74e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTRIGMVP 368
Cdd:cd03296     2 SIEVRNVSKRFGDFVALDDVSLDIPSGELVALLGPSGSGKTTLLRLIAGLERPDSGTILFGGEDA-TDVPVQERNVGFVF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTV--NQALGyaaeLRLPPDTSKADRAQV---VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:cd03296    81 QHYALFRHMTVfdNVAFG----LRVKPRSERPPEAEIrakVHELLKLVQLDWLADRYPAQLSGGQRQRVALARALAVEPK 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLV-VTHSLT-YLDVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:cd03296   157 VLLLDEPFGALDAKVRKELRRWLRRLHDELHVTTVfVTHDQEeALEVADRVVVMNK-GRIEQVGTPDEV 224
ABC_YhbG cd03218
ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the ...
 290-510 1.02e-29

ATP-binding cassette component of YhbG transport system; The ABC transporters belonging to the YhbG family are similar to members of the Mj1267_LivG family, which is involved in the transport of branched-chain amino acids. The genes yhbG and yhbN are located in a single operon and may function together in cell envelope during biogenesis. YhbG is the putative ATP-binding cassette component and YhbN is the putative periplasmic-binding protein. Depletion of each gene product leads to growth arrest, irreversible cell damage and loss of viability in E. coli. The YhbG homolog (NtrA) is essential in Rhizobium meliloti, a symbiotic nitrogen-fixing bacterium.


Pssm-ID: 213185 [Multi-domain]  Cd Length: 232  Bit Score: 118.03  E-value: 1.02e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGM--V 367
Cdd:cd03218     1 LRAENLSKRYGKRKVVNGVSLSVKQGEIVGLLGPNGAGKTTTFYMIVGLVKPDSGKILLDGQDITKLPMHKRARLGIgyL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDVVHRQLTVNQALGYAAELRLPPDTSKADRAQvvaQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03218    81 PQEASIFRKLTVEENILAVLEIRGLSKKEREEKLE---ELLEEFHITHLRKSKASSLSGGERRRVEIARALATNPKFLLL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 448 DEPTSGLDP--ALDLQvmTMLRQLADAGRVVLVVTHSL--TyLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03218   158 DEPFAGVDPiaVQDIQ--KIIKILKDRGIGVLITDHNVreT-LSITDRAYIIY-EGKVLAEGTPEEI 220
ABC_PotA_N cd03300
ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and ...
 290-510 1.09e-29

ATP-binding cassette domain of the polyamine transporter; PotA is an ABC-type transporter and the ATPase component of the spermidine/putrescine-preferential uptake system consisting of PotA, -B, -C, and -D. PotA has two domains with the N-terminal domain containing the ATPase activity and the residues required for homodimerization with PotA and heterdimerization with PotB. ABC transporters are a large family of proteins involved in the transport of a wide variety of different compounds, like sugars, ions, peptides, and more complex organic molecules. The nucleotide binding domain shows the highest similarity between all members of the family. ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213267 [Multi-domain]  Cd Length: 232  Bit Score: 117.72  E-value: 1.09e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHtEYGSLRTRIGMVPQ 369
Cdd:cd03300     1 IELENVSKFYGGFVALDGVSLDIKEGEFFTLLGPSGCGKTTLLRLIAGFETPTSGEILLDGKDIT-NLPPHKRPVNTVFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03300    80 NYALFPHLTVFENIAFGLRLK---KLPKAEIKERVAEALDLVQLEGYANRKPSQLSGGQQQRVAIARALVNEPKVLLLDE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 450 PTSGLDPAL--DLQVmtMLRQLADA-GRVVLVVTH----SLTyldVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:cd03300   157 PLGALDLKLrkDMQL--ELKRLQKElGITFVFVTHdqeeALT---MSDRIAVMNK-GKIQQIGTPEEI 218
ABCC_MsbA cd03251
ATP-binding cassette domain of the bacterial lipid flippase and related proteins, subfamily C; ...
 290-499 1.28e-29

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: 117.72  E-value: 1.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDK--NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGM 366
Cdd:cd03251     1 VEFKNVTFRYPGDgpPVLRDISLDIPAGETVALVGPSGSGKSTLVNLIPRFYDVDSGRILIDGHDVRDyTLASLRRQIGL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQlTVNQALGYAAELRLPPDTSKADRAQVVAQVLDEL--GL-TKHGDtRVDKLSGGQRKRASVALELLTGPS 443
Cdd:cd03251    81 VSQDVFLFND-TVAENIAYGRPGATREEVEEAARAANAHEFIMELpeGYdTVIGE-RGVKLSGGQRQRIAIARALLKDPP 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPGG 499
Cdd:cd03251   159 ILILDEATSALDTESERLVQAALERLM-KNRTTFVIAHRLSTIENADRIVVLEDGK 213
DppD COG0444
ABC-type dipeptide/oligopeptide/nickel transport system, ATPase component [Amino acid ...
 290-505 1.63e-29

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


Pssm-ID: 440213 [Multi-domain]  Cd Length: 320  Bit Score: 119.77  E-value: 1.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVR--EVNFSIGDKNL--LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP---TTGSVTFEGHNIHT----EYG 358
Cdd:COG0444     2 LEVRnlKVYFPTRRGVVkaVDGVSFDVRRGETLGLVGESGSGKSTLARAILGLLPPpgiTSGEILFDGEDLLKlsekELR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 359 SLRTR-IGMVPQD-----DVVHrqlTVNQALGYAaeLRLPPDTSKADRAQVVAQVLDELGLTKHGDtRVDK----LSGGQ 428
Cdd:COG0444    82 KIRGReIQMIFQDpmtslNPVM---TVGDQIAEP--LRIHGGLSKAEARERAIELLERVGLPDPER-RLDRypheLSGGM 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 429 RKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSL-TYLDVCDQVLLMapggktaYLG 505
Cdd:COG0444   156 RQRVMIARALALEPKLLIADEPTTALDVTIQAQILNLLKDLqRELGLAILFITHDLgVVAEIADRVAVM-------YAG 227
ArpD COG4618
ABC-type protease/lipase transport system, ATPase and permease components [Intracellular ...
 287-510 2.56e-29

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: 123.70  E-value: 2.56e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 287 TGGLEVREVNFSI--GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTR 363
Cdd:COG4618   328 KGRLSVENLTVVPpgSKRPILRGVSFSLEPGEVLGVIGPSGSGKSTLARLLVGVWPPTAGSVRLDGADLSQwDREELGRH 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQDdvVhrQL---TV--NQAlgyaaelRLPpdtsKADRAQVV--AQV--LDE--LGLTKHGDTRVD----KLSGGQ 428
Cdd:COG4618   408 IGYLPQD--V--ELfdgTIaeNIA-------RFG----DADPEKVVaaAKLagVHEmiLRLPDGYDTRIGeggaRLSGGQ 472

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 429 RKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYlGPPD 508
Cdd:COG4618   473 RQRIGLARALYGDPRLVVLDEPNSNLDDEGEAALAAAIRALKARGATVVVITHRPSLLAAVDKLLVLRDGRVQAF-GPRD 551


                  ..
gi 1184609190 509 QI 510
Cdd:COG4618   552 EV 553
ModC COG4148
ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and ...
 308-510 2.92e-29

ABC-type molybdate transport system, ATPase component ModC [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, ATPase component ModC is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 443319 [Multi-domain]  Cd Length: 358  Bit Score: 120.21  E-value: 2.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTF---------EGHNIHTEygslRTRIGMVPQDDVVHRQLT 378
Cdd:COG4148    18 VDFTLPGRGVTALFGPSGSGKTTLLRAIAGLERPDSGRIRLggevlqdsaRGIFLPPH----RRRIGYVFQEARLFPHLS 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAElRLPPDTSKADRAQVVAQvldeLGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPAL 458
Cdd:COG4148    94 VRGNLLYGRK-RAPRAERRISFDEVVEL----LGIGHLLDRRPATLSGGERQRVAIGRALLSSPRLLLMDEPLAALDLAR 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 459 DLQVMTMLRQLADAGRV-VLVVTHSLTylDV---CDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG4148   169 KAEILPYLERLRDELDIpILYVSHSLD--EVarlADHVVLLE-QGRVVASGPLAEV 221
type_I_sec_LssB TIGR03375
type I secretion system ATPase, LssB family; Type I protein secretion is a system in some ...
 288-510 4.76e-29

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


Pssm-ID: 274550 [Multi-domain]  Cd Length: 694  Bit Score: 123.82  E-value: 4.76e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSI--GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRI 364
Cdd:TIGR03375 462 GEIEFRNVSFAYpgQETPALDNVSLTIRPGEKVAIIGRIGSGKSTLLKLLLGLYQPTEGSVLLDGVDIRQiDPADLRRNI 541

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQDDVV-HRQLTVNQALGyaaelrlPPDTSKAD--RAQVVAQVLDELGLTKHG-DTRV----DKLSGGQRKRASVAL 436
Cdd:TIGR03375 542 GYVPQDPRLfYGTLRDNIALG-------APYADDEEilRAAELAGVTEFVRRHPDGlDMQIgergRSLSGGQRQAVALAR 614

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 437 ELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR03375 615 ALLRDPPILLLDEPTSAMDNRSEERFKDRLKRWL-AGKTLVLVTHRTSLLDLVDRIIVMD-NGRIVADGPKDQV 686
MalK COG3839
ABC-type sugar transport system, ATPase component MalK [Carbohydrate transport and metabolism]; ...
 290-510 8.88e-29

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


Pssm-ID: 443050 [Multi-domain]  Cd Length: 352  Bit Score: 118.64  E-value: 8.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTRIGMVPQ 369
Cdd:COG3839     4 LELENVSKSYGGVEALKDIDLDIEDGEFLVLLGPSGCGKSTLLRMIAGLEDPTSGEILIGGRDV-TDLPPKDRNIAMVFQ 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:COG3839    83 SYALYPHMTVYENIAFPLKLR---KVPKAEIDRRVREAAELLGLEDLLDRKPKQLSGGQRQRVALGRALVREPKVFLLDE 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 450 PTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHsltyldvcDQVLLMAPGGKTAYL--------GPPDQI 510
Cdd:COG3839   160 PLSNLDAKLRVEMRAEIKRLhRRLGTTTIYVTH--------DQVEAMTLADRIAVMndgriqqvGTPEEL 221
ABC_ModC_like cd03299
ATP-binding cassette domain similar to the molybdate transporter; Archaeal protein closely ...
 290-510 1.03e-28

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: 115.13  E-value: 1.03e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLErVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTRIGMVPQ 369
Cdd:cd03299     1 LKVENLSKDWKEFKLKN-VSLEVERGDYFVILGPTGSGKSVLLETIAGFIKPDSGKILLNGKDI-TNLPPEKRDISYVPQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03299    79 NYALFPHMTVYKNIAYGLKKRKVD---KKEIERKVLEIAEMLGIDHLLNRKPETLSGGEQQRVAIARALVVNPKILLLDE 155

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRV-VLVVTHSLT-YLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03299   156 PFSALDVRTKEKLREELKKIRKEFGVtVLHVTHDFEeAWALADKVAIML-NGKLIQVGKPEEV 217
PRK10619 PRK10619
histidine ABC transporter ATP-binding protein HisP;
290-512 1.36e-28

histidine ABC transporter ATP-binding protein HisP;


Pssm-ID: 182592 [Multi-domain]  Cd Length: 257  Bit Score: 115.45  E-value: 1.36e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH--------------T 355
Cdd:PRK10619    6 LNVIDLHKRYGEHEVLKGVSLQANAGDVISIIGSSGSGKSTFLRCINFLEKPSEGSIVVNGQTINlvrdkdgqlkvadkN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 356 EYGSLRTRIGMVPQDDVVHRQLTVNQALGYAAELRLppDTSKADRAQVVAQVLDELGLTKHGDTRVD-KLSGGQRKRASV 434
Cdd:PRK10619   86 QLRLLRTRLTMVFQHFNLWSHMTVLENVMEAPIQVL--GLSKQEARERAVKYLAKVGIDERAQGKYPvHLSGGQQQRVSI 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 435 ALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQIGG 512
Cdd:PRK10619  164 ARALAMEPEVLLFDEPTSALDPELVGEVLRIMQQLAEEGKTMVVVTHEMGFARHVSSHVIFLHQGKIEEEGAPEQLFG 241
ECF_ATPase_2 TIGR04521
energy-coupling factor transporter ATPase; Members of this family are ATP-binding cassette ...
 290-510 1.48e-28

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


Pssm-ID: 275314 [Multi-domain]  Cd Length: 277  Bit Score: 116.01  E-value: 1.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLER-----VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYG----SL 360
Cdd:TIGR04521   1 IKLKNVSYIYQPGTPFEKkalddVSLTIEDGEFVAIIGHTGSGKSTLIQHLNGLLKPTSGTVTIDGRDITAKKKkklkDL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 361 RTRIGMV---PQDdvvhrQL---TVN-------QALGYaaelrlppdtSKADRAQVVAQVLDELGLtkhGDTRVDK---- 423
Cdd:TIGR04521  81 RKKVGLVfqfPEH-----QLfeeTVYkdiafgpKNLGL----------SEEEAEERVKEALELVGL---DEEYLERspfe 142

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 424 LSGGQRKR---ASV-ALElltgPSLLILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTylDV---CDQVLLM 495
Cdd:TIGR04521 143 LSGGQMRRvaiAGVlAME----PEVLILDEPTAGLDPKGRKEILDLFKRLHKEkGLTVILVTHSME--DVaeyADRVIVM 216

                         250
                  ....*....|....*
gi 1184609190 496 ApGGKTAYLGPPDQI 510
Cdd:TIGR04521 217 H-KGKIVLDGTPREV 230
HisP COG4598
ABC-type histidine transport system, ATPase component [Amino acid transport and metabolism];
290-510 1.86e-28

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


Pssm-ID: 443652 [Multi-domain]  Cd Length: 259  Bit Score: 114.90  E-value: 1.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS---------- 359
Cdd:COG4598     9 LEVRDLHKSFGDLEVLKGVSLTARKGDVISIIGSSGSGKSTFLRCINLLETPDSGEIRVGGEEIRLKPDRdgelvpadrr 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 ----LRTRIGMVPQDDVVHRQLTVNQALGYAaelrlPPDTSKADRAQVVAQ---VLDELGLTKHGDTRVDKLSGGQRKRA 432
Cdd:COG4598    89 qlqrIRTRLGMVFQSFNLWSHMTVLENVIEA-----PVHVLGRPKAEAIERaeaLLAKVGLADKRDAYPAHLSGGQQQRA 163

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 433 SVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:COG4598   164 AIARALAMEPEVMLFDEPTSALDPELVGEVLKVMRDLAEEGRTMLVVTHEMGFArDVSSHVVFLHQ-GRIEEQGPPAEV 241
AztA NF040873
zinc ABC transporter ATP-binding protein AztA;
300-483 2.79e-28

zinc ABC transporter ATP-binding protein AztA;


Pssm-ID: 468810 [Multi-domain]  Cd Length: 191  Bit Score: 112.33  E-value: 2.79e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHnihteygslrTRIGMVPQDDVVHRQL-- 377
Cdd:NF040873    3 GGRPVLHGVDLTIPAGSLTAVVGPNGSGKSTLLKVLAGVLRPTSGTVRRAGG----------ARVAYVPQRSEVPDSLpl 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQ--ALGYAAELRLPPDTSKADRAqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:NF040873   73 TVRDlvAMGRWARRGLWRRLTRDDRA-AVDDALERVGLADLAGRQLGELSGGQRQRALLAQGLAQEADLLLLDEPTTGLD 151

                         170       180
                  ....*....|....*....|....*...
gi 1184609190 456 PALDLQVMTMLRQLADAGRVVLVVTHSL 483
Cdd:NF040873  152 AESRERIIALLAEEHARGATVVVVTHDL 179
ABCC_cytochrome_bd cd03247
ATP-binding cassette domain of CydCD, subfamily C; The CYD subfamily implicated in cytochrome ...
 290-498 3.63e-28

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


Pssm-ID: 213214 [Multi-domain]  Cd Length: 178  Bit Score: 111.64  E-value: 3.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN--LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMV 367
Cdd:cd03247     1 LSINNVSFSYPEQEqqVLKNLSLELKQGEKIALLGRSGSGKSTLLQLLTGDLKPQQGEITLDGVPVSDLEKALSSLISVL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQddvvhrqltvnQALGYAAELRlppdtskadraqvvaqvlDELGLtkhgdtrvdKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03247    81 NQ-----------RPYLFDTTLR------------------NNLGR---------RFSGGERQRLALARILLQDAPIVLL 122

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03247   123 DEPTVGLDPITERQLLSLIFEVLK-DKTLIWITHHLTGIEHMDKILFLENG 172
glnQ PRK09493
glutamine ABC transporter ATP-binding protein GlnQ;
290-510 3.97e-28

glutamine ABC transporter ATP-binding protein GlnQ;


Pssm-ID: 181906 [Multi-domain]  Cd Length: 240  Bit Score: 113.65  E-value: 3.97e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI---HTEYGSLRTRIGM 366
Cdd:PRK09493    2 IEFKNVSKHFGPTQVLHNIDLNIDQGEVVVIIGPSGSGKSTLLRCINKLEEITSGDLIVDGLKVndpKVDERLIRQEAGM 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTV--NQALGyAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK09493   82 VFQQFYLFPHLTAleNVMFG-PLRVR---GASKEEAEKQARELLAKVGLAERAHHYPSELSGGQQQRVAIARALAVKPKL 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQI 510
Cdd:PRK09493  158 MLFDEPTSALDPELRHEVLKVMQDLAEEGMTMVIVTHEIGFAEKVASRLIFIDKGRIAEDGDPQVL 223
ABCC_Protease_Secretion cd03246
ATP-binding cassette domain of PrtD, subfamily C; This family represents the ABC component of ...
 290-498 4.92e-28

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: 111.15  E-value: 4.92e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN--LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEY-GSLRTRIGM 366
Cdd:cd03246     1 LEVENVSFRYPGAEppVLRNVSFSIEPGESLAIIGPSGSGKSTLARLILGLLRPTSGRVRLDGADISQWDpNELGDHVGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDvvhrqltvnqalgyaaelRLPPDTskadraqvVAQVLdelgltkhgdtrvdkLSGGQRKRASVALELLTGPSLLI 446
Cdd:cd03246    81 LPQDD------------------ELFSGS--------IAENI---------------LSGGQRQRLGLARALYGNPRILV 119

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03246   120 LDEPNSHLDVEGERALNQAIAALKAAGATRIVIAHRPETLASADRILVLEDG 171
CydD TIGR02857
thiol reductant ABC exporter, CydD subunit; The gene pair cydCD encodes an ABC-family ...
 279-495 5.17e-28

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: 119.31  E-value: 5.17e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 279 RRQEVAARTGGLEVREVNFSIGDK-NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTE 356
Cdd:TIGR02857 311 KAPVTAAPASSLEFSGVSVAYPGRrPALRPVSFTVPPGERVALVGPSGAGKSTLLNLLLGFVDPTEGSIAVNGVPLaDAD 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 357 YGSLRTRIGMVPQddvvhRQLTVNQALgyAAELRLP-PDTSKADRAQVVAQV-LDEL--GLTKHGDTRVDK----LSGGQ 428
Cdd:TIGR02857 391 ADSWRDQIAWVPQ-----HPFLFAGTI--AENIRLArPDASDAEIREALERAgLDEFvaALPQGLDTPIGEggagLSGGQ 463

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 429 RKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTHSLTYLDVCDQVLLM 495
Cdd:TIGR02857 464 AQRLALARAFLRDAPLLLLDEPTAHLDAETEAEVLEALRALAQ-GRTVLLVTHRLALAALADRIVVL 529
PRK13537 PRK13537
nodulation factor ABC transporter ATP-binding protein NodI;
287-515 5.82e-28

nodulation factor ABC transporter ATP-binding protein NodI;


Pssm-ID: 237420 [Multi-domain]  Cd Length: 306  Bit Score: 114.90  E-value: 5.82e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 287 TGGLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGM 366
Cdd:PRK13537    5 VAPIDFRNVEKRYGDKLVVDGLSFHVQRGECFGLLGPNGAGKTTTLRMLLGLTHPDAGSISLCGEPVPSRARHARQRVGV 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQALG-YAAELRLPPDTSKAdraqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:PRK13537   85 VPQFDNLDPDFTVRENLLvFGRYFGLSAAAARA----LVPPLLEFAKLENKADAKVGELSGGMKRRLTLARALVNDPDVL 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPGGKTAYLGPPDQIGGAMG 515
Cdd:PRK13537  161 VLDEPTTGLDPQARHLMWERLRSLLARGKTILLTTHFMEEAErLCDRLCVIEEGRKIAEGAPHALIESEIG 231
ntrCD TIGR01184
nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits ...
 305-514 1.24e-27

nitrate transport ATP-binding subunits C and D; This model describes the ATP binding subunits of nitrate transport in bacteria and archaea. This protein belongs to the ATP-binding cassette (ABC) superfamily. It is thought that the two subunits encoded by ntrC and ntrD form the binding surface for interaction with ATP. This model is restricted in identifying ATP binding subunit associated with the nitrate transport. Nitrate assimilation is aided by other proteins derived from the operon which among others include products of ntrA - a regulatory protein; ntrB - a hydropbobic transmembrane permease and narB - a reductase. [Transport and binding proteins, Anions, Transport and binding proteins, Other]


Pssm-ID: 130252 [Multi-domain]  Cd Length: 230  Bit Score: 111.79  E-value: 1.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTrigMVPQDDVVHRQLTVNQALG 384
Cdd:TIGR01184   1 LKGVNLTIQQGEFISLIGHSGCGKSTLLNLISGLAQPTSGGVILEGKQI-TEPGPDRM---VVFQNYSLLPWLTVRENIA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 385 YAAElRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMT 464
Cdd:TIGR01184  77 LAVD-RVLPDLSKSERRAIVEEHIALVGLTEAADKRPGQLSGGMKQRVAIARALSIRPKVLLLDEPFGALDALTRGNLQE 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 465 MLRQLA-DAGRVVLVVTHsltylDVcDQVLLMAPGGKTAYLGPPDQIGGAM 514
Cdd:TIGR01184 156 ELMQIWeEHRVTVLMVTH-----DV-DEALLLSDRVVMLTNGPAANIGQIL 200
ABCC_Glucan_exporter_like cd03254
ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan ...
 288-509 2.24e-27

ATP-binding cassette domain of glucan transporter and related proteins, subfamily C; Glucan exporter ATP-binding protein. In A. tumefaciens cyclic beta-1, 2-glucan must be transported into the periplasmic space to exert its action as a virulence factor. This subfamily belongs to the MRP-like family and is involved in drug, peptide, and lipid export. The MRP-like family, similar to all ABC proteins, have a common four-domain core structure constituted by two membrane-spanning domains each composed of six transmembrane (TM) helices and two nucleotide-binding domains (NBD). ABC transporters are a subset of nucleotide hydrolases that contain a signature motif, Q-loop, and H-loop/switch region, in addition to, the Walker A motif/P-loop and Walker B motif commonly found in a number of ATP- and GTP-binding and hydrolyzing proteins.


Pssm-ID: 213221 [Multi-domain]  Cd Length: 229  Bit Score: 111.16  E-value: 2.24e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSIGDKNL-LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIG 365
Cdd:cd03254     1 GEIEFENVNFSYDEKKPvLKDINFSIKPGETVAIVGPTGAGKTTLINLLMRFYDPQKGQILIDGIDIRDiSRKSLRSMIG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQlTVnqalgyAAELRLPPDTSKADRAQVVAQV--LDELG--LTKHGDTRV----DKLSGGQRKRASVALE 437
Cdd:cd03254    81 VVLQDTFLFSG-TI------MENIRLGRPNATDEEVIEAAKEagAHDFImkLPNGYDTVLgengGNLSQGERQLLAIARA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQ 509
Cdd:cd03254   154 MLRDPKILILDEATSNIDTETEKLIQEALEKLMK-GRTSIIIAHRLSTIKNADKILVLD-DGKIIEEGTHDE 223
thiQ TIGR01277
thiamine ABC transporter, ATP-binding protein; This model describes the energy-transducing ...
 301-498 5.02e-27

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


Pssm-ID: 130344 [Multi-domain]  Cd Length: 213  Bit Score: 109.57  E-value: 5.02e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNiHTEYGSLRTRIGMVPQDDVVHRQLTVN 380
Cdd:TIGR01277  10 YEHLPMEFDLNVADGEIVAIMGPSGAGKSTLLNLIAGFIEPASGSIKVNDQS-HTGLAPYQRPVSMLFQENNLFAHLTVR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 Q--ALGYAAELRLppdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPAL 458
Cdd:TIGR01277  89 QniGLGLHPGLKL-----NAEQQEKVVDAAQQVGIADYLDRLPEQLSGGQRQRVALARCLVRPNPILLLDEPFSALDPLL 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1184609190 459 DLQVMTMLRQLADA-GRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:TIGR01277 164 REEMLALVKQLCSErQRTLLMVTHHLSDArAIASQIAVVSQG 205
thiQ PRK10771
thiamine ABC transporter ATP-binding protein ThiQ;
307-510 5.21e-27

thiamine ABC transporter ATP-binding protein ThiQ;


Pssm-ID: 182716 [Multi-domain]  Cd Length: 232  Bit Score: 110.06  E-value: 5.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 307 RVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNiHTEYGSLRTRIGMVPQDDVVHRQLTVNQ--ALG 384
Cdd:PRK10771   17 RFDLTVERGERVAILGPSGAGKSTLLNLIAGFLTPASGSLTLNGQD-HTTTPPSRRPVSMLFQENNLFSHLTVAQniGLG 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 385 YAAELRLppdtSKADRAQVvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMT 464
Cdd:PRK10771   96 LNPGLKL----NAAQREKL-HAIARQMGIEDLLARLPGQLSGGQRQRVALARCLVREQPILLLDEPFSALDPALRQEMLT 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 465 MLRQLADAGRV-VLVVTHSLtyldvcDQVLLMAP------GGKTAYLGPPDQI 510
Cdd:PRK10771  171 LVSQVCQERQLtLLMVSHSL------EDAARIAPrslvvaDGRIAWDGPTDEL 217
nickel_nikE TIGR02769
nickel import ATP-binding protein NikE; This family represents the NikE subunit of a ...
 286-498 8.25e-27

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


Pssm-ID: 131816 [Multi-domain]  Cd Length: 265  Bit Score: 110.67  E-value: 8.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 286 RTGGLevrevNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR-- 363
Cdd:TIGR02769  13 RTGGL-----FGAKQRAPVLTNVSLSIEEGETVGLLGRSGCGKSTLARLLLGLEKPAQGTVSFRGQDLYQLDRKQRRAfr 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 --IGMVPQD--DVVHRQLTVNQALGyaAELRLPPDTSKADRAQVVAQVLDELGL-TKHGDTRVDKLSGGQRKRASVALEL 438
Cdd:TIGR02769  88 rdVQLVFQDspSAVNPRMTVRQIIG--EPLRHLTSLDESEQKARIAELLDMVGLrSEDADKLPRQLSGGQLQRINIARAL 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:TIGR02769 166 AVKPKLIVLDEAVSNLDMVLQAVILELLRKLqQAFGTAYLFITHDLRLVQsFCQRVAVMDKG 227
ATM1 COG5265
ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components ...
 267-498 9.16e-27

ABC-type transport system involved in Fe-S cluster assembly, permease and ATPase components [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 444078 [Multi-domain]  Cd Length: 605  Bit Score: 116.07  E-value: 9.16e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 267 NVDLVFtgGILVRRQEVA---------ARTGGLEVREVNFS-IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIA 336
Cdd:COG5265   328 DMERMF--DLLDQPPEVAdapdapplvVGGGEVRFENVSFGyDPERPILKGVSFEVPAGKTVAIVGPSGAGKSTLARLLF 405

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 337 GYATPTTGSVTFEGHNI-HTEYGSLRTRIGMVPQDDVvhrqL---TVNQALGYAAelrlpPDtskADRAQVV-----AQV 407
Cdd:COG5265   406 RFYDVTSGRILIDGQDIrDVTQASLRAAIGIVPQDTV----LfndTIAYNIAYGR-----PD---ASEEEVEaaaraAQI 473

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 408 LDELGLTKHG-DTRVD----KLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHS 482
Cdd:COG5265   474 HDFIESLPDGyDTRVGerglKLSGGEKQRVAIARTLLKNPPILIFDEATSALDSRTERAIQAALREVA-RGRTTLVIAHR 552

                         250
                  ....*....|....*..
gi 1184609190 483 L-TYLDvCDQVLLMAPG 498
Cdd:COG5265   553 LsTIVD-ADEILVLEAG 568
ABC_FtsE cd03292
Cell division ATP-binding protein FtsE; The FtsEX complex resembles an ABC transporter, where ...
 305-481 1.43e-26

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: 108.26  E-value: 1.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS----LRTRIGMVPQDDVVHRQLTVN 380
Cdd:cd03292    17 LDGINISISAGEFVFLVGPSGAGKSTLLKLIYKEELPTSGTIRVNGQDVSDLRGRaipyLRRKIGVVFQDFRLLPDRNVY 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGYAAELRLPPDTSKADRaqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDL 460
Cdd:cd03292    97 ENVAFALEVTGVPPREIRKR---VPAALELVGLSHKHRALPAELSGGEQQRVAIARAIVNSPTILIADEPTGNLDPDTTW 173

                         170       180
                  ....*....|....*....|.
gi 1184609190 461 QVMTMLRQLADAGRVVLVVTH 481
Cdd:cd03292   174 EIMNLLKKINKAGTTVVVATH 194
ABC_Pro_Gly_Betaine cd03294
ATP-binding cassette domain of the osmoprotectant proline/glycine betaine uptake system; This ...
 279-510 1.68e-26

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


Pssm-ID: 213261 [Multi-domain]  Cd Length: 269  Bit Score: 109.66  E-value: 1.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 279 RRQEVAARTGG-LEVREVNFSIgdknllervsltaRPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-- 355
Cdd:cd03294    26 SKEEILKKTGQtVGVNDVSLDV-------------REGEIFVIMGLSGSGKSTLLRCINRLIEPTSGKVLIDGQDIAAms 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 356 --EYGSLR-TRIGMVPQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRA 432
Cdd:cd03294    93 rkELRELRrKKISMVFQSFALLPHRTVLENVAFGLEVQ---GVPRAEREERAAEALELVGLEGWEHKYPDELSGGMQQRV 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 433 SVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLT-YLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03294   170 GLARALAVDPDILLMDEAFSALDPLIRREMQDELLRLqAELQKTIVFITHDLDeALRLGDRIAIMK-DGRLVQVGTPEEI 248
btuD PRK09536
corrinoid ABC transporter ATPase; Reviewed
 290-510 1.76e-26

corrinoid ABC transporter ATPase; Reviewed


Pssm-ID: 236554 [Multi-domain]  Cd Length: 402  Bit Score: 112.63  E-value: 1.76e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH-TEYGSLRTRIGMVP 368
Cdd:PRK09536    4 IDVSDLSVEFGDTTVLDGVDLSVREGSLVGLVGPNGAGKTTLLRAINGTLTPTAGTVLVAGDDVEaLSARAASRRVASVP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTVNQA--LGYAAEL-RLPPDTSKADRAqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:PRK09536   84 QDTSLSFEFDVRQVveMGRTPHRsRFDTWTETDRAA--VERAMERTGVAQFADRPVTSLSGGERQRVLLARALAQATPVL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMAPGGKTAyLGPPDQI 510
Cdd:PRK09536  162 LLDEPTASLDINHQVRTLELVRRLVDDGKTAVAAIHDLDLaARYCDELVLLADGRVRA-AGPPADV 226
PstB COG1117
ABC-type phosphate transport system, ATPase component [Inorganic ion transport and metabolism]; ...
 290-483 2.09e-26

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


Pssm-ID: 440734 [Multi-domain]  Cd Length: 258  Bit Score: 108.97  E-value: 2.09e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSR-------LIAGYAtpTTGSVTFEGHNIhteYGS--- 359
Cdd:COG1117    12 IEVRNLNVYYGDKQALKDINLDIPENKVTALIGPSGCGKSTLLRclnrmndLIPGAR--VEGEILLDGEDI---YDPdvd 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 ---LRTRIGMVPQ----------DDVvhrqltvnqALGyaaeLRLPPDTSKADRAQVVAQVLDELGL---TKHgdtRVDK 423
Cdd:COG1117    87 vveLRRRVGMVFQkpnpfpksiyDNV---------AYG----LRLHGIKSKSELDEIVEESLRKAALwdeVKD---RLKK 150

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 424 ----LSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADagRV-VLVVTHSL 483
Cdd:COG1117   151 salgLSGGQQQRLCIARALAVEPEVLLMDEPTSALDPISTAKIEELILELKK--DYtIVIVTHNM 213
ABC_ThiQ_thiamine_transporter cd03298
ATP-binding cassette domain of the thiamine transport system; Part of the ...
 290-505 2.58e-26

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


Pssm-ID: 213265 [Multi-domain]  Cd Length: 211  Bit Score: 107.58  E-value: 2.58e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLleRVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTrIGMVPQ 369
Cdd:cd03298     1 VRLDKIRFSYGEQPM--HFDLTFAQGEITAIVGPSGSGKSTLLNLIAGFETPQSGRVLINGVDVTAAPPADRP-VSMLFQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQ--ALGYAAELRLPPDTSKAdraqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03298    78 ENNLFAHLTVEQnvGLGLSPGLKLTAEDRQA-----IEVALARVGLAGLEKRLPGELSGGERQRVALARVLVRDKPVLLL 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLG 505
Cdd:cd03298   153 DEPFAALDPALRAEMLDLVLDLhAETKMTVLMVTHQPEDAKRLAQRVVFLDNGRIAAQG 211
ABC_MalK_N cd03301
The N-terminal ATPase domain of the maltose transporter, MalK; ATP binding cassette (ABC) ...
 290-511 2.71e-26

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: 107.34  E-value: 2.71e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTrIGMVPQ 369
Cdd:cd03301     1 VELENVTKRFGNVTALDDLNLDIADGEFVVLLGPSGCGKTTTLRMIAGLEEPTSGRIYIGGRDVTDLPPKDRD-IAMVFQ 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03301    80 NYALYPHMTVYDNIAFGLKLR---KVPKDEIDERVREVAELLQIEHLLDRKPKQLSGGQRQRVALGRAIVREPKVFLMDE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHsltyldvcDQVLLMAPGGKTAYL--GPPDQIG 511
Cdd:cd03301   157 PLSNLDAKLRVQMRAELKRLqQRLGTTTIYVTH--------DQVEAMTMADRIAVMndGQIQQIG 213
TauB COG4525
ABC-type taurine transport system, ATPase component [Inorganic ion transport and metabolism];
305-498 3.01e-26

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


Pssm-ID: 443596 [Multi-domain]  Cd Length: 262  Bit Score: 108.80  E-value: 3.01e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRtriGMVPQDDVVHRQLTV--NQA 382
Cdd:COG4525    23 LQDVSLTIESGEFVVALGASGCGKTTLLNLIAGFLAPSSGEITLDGVPV-TGPGADR---GVVFQKDALLPWLNVldNVA 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 383 LGyaaeLRLPpDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQV 462
Cdd:COG4525    99 FG----LRLR-GVPKAERRARAEELLALVGLADFARRRIWQLSGGMRQRVGIARALAADPRFLLMDEPFGALDALTREQM 173

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1184609190 463 MTMLRQL-ADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:COG4525   174 QELLLDVwQRTGKGVFLITHSVeEALFLATRLVVMSPG 211
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 9-100 3.57e-26

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 102.79  E-value: 3.57e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190   9 LTVRSQRWEGNFAPGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVPAVDIQDGQSVNI 88
Cdd:cd22694     1 LTIRIPGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGTRVRL 80

                          90
                  ....*....|...
gi 1184609190  89 GKP-DGPLITFHV 100
Cdd:cd22694    81 GDPtDGPALTVVV 93
Uup COG0488
ATPase components of ABC transporters with duplicated ATPase domains [General function ...
 292-493 5.61e-26

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


Pssm-ID: 440254 [Multi-domain]  Cd Length: 520  Bit Score: 112.85  E-value: 5.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 292 VREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHnihteygslrTRIGMVPQDD 371
Cdd:COG0488     1 LENLSKSFGGRPLLDDVSLSINPGDRIGLVGRNGAGKSTLLKILAGELEPDSGEVSIPKG----------LRIGYLPQEP 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 372 VVHRQLTV-NQALGYAAELR---------------LPPDTSKADRAQV-------------VAQVLDELGLTKH-GDTRV 421
Cdd:COG0488    71 PLDDDLTVlDTVLDGDAELRaleaeleeleaklaePDEDLERLAELQEefealggweaearAEEILSGLGFPEEdLDRPV 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 422 DKLSGGQRKRASVALELLTGPSLLILDEPTSGLDpaLD----LQvmTMLRQLADAgrvVLVVTHSLTYLD-VCDQVL 493
Cdd:COG0488   151 SELSGGWRRRVALARALLSEPDLLLLDEPTNHLD--LEsiewLE--EFLKNYPGT---VLVVSHDRYFLDrVATRIL 220
ABCC_Hemolysin cd03252
ATP-binding cassette domain of hemolysin B, subfamily C; The ABC-transporter hemolysin B is a ...
 304-498 6.61e-26

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: 107.19  E-value: 6.61e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGMVPQDDVV-HRQLTVNQ 381
Cdd:cd03252    17 ILDNISLRIKPGEVVGIVGRSGSGKSTLTKLIQRFYVPENGRVLVDGHDLALaDPAWLRRQVGVVLQENVLfNRSIRDNI 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 382 ALGYAAelrlpPDTSKADRAQVVAQVLDELGLTKHG-DTRVDK----LSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:cd03252    97 ALADPG-----MSMERVIEAAKLAGAHDFISELPEGyDTIVGEqgagLSGGQRQRIAIARALIHNPRILIFDEATSALDY 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1184609190 457 ALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03252   172 ESEHAIMRNMHDIC-AGRTVIIIAHRLSTVKNADRIIVMEKG 212
cbiO PRK13640
energy-coupling factor transporter ATPase;
290-508 1.26e-25

energy-coupling factor transporter ATPase;


Pssm-ID: 184200 [Multi-domain]  Cd Length: 282  Bit Score: 107.58  E-value: 1.26e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGD--KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATP---TTGSVTFEGHNIHTE-YGSLRTR 363
Cdd:PRK13640    6 VEFKHVSFTYPDskKPALNDISFSIPRGSWTALIGHNGSGKSTISKLINGLLLPddnPNSKITVDGITLTAKtVWDIREK 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQD-DVVHRQLTVNQALGYAAELRLPPdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGP 442
Cdd:PRK13640   86 VGIVFQNpDNQFVGATVGDDVAFGLENRAVP---RPEMIKIVRDVLADVGMLDYIDSEPANLSGGQKQRVAIAGILAVEP 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 443 SLLILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPD 508
Cdd:PRK13640  163 KIIILDESTSMLDPAGKEQILKLIRKLKkKNNLTVISITHDIDEANMADQVLVLDDGKLLAQGSPVE 229
ABCG_PDR_domain1 cd03233
First domain of the pleiotropic drug resistance-like subfamily G of ATP-binding cassette ...
 304-498 1.95e-25

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: 104.65  E-value: 1.95e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG----YATPTtGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTV 379
Cdd:cd03233    22 ILKDFSGVVKPGEMVLVLGRPGSGCSTLLKALANrtegNVSVE-GDIHYNGIPYKEFAEKYPGEIIYVSEEDVHFPTLTV 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAELRlppdtskadraqvvaqvldelgltkhGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:cd03233   101 RETLDFALRCK--------------------------GNEFVRGISGGERKRVSIAEALVSRASVLCWDNSTRGLDSSTA 154

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1184609190 460 LQVMTMLRQLADAGRVVLVVT---HSLTYLDVCDQVLLMAPG 498
Cdd:cd03233   155 LEILKCIRTMADVLKTTTFVSlyqASDEIYDLFDKVLVLYEG 196
SufC COG0396
Fe-S cluster assembly ATPase SufC [Posttranslational modification, protein turnover, ...
 290-508 2.40e-25

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


Pssm-ID: 440165 [Multi-domain]  Cd Length: 245  Bit Score: 105.53  E-value: 2.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG---YaTPTTGSVTFEGHNIhTEygsL----RT 362
Cdd:COG0396     1 LEIKNLHVSVEGKEILKGVNLTIKPGEVHAIMGPNGSGKSTLAKVLMGhpkY-EVTSGSILLDGEDI-LE---LspdeRA 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 363 R--IGMVPQDDVVHRQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTR-VD-KLSGGQRKRASVALEL 438
Cdd:COG0396    76 RagIFLAFQYPVEIPGVSVSNFLRTALNARRGEELSAREFLKLLKEKMKELGLDEDFLDRyVNeGFSGGEKKRNEILQML 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 439 LTGPSLLILDEPTSGLDpaLD-LQVMT-MLRQLADAGRVVLVVTHS---LTYLdVCDQVLLMApGGKTAYLGPPD 508
Cdd:COG0396   156 LLEPKLAILDETDSGLD--IDaLRIVAeGVNKLRSPDRGILIITHYqriLDYI-KPDFVHVLV-DGRIVKSGGKE 226
MsbA_lipidA TIGR02203
lipid A export permease/ATP-binding protein MsbA; This family consists of a single polypeptide ...
 287-498 2.71e-25

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


Pssm-ID: 131258 [Multi-domain]  Cd Length: 571  Bit Score: 111.35  E-value: 2.71e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 287 TGGLEVREVNFSIG--DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTR 363
Cdd:TIGR02203 328 RGDVEFRNVTFRYPgrDRPALDSISLVIEPGETVALVGRSGSGKSTLVNLIPRFYEPDSGQILLDGHDLaDYTLASLRRQ 407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQDdVVHRQLTVNQALGYAAelrlppdTSKADRAQVVAQVLD----------ELGL-TKHGDTRVdKLSGGQRKRA 432
Cdd:TIGR02203 408 VALVSQD-VVLFNDTIANNIAYGR-------TEQADRAEIERALAAayaqdfvdklPLGLdTPIGENGV-LLSGGQRQRL 478

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 433 SVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:TIGR02203 479 AIARALLKDAPILILDEATSALDNESERLVQAALERLMQ-GRTTLVIAHRLSTIEKADRIVVMDDG 543
AppF COG4608
ABC-type oligopeptide transport system, ATPase component [Amino acid transport and metabolism]; ...
 308-505 2.75e-25

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


Pssm-ID: 443658 [Multi-domain]  Cd Length: 329  Bit Score: 107.51  E-value: 2.75e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPG-TLtAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS----LRTRIGMVPQD--DVVHRQLTVN 380
Cdd:COG4608    37 VSFDIRRGeTL-GLVGESGCGKSTLGRLLLRLEEPTSGEILFDGQDITGLSGRelrpLRRRMQMVFQDpyASLNPRMTVG 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGYAaeLRLPPDTSKADRAQVVAQVLDELGL-TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:COG4608   116 DIIAEP--LRIHGLASKAERRERVAELLELVGLrPEHADRYPHEFSGGQRQRIGIARALALNPKLIVCDEPVSALDVSIQ 193

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 460 LQVMTMLRQLADagrvvlvvTHSLTYL----D------VCDQVLLMapggktaYLG 505
Cdd:COG4608   194 AQVLNLLEDLQD--------ELGLTYLfishDlsvvrhISDRVAVM-------YLG 234
PhnK COG1101
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 290-495 3.40e-25

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


Pssm-ID: 440718 [Multi-domain]  Cd Length: 264  Bit Score: 105.55  E-value: 3.40e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVN--FSIG---DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI--HTEYGslRT 362
Cdd:COG1101     2 LELKNLSktFNPGtvnEKRALDGLNLTIEEGDFVTVIGSNGAGKSTLLNAIAGSLPPDSGSILIDGKDVtkLPEYK--RA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 363 R-IGMVPQD-------DvvhrqLTV--NQALgyaAELR-----LPPDTSKADRAQVVAQV--LDeLGLTKHGDTRVDKLS 425
Cdd:COG1101    80 KyIGRVFQDpmmgtapS-----MTIeeNLAL---AYRRgkrrgLRRGLTKKRRELFRELLatLG-LGLENRLDTKVGLLS 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 426 GGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTHSLTY-LDVCDQVLLM 495
Cdd:COG1101   151 GGQRQALSLLMATLTKPKLLLLDEHTAALDPKTAALVLELTEKIVEENNLtTLMVTHNMEQaLDYGNRLIMM 222
anch_rpt_ABC TIGR03771
anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ...
 310-530 4.61e-25

anchored repeat-type ABC transporter, ATP-binding subunit; This protein family is the ATP-binding cassette subunit of binding protein-dependent ABC transporter complex that strictly co-occurs with TIGR03769. TIGRFAMs model TIGR03769 describes a protein domain that occurs singly or as one of up to three repeats in proteins of a number of Actinobacteria, including Propionibacterium acnes KPA171202. The TIGR03769 domain occurs both in an adjacent gene for the substrate-binding protein and in additional (often nearby) proteins, often with LPXTG-like sortase recognition signals. Homologous ATP-binding subunits outside the scope of this family include manganese transporter MntA in Synechocystis sp. PCC 6803 and chelated iron transporter subunits. The function of this transporter complex is unknown. [Transport and binding proteins, Unknown substrate]


Pssm-ID: 163483 [Multi-domain]  Cd Length: 223  Bit Score: 104.16  E-value: 4.61e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 310 LTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihTEYGSLRTRIGMVPQD---------DVvhRQLTVN 380
Cdd:TIGR03771   1 LSADKGELLGLLGPNGAGKTTLLRAILGLIPPAKGTVKVAG----ASPGKGWRHIGYVPQRhefawdfpiSV--AHTVMS 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGYAAELRLPpdtSKADRAqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDL 460
Cdd:TIGR03771  75 GRTGHIGWLRRP---CVADFA-AVRDALRRVGLTELADRPVGELSGGQRQRVLVARALATRPSVLLLDEPFTGLDMPTQE 150

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 461 QVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMapGGKTAYLGPPDQIGGAmgtTNWAQIFAKVGADP 530
Cdd:TIGR03771 151 LLTELFIELAGAGTAILMTTHDLAQaMATCDRVVLL--NGRVIADGTPQQLQDP---APWMTTFGVSDSSP 216
PRK10895 PRK10895
lipopolysaccharide ABC transporter ATP-binding protein; Provisional
 302-510 1.16e-24

lipopolysaccharide ABC transporter ATP-binding protein; Provisional


Pssm-ID: 182817 [Multi-domain]  Cd Length: 241  Bit Score: 103.43  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR--IGMVPQDDVVHRQLTV 379
Cdd:PRK10895   16 RRVVEDVSLTVNSGEIVGLLGPNGAGKTTTFYMVVGIVPRDAGNIIIDDEDISLLPLHARARrgIGYLPQEASIFRRLSV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAELRlpPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:PRK10895   96 YDNLMAVLQIR--DDLSAEQREDRANELMEEFHIEHLRDSMGQSLSGGERRRVEIARALAANPKFILLDEPFAGVDPISV 173

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 460 LQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:PRK10895  174 IDIKRIIEHLRDSGLGVLITDHNVrETLAVCERAYIVSQGHLIAH-GTPTEI 224
nikE PRK10419
nickel ABC transporter ATP-binding protein NikE;
302-499 1.25e-24

nickel ABC transporter ATP-binding protein NikE;


Pssm-ID: 236689 [Multi-domain]  Cd Length: 268  Bit Score: 104.38  E-value: 1.25e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSLRTRIGMVPQDDV--VHR 375
Cdd:PRK10419   25 QTVLNNVSLSLKSGETVALLGRSGCGKSTLARLLVGLESPSQGNVSWRGEPLAKlnraQRKAFRRDIQMVFQDSIsaVNP 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 376 QLTVNQALgyAAELRLPPDTSKADRAQVVAQVLDELGLT-KHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:PRK10419  105 RKTVREII--REPLRHLLSLDKAERLARASEMLRAVDLDdSVLDKRPPQLSGGQLQRVCLARALAVEPKLLILDEAVSNL 182

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1184609190 455 DPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMAPGG 499
Cdd:PRK10419  183 DLVLQAGVIRLLKKLqQQFGTACLFITHDLRLVErFCQRVMVMDNGQ 229
cbiO PRK13636
cobalt transporter ATP-binding subunit; Provisional
 290-498 1.54e-24

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184196 [Multi-domain]  Cd Length: 283  Bit Score: 104.54  E-value: 1.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGD-KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYG--SLRTRIG 365
Cdd:PRK13636    6 LKVEELNYNYSDgTHALKGININIKKGEVTAILGGNGAGKSTLFQNLNGILKPSSGRILFDGKPIdYSRKGlmKLRESVG 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDvvHRQL---TVNQALGYAA-ELRLPPDTSKadraQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTG 441
Cdd:PRK13636   86 MVFQDP--DNQLfsaSVYQDVSFGAvNLKLPEDEVR----KRVDNALKRTGIEHLKDKPTHCLSFGQKKRVAIAGVLVME 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 442 PSLLILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYLDV-CDQVLLMAPG 498
Cdd:PRK13636  160 PKVLVLDEPTAGLDPMGVSEIMKLLVEMQKElGLTIIIATHDIDIVPLyCDNVFVMKEG 218
urea_trans_UrtE TIGR03410
urea ABC transporter, ATP-binding protein UrtE; Members of this protein family are ABC ...
 290-502 1.72e-24

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


Pssm-ID: 274567 [Multi-domain]  Cd Length: 230  Bit Score: 102.60  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR--IGMV 367
Cdd:TIGR03410   1 LEVSNLNVYYGQSHILRGVSLEVPKGEVTCVLGRNGVGKTTLLKTLMGLLPVKSGSIRLDGEDITKLPPHERARagIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDVVHRQLTV--NQALGYAAElrlpPDTSKA--DRAQVVAQVLDELGLTKHGDtrvdkLSGGQRKRASVALELLTGPS 443
Cdd:TIGR03410  81 PQGREIFPRLTVeeNLLTGLAAL----PRRSRKipDEIYELFPVLKEMLGRRGGD-----LSGGQQQQLAIARALVTRPK 151

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTHSLTY-LDVCDQVLLMAPGGKTA 502
Cdd:TIGR03410 152 LLLLDEPTEGIQPSIIKDIGRVIRRLRAEGGMaILLVEQYLDFaRELADRYYVMERGRVVA 212
potA TIGR01187
spermidine/putrescine ABC transporter ATP-binding subunit; This model describes spermidine ...
 320-510 1.73e-24

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


Pssm-ID: 162242 [Multi-domain]  Cd Length: 325  Bit Score: 105.27  E-value: 1.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 320 IIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTRIGMVPQDDVVHRQLTVNQALGYAAELRlppdtsKAD 399
Cdd:TIGR01187   1 LLGPSGCGKTTLLRLLAGFEQPDSGSIMLDGEDV-TNVPPHLRHINMVFQSYALFPHMTVEENVAFGLKMR------KVP 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 400 RAQVVAQVLDELG---LTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPAL----DLQVMTMLRQLada 472
Cdd:TIGR01187  74 RAEIKPRVLEALRlvqLEEFADRKPHQLSGGQQQRVALARALVFKPKILLLDEPLSALDKKLrdqmQLELKTIQEQL--- 150

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1184609190 473 GRVVLVVTHSLT-YLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR01187 151 GITFVFVTHDQEeAMTMSDRIAIMR-KGKIAQIGTPEEI 188
tauB PRK11248
taurine ABC transporter ATP-binding subunit;
290-498 1.89e-24

taurine ABC transporter ATP-binding subunit;


Pssm-ID: 183056 [Multi-domain]  Cd Length: 255  Bit Score: 103.24  E-value: 1.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRtriGMVPQ 369
Cdd:PRK11248    2 LQISHLYADYGGKPALEDINLTLESGELLVVLGPSGCGKTTLLNLIAGFVPYQHGSITLDGKPV-EGPGAER---GVVFQ 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:PRK11248   78 NEGLLPWRNVQDNVAFGLQLA---GVEKMQRLEIAHQMLKKVGLEGAEKRYIWQLSGGQRQRVGIARALAANPQLLLLDE 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 450 PTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:PRK11248  155 PFGALDAFTREQMQTLLLKLwQETGKQVLLITHDIeEAVFMATELVLLSPG 205
ABC_Carb_Monos_I cd03216
First domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 290-495 1.94e-24

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: 100.58  E-value: 1.94e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGH--NIHTEYGSLRTRIGMV 367
Cdd:cd03216     1 LELRGITKRFGGVKALDGVSLSVRRGEVHALLGENGAGKSTLMKILSGLYKPDSGEILVDGKevSFASPRDARRAGIAMV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQddvvhrqltvnqalgyaaelrlppdtskadraqvvaqvldelgltkhgdtrvdkLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03216    81 YQ------------------------------------------------------LSVGERQMVEIARALARNARLLIL 106

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLM 495
Cdd:cd03216   107 DEPTAALTPAEVERLFKVIRRLRAQGVAVIFISHRLdEVFEIADRVTVL 155
cbiO TIGR01166
cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of ...
 300-481 2.05e-24

cobalt transport protein ATP-binding subunit; This model describes the ATP binding subunit of the multisubunit cobalt transporter in bacteria and its equivalents in archaea. The model is restricted to ATP subunit that is a part of the cobalt transporter, which belongs to the ABC transporter superfamily (ATP Binding Cassette). The model excludes ATP binding subunit that are associated with other transporters belonging to ABC transporter superfamily. This superfamily includes two groups, one which catalyze the uptake of small molecules, including ions from the external milieu and the other group which is engaged in the efflux of small molecular weight compounds and ions from within the cell. Energy derived from the hydrolysis of ATP drive the both the process of uptake and efflux. [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 130234 [Multi-domain]  Cd Length: 190  Bit Score: 101.35  E-value: 2.05e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSL---RTRIGMVPQDDvvHRQ 376
Cdd:TIGR01166   3 GGPEVLKGLNFAAERGEVLALLGANGAGKSTLLLHLNGLLRPQSGAVLIDGEPLDYSRKGLlerRQRVGLVFQDP--DDQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 377 L---TVNQALGYAA-ELRLPPDTSKAdraqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:TIGR01166  81 LfaaDVDQDVAFGPlNLGLSEAEVER----RVREALTAVGASGLRERPTHCLSGGEKKRVAIAGAVAMRPDVLLLDEPTA 156

                         170       180
                  ....*....|....*....|....*....
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:TIGR01166 157 GLDPAGREQMLAILRRLRAEGMTVVISTH 185
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 305-558 2.16e-24

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 107.81  E-value: 2.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGH--NIHTEYGSLRTRIGMVPQddvvHRQL----T 378
Cdd:COG3845    21 NDDVSLTVRPGEIHALLGENGAGKSTLMKILYGLYQPDSGEILIDGKpvRIRSPRDAIALGIGMVHQ----HFMLvpnlT 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 V--NQALGYAAELRLPPDTSKAdrAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRasvaLE----LLTGPSLLILDEPTS 452
Cdd:COG3845    97 VaeNIVLGLEPTKGGRLDRKAA--RARIRELSERYGLDVDPDAKVEDLSVGEQQR----VEilkaLYRGARILILDEPTA 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTHSLT-YLDVCDQVLLMApGGKTAylgppdqiggamGTtnwaqifakvgADPD 531
Cdd:COG3845   171 VLTPQEADELFEILRRLAAEGKSIIFITHKLReVMAIADRVTVLR-RGKVV------------GT-----------VDTA 226

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1184609190 532 EANRRFLAQ----NKPPPPVESAPADLGAPA 558
Cdd:COG3845   227 ETSEEELAElmvgREVLLRVEKAPAEPGEVV 257
ArtP COG4161
ABC-type arginine transport system, ATPase component [Amino acid transport and metabolism];
289-498 2.53e-24

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


Pssm-ID: 443326 [Multi-domain]  Cd Length: 242  Bit Score: 102.78  E-value: 2.53e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-------HTEYGSLR 361
Cdd:COG4161     2 SIQLKNINCFYGSHQALFDINLECPSGETLVLLGPSGAGKSSLLRVLNLLETPDSGQLNIAGHQFdfsqkpsEKAIRLLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQDDVVHRQLTVNQALgYAAELRLPPDTSKADRAQVvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTG 441
Cdd:COG4161    82 QKVGMVFQQYNLWPHLTVMENL-IEAPCKVLGLSKEQAREKA-MKLLARLRLTDKADRFPLHLSGGQQQRVAIARALMME 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 442 PSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:COG4161   160 PQVLLFDEPTAALDPEITAQVVEIIRELSQTGITQVIVTHEVEFArKVASQVVYMEKG 217
PRK11264 PRK11264
putative amino-acid ABC transporter ATP-binding protein YecC; Provisional
 290-498 2.89e-24

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


Pssm-ID: 183063 [Multi-domain]  Cd Length: 250  Bit Score: 102.52  E-value: 2.89e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYG---------SL 360
Cdd:PRK11264    4 IEVKNLVKKFHGQTVLHGIDLEVKPGEVVAIIGPSGSGKTTLLRCINLLEQPEAGTIRVGDITIDTARSlsqqkglirQL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 361 RTRIGMVPQDDVV--HRQLTVNQALGyaaelrlPPDTSKADRAQVVA---QVLDELGLTKHGDTRVDKLSGGQRKRASVA 435
Cdd:PRK11264   84 RQHVGFVFQNFNLfpHRTVLENIIEG-------PVIVKGEPKEEATArarELLAKVGLAGKETSYPRRLSGGQQQRVAIA 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 436 LELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK11264  157 RALAMRPEVILFDEPTSALDPELVGEVLNTIRQLAQEKRTMVIVTHEMSFArDVADRAIFMDQG 220
PRK11160 PRK11160
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 281-498 3.81e-24

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


Pssm-ID: 236865 [Multi-domain]  Cd Length: 574  Bit Score: 107.60  E-value: 3.81e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 281 QEVAARTGGLEVREVNFSIGDKNL--LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEY- 357
Cdd:PRK11160  330 STAAADQVSLTLNNVSFTYPDQPQpvLKGLSLQIKAGEKVALLGRTGCGKSTLLQLLTRAWDPQQGEILLNGQPI-ADYs 408

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 358 -GSLRTRIGMVPQDdvVHRqltvnqalgYAAELR--LPPDTSKADRAQVVaQVLDELGLTKH--GDTRVD--------KL 424
Cdd:PRK11160  409 eAALRQAISVVSQR--VHL---------FSATLRdnLLLAAPNASDEALI-EVLQQVGLEKLleDDKGLNawlgeggrQL 476

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 425 SGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK11160  477 SGGEQRRLGIARALLHDAPLLLLDEPTEGLDAETERQILELLAEHA-QNKTVLMITHRLTGLEQFDRICVMDNG 549
ABC_CcmA_heme_exporter cd03231
Cytochrome c biogenesis ATP-binding export protein; CcmA, the ATP-binding component of the ...
 290-481 5.27e-24

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: 100.65  E-value: 5.27e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:cd03231     1 LEADELTCERDGRALFSGLSFTLAAGEALQVTGPNGSGKTTLLRILAGLSPPLAGRVLLNGGPLDFQRDSIARGLLYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELrlppdtskADRAQVVaQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03231    81 APGIKTTLSVLENLRFWHAD--------HSDEQVE-EALARVGLNGFEDRPVAQLSAGQQRRVALARLLLSGRPLWILDE 151

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:cd03231   152 PTTALDKAGVARFAEAMAGHCARGGMVVLTTH 183
cbiO PRK13635
energy-coupling factor ABC transporter ATP-binding protein;
290-510 9.55e-24

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184195 [Multi-domain]  Cd Length: 279  Bit Score: 102.02  E-value: 9.55e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGD--KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIGM 366
Cdd:PRK13635    6 IRVEHISFRYPDaaTYALKDVSFSVYEGEWVAIVGHNGSGKSTLAKLLNGLLLPEAGTITVGGMVLSEEtVWDVRRQVGM 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQD-DVVHRQLTVNQALGYAAELRLPPDTSKADRaqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:PRK13635   86 VFQNpDNQFVGATVQDDVAFGLENIGVPREEMVER---VDQALRQVGMEDFLNREPHRLSGGQKQRVAIAGVLALQPDII 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTHSLTYLDVCDQVLLMAPGGKTAyLGPPDQI 510
Cdd:PRK13635  163 ILDEATSMLDPRGRREVLETVRQLKEQKGItVLSITHDLDEAAQADRVIVMNKGEILE-EGTPEEI 227
ccmA TIGR01189
heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein ...
 290-481 1.18e-23

heme ABC exporter, ATP-binding protein CcmA; This model describes the cyt c biogenesis protein encoded by ccmA in bacteria. An exception is, an arabidopsis protein. Quite likely this is encoded by an organelle. Bacterial c-type cytocromes are located on the periplasmic side of the cytoplasmic membrane. Several gene products encoded in a locus designated as 'ccm' are implicated in the transport and assembly of the functional cytochrome C. This cluster includes genes: ccmA;B;C;D;E;F;G and H. The posttranslational pathway includes the transport of heme moiety, the secretion of the apoprotein and the covalent attachment of the heme with the apoprotein. The proteins ccmA and B represent an ABC transporter; ccmC and D participate in heme transfer to ccmE, which function as a periplasmic heme chaperone. The presence of ccmF, G and H is suggested to be obligatory for the final functional assembly of cytochrome c. [Protein fate, Protein and peptide secretion and trafficking, Transport and binding proteins, Other]


Pssm-ID: 273491 [Multi-domain]  Cd Length: 198  Bit Score: 99.36  E-value: 1.18e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:TIGR01189   1 LAARNLACSRGERMLFEGLSFTLNAGEALQVTGPNGIGKTTLLRILAGLLRPDSGEVRWNGTPLAEQRDEPHENILYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAelrlpPDTSKADRAqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:TIGR01189  81 LPGLKPELSALENLHFWA-----AIHGGAQRT--IEDALAAVGLTGFEDLPAAQLSAGQQRRLALARLWLSRRPLWILDE 153

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:TIGR01189 154 PTTALDKAGVALLAGLLRAHLARGGIVLLTTH 185
fbpC PRK11432
ferric ABC transporter ATP-binding protein;
290-510 1.84e-23

ferric ABC transporter ATP-binding protein;


Pssm-ID: 183133 [Multi-domain]  Cd Length: 351  Bit Score: 102.88  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEyGSLRTR-IGMVP 368
Cdd:PRK11432    7 VVLKNITKRFGSNTVIDNLNLTIKQGTMVTLLGPSGCGKTTVLRLVAGLEKPTEGQIFIDGEDV-TH-RSIQQRdICMVF 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 QDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILD 448
Cdd:PRK11432   85 QSYALFPHMSLGENVGYGLKML---GVPKEERKQRVKEALELVDLAGFEDRYVDQISGGQQQRVALARALILKPKVLLFD 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 449 EPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLT-YLDVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:PRK11432  162 EPLSNLDANLRRSMREKIRELQQQfNITSLYVTHDQSeAFAVSDTVIVMNK-GKIMQIGSPQEL 224
ABC_MTABC3_MDL1_MDL2 cd03249
ATP-binding cassette domain of a mitochondrial protein MTABC3 and related proteins; MTABC3 ...
 291-499 2.24e-23

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: 99.92  E-value: 2.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSI---GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGM 366
Cdd:cd03249     2 EFKNVSFRYpsrPDVPILKGLSLTIPPGKTVALVGSSGCGKSTVVSLLERFYDPTSGEILLDGVDIRDlNLRWLRSQIGL 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHrQLTVNQALGYAAElrlPPDTSKADRAQVVAQVLDEL-GLTKHGDTRV----DKLSGGQRKRASVALELLTG 441
Cdd:cd03249    82 VSQEPVLF-DGTIAENIRYGKP---DATDEEVEEAAKKANIHDFImSLPDGYDTLVgergSQLSGGQKQRIAIARALLRN 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 442 PSLLILDEPTSGLDPALDLQVMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPGG 499
Cdd:cd03249   158 PKILLLDEATSALDAESEKLVQEALDRAM-KGRTTIVIAHRLSTIRNADLIAVLQNGQ 214
cbiO PRK13632
cobalt transporter ATP-binding subunit; Provisional
 291-510 2.34e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237452 [Multi-domain]  Cd Length: 271  Bit Score: 100.45  E-value: 2.34e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGD--KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIGMV 367
Cdd:PRK13632    9 KVENVSFSYPNseNNALKNVSFEINEGEYVAILGHNGSGKSTISKILTGLLKPQSGEIKIDGITISKEnLKEIRKKIGII 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQD-DvvhrqltvNQALGYAAE---------LRLPPDTSKAdraqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALE 437
Cdd:PRK13632   89 FQNpD--------NQFIGATVEddiafglenKKVPPKKMKD----IIDDLAKKVGMEDYLDKEPQNLSGGQKQRVAIASV 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAG-RVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK13632  157 LALNPEIIIFDESTSMLDPKGKREIKKIMVDLRKTRkKTLISITHDMDEAILADKVIVFS-EGKLIAQGKPKEI 229
PRK10908 PRK10908
cell division ATP-binding protein FtsE;
299-484 2.91e-23

cell division ATP-binding protein FtsE;


Pssm-ID: 182829 [Multi-domain]  Cd Length: 222  Bit Score: 99.18  E-value: 2.91e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 299 IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEYGSLRTRIGMVPQDdvvH 374
Cdd:PRK10908   12 LGGRQALQGVTFHMRPGEMAFLTGHSGAGKSTLLKLICGIERPSAGKIWFSGHDItrlkNREVPFLRRQIGMIFQD---H 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:PRK10908   89 HLLMDRTVYDNVAIPLIIAGASGDDIRRRVSAALDKVGLLDKAKNFPIQLSGGEQQRVGIARAVVNKPAVLLADEPTGNL 168

                         170       180       190
                  ....*....|....*....|....*....|
gi 1184609190 455 DPALDLQVMTMLRQLADAGRVVLVVTHSLT 484
Cdd:PRK10908  169 DDALSEGILRLFEEFNRVGVTVLMATHDIG 198
cbiO PRK13648
cobalt transporter ATP-binding subunit; Provisional
 290-510 3.14e-23

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184207 [Multi-domain]  Cd Length: 269  Bit Score: 100.21  E-value: 3.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI-GDKNL-LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIGM 366
Cdd:PRK13648    8 IVFKNVSFQYqSDASFtLKDVSFNIPKGQWTSIVGHNGSGKSTIAKLMIGIEKVKSGEIFYNNQAITDDnFEKLRKHIGI 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 V---PQDDVVHRQLTVNQALGYAAELrLPPDtskaDRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:PRK13648   88 VfqnPDNQFVGSIVKYDVAFGLENHA-VPYD----EMHRRVSEALKQVDMLERADYEPNALSGGQKQRVAIAGVLALNPS 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLV-VTHSLTYLDVCDQVLLMAPGgkTAY-LGPPDQI 510
Cdd:PRK13648  163 VIILDEATSMLDPDARQNLLDLVRKVKSEHNITIIsITHDLSEAMEADHVIVMNKG--TVYkEGTPTEI 229
artP PRK11124
arginine transporter ATP-binding subunit; Provisional
 290-481 4.14e-23

arginine transporter ATP-binding subunit; Provisional


Pssm-ID: 182980 [Multi-domain]  Cd Length: 242  Bit Score: 98.93  E-value: 4.14e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGH--NIHTEYG-----SLRT 362
Cdd:PRK11124    3 IQLNGINCFYGAHQALFDITLDCPQGETLVLLGPSGAGKSSLLRVLNLLEMPRSGTLNIAGNhfDFSKTPSdkairELRR 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 363 RIGMVPQDDVVHRQLTVNQALGYAaelrlPPDTSKADRAQVVAQ---VLDELGLTKHGDTRVDKLSGGQRKRASVALELL 439
Cdd:PRK11124   83 NVGMVFQQYNLWPHLTVQQNLIEA-----PCRVLGLSKDQALARaekLLERLRLKPYADRFPLHLSGGQQQRVAIARALM 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:PRK11124  158 MEPQVLLFDEPTAALDPEITAQIVSIIRELAETGITQVIVTH 199
PRK10851 PRK10851
sulfate/thiosulfate ABC transporter ATP-binding protein CysA;
290-510 4.87e-23

sulfate/thiosulfate ABC transporter ATP-binding protein CysA;


Pssm-ID: 182778 [Multi-domain]  Cd Length: 353  Bit Score: 101.70  E-value: 4.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRtRIGMVPQ 369
Cdd:PRK10851    3 IEIANIKKSFGRTQVLNDISLDIPSGQMVALLGPSGSGKTTLLRIIAGLEHQTSGHIRFHGTDVSRLHARDR-KVGFVFQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTV--NQALGyaaeLRLPPDTSKADRA---QVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK10851   82 HYALFRHMTVfdNIAFG----LTVLPRRERPNAAaikAKVTQLLEMVQLAHLADRYPAQLSGGQKQRVALARALAVEPQI 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLADAGRVVLV-VTHSLT-YLDVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:PRK10851  158 LLLDEPFGALDAQVRKELRRWLRQLHEELKFTSVfVTHDQEeAMEVADRVVVMSQ-GNIEQAGTPDQV 224
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 305-498 5.81e-23

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 105.87  E-value: 5.81e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTVNQALG 384
Cdd:TIGR01257  946 VDRLNITFYENQITAFLGHNGAGKTTTLSILTGLLPPTSGTVLVGGKDIETNLDAVRQSLGMCPQHNILFHHLTVAEHIL 1025

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  385 YAAELRlppdTSKADRAQV-VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:TIGR01257 1026 FYAQLK----GRSWEEAQLeMEAMLEDTGLHHKRNEEAQDLSGGMQRKLSVAIAFVGDAKVVVLDEPTSGVDPYSRRSIW 1101

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1184609190  464 TMLRQLAdAGRVVLVVTHSLTYLDVC-DQVLLMAPG 498
Cdd:TIGR01257 1102 DLLLKYR-SGRTIIMSTHHMDEADLLgDRIAIISQG 1136
CydC TIGR02868
thiol reductant ABC exporter, CydC subunit; The gene pair cydCD encodes an ABC-family ...
 289-483 5.95e-23

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: 103.59  E-value: 5.95e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSI-GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS-LRTRIGM 366
Cdd:TIGR02868 334 TLELRDLSAGYpGAPPVLDGVSLDLPPGERVAILGPSGSGKSTLLATLAGLLDPLQGEVTLDGVPVSSLDQDeVRRRVSV 413

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQlTVNQALGYAAelrlpPDTSKADRAQVVAQV--LDELGLTKHG-DTRVD----KLSGGQRKRASVALELL 439
Cdd:TIGR02868 414 CAQDAHLFDT-TVRENLRLAR-----PDATDEELWAALERVglADWLRALPDGlDTVLGeggaRLSGGERQRLALARALL 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQlADAGRVVLVVTHSL 483
Cdd:TIGR02868 488 ADAPILLLDEPTEHLDAETADELLEDLLA-ALSGRTVVLITHHL 530
PRK13539 PRK13539
cytochrome c biogenesis protein CcmA; Provisional
 290-497 6.22e-23

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 237421 [Multi-domain]  Cd Length: 207  Bit Score: 97.64  E-value: 6.22e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteYGSLRTRIGMVPQ 369
Cdd:PRK13539    3 LEGEDLACVRGGRVLFSGLSFTLAAGEALVLTGPNGSGKTTLLRLIAGLLPPAAGTIKLDGGDID--DPDVAEACHYLGH 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPDTSkadraqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:PRK13539   81 RNAMKPALTVAENLEFWAAFLGGEELD-------IAAALEAVGLAPLAHLPFGYLSAGQKRRVALARLLVSNRPIWILDE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCdQVLLMAP 497
Cdd:PRK13539  154 PTAALDAAAVALFAELIRAHLAQGGIVIAATHIPLGLPGA-RELDLGP 200
modC_ABC TIGR02142
molybdenum ABC transporter, ATP-binding protein; This model represents the ATP-binding ...
 308-510 7.17e-23

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: 100.96  E-value: 7.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSL-----RTRIGMVPQDDVVHRQLTVNQA 382
Cdd:TIGR02142  16 ADFTLPGQGVTAIFGRSGSGKTTLIRLIAGLTRPDEGEIVLNGRTLFDSRKGIflppeKRRIGYVFQEARLFPHLSVRGN 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 383 LGYAAELRLPPDTSKADraqvvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQV 462
Cdd:TIGR02142  96 LRYGMKRARPSERRISF-----ERVIELLGIGHLLGRLPGRLSGGEKQRVAIGRALLSSPRLLLMDEPLAALDDPRKYEI 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 463 MTMLRQLADAGRV-VLVVTHSLT-YLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR02142 171 LPYLERLHAEFGIpILYVSHSLQeVLRLADRVVVLE-DGRVAAAGPIAEV 219
PRK14239 PRK14239
phosphate transporter ATP-binding protein; Provisional
 290-483 7.50e-23

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184585 [Multi-domain]  Cd Length: 252  Bit Score: 98.69  E-value: 7.50e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLI--AGYATP---TTGSVTFEGHNIH---TEYGSLR 361
Cdd:PRK14239    6 LQVSDLSVYYNKKKALNSVSLDFYPNEITALIGPSGSGKSTLLRSInrMNDLNPevtITGSIVYNGHNIYsprTDTVDLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQddvvhrQ-----LTVNQALGYAAELRLPPDTSKADRA----QVVAQVLDELGLTKHgDTRVDkLSGGQRKRA 432
Cdd:PRK14239   86 KEIGMVFQ------QpnpfpMSIYENVVYGLRLKGIKDKQVLDEAveksLKGASIWDEVKDRLH-DSALG-LSGGQQQRV 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 433 SVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAgRVVLVVTHSL 483
Cdd:PRK14239  158 CIARVLATSPKIILLDEPTSALDPISAGKIEETLLGLKDD-YTMLLVTRSM 207
metN PRK11153
DL-methionine transporter ATP-binding subunit; Provisional
 305-498 1.24e-22

DL-methionine transporter ATP-binding subunit; Provisional


Pssm-ID: 236863 [Multi-domain]  Cd Length: 343  Bit Score: 100.26  E-value: 1.24e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSLRTRIGMVPQddvvHRQL--- 377
Cdd:PRK11153   21 LNNVSLHIPAGEIFGVIGASGAGKSTLIRCINLLERPTSGRVLVDGQDLTAlsekELRKARRQIGMIFQ----HFNLlss 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 -TV--NQALgyaaELRLPpDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:PRK11153   97 rTVfdNVAL----PLELA-GTPKAEIKARVTELLELVGLSDKADRYPAQLSGGQKQRVAIARALASNPKVLLCDEATSAL 171

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1184609190 455 DPALDLQVMTMLRQL-ADAGRVVLVVTHSltyLDV----CDQVLLMAPG 498
Cdd:PRK11153  172 DPATTRSILELLKDInRELGLTIVLITHE---MDVvkriCDRVAVIDAG 217
ABC_OpuCA_Osmoprotection cd03295
ATP-binding cassette domain of the osmoprotectant transporter; OpuCA is a the ATP binding ...
 290-510 1.40e-22

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: 97.37  E-value: 1.40e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGD-KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYG--SLRTRIGM 366
Cdd:cd03295     1 IEFENVTKRYGGgKKAVNNLNLEIAKGEFLVLIGPSGSGKTTTMKMINRLIEPTSGEIFIDGEDI-REQDpvELRRKIGY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQALGyaaelrLPPDTSKADRAQVVAQVLDELGL-----TKHGDTRVDKLSGGQRKRASVALELLTG 441
Cdd:cd03295    80 VIQQIGLFPHMTVEENIA------LVPKLLKWPKEKIRERADELLALvgldpAEFADRYPHELSGGQQQRVGVARALAAD 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 442 PSLLILDEPTSGLDP----ALDLQVMTMLRQLadaGRVVLVVTHSL-TYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:cd03295   154 PPLLLMDEPFGALDPitrdQLQEEFKRLQQEL---GKTIVFVTHDIdEAFRLADRIAIMK-NGEIVQVGTPDEI 223
ABCC_MRP_domain2 cd03244
ATP-binding cassette domain 2 of multidrug resistance-associated protein; The ABC subfamily C ...
 288-498 1.49e-22

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


Pssm-ID: 213211 [Multi-domain]  Cd Length: 221  Bit Score: 96.79  E-value: 1.49e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSIGD--KNLLERVSLTARPGTLTAIIGGSGAGKTTLS----RLIagyaTPTTGSVTFEGHNIhTEYG--S 359
Cdd:cd03244     1 GDIEFKNVSLRYRPnlPPVLKNISFSIKPGEKVGIVGRTGSGKSSLLlalfRLV----ELSSGSILIDGVDI-SKIGlhD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQDDVVhrqltvnqalgYAAELR--LPPDTSKADRAqvVAQVLDELGLTKH-------GDTRV----DKLSG 426
Cdd:cd03244    76 LRSRISIIPQDPVL-----------FSGTIRsnLDPFGEYSDEE--LWQALERVGLKEFveslpggLDTVVeeggENLSV 142

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 427 GQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQlADAGRVVLVVTHSL-TYLDvCDQVLLMAPG 498
Cdd:cd03244   143 GQRQLLCLARALLRKSKILVLDEATASVDPETDALIQKTIRE-AFKDCTVLTIAHRLdTIID-SDRILVLDKG 213
ABCC_TAP cd03248
ATP-binding cassette domain of the Transporter Associated with Antigen Processing, subfamily C; ...
 288-498 1.61e-22

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: 96.77  E-value: 1.61e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSI---GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTR 363
Cdd:cd03248    10 GIVKFQNVTFAYptrPDTLVLQDVSFTLHPGEVTALVGPSGSGKSTVVALLENFYQPQGGQVLLDGKPISQyEHKYLHSK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQDDVVH-RQLTVNQALGYAAElrlppDTSKADRAQVVAQVLDELGLTKHG-DTRVDK----LSGGQRKRASVALE 437
Cdd:cd03248    90 VSLVGQEPVLFaRSLQDNIAYGLQSC-----SFECVKEAAQKAHAHSFISELASGyDTEVGEkgsqLSGGQKQRVAIARA 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQlADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03248   165 LIRNPQVLILDEATSALDAESEQQVQQALYD-WPERRTVLVIAHRLSTVERADQILVLDGG 224
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 308-495 1.67e-22

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 102.46  E-value: 1.67e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPG-TLtAIIGGSGAGKTTLS----RLIagyatPTTGSVTFEGHNIHT----EYGSLRTRIGMVPQDdvv--hrq 376
Cdd:COG4172   305 VSLTLRRGeTL-GLVGESGSGKSTLGlallRLI-----PSEGEIRFDGQDLDGlsrrALRPLRRRMQVVFQDpfgslspr 378

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 377 LTVNQALgyaAE-LRL-PPDTSKADRAQVVAQVLDELGLTKhgDTRvDK----LSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:COG4172   379 MTVGQII---AEgLRVhGPGLSAAERRARVAEALEEVGLDP--AAR-HRypheFSGGQRQRIAIARALILEPKLLVLDEP 452

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 451 TSGLDPALDLQVMTMLRQLADagrvvlvvTHSLTYL----D------VCDQVLLM 495
Cdd:COG4172   453 TSALDVSVQAQILDLLRDLQR--------EHGLAYLfishDlavvraLAHRVMVM 499
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 201-273 1.74e-22

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 92.56  E-value: 1.74e-22
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 201 GAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVFT 273
Cdd:cd22737    21 QAVRIGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTFVNGLRVDAALLHDGDVVTIGDIDFVFE 93
rim_protein TIGR01257
retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim ...
 305-498 2.04e-22

retinal-specific rim ABC transporter; This model describes the photoreceptor protein (rim protein) in eukaryotes. It is the member of ABC transporter superfamily. Rim protein is a membrane glycoprotein which is localized in the photoreceptor outer segment discs. Mutation/s in its genetic loci is implicated in the recessive Stargardt's disease. [Transport and binding proteins, Other]


Pssm-ID: 130324 [Multi-domain]  Cd Length: 2272  Bit Score: 103.94  E-value: 2.04e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTVNQALG 384
Cdd:TIGR01257 1955 VDRLCVGVRPGECFGLLGVNGAGKTTTFKMLTGDTTVTSGDATVAGKSILTNISDVHQNMGYCPQFDAIDDLLTGREHLY 2034

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  385 YAAELRLPPdtskADRAQVVAQ-VLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:TIGR01257 2035 LYARLRGVP----AEEIEKVANwSIQSLGLSLYADRLAGTYSGGNKRKLSTAIALIGCPPLVLLDEPTTGMDPQARRMLW 2110

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1184609190  464 TMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:TIGR01257 2111 NTIVSIIREGRAVVLTSHSMEECEaLCTRLAIMVKG 2146
ABC_FeS_Assembly cd03217
ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of ...
 290-508 2.48e-22

ABC-type transport system involved in Fe-S cluster assembly, ATPase component; Biosynthesis of iron-sulfur clusters (Fe-S) depends on multi-protein systems. The SUF system of E. coli and Erwinia chrysanthemi is important for Fe-S biogenesis under stressful conditions. The SUF system is made of six proteins: SufC is an atypical cytoplasmic ABC-ATPase, which forms a complex with SufB and SufD; SufA plays the role of a scaffold protein for assembly of iron-sulfur clusters and delivery to target proteins; SufS is a cysteine desulfurase which mobilizes the sulfur atom from cysteine and provides it to the cluster; SufE has no associated function yet.


Pssm-ID: 213184 [Multi-domain]  Cd Length: 200  Bit Score: 95.67  E-value: 2.48e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYA--TPTTGSVTFEGHNIHTEYGSLRTR--IG 365
Cdd:cd03217     1 LEIKDLHVSVGGKEILKGVNLTIKKGEVHALMGPNGSGKSTLAKTIMGHPkyEVTEGEILFKGEDITDLPPEERARlgIF 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQLTVNQALGYaaelrlppdtskadraqvvaqvLDElgltkhgdtrvdKLSGGQRKRASVALELLTGPSLL 445
Cdd:cd03217    81 LAFQYPPEIPGVKNADFLRY----------------------VNE------------GFSGGEKKRNEILQLLLLEPDLA 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 446 ILDEPTSGLD-PALDLQVMTmLRQLADAGRVVLVVTHSLTYLD--VCDQVLLMApGGKTAYLGPPD 508
Cdd:cd03217   127 ILDEPDSGLDiDALRLVAEV-INKLREEGKSVLIITHYQRLLDyiKPDRVHVLY-DGRIVKSGDKE 190
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 255-510 2.58e-22

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


Pssm-ID: 132313 [Multi-domain]  Cd Length: 520  Bit Score: 101.80  E-value: 2.58e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 255 AVLAE-GDVVTIGNVDLV---FTGGILVRRQEVAARTGG--LEVREVN---FSIgDKNLL---ERVSLTARPGTLTAIIG 322
Cdd:TIGR03269 239 AIWLEnGEIKEEGTPDEVvavFMEGVSEVEKECEVEVGEpiIKVRNVSkryISV-DRGVVkavDNVSLEVKEGEIFGIVG 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 323 GSGAGKTTLSRLIAGYATPTTGSVTF---EGHNIHTEYGSL-RTR----IGMVPQDDVVHRQLTVNQALGYAAELRLPPD 394
Cdd:TIGR03269 318 TSGAGKTTLSKIIAGVLEPTSGEVNVrvgDEWVDMTKPGPDgRGRakryIGILHQEYDLYPHRTVLDNLTEAIGLELPDE 397

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 395 TSKADRAQVVAQV-LDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM-TMLRQLADA 472
Cdd:TIGR03269 398 LARMKAVITLKMVgFDEEKAEEILDKYPDELSEGERHRVALAQVLIKEPRIVILDEPTGTMDPITKVDVThSILKAREEM 477

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1184609190 473 GRVVLVVTHSLTY-LDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR03269 478 EQTFIIVSHDMDFvLDVCDRAALMR-DGKIVKIGDPEEI 515
lolD PRK11629
lipoprotein-releasing ABC transporter ATP-binding protein LolD;
303-504 2.77e-22

lipoprotein-releasing ABC transporter ATP-binding protein LolD;


Pssm-ID: 183244 [Multi-domain]  Cd Length: 233  Bit Score: 96.42  E-value: 2.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 303 NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH----TEYGSLRTR-IGMVPQddvVHRQL 377
Cdd:PRK11629   23 DVLHNVSFSIGEGEMMAIVGSSGSGKSTLLHLLGGLDTPTSGDVIFNGQPMSklssAAKAELRNQkLGFIYQ---FHHLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQALGYAAelrLPPDTSKADRAQVVAQVLDEL---GLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:PRK11629  100 PDFTALENVA---MPLLIGKKKPAEINSRALEMLaavGLEHRANHRPSELSGGERQRVAIARALVNNPRLVLADEPTGNL 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 455 DPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYL 504
Cdd:PRK11629  177 DARNADSIFQLLGELnRLQGTAFLVVTHDLQLAKRMSRQLEMRDGRLTAEL 227
ABCF_EF-3 cd03221
ATP-binding cassette domain of elongation factor 3, subfamily F; Elongation factor 3 (EF-3) is ...
 290-499 2.88e-22

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: 93.67  E-value: 2.88e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFeghnihteygSLRTRIGMVPQ 369
Cdd:cd03221     1 IELENLSKTYGGKLLLKDISLTINPGDRIGLVGRNGAGKSTLLKLIAGELEPDEGIVTW----------GSTVKIGYFEQ 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 ddvvhrqltvnqalgyaaelrlppdtskadraqvvaqvldelgltkhgdtrvdkLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:cd03221    71 ------------------------------------------------------LSGGEKMRLALAKLLLENPNLLLLDE 96

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDpaldlqvMTMLRQLADA----GRVVLVVTHSLTYLD-VCDQVLLMAPGG 499
Cdd:cd03221    97 PTNHLD-------LESIEALEEAlkeyPGTVILVSHDRYFLDqVATKIIELEDGK 144
cbiO PRK13639
cobalt transporter ATP-binding subunit; Provisional
 290-510 3.06e-22

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184199 [Multi-domain]  Cd Length: 275  Bit Score: 97.46  E-value: 3.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL-LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSL---RTRIG 365
Cdd:PRK13639    2 LETRDLKYSYPDGTEaLKGINFKAEKGEMVALLGPNGAGKSTLFLHFNGILKPTSGEVLIKGEPIKYDKKSLlevRKTVG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQ--DDvvhrQL---TVNQALGYAA-ELRLPPDtskaDRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELL 439
Cdd:PRK13639   82 IVFQnpDD----QLfapTVEEDVAFGPlNLGLSKE----EVEKRVKEALKAVGMEGFENKPPHHLSGGQKKRVAIAGILA 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDV-CDQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK13639  154 MKPEIIVLDEPTSGLDPMGASQIMKLLYDLNKEGITIIISTHDVDLVPVyADKVYVMS-DGKIIKEGTPKEV 224
PRK10247 PRK10247
putative ABC transporter ATP-binding protein YbbL; Provisional
 290-499 4.66e-22

putative ABC transporter ATP-binding protein YbbL; Provisional


Pssm-ID: 182331 [Multi-domain]  Cd Length: 225  Bit Score: 95.55  E-value: 4.66e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYgslRTRIG 365
Cdd:PRK10247    8 LQLQNVGYLAGDAKILNNISFSLRAGEFKLITGPSGCGKSTLLKIVASLISPTSGTLLFEGEDISTlkpeIY---RQQVS 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQlTVNQALGYAAELRlppdtSKADRAQVVAQVLDELGLTKHG-DTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK10247   85 YCAQTPTLFGD-TVYDNLIFPWQIR-----NQQPDPAIFLDDLERFALPDTIlTKNIAELSGGEKQRISLIRNLQFMPKV 158

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTYLDVCDQVLLMAPGG 499
Cdd:PRK10247  159 LLLDEITSALDESNKHNVNEIIHRYVrEQNIAVLWVTHDKDEINHADKVITLQPHA 214
potG PRK11607
putrescine ABC transporter ATP-binding subunit PotG;
290-511 7.52e-22

putrescine ABC transporter ATP-binding subunit PotG;


Pssm-ID: 183226 [Multi-domain]  Cd Length: 377  Bit Score: 98.37  E-value: 7.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTrIGMVPQ 369
Cdd:PRK11607   20 LEIRNLTKSFDGQHAVDDVSLTIYKGEIFALLGASGCGKSTLLRMLAGFEQPTAGQIMLDGVDLSHVPPYQRP-INMMFQ 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYA-AELRLPpdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILD 448
Cdd:PRK11607   99 SYALFPHMTVEQNIAFGlKQDKLP----KAEIASRVNEMLGLVHMQEFAKRKPHQLSGGQRQRVALARSLAKRPKLLLLD 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 449 EPTSGLDPAL----DLQVMTMLRQLadaGRVVLVVTHsltyldvcDQVLLMAPGGKTAYL--GPPDQIG 511
Cdd:PRK11607  175 EPMGALDKKLrdrmQLEVVDILERV---GVTCVMVTH--------DQEEAMTMAGRIAIMnrGKFVQIG 232
ABC_Carb_Monos_II cd03215
Second domain of the ATP-binding cassette component of monosaccharide transport system; This ...
 290-498 7.54e-22

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: 93.65  E-value: 7.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVRevNFSIGDKnlLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH--TEYGSLRTRIGMV 367
Cdd:cd03215     5 LEVR--GLSVKGA--VRDVSFEVRAGEIVGIAGLVGNGQTELAEALFGLRPPASGEITLDGKPVTrrSPRDAIRAGIAYV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDDvvHRQLTVnqalgyaaeLRLPpdtskadraqvvaqVLDELGLTKHgdtrvdkLSGGQRKRASVALELLTGPSLLIL 447
Cdd:cd03215    81 PEDR--KREGLV---------LDLS--------------VAENIALSSL-------LSGGNQQKVVLARWLARDPRVLIL 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADAGRVVLVVThslTYLD----VCDQVLLMAPG 498
Cdd:cd03215   129 DEPTRGVDVGAKAEIYRLIRELADAGKAVLLIS---SELDellgLCDRILVMYEG 180
cbiO PRK13644
energy-coupling factor transporter ATPase;
305-510 7.68e-22

energy-coupling factor transporter ATPase;


Pssm-ID: 106587 [Multi-domain]  Cd Length: 274  Bit Score: 96.21  E-value: 7.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI--HTEYGSLRTRIGMV---PQDDVVHRqlTV 379
Cdd:PRK13644   18 LENINLVIKKGEYIGIIGKNGSGKSTLALHLNGLLRPQKGKVLVSGIDTgdFSKLQGIRKLVGIVfqnPETQFVGR--TV 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAE-LRLPPDT--SKADRAqvvaqvLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:PRK13644   96 EEDLAFGPEnLCLPPIEirKRVDRA------LAEIGLEKYRHRSPKTLSGGQGQCVALAGILTMEPECLIFDEVTSMLDP 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 457 ALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:PRK13644  170 DSGIAVLERIKKLHEKGKTIVYITHNLEELHDADRIIVMDR-GKIVLEGEPENV 222
type_I_sec_PrtD TIGR01842
type I secretion system ABC transporter, PrtD family; Type I protein secretion is a system in ...
 288-510 1.06e-21

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


Pssm-ID: 200134 [Multi-domain]  Cd Length: 544  Bit Score: 99.73  E-value: 1.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNF--SIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRI 364
Cdd:TIGR01842 315 GHLSVENVTIvpPGGKKPTLRGISFSLQAGEALAIIGPSGSGKSTLARLIVGIWPPTSGSVRLDGADLKQwDRETFGKHI 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQDdvvhRQL---TVNQALgyaAELRLPPDTSKADRAQVVAQVLDE-LGLTKHGDTRV----DKLSGGQRKRASVAL 436
Cdd:TIGR01842 395 GYLPQD----VELfpgTVAENI---ARFGENADPEKIIEAAKLAGVHELiLRLPDGYDTVIgpggATLSGGQRQRIALAR 467

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 437 ELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:TIGR01842 468 ALYGDPKLVVLDEPNSNLDEEGEQALANAIKALKARGITVVVITHRPSLLGCVDKILVLQDGRIARF-GERDEV 540
dppF PRK11308
dipeptide transporter ATP-binding subunit; Provisional
 308-525 1.40e-21

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 236898 [Multi-domain]  Cd Length: 327  Bit Score: 96.57  E-value: 1.40e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEYGSLRTRIGMVPQD---DVVHRQlTVN 380
Cdd:PRK11308   34 VSFTLERGKTLAVVGESGCGKSTLARLLTMIETPTGGELYYQGQDLlkadPEAQKLLRQKIQIVFQNpygSLNPRK-KVG 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALgyAAELRLPPDTSKADRAQVVAQVLDELGL-TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:PRK11308  113 QIL--EEPLLINTSLSAAERREKALAMMAKVGLrPEHYDRYPHMFSGGQRQRIAIARALMLDPDVVVADEPVSALDVSVQ 190

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 460 LQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMapggktaYLGPPDQIGGAmgttnwAQIFAK 525
Cdd:PRK11308  191 AQVLNLMMDLqQELGLSYVFISHDLSVVEhIADEVMVM-------YLGRCVEKGTK------EQIFNN 245
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
305-492 1.42e-21

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 98.94  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEG--HNIHTEYGSLRTRIGMVPQDDVVHRQLTV--N 380
Cdd:COG1129    20 LDGVSLELRPGEVHALLGENGAGKSTLMKILSGVYQPDSGEILLDGepVRFRSPRDAQAAGIAIIHQELNLVPNLSVaeN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGyaaelRLPPDTSKADRAQVVA---QVLDELGLTKHGDTRVDKLSGGQRK-----RAsvaleLLTGPSLLILDEPTS 452
Cdd:COG1129   100 IFLG-----REPRRGGLIDWRAMRRrarELLARLGLDIDPDTPVGDLSVAQQQlveiaRA-----LSRDARVLILDEPTA 169

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1184609190 453 GLDPA-----LDLqvmtmLRQLADAGRVVLVVTHsltYLD----VCDQV 492
Cdd:COG1129   170 SLTEReverlFRI-----IRRLKAQGVAIIYISH---RLDevfeIADRV 210
3a01208 TIGR00958
Conjugate Transporter-2 (CT2) Family protein; [Transport and binding proteins, Other]
 287-498 1.42e-21

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


Pssm-ID: 273363 [Multi-domain]  Cd Length: 711  Bit Score: 100.18  E-value: 1.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 287 TGGLEVREVNFSI---GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRT 362
Cdd:TIGR00958 476 EGLIEFQDVSFSYpnrPDVPVLKGLTFTLHPGEVVALVGPSGSGKSTVAALLQNLYQPTGGQVLLDGVPLvQYDHHYLHR 555

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 363 RIGMVPQDDVVHRQlTVNQALGYAaeLRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDK----LSGGQRKRASVALEL 438
Cdd:TIGR00958 556 QVALVGQEPVLFSG-SVRENIAYG--LTDTPDEEIMAAAKAANAHDFIMEFPNGYDTEVGEkgsqLSGGQKQRIAIARAL 632

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 439 LTGPSLLILDEPTSgldpALDLQVMTMLRQLAD-AGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:TIGR00958 633 VRKPRVLILDEATS----ALDAECEQLLQESRSrASRTVLLIAHRLSTVERADQILVLKKG 689
galliderm_ABC TIGR03740
gallidermin-class lantibiotic protection ABC transporter, ATP-binding subunit; Model TIGR03731 ...
 290-484 1.63e-21

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


Pssm-ID: 163452 [Multi-domain]  Cd Length: 223  Bit Score: 94.00  E-value: 1.63e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHniHTEYGSLRtRIGMVPQ 369
Cdd:TIGR03740   1 LETKNLSKRFGKQTAVNNISLTVPKNSVYGLLGPNGAGKSTLLKMITGILRPTSGEIIFDGH--PWTRKDLH-KIGSLIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPDTSkadraqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:TIGR03740  78 SPPLYENLTARENLKVHTTLLGLPDSR-------IDEVLNIVDLTNTGKKKAKQFSLGMKQRLGIAIALLNHPKLLILDE 150

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLT 484
Cdd:TIGR03740 151 PTNGLDPIGIQELRELIRSFPEQGITVILSSHILS 185
livG PRK11300
leucine/isoleucine/valine transporter ATP-binding subunit; Provisional
 308-510 1.87e-21

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


Pssm-ID: 183080 [Multi-domain]  Cd Length: 255  Bit Score: 94.67  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVP--QDDVVHRQLTVNQAL-- 383
Cdd:PRK11300   24 VNLEVREQEIVSLIGPNGAGKTTVFNCLTGFYKPTGGTILLRGQHIEGLPGHQIARMGVVRtfQHVRLFREMTVIENLlv 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 --------GYAAELRLPPDTSKADRAQV--VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSG 453
Cdd:PRK11300  104 aqhqqlktGLFSGLLKTPAFRRAESEALdrAATWLERVGLLEHANRQAGNLAYGQQRRLEIARCMVTQPEILMLDEPAAG 183

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 454 LDPALDLQVMTMLRQLADAGRV-VLVVTHSLTY-LDVCDQVLLMAPGGKTAyLGPPDQI 510
Cdd:PRK11300  184 LNPKETKELDELIAELRNEHNVtVLLIEHDMKLvMGISDRIYVVNQGTPLA-NGTPEEI 241
YbbA COG4181
Predicted ABC-type transport system involved in lysophospholipase L1 biosynthesis, ATPase ...
 290-498 1.95e-21

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: 94.04  E-value: 1.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDK----NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT--EYGSLRTR 363
Cdd:COG4181     9 IELRGLTKTVGTGagelTILKGISLEVEAGESVAIVGASGSGKSTLLGLLAGLDRPTSGTVRLAGQDLFAldEDARARLR 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 ---IGMVPQDDVVHRQLTV--NQALgyAAELRlppdtSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALEL 438
Cdd:COG4181    89 arhVGFVFQSFQLLPTLTAleNVML--PLELA-----GRRDARARARALLERVGLGHRLDHYPAQLSGGEQQRVALARAF 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:COG4181   162 ATEPAILFADEPTGNLDAATGEQIIDLLFELnRERGTTLVLVTHDPALAARCDRVLRLRAG 222
PRK11176 PRK11176
lipid A ABC transporter ATP-binding protein/permease MsbA;
282-498 2.07e-21

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


Pssm-ID: 183016 [Multi-domain]  Cd Length: 582  Bit Score: 99.32  E-value: 2.07e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 282 EVAARTGGLEVREVNFSIGDKNL--LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHtEY-- 357
Cdd:PRK11176  334 VIERAKGDIEFRNVTFTYPGKEVpaLRNINFKIPAGKTVALVGRSGSGKSTIANLLTRFYDIDEGEILLDGHDLR-DYtl 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 358 GSLRTRIGMVPQDdvVHrqL---TVNQALGYAAELRLppdtSKAD--RAQVVAQVLDELGLTKHG-DTRVDK----LSGG 427
Cdd:PRK11176  413 ASLRNQVALVSQN--VH--LfndTIANNIAYARTEQY----SREQieEAARMAYAMDFINKMDNGlDTVIGEngvlLSGG 484

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 428 QRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLaDAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK11176  485 QRQRIAIARALLRDSPILILDEATSALDTESERAIQAALDEL-QKNRTSLVIAHRLSTIEKADEILVVEDG 554
PRK13538 PRK13538
cytochrome c biogenesis heme-transporting ATPase CcmA;
290-481 2.42e-21

cytochrome c biogenesis heme-transporting ATPase CcmA;


Pssm-ID: 184125 [Multi-domain]  Cd Length: 204  Bit Score: 92.94  E-value: 2.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT---EYGSLRTRIGM 366
Cdd:PRK13538    2 LEARNLACERDERILFSGLSFTLNAGELVQIEGPNGAGKTSLLRILAGLARPDAGEVLWQGEPIRRqrdEYHQDLLYLGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQddvVHRQLTVNQALGYAAELRLPPDtskadrAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLI 446
Cdd:PRK13538   82 QPG---IKTELTALENLRFYQRLHGPGD------DEALWEALAQVGLAGFEDVPVRQLSAGQQRRVALARLWLTRAPLWI 152

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:PRK13538  153 LDEPFTAIDKQGVARLEALLAQHAEQGGMVILTTH 187
ABC_NatA_like cd03267
ATP-binding cassette domain of an uncharacterized transporter similar in sequence to NatA; ...
 305-498 2.46e-21

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


Pssm-ID: 213234 [Multi-domain]  Cd Length: 236  Bit Score: 93.94  E-value: 2.46e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMV-PQDDVVHRQLTVNQAL 383
Cdd:cd03267    37 LKGISFTIEKGEIVGFIGPNGAGKTTTLKILSGLLQPTSGEVRVAGLVPWKRRKKFLRRIGVVfGQKTQLWWDLPVIDSF 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 GYAAEL-RLPPDTSKADRAQVVaqvlDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQV 462
Cdd:cd03267   117 YLLAAIyDLPPARFKKRLDELS----ELLDLEELLDTPVRQLSLGQRMRAEIAAALLHEPEILFLDEPTIGLDVVAQENI 192

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1184609190 463 MTMLRQL-ADAGRVVLVVTHSLTylDV---CDQVLLMAPG 498
Cdd:cd03267   193 RNFLKEYnRERGTTVLLTSHYMK--DIealARRVLVIDKG 230
PRK11831 PRK11831
phospholipid ABC transporter ATP-binding protein MlaF;
290-481 3.23e-21

phospholipid ABC transporter ATP-binding protein MlaF;


Pssm-ID: 236997 [Multi-domain]  Cd Length: 269  Bit Score: 94.45  E-value: 3.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEYGSLRTRIG 365
Cdd:PRK11831    8 VDMRGVSFTRGNRCIFDNISLTVPRGKITAIMGPSGIGKTTLLRLIGGQIAPDHGEILFDGENIpamsRSRLYTVRKRMS 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQLTV--NQALGYAAELRLPPDTSKAdraqVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:PRK11831   88 MLFQSGALFTDMNVfdNVAYPLREHTQLPAPLLHS----TVMMKLEAVGLRGAAKLMPSELSGGMARRAALARAIALEPD 163

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1184609190 444 LLILDEPTSGLDPAldlqVMTMLRQLADA-----GRVVLVVTH 481
Cdd:PRK11831  164 LIMFDEPFVGQDPI----TMGVLVKLISElnsalGVTCVVVSH 202
cbiO PRK13646
energy-coupling factor transporter ATPase;
305-498 8.54e-21

energy-coupling factor transporter ATPase;


Pssm-ID: 184205 [Multi-domain]  Cd Length: 286  Bit Score: 93.31  E-value: 8.54e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-----EYGSLRTRIGMVPQ-------DDV 372
Cdd:PRK13646   23 IHDVNTEFEQGKYYAIVGQTGSGKSTLIQNINALLKPTTGTVTVDDITITHktkdkYIRPVRKRIGMVFQfpesqlfEDT 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 373 VHRqltvnqalgyaaELRLPPDTSKADRAQVVA---QVLDELGLTKHGDTRVD-KLSGGQ-RKRASVALeLLTGPSLLIL 447
Cdd:PRK13646  103 VER------------EIIFGPKNFKMNLDEVKNyahRLLMDLGFSRDVMSQSPfQMSGGQmRKIAIVSI-LAMNPDIIVL 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTylDVC---DQVLLMAPG 498
Cdd:PRK13646  170 DEPTAGLDPQSKRQVMRLLKSLQtDENKTIILVSHDMN--EVAryaDEVIVMKEG 222
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 299-498 9.57e-21

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 96.70  E-value: 9.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 299 IGDKNLLERVSLTARPGTLTAIIGGSGAGKTT----LSRLIAgyatpTTGSVTFEGHNIHT----EYGSLRTRIGMVPQD 370
Cdd:PRK15134  296 VDHNVVVKNISFTLRPGETLGLVGESGSGKSTtglaLLRLIN-----SQGEIWFDGQPLHNlnrrQLLPVRHRIQVVFQD 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 371 --DVVHRQLTVNQALgyAAELRL-PPDTSKADRAQVVAQVLDELGLTKHGDTRV-DKLSGGQRKRASVALELLTGPSLLI 446
Cdd:PRK15134  371 pnSSLNPRLNVLQII--EEGLRVhQPTLSAAQREQQVIAVMEEVGLDPETRHRYpAEFSGGQRQRIAIARALILKPSLII 448

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADAGRVV-LVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK15134  449 LDEPTSSLDKTVQAQILALLKSLQQKHQLAyLFISHDLHVVrALCHQVIVLRQG 502
cbiO PRK13643
energy-coupling factor transporter ATPase;
308-508 1.23e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184203 [Multi-domain]  Cd Length: 288  Bit Score: 93.26  E-value: 1.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSV-----TFEGHNIHTEYGSLRTRIGMV---PQDDVVHRQLTV 379
Cdd:PRK13643   25 IDLEVKKGSYTALIGHTGSGKSTLLQHLNGLLQPTEGKVtvgdiVVSSTSKQKEIKPVRKKVGVVfqfPESQLFEETVLK 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGyaaelrlPPD--TSKADRAQVVAQVLDELGLTKH-GDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:PRK13643  105 DVAFG-------PQNfgIPKEKAEKIAAEKLEMVGLADEfWEKSPFELSGGQMRRVAIAGILAMEPEVLVLDEPTAGLDP 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 457 ALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPGGKTAYLGPPD 508
Cdd:PRK13643  178 KARIEMMQLFESIHQSGQTVVLVTHLMDDVaDYADYVYLLEKGHIISCGTPSD 230
ABC_ATP_DarD NF038007
darobactin export ABC transporter ATP-binding protein;
303-498 1.29e-20

darobactin export ABC transporter ATP-binding protein;


Pssm-ID: 411600 [Multi-domain]  Cd Length: 218  Bit Score: 91.32  E-value: 1.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 303 NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEYGSLRTR-IGMVPQDDVVHRQL 377
Cdd:NF038007   19 KVLNHLNFSVEKGDFVSIMGPSGSGKSTLLNIIGMFDSLDSGSLTLAGKEVtnlsYSQKIILRRElIGYIFQSFNLIPHL 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPA 457
Cdd:NF038007   99 SIFDNVALPLKYR---GVAKKERIERVNQVLNLFGIDNRRNHKPMQLSGGQQQRVAIARAMVSNPALLLADEPTGNLDSK 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1184609190 458 LDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:NF038007  176 NARAVLQQLKYINQKGTTIIMVTHSDEASTYGNRIINMKDG 216
bacteriocin_ABC TIGR01193
ABC-type bacteriocin transporter; This model describes ABC-type bacteriocin transporter. The ...
 288-499 2.21e-20

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: 96.35  E-value: 2.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSIG-DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRIG 365
Cdd:TIGR01193 472 GDIVINDVSYSYGyGSNILSDISLTIKMNSKTTIVGMSGSGKSTLAKLLVGFFQARSGEILLNGFSLkDIDRHTLRQFIN 551

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDVVHRQlTVNQALGYAAELRLPPDtsKADRAQVVAQVLDELGLTKHG-DTRVDK----LSGGQRKRASVALELLT 440
Cdd:TIGR01193 552 YLPQEPYIFSG-SILENLLLGAKENVSQD--EIWAACEIAEIKDDIENMPLGyQTELSEegssISGGQKQRIALARALLT 628

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQLADagRVVLVVTHSLTYLDVCDQVLLMAPGG 499
Cdd:TIGR01193 629 DSKVLILDESTSNLDTITEKKIVNNLLNLQD--KTIIFVAHRLSVAKQSDKIIVLDHGK 685
PRK10253 PRK10253
iron-enterobactin ABC transporter ATP-binding protein;
282-510 2.66e-20

iron-enterobactin ABC transporter ATP-binding protein;


Pssm-ID: 182336 [Multi-domain]  Cd Length: 265  Bit Score: 91.59  E-value: 2.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 282 EVAARTGGlevREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHtEYGS-- 359
Cdd:PRK10253    3 ESVARLRG---EQLTLGYGKYTVAENLTVEIPDGHFTAIIGPNGCGKSTLLRTLSRLMTPAHGHVWLDGEHIQ-HYASke 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQDDVVHRQLTVNQALGYAAELRLPPDTS-KADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALEL 438
Cdd:PRK10253   79 VARRIGLLAQNATTPGDITVQELVARGRYPHQPLFTRwRKEDEEAVTKAMQATGITHLADQSVDTLSGGQRQRAWIAMVL 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQI 510
Cdd:PRK10253  159 AQETAIMLLDEPTTWLDISHQIDLLELLSELnREKGYTLAAVLHDLNQACRYASHLIALREGKIVAQGAPKEI 231
potA PRK09452
spermidine/putrescine ABC transporter ATP-binding protein PotA;
290-510 2.75e-20

spermidine/putrescine ABC transporter ATP-binding protein PotA;


Pssm-ID: 236523 [Multi-domain]  Cd Length: 375  Bit Score: 93.86  E-value: 2.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGSLRTRIGMVPQ 369
Cdd:PRK09452   15 VELRGISKSFDGKEVISNLDLTINNGEFLTLLGPSGCGKTTVLRLIAGFETPDSGRIMLDGQDI-THVPAENRHVNTVFQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTV--NQALGyaaeLRLppdtSKADRAQVVAQVLDELG---LTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK09452   94 SYALFPHMTVfeNVAFG----LRM----QKTPAAEITPRVMEALRmvqLEEFAQRKPHQLSGGQQQRVAIARAVVNKPKV 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTH----SLTyldVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK09452  166 LLLDESLSALDYKLRKQMQNELKALQrKLGITFVFVTHdqeeALT---MSDRIVVMR-DGRIEQDGTPREI 232
cbiO PRK13649
energy-coupling factor transporter ATPase;
289-510 4.04e-20

energy-coupling factor transporter ATPase;


Pssm-ID: 184208 [Multi-domain]  Cd Length: 280  Bit Score: 91.34  E-value: 4.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLER-----VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-----HTEYG 358
Cdd:PRK13649    2 GINLQNVSYTYQAGTPFEGralfdVNLTIEDGSYTAFIGHTGSGKSTIMQLLNGLHVPTQGSVRVDDTLItstskNKDIK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 359 SLRTRIGMV---PQDDVVHRQLTVNQALGyaaelrlpPDTSKADRAQVVAQVLDELGLTKHGDTRVDK----LSGGQRKR 431
Cdd:PRK13649   82 QIRKKVGLVfqfPESQLFEETVLKDVAFG--------PQNFGVSQEEAEALAREKLALVGISESLFEKnpfeLSGGQMRR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 432 ASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTylDV---CDQVLLMApGGKTAYLGPPD 508
Cdd:PRK13649  154 VAIAGILAMEPKILVLDEPTAGLDPKGRKELMTLFKKLHQSGMTIVLVTHLMD--DVanyADFVYVLE-KGKLVLSGKPK 230


                  ..
gi 1184609190 509 QI 510
Cdd:PRK13649  231 DI 232
PRK13657 PRK13657
glucan ABC transporter ATP-binding protein/ permease;
288-498 4.48e-20

glucan ABC transporter ATP-binding protein/ permease;


Pssm-ID: 184214 [Multi-domain]  Cd Length: 588  Bit Score: 95.03  E-value: 4.48e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSI-GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRIG 365
Cdd:PRK13657  333 GAVEFDDVSFSYdNSRQGVEDVSFEAKPGQTVAIVGPTGAGKSTLINLLQRVFDPQSGRILIDGTDIRTvTRASLRRNIA 412

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDD-VVHRQLTVNQALGyaaelrlPPDTSKAD--RAQVVAQVLD-----ELGLTKHGDTRVDKLSGGQRKRASVALE 437
Cdd:PRK13657  413 VVFQDAgLFNRSIEDNIRVG-------RPDATDEEmrAAAERAQAHDfierkPDGYDTVVGERGRQLSGGERQRLAIARA 485

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK13657  486 LLKDPPILILDEATSALDVETEAKVKAALDELMK-GRTTFIIAHRLSTVRNADRILVFDNG 545
cbiO PRK13631
cobalt transporter ATP-binding subunit; Provisional
 320-510 9.87e-20

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237451 [Multi-domain]  Cd Length: 320  Bit Score: 91.07  E-value: 9.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 320 IIGGSGAGKTTLSRLIAGYATPTTGSVTFE----GHNIHTEYGS-------------LRTRIGMVPQ-------DDVVHR 375
Cdd:PRK13631   57 IIGNSGSGKSTLVTHFNGLIKSKYGTIQVGdiyiGDKKNNHELItnpyskkiknfkeLRRRVSMVFQfpeyqlfKDTIEK 136

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 376 QLTVNQ-ALGyaaelrlppdTSKADRAQVVAQVLDELGLtkhGDTRVDK----LSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:PRK13631  137 DIMFGPvALG----------VKKSEAKKLAKFYLNKMGL---DDSYLERspfgLSGGQKRRVAIAGILAIQPEILIFDEP 203

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 451 TSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:PRK13631  204 TAGLDPKGEHEMMQLILDAKANNKTVFVITHTMEHvLEVADEVIVMDK-GKILKTGTPYEI 263
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
205-272 1.82e-19

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 83.85  E-value: 1.82e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRV-GSAVLAEGDVVTIGNVDLVF 272
Cdd:COG1716    25 IGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVtEPAPLRDGDVIRLGKTELRF 93
cbiO PRK13634
cobalt transporter ATP-binding subunit; Provisional
 308-499 2.15e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237454 [Multi-domain]  Cd Length: 290  Bit Score: 89.31  E-value: 2.15e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-----HTEYGSLRTRIGMVPQddVVHRQL---TV 379
Cdd:PRK13634   26 VNVSIPSGSYVAIIGHTGSGKSTLLQHLNGLLQPTSGTVTIGERVItagkkNKKLKPLRKKVGIVFQ--FPEHQLfeeTV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAaelrlPPD--TSKADRAQVVAQVLDELGLTKHGDTRVD-KLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:PRK13634  104 EKDICFG-----PMNfgVSEEDAKQKAREMIELVGLPEELLARSPfELSGGQMRRVAIAGVLAMEPEVLVLDEPTAGLDP 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1184609190 457 ALDLQVMTMLRQL-ADAGRVVLVVTHSLTylDV---CDQVLLMAPGG 499
Cdd:PRK13634  179 KGRKEMMEMFYKLhKEKGLTTVLVTHSME--DAaryADQIVVMHKGT 223
PRK15112 PRK15112
peptide ABC transporter ATP-binding protein SapF;
308-502 2.53e-19

peptide ABC transporter ATP-binding protein SapF;


Pssm-ID: 185067 [Multi-domain]  Cd Length: 267  Bit Score: 88.69  E-value: 2.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH-TEYGSLRTRIGMVPQDDVVhrQLTVNQALGYA 386
Cdd:PRK15112   32 LSFTLREGQTLAIIGENGSGKSTLAKMLAGMIEPTSGELLIDDHPLHfGDYSYRSQRIRMIFQDPST--SLNPRQRISQI 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 387 AE--LRLPPDTSKADRAQVVAQVLDELGL-TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:PRK15112  110 LDfpLRLNTDLEPEQREKQIIETLRQVGLlPDHASYYPHMLAPGQKQRLGLARALILRPKVIIADEALASLDMSMRSQLI 189

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1184609190 464 TMLRQLADA-GRVVLVVTHSLTYLD-VCDQVLLMAPG-----GKTA 502
Cdd:PRK15112  190 NLMLELQEKqGISYIYVTQHLGMMKhISDQVLVMHQGevverGSTA 235
cbiO PRK13652
cobalt transporter ATP-binding subunit; Provisional
 290-510 3.87e-19

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 172200 [Multi-domain]  Cd Length: 277  Bit Score: 88.32  E-value: 3.87e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI-GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIGMV 367
Cdd:PRK13652    4 IETRDLCYSYsGSKEALNNINFIAPRNSRIAVIGPNGAGKSTLFRHFNGILKPTSGSVLIRGEPITKEnIREVRKFVGLV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQ--DDVVHRQlTVNQALGYAAeLRLPPDTSKAdrAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLL 445
Cdd:PRK13652   84 FQnpDDQIFSP-TVEQDIAFGP-INLGLDEETV--AHRVSSALHMLGLEELRDRVPHHLSGGEKKRVAIAGVIAMEPQVL 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 446 ILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYL-DVCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:PRK13652  160 VLDEPTAGLDPQGVKELIDFLNDLPETyGMTVIFSTHQLDLVpEMADYIYVMDKGRIVAY-GTVEEI 225
PRK14247 PRK14247
phosphate ABC transporter ATP-binding protein; Provisional
 290-510 4.20e-19

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172735 [Multi-domain]  Cd Length: 250  Bit Score: 87.66  E-value: 4.20e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTL----SRLIAGYATP-TTGSVTFEGHNI-HTEYGSLRTR 363
Cdd:PRK14247    4 IEIRDLKVSFGQVEVLDGVNLEIPDNTITALMGPSGSGKSTLlrvfNRLIELYPEArVSGEVYLDGQDIfKMDVIELRRR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQ--DDVVHRQLTVNQALGYAAElRLPpdTSKADRAQVVAQVLDELGLTKHGDTRVD----KLSGGQRKRASVALE 437
Cdd:PRK14247   84 VQMVFQipNPIPNLSIFENVALGLKLN-RLV--KSKKELQERVRWALEKAQLWDEVKDRLDapagKLSGGQQQRLCIARA 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK14247  161 LAFQPEVLLADEPTANLDPENTAKIESLFLELKKDMTIVLVTHFPQQAARISDYVAFLY-KGQIVEWGPTREV 232
cbiO PRK13650
energy-coupling factor transporter ATPase;
290-498 6.38e-19

energy-coupling factor transporter ATPase;


Pssm-ID: 184209 [Multi-domain]  Cd Length: 279  Bit Score: 87.86  E-value: 6.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNF---SIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIG 365
Cdd:PRK13650    5 IEVKNLTFkykEDQEKYTLNDVSFHVKQGEWLSIIGHNGSGKSTTVRLIDGLLEAESGQIIIDGDLLTEEnVWDIRHKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQD-DVVHRQLTVNQALGYAAELRLPPDTSKADRaqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK13650   85 MVFQNpDNQFVGATVEDDVAFGLENKGIPHEEMKER---VNEALELVGMQDFKEREPARLSGGQKQRVAIAGAVAMRPKI 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK13650  162 IILDEATSMLDPEGRLELIKTIKGIRDDyQMTVISITHDLDEVALSDRVLVMKNG 216
MglA COG1129
ABC-type sugar transport system, ATPase component [Carbohydrate transport and metabolism];
290-504 9.82e-19

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


Pssm-ID: 440745 [Multi-domain]  Cd Length: 497  Bit Score: 90.46  E-value: 9.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVRevNFSIGDKnlLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGH--NIHTEYGSLRTRIGMV 367
Cdd:COG1129   257 LEVE--GLSVGGV--VRDVSFSVRAGEILGIAGLVGAGRTELARALFGADPADSGEIRLDGKpvRIRSPRDAIRAGIAYV 332

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDdvvhRQ-------LTV--NQALGYAAELRLPPDTSKADRAQVVAQVLDELGL-TKHGDTRVDKLSGG-QRKrasVAL 436
Cdd:COG1129   333 PED----RKgeglvldLSIreNITLASLDRLSRGGLLDRRRERALAEEYIKRLRIkTPSPEQPVGNLSGGnQQK---VVL 405

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 437 E--LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVThslTYLD----VCDQVLLMAPGGKTAYL 504
Cdd:COG1129   406 AkwLATDPKVLILDEPTRGIDVGAKAEIYRLIRELAAEGKAVIVIS---SELPellgLSDRILVMREGRIVGEL 476
PRK11174 PRK11174
cysteine/glutathione ABC transporter membrane/ATP-binding component; Reviewed
 297-498 1.29e-18

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


Pssm-ID: 236870 [Multi-domain]  Cd Length: 588  Bit Score: 90.29  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 297 FSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYAtPTTGSVTFEGHNIHT-EYGSLRTRIGMVPQD-DVVH 374
Cdd:PRK11174  358 LSPDGKTLAGPLNFTLPAGQRIALVGPSGAGKTSLLNALLGFL-PYQGSLKINGIELRElDPESWRKHLSWVGQNpQLPH 436

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVNQALGyaaelrlPPDTSKADRAQVV--AQVLDELGLTKHG-DTRVDK----LSGGQRKRASVALELLTGPSLLIL 447
Cdd:PRK11174  437 GTLRDNVLLG-------NPDASDEQLQQALenAWVSEFLPLLPQGlDTPIGDqaagLSVGQAQRLALARALLQPCQLLLL 509

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQlADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK11174  510 DEPTASLDAHSEQLVMQALNA-ASRRQTTLMVTHQLEDLAQWDQIWVMQDG 559
3a01205 TIGR00956
Pleiotropic Drug Resistance (PDR) Family protein; [Transport and binding proteins, Other]
 302-527 1.37e-18

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


Pssm-ID: 273362 [Multi-domain]  Cd Length: 1394  Bit Score: 91.32  E-value: 1.37e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIA----GYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQL 377
Cdd:TIGR00956   74 FDILKPMDGLIKPGELTVVLGRPGSGCSTLLKTIAsntdGFHIGVEGVITYDGITPEEIKKHYRGDVVYNAETDVHFPHL 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  378 TVNQALGYAAELRLP---PD-TSKADRAQVVAQV-LDELGL-----TKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:TIGR00956  154 TVGETLDFAARCKTPqnrPDgVSREEYAKHIADVyMATYGLshtrnTKVGNDFVRGVSGGERKRVSIAEASLGGAKIQCW 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  448 DEPTSGLDPALDLQVMTMLRQLADAGRVVLVVT---HSLTYLDVCDQVLLMAPgGKTAYLGPPDQIggamgttnwAQIFA 524
Cdd:TIGR00956  234 DNATRGLDSATALEFIRALKTSANILDTTPLVAiyqCSQDAYELFDKVIVLYE-GYQIYFGPADKA---------KQYFE 303


                   ...
gi 1184609190  525 KVG 527
Cdd:TIGR00956  304 KMG 306
PRK10535 PRK10535
macrolide ABC transporter ATP-binding protein/permease MacB;
305-481 1.53e-18

macrolide ABC transporter ATP-binding protein/permease MacB;


Pssm-ID: 182528 [Multi-domain]  Cd Length: 648  Bit Score: 90.55  E-value: 1.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSL-RTRIGMVPQDDVVHRQLTV 379
Cdd:PRK10535   24 LKGISLDIYAGEMVAIVGASGSGKSTLMNILGCLDKPTSGTYRVAGQDVATldadALAQLrREHFGFIFQRYHLLSHLTA 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAelrLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:PRK10535  104 AQNVEVPA---VYAGLERKQRLLRAQELLQRLGLEDRVEYQPSQLSGGQQQRVSIARALMNGGQVILADEPTGALDSHSG 180

                         170       180
                  ....*....|....*....|..
gi 1184609190 460 LQVMTMLRQLADAGRVVLVVTH 481
Cdd:PRK10535  181 EEVMAILHQLRDRGHTVIIVTH 202
cbiO PRK13647
cobalt transporter ATP-binding subunit; Provisional
 290-506 1.59e-18

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 237457 [Multi-domain]  Cd Length: 274  Bit Score: 86.33  E-value: 1.59e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN-LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH--TEYgSLRTRIGM 366
Cdd:PRK13647    5 IEVEDLHFRYKDGTkALKGLSLSIPEGSKTALLGPNGAGKSTLLLHLNGIYLPQRGRVKVMGREVNaeNEK-WVRSKVGL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 V---PQDDVVHRQLTVNQALGyaaelrlpPDTSKADRAQVVAQVLDELGLTKHGDTRvDK----LSGGQRKRASVALELL 439
Cdd:PRK13647   84 VfqdPDDQVFSSTVWDDVAFG--------PVNMGLDKDEVERRVEEALKAVRMWDFR-DKppyhLSYGQKKRVAIAGVLA 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMAPGGKTAYLGP 506
Cdd:PRK13647  155 MDPDVIVLDEPMAYLDPRGQETLMEILDRLHNQGKTVIVATHDVDLaAEWADQVIVLKEGRVLAEGDK 222
cbiO PRK13642
energy-coupling factor transporter ATPase;
290-498 1.66e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 184202 [Multi-domain]  Cd Length: 277  Bit Score: 86.69  E-value: 1.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSI---GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIG 365
Cdd:PRK13642    5 LEVENLVFKYekeSDVNQLNGVSFSITKGEWVSIIGQNGSGKSTTARLIDGLFEEFEGKVKIDGELLTAEnVWNLRRKIG 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQD-DVVHRQLTVNQALGYAAELRLPPDTSKADRaqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK13642   85 MVFQNpDNQFVGATVEDDVAFGMENQGIPREEMIKR---VDEALLAVNMLDFKTREPARLSGGQKQRVAVAGIIALRPEI 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK13642  162 IILDESTSMLDPTGRQEIMRVIHEIKEKYQLtVLSITHDLDEAASSDRILVMKAG 216
PRK10575 PRK10575
Fe3+-hydroxamate ABC transporter ATP-binding protein FhuC;
292-510 2.24e-18

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


Pssm-ID: 182561 [Multi-domain]  Cd Length: 265  Bit Score: 85.99  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 292 VREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTR-IGMVPQD 370
Cdd:PRK10575   14 LRNVSFRVPGRTLLHPLSLTFPAGKVTGLIGHNGSGKSTLLKMLGRHQPPSEGEILLDAQPLESWSSKAFARkVAYLPQQ 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 371 DVVHRQLTVNQ--ALG----YAAELRLppdtSKADRAQVvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK10575   94 LPAAEGMTVRElvAIGrypwHGALGRF----GAADREKV-EEAISLVGLKPLAHRLVDSLSGGERQRAWIAMLVAQDSRC 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTY-LDVCDQvLLMAPGGKTAYLGPPDQI 510
Cdd:PRK10575  169 LLLDEPTSALDIAHQVDVLALVHRLSqERGLTVIAVLHDINMaARYCDY-LVALRGGEMIAQGTPAEL 235
znuC PRK09544
high-affinity zinc transporter ATPase; Reviewed
 295-483 2.55e-18

high-affinity zinc transporter ATPase; Reviewed


Pssm-ID: 181939 [Multi-domain]  Cd Length: 251  Bit Score: 85.55  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 295 VNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihteygslRTRIGMVPQDdvVH 374
Cdd:PRK09544   10 VSVSFGQRRVLSDVSLELKPGKILTLLGPNGAGKSTLVRVVLGLVAPDEGVIKRNG----------KLRIGYVPQK--LY 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVnqALGYAAELRLPPDTSKADraqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:PRK09544   78 LDTTL--PLTVNRFLRLRPGTKKED----ILPALKRVQAGHLIDAPMQKLSGGETQRVLLARALLNRPQLLVLDEPTQGV 151

                         170       180       190
                  ....*....|....*....|....*....|
gi 1184609190 455 DPALDLQVMTMLRQL-ADAGRVVLVVTHSL 483
Cdd:PRK09544  152 DVNGQVALYDLIDQLrRELDCAVLMVSHDL 181
livF PRK11614
high-affinity branched-chain amino acid ABC transporter ATP-binding protein LivF;
290-479 2.97e-18

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


Pssm-ID: 183231 [Multi-domain]  Cd Length: 237  Bit Score: 84.93  E-value: 2.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYGS---LRTRIGM 366
Cdd:PRK11614    6 LSFDKVSAHYGKIQALHEVSLHINQGEIVTLIGANGAGKTTLLGTLCGDPRATSGRIVFDGKDI-TDWQTakiMREAVAI 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQAL---GYAAElrlppDTSKADRAQVVAQVLDELGLTKHgdTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:PRK11614   85 VPEGRRVFSRMTVEENLamgGFFAE-----RDQFQERIKWVYELFPRLHERRI--QRAGTMSGGEQQMLAIGRALMSQPR 157

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVV 479
Cdd:PRK11614  158 LLLLDEPSLGLAPIIIQQIFDTIEQLREQGMTIFLV 193
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 283-487 3.73e-18

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: 88.84  E-value: 3.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 283 VAARTGG--LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVtfeghnihteygsl 360
Cdd:TIGR03719 314 PGPRLGDkvIEAENLTKAFGDKLLIDDLSFKLPPGGIVGVIGPNGAGKSTLFRMITGQEQPDSGTI-------------- 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 361 rtRIGmvpqdDVVHrqltvnqaLGYAAELRLPPDTSKAdRAQVVAQVLDELGLTKH---------------GD--TRVDK 423
Cdd:TIGR03719 380 --EIG-----ETVK--------LAYVDQSRDALDPNKT-VWEEISGGLDIIKLGKReipsrayvgrfnfkgSDqqKKVGQ 443

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 424 LSGGQRKRASVALELLTGPSLLILDEPTSgldpalDLQVMTmLRQLADA----GRVVLVVTHSLTYLD 487
Cdd:TIGR03719 444 LSGGERNRVHLAKTLKSGGNVLLLDEPTN------DLDVET-LRALEEAllnfAGCAVVISHDRWFLD 504
cbiO PRK13641
energy-coupling factor transporter ATPase;
305-498 4.72e-18

energy-coupling factor transporter ATPase;


Pssm-ID: 237456 [Multi-domain]  Cd Length: 287  Bit Score: 85.27  E-value: 4.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS-----LRTRIGMVPQddVVHRQLTV 379
Cdd:PRK13641   23 LDNISFELEEGSFVALVGHTGSGKSTLMQHFNALLKPSSGTITIAGYHITPETGNknlkkLRKKVSLVFQ--FPEAQLFE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALgyaAELRLPPDTSKA--DRAQVVA-QVLDELGLTkhgDTRVDK----LSGGQRKRASVALELLTGPSLLILDEPTS 452
Cdd:PRK13641  101 NTVL---KDVEFGPKNFGFseDEAKEKAlKWLKKVGLS---EDLISKspfeLSGGQMRRVAIAGVMAYEPEILCLDEPAA 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1184609190 453 GLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK13641  175 GLDPEGRKEMMQLFKDYQKAGHTVILVTHNMDDVaEYADDVLVLEHG 221
COG4586 COG4586
ABC-type uncharacterized transport system, ATPase component [General function prediction only]; ...
 277-510 8.74e-18

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


Pssm-ID: 443643 [Multi-domain]  Cd Length: 323  Bit Score: 85.14  E-value: 8.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 277 LVRRQ--EVAArtggleVREVNFSIGdknllervsltarPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIH 354
Cdd:COG4586    27 LFRREyrEVEA------VDDISFTIE-------------PGEIVGFIGPNGAGKSTTIKMLTGILVPTSGEVRVLGYVPF 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 355 TEYGSLRTRIGMV------------PQDdvvhrQLTVNQALgYaaelRLPPDTSKADRAQVVaqvlDELGLTKHGDTRVD 422
Cdd:COG4586    88 KRRKEFARRIGVVfgqrsqlwwdlpAID-----SFRLLKAI-Y----RIPDAEYKKRLDELV----ELLDLGELLDTPVR 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 423 KLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHsltYLD----VCDQVLLMAp 497
Cdd:COG4586   154 QLSLGQRMRCELAAALLHRPKILFLDEPTIGLDVVSKEAIREFLKEYnRERGTTILLTSH---DMDdieaLCDRVIVID- 229

                         250
                  ....*....|...
gi 1184609190 498 GGKTAYLGPPDQI 510
Cdd:COG4586   230 HGRIIYDGSLEEL 242
YddA COG4178
ABC-type uncharacterized transport system, permease and ATPase components [General function ...
 288-499 1.19e-17

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


Pssm-ID: 443337 [Multi-domain]  Cd Length: 571  Bit Score: 87.17  E-value: 1.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVREVNFSIGD-KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNihteygslrtRIGM 366
Cdd:COG4178   361 GALALEDLTLRTPDgRPLLEDLSLSLKPGERLLITGPSGSGKSTLLRAIAGLWPYGSGRIARPAGA----------RVLF 430

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQddvvhR----QLTVNQALGYaaelrlPPDTSKADRAQVvAQVLDELGLTKHGDtRVDK-------LSGGQRKRASVA 435
Cdd:COG4178   431 LPQ-----RpylpLGTLREALLY------PATAEAFSDAEL-REALEAVGLGHLAE-RLDEeadwdqvLSLGEQQRLAFA 497

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 436 LELLTGPSLLILDEPTSGLDPALDLQVMTMLRQ-LADAGrvVLVVTHSLTYLDVCDQVLLMAPGG 499
Cdd:COG4178   498 RLLLHKPDWLFLDEATSALDEENEAALYQLLREeLPGTT--VISVGHRSTLAAFHDRVLELTGDG 560
phnK PRK11701
phosphonate C-P lyase system protein PhnK; Provisional
 290-483 1.20e-17

phosphonate C-P lyase system protein PhnK; Provisional


Pssm-ID: 183280 [Multi-domain]  Cd Length: 258  Bit Score: 83.44  E-value: 1.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEG-----HNIHTEYGS----- 359
Cdd:PRK11701    7 LSVRGLTKLYGPRKGCRDVSFDLYPGEVLGIVGESGSGKTTLLNALSARLAPDAGEVHYRMrdgqlRDLYALSEAerrrl 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQDDVVHRQLTVNqALGYAAElRLppdTSKADR--AQVVAQVLDELGLTKHGDTRVDKL----SGGQRKRAS 433
Cdd:PRK11701   87 LRTEWGFVHQHPRDGLRMQVS-AGGNIGE-RL---MAVGARhyGDIRATAGDWLERVEIDAARIDDLpttfSGGMQQRLQ 161

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 434 VALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSL 483
Cdd:PRK11701  162 IARNLVTHPRLVFMDEPTGGLDVSVQARLLDLLRGLvRELGLAVVIVTHDL 212
MK0520 COG2401
ABC-type ATPase fused to a predicted acetyltransferase domain [General function prediction ...
 267-481 1.48e-17

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


Pssm-ID: 441957 [Multi-domain]  Cd Length: 222  Bit Score: 82.31  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 267 NVDLVFTGGI-LVRRQEVAARTGGLEVREVNFSIgdknlLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGS 345
Cdd:COG2401    12 RVTKVYSSVLdLSERVAIVLEAFGVELRVVERYV-----LRDLNLEIEPGEIVLIVGASGSGKSTLLRLLAGALKGTPVA 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 346 VTFEghnihteygslrtrigmVPqDDVVHRQLTVNQALgyaaelrlPPDTSKADRAQVVAQVldelGLtkhGD-----TR 420
Cdd:COG2401    87 GCVD-----------------VP-DNQFGREASLIDAI--------GRKGDFKDAVELLNAV----GL---SDavlwlRR 133

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 421 VDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAD-AGRVVLVVTH 481
Cdd:COG2401   134 FKELSTGQKFRFRLALLLAERPKLLVIDEFCSHLDRQTAKRVARNLQKLARrAGITLVVATH 195
PRK10789 PRK10789
SmdA family multidrug ABC transporter permease/ATP-binding protein;
255-510 1.52e-17

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


Pssm-ID: 182732 [Multi-domain]  Cd Length: 569  Bit Score: 87.08  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 255 AVLAEGDVVTIGNVDLVFTGGILVrrqevaartggLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRL 334
Cdd:PRK10789  292 AMLAEAPVVKDGSEPVPEGRGELD-----------VNIRQFTYPQTDHPALENVNFTLKPGQMLGICGPTGSGKSTLLSL 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 335 IAGYATPTTGSVTFEGHNIHT-EYGSLRTRIGMVPQ-----DDVVHRqltvNQALGYaaelrlpPDTSKADRAQV--VAQ 406
Cdd:PRK10789  361 IQRHFDVSEGDIRFHDIPLTKlQLDSWRSRLAVVSQtpflfSDTVAN----NIALGR-------PDATQQEIEHVarLAS 429

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 407 VLDE-LGLTKHGDTRVDK----LSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADaGRVVLVVTH 481
Cdd:PRK10789  430 VHDDiLRLPQGYDTEVGErgvmLSGGQKQRISIARALLLNAEILILDDALSAVDGRTEHQILHNLRQWGE-GRTVIISAH 508

                         250       260
                  ....*....|....*....|....*....
gi 1184609190 482 SLTYLDVCDQVLLMAPGGkTAYLGPPDQI 510
Cdd:PRK10789  509 RLSALTEASEILVMQHGH-IAQRGNHDQL 536
cbiO PRK13638
energy-coupling factor ABC transporter ATP-binding protein;
290-510 1.54e-17

energy-coupling factor ABC transporter ATP-binding protein;


Pssm-ID: 184198 [Multi-domain]  Cd Length: 271  Bit Score: 83.52  E-value: 1.54e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYG--SLRTRIGM 366
Cdd:PRK13638    2 LATSDLWFRYQDEPVLKGLNLDFSLSPVTGLVGANGCGKSTLFMNLSGLLRPQKGAVLWQGKPLdYSKRGllALRQQVAT 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDvvhrqltvNQALGYA---AELRLPPDTSKADRAQVVAQVLDELGLTKHGDTR---VDKLSGGQRKRASVALELLT 440
Cdd:PRK13638   82 VFQDP--------EQQIFYTdidSDIAFSLRNLGVPEAEITRRVDEALTLVDAQHFRhqpIQCLSHGQKKRVAIAGALVL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPGGKTAYlGPPDQI 510
Cdd:PRK13638  154 QARYLLLDEPTAGLDPAGRTQMIAIIRRIVAQGNHVIISSHDIDLIyEISDAVYVLRQGQILTH-GAPGEV 223
PRK11000 PRK11000
maltose/maltodextrin ABC transporter ATP-binding protein MalK;
293-507 1.56e-17

maltose/maltodextrin ABC transporter ATP-binding protein MalK;


Pssm-ID: 182893 [Multi-domain]  Cd Length: 369  Bit Score: 85.08  E-value: 1.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 293 REVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTrIGMVPQDDV 372
Cdd:PRK11000    7 RNVTKAYGDVVISKDINLDIHEGEFVVFVGPSGCGKSTLLRMIAGLEDITSGDLFIGEKRMNDVPPAERG-VGMVFQSYA 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 373 VHRQLTV--NQALGyaaeLRLPpDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:PRK11000   86 LYPHLSVaeNMSFG----LKLA-GAKKEEINQRVNQVAEVLQLAHLLDRKPKALSGGQRQRVAIGRTLVAEPSVFLLDEP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 451 TSGLDPALDLQVMTMLRQLADA-GRVVLVVTHsltyldvcDQVLLMA--------PGGKTAYLGPP 507
Cdd:PRK11000  161 LSNLDAALRVQMRIEISRLHKRlGRTMIYVTH--------DQVEAMTladkivvlDAGRVAQVGKP 218
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 205-272 1.84e-17

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 78.09  E-value: 1.84e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRV-GSAVLAEGDVVTIGNVDLVF 272
Cdd:cd00060    23 IGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRItPPVPLQDGDVIRLGDTTFRF 91
YejF COG4172
ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites ...
 290-495 2.08e-17

ABC-type microcin C transport system, duplicated ATPase component YejF [Secondary metabolites biosynthesis, transport and catabolism];


Pssm-ID: 443332 [Multi-domain]  Cd Length: 533  Bit Score: 86.28  E-value: 2.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGD----KNLLERVSLTARPGTLTAIIGGSGAGK--TTLS--RLIAGYATPTTGSVTFEGHNI-HTEYGSL 360
Cdd:COG4172     7 LSVEDLSVAFGQgggtVEAVKGVSFDIAAGETLALVGESGSGKsvTALSilRLLPDPAAHPSGSILFDGQDLlGLSEREL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 361 RT----RIGMVPQD-----DVVH---RQLtvnqalgyaAE-LRLPPDTSKADRAQVVAQVLDELGLtKHGDTRVDK---- 423
Cdd:COG4172    87 RRirgnRIAMIFQEpmtslNPLHtigKQI---------AEvLRLHRGLSGAAARARALELLERVGI-PDPERRLDAyphq 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 424 LSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYL-DVCDQVLLM 495
Cdd:COG4172   157 LSGGQRQRVMIAMALANEPDLLIADEPTTALDVTVQAQILDLLKDLqRELGMALLLITHDLGVVrRFADRVAVM 230
cbiO PRK13637
energy-coupling factor transporter ATPase;
301-510 2.26e-17

energy-coupling factor transporter ATPase;


Pssm-ID: 237455 [Multi-domain]  Cd Length: 287  Bit Score: 83.56  E-value: 2.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSL---RTRIGMVPQddVVHRQL 377
Cdd:PRK13637   19 EKKALDNVNIEIEDGEFVGLIGHTGSGKSTLIQHLNGLLKPTSGKIIIDGVDITDKKVKLsdiRKKVGLVFQ--YPEYQL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 ---TVNQALGYA-AELRLppdtSKADRAQVVAQVLDELGLTKhgDTRVDK----LSGGQRKRASVALELLTGPSLLILDE 449
Cdd:PRK13637   97 feeTIEKDIAFGpINLGL----SEEEIENRVKRAMNIVGLDY--EDYKDKspfeLSGGQKRRVAIAGVVAMEPKILILDE 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADA-GRVVLVVTHSLTylDVC---DQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK13637  171 PTAGLDPKGRDEILNKIKELHKEyNMTIILVSHSME--DVAklaDRIIVMN-KGKCELQGTPREV 232
PRK03695 PRK03695
vitamin B12-transporter ATPase; Provisional
 305-524 3.08e-17

vitamin B12-transporter ATPase; Provisional


Pssm-ID: 235150 [Multi-domain]  Cd Length: 248  Bit Score: 82.29  E-value: 3.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGyATPTTGSVTFEGHNIHT-EYGSLRTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:PRK03695   12 LGPLSAEVRAGEILHLVGPNGAGKSTLLARMAG-LLPGSGSIQFAGQPLEAwSAAELARHRAYLSQQQTPPFAMPVFQYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 gyaaELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGG--QRKR-ASVALEL--LTGPS--LLILDEPTSGLDP 456
Cdd:PRK03695   91 ----TLHQPDKTRTEAVASALNEVAEALGLDDKLGRSVNQLSGGewQRVRlAAVVLQVwpDINPAgqLLLLDEPMNSLDV 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 457 ALDLQVMTMLRQLADAGRVVLVVTHSLTY-LDVCDQVLLMAPGGKTAYlGPPDQIggaMGTTNWAQIFA 524
Cdd:PRK03695  167 AQQAALDRLLSELCQQGIAVVMSSHDLNHtLRHADRVWLLKQGKLLAS-GRRDEV---LTPENLAQVFG 231
TagH COG1134
ABC-type polysaccharide/polyol phosphate transport system, ATPase component [Carbohydrate ...
 305-510 3.49e-17

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


Pssm-ID: 440749 [Multi-domain]  Cd Length: 245  Bit Score: 81.67  E-value: 3.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhNIHT--EYGSlrtriGMVPqddvvhrQLTV--N 380
Cdd:COG1134    42 LKDVSFEVERGESVGIIGRNGAGKSTLLKLIAGILEPTSGRVEVNG-RVSAllELGA-----GFHP-------ELTGreN 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 -----QALGYaaelrlppdtSKADRAQVVAQVLD--ELGltKHGDTRVDKLSGGQRKR----ASVALElltgPSLLILDE 449
Cdd:COG1134   109 iylngRLLGL----------SRKEIDEKFDEIVEfaELG--DFIDQPVKTYSSGMRARlafaVATAVD----PDILLVDE 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG1134   173 VLAVGDAAFQKKCLARIRELRESGRTVIFVSHSMGAVrRLCDRAIWLE-KGRLVMDGDPEEV 233
PRK13540 PRK13540
cytochrome c biogenesis protein CcmA; Provisional
 290-490 3.60e-17

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184127 [Multi-domain]  Cd Length: 200  Bit Score: 80.76  E-value: 3.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQ 369
Cdd:PRK13540    2 LDVIELDFDYHDQPLLQQISFHLPAGGLLHLKGSNGAGKTTLLKLIAGLLNPEKGEILFERQSIKKDLCTYQKQLCFVGH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYaaelrlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:PRK13540   82 RSGINPYLTLRENCLY--------DIHFSPGAVGITELCRLFSLEHLIDYPCGLLSSGQKRQVALLRLWMSKAKLWLLDE 153

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCD 490
Cdd:PRK13540  154 PLVALDELSLLTIITKIQEHRAKGGAVLLTSHQDLPLNKAD 194
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
305-498 6.19e-17

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 84.84  E-value: 6.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEG-------HNIHTEYGslrtrIGMVPQDDVVHRQL 377
Cdd:PRK09700   21 LKSVNLTVYPGEIHALLGENGAGKSTLMKVLSGIHEPTKGTITINNinynkldHKLAAQLG-----IGIIYQELSVIDEL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TVNQALgYAAelRLP-------PDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:PRK09700   96 TVLENL-YIG--RHLtkkvcgvNIIDWREMRVRAAMMLLRVGLKVDLDEKVANLSISHKQMLEIAKTLMLDAKVIIMDEP 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1184609190 451 TSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK09700  173 TSSLTNKEVDYLFLIMNQLRKEGTAIVYISHKLAEIrRICDRYTVMKDG 221
PRK15079 PRK15079
oligopeptide ABC transporter ATP-binding protein OppF; Provisional
 290-511 8.90e-17

oligopeptide ABC transporter ATP-binding protein OppF; Provisional


Pssm-ID: 185037 [Multi-domain]  Cd Length: 331  Bit Score: 82.45  E-value: 8.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVRE--VNFSIGDKNLL-----------ERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI--- 353
Cdd:PRK15079    9 LEVADlkVHFDIKDGKQWfwqppktlkavDGVTLRLYEGETLGVVGESGCGKSTFARAIIGLVKATDGEVAWLGKDLlgm 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 354 -HTEYGSLRTRIGMVPQDDV--VHRQLTVNQALgyAAELRL-PPDTSKADRAQVVAQVLDELGLTKHGDTRV-DKLSGGQ 428
Cdd:PRK15079   89 kDDEWRAVRSDIQMIFQDPLasLNPRMTIGEII--AEPLRTyHPKLSRQEVKDRVKAMMLKVGLLPNLINRYpHEFSGGQ 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 429 RKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMapggktaYLGP 506
Cdd:PRK15079  167 CQRIGIARALILEPKLIICDEPVSALDVSIQAQVVNLLQQLqREMGLSLIFIAHDLAVVKhISDRVLVM-------YLGH 239


                  ....*
gi 1184609190 507 PDQIG 511
Cdd:PRK15079  240 AVELG 244
PRK10584 PRK10584
putative ABC transporter ATP-binding protein YbbA; Provisional
 290-498 9.53e-17

putative ABC transporter ATP-binding protein YbbA; Provisional


Pssm-ID: 182569 [Multi-domain]  Cd Length: 228  Bit Score: 80.21  E-value: 9.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDK----NLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSLR 361
Cdd:PRK10584    7 VEVHHLKKSVGQGehelSILTGVELVVKRGETIALIGESGSGKSTLLAILAGLDDGSSGEVSLVGQPLHQmdeeARAKLR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TR-IGMVPQDDVVHRQLTVNQALGYAAELRLPPDTSKADRAqvvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLT 440
Cdd:PRK10584   87 AKhVGFVFQSFMLIPTLNALENVELPALLRGESSRQSRNGA---KALLEQLGLGKRLDHLPAQLSGGEQQRVALARAFNG 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK10584  164 RPDVLFADEPTGNLDRQTGDKIADLLFSLnREHGTTLILVTHDLQLAARCDRRLRLVNG 222
oppD PRK09473
oligopeptide transporter ATP-binding component; Provisional
 290-503 1.49e-16

oligopeptide transporter ATP-binding component; Provisional


Pssm-ID: 181888 [Multi-domain]  Cd Length: 330  Bit Score: 81.69  E-value: 1.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVRE--VNFSI--GDKNLLERVSLTARPGTLTAIIGGSGAGKT----TLSRLIAGYATpTTGSVTFEGHNI----HTEY 357
Cdd:PRK09473   13 LDVKDlrVTFSTpdGDVTAVNDLNFSLRAGETLGIVGESGSGKSqtafALMGLLAANGR-IGGSATFNGREIlnlpEKEL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 358 GSLRT-RIGMVPQDDV--------VHRQLTvnqalgyaAELRLPPDTSKADRAQVVAQVLD---------ELGLTKHgdt 419
Cdd:PRK09473   92 NKLRAeQISMIFQDPMtslnpymrVGEQLM--------EVLMLHKGMSKAEAFEESVRMLDavkmpearkRMKMYPH--- 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 420 rvdKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLA-DAGRVVLVVTHSLTYL-DVCDQVLLMAP 497
Cdd:PRK09473  161 ---EFSGGMRQRVMIAMALLCRPKLLIADEPTTALDVTVQAQIMTLLNELKrEFNTAIIMITHDLGVVaGICDKVLVMYA 237


                  ....*.
gi 1184609190 498 GGKTAY 503
Cdd:PRK09473  238 GRTMEY 243
ABCC_NFT1 cd03369
ATP-binding cassette domain 2 of NFT1, subfamily C; Domain 2 of NFT1 (New full-length MRP-type ...
 305-498 1.72e-16

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


Pssm-ID: 213269 [Multi-domain]  Cd Length: 207  Bit Score: 78.99  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-HTEYGSLRTRIGMVPQDDVVhrqltvnqal 383
Cdd:cd03369    24 LKNVSFKVKAGEKIGIVGRTGAGKSTLILALFRFLEAEEGKIEIDGIDIsTIPLEDLRSSLTIIPQDPTL---------- 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 gYAAELR--LPPDTSKADRaqvvaQVLDELGLTKHGDTrvdkLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQ 461
Cdd:cd03369    94 -FSGTIRsnLDPFDEYSDE-----EIYGALRVSEGGLN----LSQGQRQLLCLARALLKRPRVLVLDEATASIDYATDAL 163

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1184609190 462 VMTMLRQLAdAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03369   164 IQKTIREEF-TNSTILTIAHRLRTIIDYDKILVMDAG 199
PRK10070 PRK10070
proline/glycine betaine ABC transporter ATP-binding protein ProV;
309-510 2.62e-16

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


Pssm-ID: 182221 [Multi-domain]  Cd Length: 400  Bit Score: 82.00  E-value: 2.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 309 SLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS-----LRTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:PRK10070   48 SLAIEEGEIFVIMGLSGSGKSTMVRLLNRLIEPTRGQVLIDGVDIAKISDAelrevRRKKIAMVFQSFALMPHMTVLDNT 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 GYAAELRLPPdtsKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:PRK10070  128 AFGMELAGIN---AEERREKALDALRQVGLENYAHSYPDELSGGMRQRVGLARALAINPDILLMDEAFSALDPLIRTEMQ 204

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1184609190 464 TMLRQL-ADAGRVVLVVTHSL-TYLDVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK10070  205 DELVKLqAKHQRTIVFISHDLdEAMRIGDRIAIMQ-NGEVVQVGTPDEI 252
PRK15056 PRK15056
manganese/iron ABC transporter ATP-binding protein;
273-495 2.72e-16

manganese/iron ABC transporter ATP-binding protein;


Pssm-ID: 185016 [Multi-domain]  Cd Length: 272  Bit Score: 79.93  E-value: 2.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 273 TGGILVRRQEVAARTGGLEVREVNFSIGDknllervsltarpGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhn 352
Cdd:PRK15056    4 QAGIVVNDVTVTWRNGHTALRDASFTVPG-------------GSIAALVGVNGSGKSTLFKALMGFVRLASGKISILG-- 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 353 IHTEYGSLRTRIGMVPQDD-------VVHRQLTVNQALGYAAELRLPpdtsKADRAQVVAQVLDELGLTKHGDTRVDKLS 425
Cdd:PRK15056   69 QPTRQALQKNLVAYVPQSEevdwsfpVLVEDVVMMGRYGHMGWLRRA----KKRDRQIVTAALARVDMVEFRHRQIGELS 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 426 GGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLM 495
Cdd:PRK15056  145 GGQKKRVFLARAIAQQGQVILLDEPFTGVDVKTEARIISLLRELRDEGKTMLVSTHNLgSVTEFCDYTVMV 215
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 283-514 2.77e-16

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 82.79  E-value: 2.77e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 283 VAARTGGLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRT 362
Cdd:PRK15439    5 DTTAPPLLCARSISKQYSGVEVLKGIDFTLHAGEVHALLGGNGAGKSTLMKIIAGIVPPDSGTLEIGGNPCARLTPAKAH 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 363 RIG--MVPQDDVVHRQLTVNQALGYaaelRLPpdtSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLT 440
Cdd:PRK15439   85 QLGiyLVPQEPLLFPNLSVKENILF----GLP---KRQASMQKMKQLLAALGCQLDLDSSAGSLEVADRQIVEILRGLMR 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG-----GKTAYLgPPDQIGGAM 514
Cdd:PRK15439  158 DSRILILDEPTASLTPAETERLFSRIRELLAQGVGIVFISHKLPEIrQLADRISVMRDGtialsGKTADL-STDDIIQAI 236
PRK14258 PRK14258
phosphate ABC transporter ATP-binding protein; Provisional
 289-483 3.29e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184593 [Multi-domain]  Cd Length: 261  Bit Score: 79.31  E-value: 3.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTT----LSRL--IAGyATPTTGSVTFEGHNIH---TEYGS 359
Cdd:PRK14258    7 AIKVNNLSFYYDTQKILEGVSMEIYQSKVTAIIGPSGCGKSTflkcLNRMneLES-EVRVEGRVEFFNQNIYerrVNLNR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMV-PQDDVVHRQLTVNQA-----LGYAAELRLPPDTSKADRAqvvAQVLDELGLTKHGDTRvdKLSGGQRKRAS 433
Cdd:PRK14258   86 LRRQVSMVhPKPNLFPMSVYDNVAygvkiVGWRPKLEIDDIVESALKD---ADLWDEIKHKIHKSAL--DLSGGQQQRLC 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 434 VALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLV-VTHSL 483
Cdd:PRK14258  161 IARALAVKPKVLLMDEPCFGLDPIASMKVESLIQSLRLRSELTMViVSHNL 211
ABC_KpsT_Wzt cd03220
ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC ...
 263-498 3.51e-16

ATP-binding cassette component of polysaccharide transport system; The KpsT/Wzt ABC transporter subfamily is involved in extracellular polysaccharide export. Among the variety of membrane-linked or extracellular polysaccharides excreted by bacteria, only capsular polysaccharides, lipopolysaccharides, and teichoic acids have been shown to be exported by ABC transporters. A typical system is made of a conserved integral membrane and an ABC. In addition to these proteins, capsular polysaccharide exporter systems require two 'accessory' proteins to perform their function: a periplasmic (E.coli) or a lipid-anchored outer membrane protein called OMA (Neisseria meningitidis and Haemophilus influenza) and a cytoplasmic membrane protein MPA2.


Pssm-ID: 213187 [Multi-domain]  Cd Length: 224  Bit Score: 78.34  E-value: 3.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 263 VTIGNVDLVF----TGGILVRRQEVAARTGGLEVREVnfsigdknlLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGY 338
Cdd:cd03220     1 IELENVSKSYptykGGSSSLKKLGILGRKGEVGEFWA---------LKDVSFEVPRGERIGLIGRNGAGKSTLLRLLAGI 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 339 ATPTTGSVTFEGhNIHT--EYGSlrtriGMVPqddvvhrQLTV--NQALgYAAELRLppdtSKADRAQVVAQVLDELGLT 414
Cdd:cd03220    72 YPPDSGTVTVRG-RVSSllGLGG-----GFNP-------ELTGreNIYL-NGRLLGL----SRKEIDEKIDEIIEFSELG 133

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 415 KHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVL 493
Cdd:cd03220   134 DFIDLPVKTYSSGMKARLAFAIATALEPDILLIDEVLAVGDAAFQEKCQRRLRELLKQGKTVILVSHDPSSIkRLCDRAL 213


                  ....*
gi 1184609190 494 LMAPG 498
Cdd:cd03220   214 VLEKG 218
cbiO PRK13645
energy-coupling factor transporter ATPase;
305-510 3.67e-16

energy-coupling factor transporter ATPase;


Pssm-ID: 184204 [Multi-domain]  Cd Length: 289  Bit Score: 80.05  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT------EYGSLRTRIGMV---PQDDVVHR 375
Cdd:PRK13645   27 LNNTSLTFKKNKVTCVIGTTGSGKSTMIQLTNGLIISETGQTIVGDYAIPAnlkkikEVKRLRKEIGLVfqfPEYQLFQE 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 376 QLTVNQALGyaaelrlpPDTSKADRAQVVAQVLDELGLTKHGDTRVDK----LSGGQRKRASVALELLTGPSLLILDEPT 451
Cdd:PRK13645  107 TIEKDIAFG--------PVNLGENKQEAYKKVPELLKLVQLPEDYVKRspfeLSGGQKRRVALAGIIAMDGNTLVLDEPT 178

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 452 SGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSL-TYLDVCDQVLLMAPgGKTAYLGPPDQI 510
Cdd:PRK13645  179 GGLDPKGEEDFINLFERLnKEYKKRIIMVTHNMdQVLRIADEVIVMHE-GKVISIGSPFEI 238
modC PRK11144
molybdenum ABC transporter ATP-binding protein ModC;
294-503 4.59e-16

molybdenum ABC transporter ATP-binding protein ModC;


Pssm-ID: 182993 [Multi-domain]  Cd Length: 352  Bit Score: 80.69  E-value: 4.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 294 EVNFS--IGDKNLLERVSLTARpgTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGH---------NIHTEygslRT 362
Cdd:PRK11144    3 ELNFKqqLGDLCLTVNLTLPAQ--GITAIFGRSGAGKTSLINAISGLTRPQKGRIVLNGRvlfdaekgiCLPPE----KR 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 363 RIGMVPQDDVVHRQLTVNQALGYAaelrlppdTSKADRAQvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGP 442
Cdd:PRK11144   77 RIGYVFQDARLFPHYKVRGNLRYG--------MAKSMVAQ-FDKIVALLGIEPLLDRYPGSLSGGEKQRVAIGRALLTAP 147

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 443 SLLILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTHSL-TYLDVCDQVLLMAPGGKTAY 503
Cdd:PRK11144  148 ELLLMDEPLASLDLPRKRELLPYLERLAREINIpILYVSHSLdEILRLADRVVVLEQGKVKAF 210
PhnL COG4778
Alpha-D-ribose 1-methylphosphonate 5-triphosphate synthase subunit PhnL [Inorganic ion ...
 305-498 5.57e-16

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: 77.86  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFeghnihteygslRTRIGMVpqdDVVH---RQLTV-- 379
Cdd:COG4778    27 LDGVSFSVAAGECVALTGPSGAGKSTLLKCIYGNYLPDSGSILV------------RHDGGWV---DLAQaspREILAlr 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAE-LRLPPDTSKADraqVVAQVLDELGLTKH-GDTRVDKL------------------SGGQRKRASVALELL 439
Cdd:COG4778    92 RRTIGYVSQfLRVIPRVSALD---VVAEPLLERGVDREeARARARELlarlnlperlwdlppatfSGGEQQRVNIARGFI 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:COG4778   169 ADPPLLLLDEPTASLDAANRAVVVELIEEAKARGTAIIGIFHDEEVREaVADRVVDVTPF 228
PRK14271 PRK14271
phosphate ABC transporter ATP-binding protein; Provisional
 295-535 9.90e-16

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172759 [Multi-domain]  Cd Length: 276  Bit Score: 78.21  E-value: 9.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 295 VNFSIG--DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRL-------IAGYATptTGSVTFEGHNI--HTEYGSLRTR 363
Cdd:PRK14271   25 VNLTLGfaGKTVLDQVSMGFPARAVTSLMGPTGSGKTTFLRTlnrmndkVSGYRY--SGDVLLGGRSIfnYRDVLEFRRR 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 364 IGMVPQDDVVHRQLTVNQALGYAAELRLPPdtsKADRAQVVAQVLDELGLTKHGDTRVD----KLSGGQRKRASVALELL 439
Cdd:PRK14271  103 VGMLFQRPNPFPMSIMDNVLAGVRAHKLVP---RKEFRGVAQARLTEVGLWDAVKDRLSdspfRLSGGQQQLLCLARTLA 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAgRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQIGGAMGTTNW 519
Cdd:PRK14271  180 VNPEVLLLDEPTSALDPTTTEKIEEFIRSLADR-LTVIIVTHNLAQAARISDRAALFFDGRLVEEGPTEQLFSSPKHAET 258

                         250
                  ....*....|....*.
gi 1184609190 520 AQIFAKVGADPDEANR 535
Cdd:PRK14271  259 ARYVAGLSGDVKDAKR 274
PRK09984 PRK09984
phosphonate ABC transporter ATP-binding protein;
305-498 1.45e-15

phosphonate ABC transporter ATP-binding protein;


Pssm-ID: 182182 [Multi-domain]  Cd Length: 262  Bit Score: 77.75  E-value: 1.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSR----LIAGYATPTTgSVTFEGHNIHTEyGSL-------RTRIGMVPQDDVV 373
Cdd:PRK09984   20 LHAVDLNIHHGEMVALLGPSGSGKSTLLRhlsgLITGDKSAGS-HIELLGRTVQRE-GRLardirksRANTGYIFQQFNL 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 374 HRQLTVNQ-----ALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILD 448
Cdd:PRK09984   98 VNRLSVLEnvligALGSTPFWRTCFSWFTREQKQRALQALTRVGMVHFAHQRVSTLSGGQQQRVAIARALMQQAKVILAD 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 449 EPTSGLDPALDLQVMTMLRQLADAGRVVLVVT-HSLTY-LDVCDQVLLMAPG 498
Cdd:PRK09984  178 EPIASLDPESARIVMDTLRDINQNDGITVVVTlHQVDYaLRYCERIVALRQG 229
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 308-498 1.63e-15

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: 80.25  E-value: 1.63e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAG-YATPTTGSVTFEGH--NIHTEYGSLRTRIGMVPQDDVVH---RQLTVNQ 381
Cdd:TIGR02633 279 VSFSLRRGEILGVAGLVGAGRTELVQALFGaYPGKFEGNVFINGKpvDIRNPAQAIRAGIAMVPEDRKRHgivPILGVGK 358

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 382 ALGYAAELRLPPDTSKADRA--QVVAQVLDELGL-TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPAL 458
Cdd:TIGR02633 359 NITLSVLKSFCFKMRIDAAAelQIIGSAIQRLKVkTASPFLPIGRLSGGNQQKAVLAKMLLTNPRVLILDEPTRGVDVGA 438

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1184609190 459 DLQVMTMLRQLADAGRVVLVVTHSLT-YLDVCDQVLLMAPG 498
Cdd:TIGR02633 439 KYEIYKLINQLAQEGVAIIVVSSELAeVLGLSDRVLVIGEG 479
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
305-492 2.07e-15

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 79.96  E-value: 2.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHteYGSLRTRI--GMVpqddVVHRQL----- 377
Cdd:PRK11288   20 LDDISFDCRAGQVHALMGENGAGKSTLLKILSGNYQPDAGSILIDGQEMR--FASTTAALaaGVA----IIYQELhlvpe 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 -TV--NQALGyaaelRLPPDTSKADRAQVVAQV---LDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPT 451
Cdd:PRK11288   94 mTVaeNLYLG-----QLPHKGGIVNRRLLNYEAreqLEHLGVDIDPDTPLKYLSIGQRQMVEIAKALARNARVIAFDEPT 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1184609190 452 SGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQV 492
Cdd:PRK11288  169 SSLSAREIEQLFRVIRELRAEGRVILYVSHRMEEIFaLCDAI 210
ABCC_MRP_domain1 cd03250
ATP-binding cassette domain 1 of multidrug resistance-associated protein, subfamily C; This ...
 290-498 2.56e-15

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


Pssm-ID: 213217 [Multi-domain]  Cd Length: 204  Bit Score: 75.20  E-value: 2.56e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKN-----LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihteygslrtRI 364
Cdd:cd03250     1 ISVEDASFTWDSGEqetsfTLKDINLEVPKGELVAIVGPVGSGKSSLLSALLGELEKLSGSVSVPG------------SI 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQddvvhrqltvnQALGYAAELR------LPPDTSKADRAQVVAQVLDELGLTKHGD-TRV-DK---LSGGQRKRAS 433
Cdd:cd03250    69 AYVSQ-----------EPWIQNGTIRenilfgKPFDEERYEKVIKACALEPDLEILPDGDlTEIgEKginLSGGQKQRIS 137

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 434 VALELLTGPSLLILDEPTSGLDPALDLQVMTM-LRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03250   138 LARAVYSDADIYLLDDPLSAVDAHVGRHIFENcILGLLLNNKTRILVTHQLQLLPHADQIVVLDNG 203
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 195-272 3.73e-15

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 71.64  E-value: 3.73e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 195 LEAPVTGAawiGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVF 272
Cdd:cd22684    18 LDQDVTTA---GRHPESDIFLDDVTVSRRHAEFRRAEGGFVVRDVGSLNGTYVNRERIDSAVLRNGDEVQIGKFRLVF 92
PRK14243 PRK14243
phosphate transporter ATP-binding protein; Provisional
 290-483 3.82e-15

phosphate transporter ATP-binding protein; Provisional


Pssm-ID: 184588 [Multi-domain]  Cd Length: 264  Bit Score: 76.36  E-value: 3.82e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSR-------LIAGYATptTGSVTFEGHNI---HTEYGS 359
Cdd:PRK14243   11 LRTENLNVYYGSFLAVKNVWLDIPKNQITAFIGPSGCGKSTILRcfnrlndLIPGFRV--EGKVTFHGKNLyapDVDPVE 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQDDVVHRQlTVNQALGYAAELrlppDTSKADRAQVVAQVLDELGLTkhgDTRVDKL-------SGGQRKRA 432
Cdd:PRK14243   89 VRRRIGMVFQKPNPFPK-SIYDNIAYGARI----NGYKGDMDELVERSLRQAALW---DEVKDKLkqsglslSGGQQQRL 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 433 SVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVlVVTHSL 483
Cdd:PRK14243  161 CIARAIAVQPEVILMDEPCSALDPISTLRIEELMHELKEQYTII-IVTHNM 210
YadH COG0842
ABC-type multidrug transport system, permease component [Defense mechanisms];
623-832 5.52e-15

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


Pssm-ID: 440604 [Multi-domain]  Cd Length: 200  Bit Score: 74.47  E-value: 5.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 623 ILTLTSVAAVFMGTALTI-RDLigERAIFRREQAVGLSTGAYLAAKLAVFCVFAVVQAAIVTVIVLVGKGAPtqpavLLG 701
Cdd:COG0842     9 LLAMSLLFTALMLTALSIaRER--EQGTLERLLVTPVSRLEILLGKVLAYLLRGLLQALLVLLVALLFFGVP-----LRG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 702 NPSFELFVTIAAMCVASAVLGLVLSSLARSSEQIMPLLVVSLMLQLVLAGGMVPVTG-RIFLDQLSWLLPSRWGyaasas 780
Cdd:COG0842    82 LSLLLLLLVLLLFALAFSGLGLLISTLARSQEQASAISNLVILPLTFLSGAFFPIESlPGWLQAIAYLNPLTYF------ 155

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 781 tvnVRLLVPGSLVQQDshwahtPAAWLLDMGMLVALSVLYAAIVRWRIRLRR 832
Cdd:COG0842   156 ---VEALRALFLGGAG------LADVWPSLLVLLAFAVVLLALALRLFRRRL 198
PRK13651 PRK13651
cobalt transporter ATP-binding subunit; Provisional
 305-493 5.81e-15

cobalt transporter ATP-binding subunit; Provisional


Pssm-ID: 184210 [Multi-domain]  Cd Length: 305  Bit Score: 76.66  E-value: 5.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS------------------------- 359
Cdd:PRK13651   23 LDNVSVEINQGEFIAIIGQTGSGKTTFIEHLNALLLPDTGTIEWIFKDEKNKKKTkekekvleklviqktrfkkikkike 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQddVVHRQL---TVNQALGYAAelrLPPDTSKADRAQVVAQVLDELGLTKHGDTRVD-KLSGGQRKRASVA 435
Cdd:PRK13651  103 IRRRVGVVFQ--FAEYQLfeqTIEKDIIFGP---VSMGVSKEEAKKRAAKYIELVGLDESYLQRSPfELSGGQKRRVALA 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 436 LELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLtyldvcDQVL 493
Cdd:PRK13651  178 GILAMEPDFLVFDEPTAGLDPQGVKEILEIFDNLNKQGKTIILVTHDL------DNVL 229
FHA cd00060
forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small ...
 22-90 6.67e-15

forkhead associated (FHA) domain superfamily; Forkhead-associated (FHA) domains are small phosphopeptide recognition modules mostly found in eubacteria and eukaryotes. It is about 95-120 residues long that fold into an 11-stranded beta-sandwich. FHA domains can mediate the recognition of phosphorylated and non-phosphorylated substrates, as well as protein oligomerization. They specifically recognize threonine phosphorylation (pThr) accompanying activation of protein serine/threonine kinases. FHA domains show diverse ligand specificity. They may recognize the pTXXD motif, the pTXXI/L motif, and TQ clusters (singly and multiply phosphorylated). In eukaryotes, FHA superfamily members include forkhead-type transcription factors, as well as other signaling proteins, such as many regulatory proteins, kinases, phosphatases, motor proteins called kinesins, and metabolic enzymes. Many of them localize to the nucleus, where they participate in establishing or maintaining cell cycle checkpoints, DNA repair, or transcriptional regulation. FHA domains play important roles in human diseases, particularly in relation to DNA damage responses and cancers. In bacteria, FHA domain-containing proteins may participate in injection of viral proteins into host cells, transmembrane transporters, and cell division. FHA domain-containing proteins rarely include more than one copy of the domain. The only exception in eukaryotes is the checkpoint kinase Rad53 from Saccharomyces cerevisiae, which harbors two FHA domains (FHA1 and FHA2) flanking a central kinase domain. The two FHA domains recognize different phosphorylated targets and function independently from one another. In contrast, Mycobacterium tuberculosis ABC transporter Rv1747 contains two FHA domains but only one of them is essential for protein function.


Pssm-ID: 438714 [Multi-domain]  Cd Length: 92  Bit Score: 70.77  E-value: 6.67e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRV-PAVDIQDGQSVNIGK 90
Cdd:cd00060    17 TKGVVTIGRSPDCDIVLDDPSVSRRHARIEVDGGGVYLEDLGSTNGTFVNGKRItPPVPLQDGDVIRLGD 86
PRK13633 PRK13633
energy-coupling factor transporter ATPase;
305-510 7.55e-15

energy-coupling factor transporter ATPase;


Pssm-ID: 237453 [Multi-domain]  Cd Length: 280  Bit Score: 75.89  E-value: 7.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYG--SLRTRIGMV---PQDDVVHRQLTV 379
Cdd:PRK13633   26 LDDVNLEVKKGEFLVILGRNGSGKSTIAKHMNALLIPSEGKVYVDGLDTSDEENlwDIRNKAGMVfqnPDNQIVATIVEE 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGyAAELRLPPDTSKADraqvVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:PRK13633  106 DVAFG-PENLGIPPEEIRER----VDESLKKVGMYEYRRHAPHLLSGGQKQRVAIAGILAMRPECIIFDEPTAMLDPSGR 180

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 460 LQVMTMLRQLAD-AGRVVLVVTHSLTYLDVCDQVLLMaPGGKTAYLGPPDQI 510
Cdd:PRK13633  181 REVVNTIKELNKkYGITIILITHYMEEAVEADRIIVM-DSGKVVMEGTPKEI 231
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
307-595 1.10e-14

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 78.24  E-value: 1.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 307 RVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTVNQALGYA 386
Cdd:NF033858  284 HVSFRIRRGEIFGFLGSNGCGKSTTMKMLTGLLPASEGEAWLFGQPVDAGDIATRRRVGYMSQAFSLYGELTVRQNLELH 363

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 387 AEL-RLPPdtskADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTM 465
Cdd:NF033858  364 ARLfHLPA----AEIAARVAEMLERFDLADVADALPDSLPLGIRQRLSLAVAVIHKPELLILDEPTSGVDPVARDMFWRL 439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 466 LRQLADAGRV-VLVVTHSLTYLDVCDQVLLM-ApgGKTAYLGPPDQIGGAMGTTNWAQIFAKVGADPDEAnrrflAQNKP 543
Cdd:NF033858  440 LIELSREDGVtIFISTHFMNEAERCDRISLMhA--GRVLASDTPAALVAARGAATLEEAFIAYLEEAAGA-----AAAPA 512

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 544 PPPVESAPADLGAPAHTSVRHQFS-----TIARRQVRLVVSD--RAYFVFL--ALLPFVLG 595
Cdd:NF033858  513 AAAAPAAAAAAPAAPAPAPRRRFSlrrllAYARREALELLRDpiRLTFALLgsVILMFVMG 573
PRK10790 PRK10790
SmdB family multidrug efflux ABC transporter permease/ATP-binding protein;
287-498 1.25e-14

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


Pssm-ID: 182733 [Multi-domain]  Cd Length: 592  Bit Score: 77.84  E-value: 1.25e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 287 TGGLEVREVNFSI-GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT-EYGSLRTRI 364
Cdd:PRK10790  338 SGRIDIDNVSFAYrDDNLVLQNINLSVPSRGFVALVGHTGSGKSTLASLLMGYYPLTEGEIRLDGRPLSSlSHSVLRQGV 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 365 GMVPQDDVVhrqltvnQALGYAAELRLPPDTSKADRAQVVAQV-LDEL--GLTKHGDTRV----DKLSGGQRKRASVALE 437
Cdd:PRK10790  418 AMVQQDPVV-------LADTFLANVTLGRDISEEQVWQALETVqLAELarSLPDGLYTPLgeqgNNLSVGQKQLLALARV 490

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVlVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK10790  491 LVQTPQILILDEATANIDSGTEQAIQQALAAVREHTTLV-VIAHRLSTIVEADTILVLHRG 550
ABC_RNaseL_inhibitor_domain1 cd03236
The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 313-503 1.75e-14

The ATP-binding cassette domain 1 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI s are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLIs have an N-terminal Fe-S domain and two nucleotide binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213203 [Multi-domain]  Cd Length: 255  Bit Score: 74.33  E-value: 1.75e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 313 RPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVT-----------FEGHNIHTEYGSLR---TRIGMVPQddvvHRQLT 378
Cdd:cd03236    24 REGQVLGLVGPNGIGKSTALKILAGKLKPNLGKFDdppdwdeildeFRGSELQNYFTKLLegdVKVIVKPQ----YVDLI 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAELrlppdTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPAL 458
Cdd:cd03236   100 PKAVKGKVGEL-----LKKKDERGKLDELVDQLELRHVLDRNIDQLSGGELQRVAIAAALARDADFYFFDEPSSYLDIKQ 174

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1184609190 459 DLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAY 503
Cdd:cd03236   175 RLNAARLIRELAEDDNYVLVVEHDLAVLDYLSDYIHCLYGEPGAY 219
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 290-487 2.61e-14

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 76.70  E-value: 2.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVtfeghnihteygslrtRIGmvpq 369
Cdd:PRK11819  325 IEAENLSKSFGDRLLIDDLSFSLPPGGIVGIIGPNGAGKSTLFKMITGQEQPDSGTI----------------KIG---- 384

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 dDVVHrqltvnqaLGYAAELR--LPPDTSKadrAQVVAQVLDELGLTKH---------------GD--TRVDKLSGGQRK 430
Cdd:PRK11819  385 -ETVK--------LAYVDQSRdaLDPNKTV---WEEISGGLDIIKVGNReipsrayvgrfnfkgGDqqKKVGVLSGGERN 452

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 431 RASVALELLTGPSLLILDEPTSgldpalDLQVMTmLRQLADA-----GRVVlVVTHSLTYLD 487
Cdd:PRK11819  453 RLHLAKTLKQGGNVLLLDEPTN------DLDVET-LRALEEAllefpGCAV-VISHDRWFLD 506
ycf16 CHL00131
sulfate ABC transporter protein; Validated
 290-498 2.97e-14

sulfate ABC transporter protein; Validated


Pssm-ID: 214372 [Multi-domain]  Cd Length: 252  Bit Score: 73.52  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYA--TPTTGSVTFEGHNIHTEYGSLRTRIGmv 367
Cdd:CHL00131    8 LEIKNLHASVNENEILKGLNLSINKGEIHAIMGPNGSGKSTLSKVIAGHPayKILEGDILFKGESILDLEPEERAHLG-- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 pqddvvhrqltVNQALGYAAE---------LRLP----------PDTSKADRAQVVAQVLDELGLTKHGDTRV--DKLSG 426
Cdd:CHL00131   86 -----------IFLAFQYPIEipgvsnadfLRLAynskrkfqglPELDPLEFLEIINEKLKLVGMDPSFLSRNvnEGFSG 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 427 GQRKRASVALELLTGPSLLILDEPTSGLD-PALDlQVMTMLRQLADAGRVVLVVTHSLTYLD--VCDQVLLMAPG 498
Cdd:CHL00131  155 GEKKRNEILQMALLDSELAILDETDSGLDiDALK-IIAEGINKLMTSENSIILITHYQRLLDyiKPDYVHVMQNG 228
NupO COG3845
ABC-type guanosine uptake system NupNOPQ, ATPase component NupO [Nucleotide transport and ...
 274-515 4.67e-14

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


Pssm-ID: 443055 [Multi-domain]  Cd Length: 504  Bit Score: 75.45  E-value: 4.67e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 274 GGILVRRQEVAARTGG---LEVREVNFsIGDKNL--LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTF 348
Cdd:COG3845   239 GREVLLRVEKAPAEPGevvLEVENLSV-RDDRGVpaLKDVSLEVRAGEILGIAGVAGNGQSELAEALAGLRPPASGSIRL 317

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 349 EGHNIHTEYGSLRTRIGM--VPQDdvvhRQ-------LTV--NQALGYaaeLRLPPDTSKA--DRAQVVA---QVLDELG 412
Cdd:COG3845   318 DGEDITGLSPRERRRLGVayIPED----RLgrglvpdMSVaeNLILGR---YRRPPFSRGGflDRKAIRAfaeELIEEFD 390

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 413 L-TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLT-YLDVCD 490
Cdd:COG3845   391 VrTPGPDTPARSLSGGNQQKVILARELSRDPKLLIAAQPTRGLDVGAIEFIHQRLLELRDAGAAVLLISEDLDeILALSD 470

                         250       260       270
                  ....*....|....*....|....*....|
gi 1184609190 491 QVLLMApGGKTAYLGPPD-----QIGGAMG 515
Cdd:COG3845   471 RIAVMY-EGRIVGEVPAAeatreEIGLLMA 499
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 290-498 6.45e-14

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 75.35  E-value: 6.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVRevNFSIGDKNLLER-----VSLTARPGTLTAIIGGSGAGKTTLSRLIAG-YATPTTGSVTFEGH--NIHTEYGSLR 361
Cdd:PRK13549  260 LEVR--NLTAWDPVNPHIkrvddVSFSLRRGEILGIAGLVGAGRTELVQCLFGaYPGRWEGEIFIDGKpvKIRNPQQAIA 337

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQD----------DVVH-------RQLTVNQALGYAAELRlppdtskadraqVVAQVLDELGL-TKHGDTRVDK 423
Cdd:PRK13549  338 QGIAMVPEDrkrdgivpvmGVGKnitlaalDRFTGGSRIDDAAELK------------TILESIQRLKVkTASPELAIAR 405

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 424 LSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:PRK13549  406 LSGGNQQKAVLAKCLLLNPKILILDEPTRGIDVGAKYEIYKLINQLVQQGVAIIVISSELpEVLGLSDRVLVMHEG 481
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 282-487 8.57e-14

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 74.99  E-value: 8.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 282 EVAARTGGL--EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVT---------FEG 350
Cdd:PRK11147  310 EEASRSGKIvfEMENVNYQIDGKQLVKDFSAQVQRGDKIALIGPNGCGKTTLLKLMLGQLQADSGRIHcgtklevayFDQ 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 351 HnihteygslrtRIGMVPQDDVV------HRQLTVN----QALGYAAELRLPPdtskaDRAQvvaqvldelgltkhgdTR 420
Cdd:PRK11147  390 H-----------RAELDPEKTVMdnlaegKQEVMVNgrprHVLGYLQDFLFHP-----KRAM----------------TP 437

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 421 VDKLSGGQRKRASVALELLTGPSLLILDEPTSGldpaLDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD 487
Cdd:PRK11147  438 VKALSGGERNRLLLARLFLKPSNLLILDEPTND----LDVETLELLEELlDSYQGTVLLVSHDRQFVD 501
PRK15134 PRK15134
microcin C ABC transporter ATP-binding protein YejF; Provisional
 283-498 9.54e-14

microcin C ABC transporter ATP-binding protein YejF; Provisional


Pssm-ID: 237917 [Multi-domain]  Cd Length: 529  Bit Score: 74.74  E-value: 9.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 283 VAARTGGlEVREVnfsigdknlLERVSLTARPGTLTAIIGGSGAGK--TTLSRLIAGYATP---TTGSVTFEGHNI-HTE 356
Cdd:PRK15134   13 VAFRQQQ-TVRTV---------VNDVSLQIEAGETLALVGESGSGKsvTALSILRLLPSPPvvyPSGDIRFHGESLlHAS 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 357 YGSLR----TRIGMVPQDDVV--------HRQLTvnQALGYAAELRlppdtSKADRAQVVaQVLDELGLtKHGDTRVD-- 422
Cdd:PRK15134   83 EQTLRgvrgNKIAMIFQEPMVslnplhtlEKQLY--EVLSLHRGMR-----REAARGEIL-NCLDRVGI-RQAAKRLTdy 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 423 --KLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK15134  154 phQLSGGERQRVMIAMALLTRPELLIADEPTTALDVSVQAQILQLLRELqQELNMGLLFITHNLSIVrKLADRVAVMQNG 233
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 313-495 1.07e-13

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 74.82  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 313 RPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVT-----------FEGHNIHTEYGSLR---TRIGMVPQD-DVVHRQL 377
Cdd:COG1245    97 KKGKVTGILGPNGIGKSTALKILSGELKPNLGDYDeepswdevlkrFRGTELQDYFKKLAngeIKVAHKPQYvDLIPKVF 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 --TVNQALgyaaelrlppdtSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:COG1245   177 kgTVRELL------------EKVDERGKLDELAEKLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPSSYLD 244

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1184609190 456 PALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLM 495
Cdd:COG1245   245 IYQRLNVARLIRELAEEGKYVLVVEHDLAILDyLADYVHIL 285
sufC PRK09580
cysteine desulfurase ATPase component; Reviewed
 290-487 1.19e-13

cysteine desulfurase ATPase component; Reviewed


Pssm-ID: 181965 [Multi-domain]  Cd Length: 248  Bit Score: 71.75  E-value: 1.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYA--TPTTGSVTFEGHNIHTEYGSLRTRIG-- 365
Cdd:PRK09580    2 LSIKDLHVSVEDKAILRGLNLEVRPGEVHAIMGPNGSGKSTLSATLAGREdyEVTGGTVEFKGKDLLELSPEDRAGEGif 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQDDV----VHRQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKL--SGGQRKRASVALELL 439
Cdd:PRK09580   82 MAFQYPVeipgVSNQFFLQTALNAVRSYRGQEPLDRFDFQDLMEEKIALLKMPEDLLTRSVNVgfSGGEKKRNDILQMAV 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1184609190 440 TGPSLLILDEPTSGLD-PALDLqVMTMLRQLADAGRVVLVVTHSLTYLD 487
Cdd:PRK09580  162 LEPELCILDESDSGLDiDALKI-VADGVNSLRDGKRSFIIVTHYQRILD 209
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 205-265 1.94e-13

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 65.68  E-value: 1.94e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGT-EIRDAHSINGTFVNGIRVGS--AVLAEGDVVTI 265
Cdd:pfam00498   3 IGRSPDCDIVLDDPSVSRRHAEIRYDGGGRfYLEDLGSTNGTFVNGQRLGPepVRLKDGDVIRL 66
PRK10522 PRK10522
multidrug transporter membrane component/ATP-binding component; Provisional
 290-498 2.04e-13

multidrug transporter membrane component/ATP-binding component; Provisional


Pssm-ID: 236707 [Multi-domain]  Cd Length: 547  Bit Score: 73.85  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL-LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTE-YGSLRTRIGMV 367
Cdd:PRK10522  323 LELRNVTFAYQDNGFsVGPINLTIKRGELLFLIGGNGSGKSTLAMLLTGLYQPQSGEILLDGKPVTAEqPEDYRKLFSAV 402

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQDdvVHrqlTVNQALGyaaelrlpPDTSKADRAQvVAQVLDELGL---TKHGDTRVD--KLSGGQRKRASVALELLTGP 442
Cdd:PRK10522  403 FTD--FH---LFDQLLG--------PEGKPANPAL-VEKWLERLKMahkLELEDGRISnlKLSKGQKKRLALLLALAEER 468

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 443 SLLILDEPTSGLDPALD---LQVmtMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK10522  469 DILLLDEWAADQDPHFRrefYQV--LLPLLQEMGKTIFAISHDDHYFIHADRLLEMRNG 525
FHA COG1716
Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];
22-101 2.12e-13

Forkhead associated (FHA) domain, binds pSer, pThr, pTyr [Signal transduction mechanisms];


Pssm-ID: 441322 [Multi-domain]  Cd Length: 96  Bit Score: 66.52  E-value: 2.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVP-AVDIQDGQSVNIGKpdgPLITFHV 100
Cdd:COG1716    19 DGGPLTIGRAPDNDIVLDDPTVSRRHARIRRDGGGWVLEDLGSTNGTFVNGQRVTePAPLRDGDVIRLGK---TELRFRL 95


                  .
gi 1184609190 101 G 101
Cdd:COG1716    96 S 96
PRK14246 PRK14246
phosphate ABC transporter ATP-binding protein; Provisional
 299-498 2.29e-13

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 172734 [Multi-domain]  Cd Length: 257  Bit Score: 70.85  E-value: 2.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 299 IGDKNLLERVSLTARPGTLTAIIGGSGAGKTTL----SRLIAGYATP--TTGSVTFEGHNI-HTEYGSLRTRIGMVPQDD 371
Cdd:PRK14246   20 INDKAILKDITIKIPNNSIFGIMGPSGSGKSTLlkvlNRLIEIYDSKikVDGKVLYFGKDIfQIDAIKLRKEVGMVFQQP 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 372 VVHRQLTVNQALGYAaeLRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVD----KLSGGQRKRASVALELLTGPSLLIL 447
Cdd:PRK14246  100 NPFPHLSIYDNIAYP--LKSHGIKEKREIKKIVEECLRKVGLWKEVYDRLNspasQLSGGQQQRLTIARALALKPKVLLM 177

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PRK14246  178 DEPTSMIDIVNSQAIEKLITELKNEIAIVIVSHNPQQVARVADYVAFLYNG 228
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
313-492 3.47e-13

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 73.30  E-value: 3.47e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 313 RPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVT-----------FEGHNIHTEYGSLRT---RIGMVPQD-DVVHRQL 377
Cdd:PRK13409   97 KEGKVTGILGPNGIGKTTAVKILSGELIPNLGDYEeepswdevlkrFRGTELQNYFKKLYNgeiKVVHKPQYvDLIPKVF 176

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 --TVNQALgyaaelrlppdtSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:PRK13409  177 kgKVRELL------------KKVDERGKLDEVVERLGLENILDRDISELSGGELQRVAIAAALLRDADFYFFDEPTSYLD 244

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1184609190 456 PALDLQVMTMLRQLADaGRVVLVVTHSLTYLD-VCDQV 492
Cdd:PRK13409  245 IRQRLNVARLIRELAE-GKYVLVVEHDLAVLDyLADNV 281
ssuB PRK11247
aliphatic sulfonates transport ATP-binding subunit; Provisional
 290-498 3.61e-13

aliphatic sulfonates transport ATP-binding subunit; Provisional


Pssm-ID: 183055 [Multi-domain]  Cd Length: 257  Bit Score: 70.48  E-value: 3.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVtFEGHnihTEYGSLRTRIGMVPQ 369
Cdd:PRK11247   13 LLLNAVSKRYGERTVLNQLDLHIPAGQFVAVVGRSGCGKSTLLRLLAGLETPSAGEL-LAGT---APLAEAREDTRLMFQ 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTV--NQALGYAAELRlppdtskaDRAQvvaQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLIL 447
Cdd:PRK11247   89 DARLLPWKKVidNVGLGLKGQWR--------DAAL---QALAAVGLADRANEWPAALSGGQKQRVALARALIHRPGLLLL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 448 DEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLT-YLDVCDQVLLMAPG 498
Cdd:PRK11247  158 DEPLGALDALTRIEMQDLIESLwQQHGFTVLLVTHDVSeAVAMADRVLLIEEG 210
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 205-273 5.24e-13

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 65.51  E-value: 5.24e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVFT 273
Cdd:cd22698    25 IGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTFLNGIRVGTHELKHGDRIQLGETIFRFI 93
ABC_ABC_ChvD TIGR03719
ATP-binding cassette protein, ChvD family; Members of this protein family have two copies of ...
 300-487 6.60e-13

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: 72.28  E-value: 6.60e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFeghnihteygSLRTRIGMVPQDDVVHRQLTV 379
Cdd:TIGR03719  16 PKKEILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKDFNGEARP----------QPGIKVGYLPQEPQLDPTKTV 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQ-------------------ALGYA-------------AELRLPPDTSKA-DRAQVVAQVLDELGLTKhGDTRVDKLSG 426
Cdd:TIGR03719  86 REnveegvaeikdaldrfneiSAKYAepdadfdklaaeqAELQEIIDAADAwDLDSQLEIAMDALRCPP-WDADVTKLSG 164

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 427 GQRKRASVALELLTGPSLLILDEPTSGLDPAldlQVMTMLRQLADAGRVVLVVTHSLTYLD 487
Cdd:TIGR03719 165 GERRRVALCRLLLSKPDMLLLDEPTNHLDAE---SVAWLERHLQEYPGTVVAVTHDRYFLD 222
PRK09700 PRK09700
D-allose ABC transporter ATP-binding protein AlsA;
253-510 6.76e-13

D-allose ABC transporter ATP-binding protein AlsA;


Pssm-ID: 182036 [Multi-domain]  Cd Length: 510  Bit Score: 72.12  E-value: 6.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 253 GSAVlAEGDVVTIGNVDLVftgGILVRR---------QEVAARTGGLEVREV-NFSIGDKNLLERVSLTARPGTLTAIIG 322
Cdd:PRK09700  221 GSSV-CSGMVSDVSNDDIV---RLMVGRelqnrfnamKENVSNLAHETVFEVrNVTSRDRKKVRDISFSVCRGEILGFAG 296

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 323 GSGAGKTTLSRLIAGYATPTTGSVTFEGHNI--HTEYGSLRTRIGMVPQDD---------VVHRQLTVNQAL---GYAAE 388
Cdd:PRK09700  297 LVGSGRTELMNCLFGVDKRAGGEIRLNGKDIspRSPLDAVKKGMAYITESRrdngffpnfSIAQNMAISRSLkdgGYKGA 376

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 389 LRLppdTSKADRAQVVAQVLDELGLTKHG-DTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLR 467
Cdd:PRK09700  377 MGL---FHEVDEQRTAENQRELLALKCHSvNQNITELSGGNQQKVLISKWLCCCPEVIIFDEPTRGIDVGAKAEIYKVMR 453

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 468 QLADAGRVVLVVTHSL-TYLDVCDQVLLMAPGGKTAYLGPPDQI 510
Cdd:PRK09700  454 QLADDGKVILMVSSELpEIITVCDRIAVFCEGRLTQILTNRDDM 497
Rli1 COG1245
Translation initiation factor RLI1, contains Fe-S and AAA+ ATPase domains [Translation, ...
 309-487 1.15e-12

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


Pssm-ID: 440858 [Multi-domain]  Cd Length: 592  Bit Score: 71.35  E-value: 1.15e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 309 SLTARPGTL-----TAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEghnihteygslrTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:COG1245   355 SLEVEGGEIregevLGIVGPNGIGKTTFAKILAGVLKPDEGEVDED------------LKISYKPQYISPDYDGTVEEFL 422

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 GYAAELRLppDTSKADraqvvAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:COG1245   423 RSANTDDF--GSSYYK-----TEIIKPLGLEKLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 495

                         170       180
                  ....*....|....*....|....*
gi 1184609190 464 TMLRQLADA-GRVVLVVTHSLTYLD 487
Cdd:COG1245   496 KAIRRFAENrGKTAMVVDHDIYLID 520
FHA_Rv1747-like_rpt1 cd22694
first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 190-267 1.20e-12

first forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the first FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438746 [Multi-domain]  Cd Length: 93  Bit Score: 64.27  E-value: 1.20e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 190 LGSGKLEAPVTGAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGN 267
Cdd:cd22694     5 IPGGELRFDPGSSVRIGRDPDADVRLDDPRVSRRHALLEFDGDGWVYTDLGSRNGTYLNGRRVQQVKLSDGTRVRLGD 82
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 191-272 1.27e-12

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 64.47  E-value: 1.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 191 GSGKlEAPVT-GAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVG---SAVLAEGDVVTIG 266
Cdd:cd22682    10 GVGK-QFPITeSTIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVSIIDLGSTNGTIVNGKKIPklaSCDLQNGDQIKIG 88


                  ....*.
gi 1184609190 267 NVDLVF 272
Cdd:cd22682    89 NTIFKF 94
ABC2_membrane pfam01061
ABC-2 type transporter;
569-777 1.86e-12

ABC-2 type transporter;


Pssm-ID: 426023 [Multi-domain]  Cd Length: 204  Bit Score: 66.91  E-value: 1.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 569 IARRQVRLVVSDRAYFVFLALLPFVLGALSLTVPGNTGFGIASPTSGtpdeSAQILTLTSVAAVFMGTALTIRDLigERA 648
Cdd:pfam01061   1 LLKREFLRRWRDPSLGLWRLIQPILMALIFGTLFGNLGNQQGGLNRP----GLLFFSILFNAFSALSGISPVFEK--ERG 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 649 IFRREQAVGL-STGAYLAAKLAVFCVFAVVQAAIVTVIVLVGKGAPTQPAVLLgnpsFELFVTIAAMCVASAvLGLVLSS 727
Cdd:pfam01061  75 VLYRELASPLySPSAYVLAKILSELPLSLLQSLIFLLIVYFMVGLPPSAGRFF----LFLLVLLLTALAASS-LGLFISA 149

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 728 LARSSEQIMPLLVVSLMLQLVLAGGMVPVTgRI--FLDQLSWLLPSRWGYAA 777
Cdd:pfam01061 150 LAPSFEDASQLGPLVLLPLLLLSGFFIPID-SMpvWWQWIYYLNPLTYAIEA 200
PRK14267 PRK14267
phosphate ABC transporter ATP-binding protein; Provisional
 290-482 1.94e-12

phosphate ABC transporter ATP-binding protein; Provisional


Pssm-ID: 184596 [Multi-domain]  Cd Length: 253  Bit Score: 67.94  E-value: 1.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTL----SRLIA-GYATPTTGSVTFEGHNIHTEYGS---LR 361
Cdd:PRK14267    5 IETVNLRVYYGSNHVIKGVDLKIPQNGVFALMGPSGCGKSTLlrtfNRLLElNEEARVEGEVRLFGRNIYSPDVDpieVR 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQ--DDVVHRQLTVNQALGYAAELRLppdTSKADRAQVVAQVLDELGLTKHGDTRVD----KLSGGQRKRASVA 435
Cdd:PRK14267   85 REVGMVFQypNPFPHLTIYDNVAIGVKLNGLV---KSKKELDERVEWALKKAALWDEVKDRLNdypsNLSGGQRQRLVIA 161

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1184609190 436 LELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLvVTHS 482
Cdd:PRK14267  162 RALAMKPKILLMDEPTANIDPVGTAKIEELLFELKKEYTIVL-VTHS 207
ugpC PRK11650
sn-glycerol-3-phosphate ABC transporter ATP-binding protein UgpC;
288-495 4.40e-12

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


Pssm-ID: 236947 [Multi-domain]  Cd Length: 356  Bit Score: 68.33  E-value: 4.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEV-REVNFSIGDknllervsltarpGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTrIGM 366
Cdd:PRK11650   15 GKTQViKGIDLDVAD-------------GEFIVLVGPSGCGKSTLLRMVAGLERITSGEIWIGGRVVNELEPADRD-IAM 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQDDVVHRQLTVNQALGYAAELRlppDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLI 446
Cdd:PRK11650   81 VFQNYALYPHMSVRENMAYGLKIR---GMPKAEIEERVAEAARILELEPLLDRKPRELSGGQRQRVAMGRAIVREPAVFL 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 447 LDEPTSGLDPALDLQVMTMLRQLADAGRVV-LVVTHsltyldvcDQVLLM 495
Cdd:PRK11650  158 FDEPLSNLDAKLRVQMRLEIQRLHRRLKTTsLYVTH--------DQVEAM 199
ABCD_peroxisomal_ALDP cd03223
ATP-binding cassette domain of peroxisomal transporter, subfamily D; Peroxisomal ATP-binding ...
 304-500 4.77e-12

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: 64.87  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVtfeghNIHTEYGSLrtrigMVPQddvvhrqltvnqaL 383
Cdd:cd03223    16 LLKDLSFEIKPGDRLLITGPSGTGKSSLFRALAGLWPWGSGRI-----GMPEGEDLL-----FLPQ-------------R 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 GYaaelrLPPDTSKadraQVVAQVLDelgltkhgdtrvDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:cd03223    73 PY-----LPLGTLR----EQLIYPWD------------DVLSGGEQQRLAFARLLLHKPKFVFLDEATSALDEESEDRLY 131

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1184609190 464 TMLRqlaDAGRVVLVVTHSLTYLDVCDQVLLMAPGGK 500
Cdd:cd03223   132 QLLK---ELGITVISVGHRPSLWKFHDRVLDLDGEGG 165
ABCC_SUR1_N cd03290
ATP-binding cassette domain of the sulfonylurea receptor, subfamily C; The SUR domain 1. The ...
 305-498 6.75e-12

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: 65.82  E-value: 6.75e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMVPQDDVVHRQLTVNQALG 384
Cdd:cd03290    17 LSNINIRIPTGQLTMIVGQVGCGKSSLLLAILGEMQTLEGKVHWSNKNESEPSFEATRSRNRYSVAYAAQKPWLLNATVE 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 385 YAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDT-----RVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:cd03290    97 ENITFGSPFNKQRYKAVTDACSLQPDIDLLPFGDQteigeRGINLSGGQRQRICVARALYQNTNIVFLDDPFSALDIHLS 176

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1184609190 460 LQVMT--MLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03290   177 DHLMQegILKFLQDDKRTLVLVTHKLQYLPHADWIIAMKDG 217
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 305-498 8.81e-12

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 68.22  E-value: 8.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGH--NIHTEYGSLRTRIGMVPQDDVVHRQLTV--N 380
Cdd:PRK10982   14 LDNVNLKVRPHSIHALMGENGAGKSTLLKCLFGIYQKDSGSILFQGKeiDFKSSKEALENGISMVHQELNLVLQRSVmdN 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGyaaelRLPPDTSKADRAQV---VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPA 457
Cdd:PRK10982   94 MWLG-----RYPTKGMFVDQDKMyrdTKAIFDELDIDIDPRAKVATLSVSQMQMIEIAKAFSYNAKIVIMDEPTSSLTEK 168

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1184609190 458 LDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:PRK10982  169 EVNHLFTIIRKLKERGCGIVYISHKMeEIFQLCDEITILRDG 210
40850658_otr NF000106
oxytetracycline efflux ABC transporter Otr(C) ATP-binding subunit;
289-515 1.37e-11

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


Pssm-ID: 411078 [Multi-domain]  Cd Length: 351  Bit Score: 67.07  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 289 GLEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTlSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMvp 368
Cdd:NF000106   13 AVEVRGLVKHFGEVKAVDGVDLDVREGTVLGVLGP*GAA**R-GALPAHV*GPDAGRRPWRF*TWCANRRALRRTIG*-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 369 qddvvHRQLTVNQALGYAAELRL-----PPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPS 443
Cdd:NF000106   90 -----HRPVR*GRRESFSGRENLymigr*LDLSRKDARARADELLERFSLTEAAGRAAAKYSGGMRRRLDLAASMIGRPA 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQIGGAMG 515
Cdd:NF000106  165 VLYLDEPTTGLDPRTRNEVWDEVRSMVRDGATVLLTTQYMEEAEQLAHELTVIDRGRVIADGKVDELKTKVG 236
ABC_UvrA cd03238
ATP-binding cassette domain of the excision repair protein UvrA; Nucleotide excision repair in ...
 305-499 1.46e-11

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: 63.88  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLsrliagyatpttgsvtfeghnihteygslrtrigmvpqddvvhrqltVNQALG 384
Cdd:cd03238    11 LQNLDVSIPLNVLVVVTGVSGSGKSTL-----------------------------------------------VNEGLY 43

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 385 YAAELRLPPDTSKADRAQVVaqVLDELG-LTKHG------DTRVDKLSGGQRKRASVALELL--TGPSLLILDEPTSGLD 455
Cdd:cd03238    44 ASGKARLISFLPKFSRNKLI--FIDQLQfLIDVGlgyltlGQKLSTLSGGELQRVKLASELFsePPGTLFILDEPSTGLH 121

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 456 PALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGG 499
Cdd:cd03238   122 QQDINQLLEVIKGLIDLGNTVILIEHNLDVLSSADWIIDFGPGS 165
PRK13409 PRK13409
ribosome biogenesis/translation initiation ATPase RLI;
309-487 2.18e-11

ribosome biogenesis/translation initiation ATPase RLI;


Pssm-ID: 184037 [Multi-domain]  Cd Length: 590  Bit Score: 67.53  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 309 SLTARPGTL-----TAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEghnihteygslrTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:PRK13409  354 SLEVEGGEIyegevIGIVGPNGIGKTTFAKLLAGVLKPDEGEVDPE------------LKISYKPQYIKPDYDGTVEDLL 421

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 GYAaelrlppdTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:PRK13409  422 RSI--------TDDLGSSYYKSEIIKPLQLERLLDKNVKDLSGGELQRVAIAACLSRDADLYLLDEPSAHLDVEQRLAVA 493

                         170       180
                  ....*....|....*....|....*
gi 1184609190 464 TMLRQLADA-GRVVLVVTHSLTYLD 487
Cdd:PRK13409  494 KAIRRIAEErEATALVVDHDIYMID 518
ABC_RNaseL_inhibitor_domain2 cd03237
The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI) ...
 309-493 2.77e-11

The ATP-binding cassette domain 2 of RNase L inhibitor; The ABC ATPase, RNase L inhibitor (RLI), is a key enzyme in ribosomal biogenesis, formation of translation preinitiation complexes, and assembly of HIV capsids. RLI's are not transport proteins and thus cluster with a group of soluble proteins that lack the transmembrane components commonly found in other members of the family. Structurally, RLI's have an N-terminal Fe-S domain and two nucleotide-binding domains which are arranged to form two composite active sites in their interface cleft. RLI is one of the most conserved enzymes between archaea and eukaryotes with a sequence identity of more than 48%. The high degree of evolutionary conservation suggests that RLI performs a central role in archaeal and eukaryotic physiology.


Pssm-ID: 213204 [Multi-domain]  Cd Length: 246  Bit Score: 64.35  E-value: 2.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 309 SLTARPGTLT-----AIIGGSGAGKTTLSRLIAGYATPTTGsvtfeghnihtEYGSLRTRIGMVPQDDVVHRQLTVNQAL 383
Cdd:cd03237    14 TLEVEGGSISeseviGILGPNGIGKTTFIKMLAGVLKPDEG-----------DIEIELDTVSYKPQYIKADYEGTVRDLL 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 gyaaelrlppdTSKADRAQVVAQ----VLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALD 459
Cdd:cd03237    83 -----------SSITKDFYTHPYfkteIAKPLQIEQILDREVPELSGGELQRVAIAACLSKDADIYLLDEPSAYLDVEQR 151

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1184609190 460 LQVMTMLRQLAD-AGRVVLVVTHSLTYLD-VCDQVL 493
Cdd:cd03237   152 LMASKVIRRFAEnNEKTAFVVEHDIIMIDyLADRLI 187
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 305-483 5.12e-11

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 66.42  E-value: 5.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHT----EYGSLRTRIGMVPQDDvvHRQLTVN 380
Cdd:PRK10261  340 VEKVSFDLWPGETLSLVGESGSGKSTTGRALLRLVESQGGEIIFNGQRIDTlspgKLQALRRDIQFIFQDP--YASLDPR 417

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGYA--AELRLPPDTSKADRAQVVAQVLDELGLT-KHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPA 457
Cdd:PRK10261  418 QTVGDSimEPLRVHGLLPGKAAAARVAWLLERVGLLpEHAWRYPHEFSGGQRQRICIARALALNPKVIIADEAVSALDVS 497

                         170       180
                  ....*....|....*....|....*..
gi 1184609190 458 LDLQVMTMLRQLA-DAGRVVLVVTHSL 483
Cdd:PRK10261  498 IRGQIINLLLDLQrDFGIAYLFISHDM 524
PRK11819 PRK11819
putative ABC transporter ATP-binding protein; Reviewed
 300-487 5.38e-11

putative ABC transporter ATP-binding protein; Reviewed


Pssm-ID: 236992 [Multi-domain]  Cd Length: 556  Bit Score: 65.91  E-value: 5.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTF-EGhnihteygslrTRIGMVPQDDVVHRQLT 378
Cdd:PRK11819   18 PKKQILKDISLSFFPGAKIGVLGLNGAGKSTLLRIMAGVDKEFEGEARPaPG-----------IKVGYLPQEPQLDPEKT 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 V----NQALG-----------YAAELRLPPDTSKA------------------DRAQVVAQVLDELGLTKhGDTRVDKLS 425
Cdd:PRK11819   87 VrenvEEGVAevkaaldrfneIYAAYAEPDADFDAlaaeqgelqeiidaadawDLDSQLEIAMDALRCPP-WDAKVTKLS 165

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 426 GGQRKRasVAL--ELLTGPSLLILDEPTSGLDPAldlQVMTMLRQLADAGRVVLVVTHSLTYLD 487
Cdd:PRK11819  166 GGERRR--VALcrLLLEKPDMLLLDEPTNHLDAE---SVAWLEQFLHDYPGTVVAVTHDRYFLD 224
xylG TIGR02633
D-xylose ABC transporter, ATP-binding protein; Several bacterial species have enzymes xylose ...
 290-498 6.13e-11

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: 65.62  E-value: 6.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG-YATPT-TGSVTFEGHNIHTEYGSLRTRIGMV 367
Cdd:TIGR02633   2 LEMKGIVKTFGGVKALDGIDLEVRPGECVGLCGENGAGKSTLMKILSGvYPHGTwDGEIYWSGSPLKASNIRDTERAGIV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 pqddVVHRQLTVNQALGYAA------ELRLPPDTSKADRAQVVAQ-VLDELGLTKHGDTR-VDKLSGGQRKRASVALELL 439
Cdd:TIGR02633  82 ----IIHQELTLVPELSVAEniflgnEITLPGGRMAYNAMYLRAKnLLRELQLDADNVTRpVGDYGGGQQQLVEIAKALN 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 440 TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:TIGR02633 158 KQARLLILDEPSSSLTEKETEILLDIIRDLKAHGVACVYISHKLNEVKaVCDTICVIRDG 217
PvdE COG4615
ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion ...
 308-498 7.15e-11

ABC-type siderophore export system, fused ATPase and permease components [Inorganic ion transport and metabolism];


Pssm-ID: 443659 [Multi-domain]  Cd Length: 547  Bit Score: 65.59  E-value: 7.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHnihteygslrtRIGMVPQDDvvHRQLtvnqalgYAA 387
Cdd:COG4615   351 IDLTIRRGELVFIVGGNGSGKSTLAKLLTGLYRPESGEILLDGQ-----------PVTADNREA--YRQL-------FSA 410

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 388 EL-------RLPPDTSKADRAQvVAQVLDELGLtkHGDTRVD-------KLSGGQRKRASVALELLTGPSLLILDEPTSG 453
Cdd:COG4615   411 VFsdfhlfdRLLGLDGEADPAR-ARELLERLEL--DHKVSVEdgrfsttDLSQGQRKRLALLVALLEDRPILVFDEWAAD 487

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1184609190 454 LDPAL-DLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:COG4615   488 QDPEFrRVFYTELLPELKARGKTVIAISHDDRYFDLADRVLKMDYG 533
PRK13543 PRK13543
heme ABC exporter ATP-binding protein CcmA;
290-481 8.67e-11

heme ABC exporter ATP-binding protein CcmA;


Pssm-ID: 184129 [Multi-domain]  Cd Length: 214  Bit Score: 62.56  E-value: 8.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEYGSLRTRIG 365
Cdd:PRK13543   12 LAAHALAFSRNEEPVFGPLDFHVDAGEALLVQGDNGAGKTTLLRVLAGLLHVESGQIQIDGKTAtrgdRSRFMAYLGHLP 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 366 MVPQD-DVVHRQLTVNQALGYAAElrlppdtskadraQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSL 444
Cdd:PRK13543   92 GLKADlSTLENLHFLCGLHGRRAK-------------QMPGSALAIVGLAGYEDTLVRQLSAGQKKRLALARLWLSPAPL 158

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:PRK13543  159 WLLDEPYANLDLEGITLVNRMISAHLRGGGAALVTTH 195
PRK15439 PRK15439
autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional
 308-498 8.77e-11

autoinducer 2 ABC transporter ATP-binding protein LsrA; Provisional


Pssm-ID: 185336 [Multi-domain]  Cd Length: 510  Bit Score: 65.07  E-value: 8.77e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 308 VSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGMV--PQDdvvhRQ--------- 376
Cdd:PRK15439  282 ISLEVRAGEILGLAGVVGAGRTELAETLYGLRPARGGRIMLNGKEINALSTAQRLARGLVylPED----RQssglyldap 357

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 377 LTVNQ-ALGYAaelRLPPDTSKADRAQVVAQVLDELGLT-KHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:PRK15439  358 LAWNVcALTHN---RRGFWIKPARENAVLERYRRALNIKfNHAEQAARTLSGGNQQKVLIAKCLEASPQLLIVDEPTRGV 434

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1184609190 455 DPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVLLMAPG 498
Cdd:PRK15439  435 DVSARNDIYQLIRSIAAQNVAVLFISSDLEEIEqMADRVLVMHQG 479
ABC_UvrA_II cd03271
ATP-binding cassette domain II of the excision repair protein UvrA; Nucleotide excision repair ...
 340-507 9.95e-11

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: 63.02  E-value: 9.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 340 TPTTGSVTFEGHNIHteygslrtrigmvpqdDVVhrQLTVNQALGYaaelrLPPDTSKADRAQVVAQV-LDELGLTKHGD 418
Cdd:cd03271   112 NRETLEVRYKGKSIA----------------DVL--DMTVEEALEF-----FENIPKIARKLQTLCDVgLGYIKLGQPAT 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 419 TrvdkLSGGQRKRASVALELL---TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLM 495
Cdd:cd03271   169 T----LSGGEAQRIKLAKELSkrsTGKTLYILDEPTTGLHFHDVKKLLEVLQRLVDKGNTVVVIEHNLDVIKCADWIIDL 244

                         170
                  ....*....|....*..
gi 1184609190 496 AP-----GGKTAYLGPP 507
Cdd:cd03271   245 GPeggdgGGQVVASGTP 261
FHA pfam00498
FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.
 26-88 1.56e-10

FHA domain; The FHA (Forkhead-associated) domain is a phosphopeptide binding motif.


Pssm-ID: 459831 [Multi-domain]  Cd Length: 66  Bit Score: 57.59  E-value: 1.56e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190  26 VVVGSDVRADLRVAHPLVARAHLLLRFDKG-RWVAVDNHSLNGVFLNGQRVP--AVDIQDGQSVNI 88
Cdd:pfam00498   1 VTIGRSPDCDIVLDDPSVSRRHAEIRYDGGgRFYLEDLGSTNGTFVNGQRLGpePVRLKDGDVIRL 66
PLN03232 PLN03232
ABC transporter C family member; Provisional
 301-498 2.54e-10

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 64.61  E-value: 2.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPT-TGSVTfeghnihteygsLRTRIGMVPQDDVVHRQlTV 379
Cdd:PLN03232   629 SKPTLSDINLEIPVGSLVAIVGGTGEGKTSLISAMLGELSHAeTSSVV------------IRGSVAYVPQVSWIFNA-TV 695

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  380 NQALGYAAELRlPPDTSKADRAQVVAQVLDELG---LTKHGDTRVDkLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:PLN03232   696 RENILFGSDFE-SERYWRAIDVTALQHDLDLLPgrdLTEIGERGVN-ISGGQKQRVSMARAVYSNSDIYIFDDPLSALDA 773

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1184609190  457 ALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PLN03232   774 HVAHQVFDSCMKDELKGKTRVLVTNQLHFLPLMDRIILVSEG 815
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 424-510 2.69e-10

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: 64.26  E-value: 2.69e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 424 LSGGQRKRASVALELL---TGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAP--- 497
Cdd:TIGR00630 830 LSGGEAQRIKLAKELSkrsTGRTLYILDEPTTGLHFDDIKKLLEVLQRLVDKGNTVVVIEHNLDVIKTADYIIDLGPegg 909

                          90
                  ....*....|....*
gi 1184609190 498 --GGKTAYLGPPDQI 510
Cdd:TIGR00630 910 dgGGTVVASGTPEEV 924
met_CoM_red_A2 TIGR03269
methyl coenzyme M reductase system, component A2; The enzyme that catalyzes the final step in ...
 290-510 3.01e-10

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: 63.67  E-value: 3.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYAT--PTTGSV----------------TFEGH 351
Cdd:TIGR03269   1 IEVKNLTKKFDGKEVLKNISFTIEEGEVLGILGRSGAGKSVLMHVLRGMDQyePTSGRIiyhvalcekcgyverpSKVGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 352 NI------------------HTEYGSLRTRIGMVPQ--------DDVVHRQLTVNQALGYAAELRLppdtskaDRAqvvA 405
Cdd:TIGR03269  81 PCpvcggtlepeevdfwnlsDKLRRRIRKRIAIMLQrtfalygdDTVLDNVLEALEEIGYEGKEAV-------GRA---V 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 406 QVLDELGLTkHGDTRVDK-LSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLT 484
Cdd:TIGR03269 151 DLIEMVQLS-HRITHIARdLSGGEKQRVVLARQLAKEPFLFLADEPTGTLDPQTAKLVHNALEEAVKASGISMVLTSHWP 229

                         250       260
                  ....*....|....*....|....*...
gi 1184609190 485 YL--DVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:TIGR03269 230 EVieDLSDKAIWLE-NGEIKEEGTPDEV 256
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 305-455 3.72e-10

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 63.10  E-value: 3.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGS--LRTRIGMVPQD---DVVHRQLTV 379
Cdd:PRK10762  268 VNDVSFTLRKGEILGVSGLMGAGRTELMKVLYGALPRTSGYVTLDGHEVVTRSPQdgLANGIVYISEDrkrDGLVLGMSV 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGYAAELRLPPDTSKADRAQVVAQVLDELGL----TKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:PRK10762  348 KENMSLTALRYFSRAGGSLKHADEQQAVSDFIRLfnikTPSMEQAIGLLSGGNQQKVAIARGLMTRPKVLILDEPTRGVD 427
PRK13541 PRK13541
cytochrome c biogenesis protein CcmA; Provisional
 290-482 5.03e-10

cytochrome c biogenesis protein CcmA; Provisional


Pssm-ID: 184128 [Multi-domain]  Cd Length: 195  Bit Score: 59.89  E-value: 5.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLErVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSLRTRIGmvpQ 369
Cdd:PRK13541    2 LSLHQLQFNIEQKNLFD-LSITFLPSAITYIKGANGCGKSSLLRMIAGIMQPSSGNIYYKNCNINNIAKPYCTYIG---H 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRlppdtskaDRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:PRK13541   78 NLGLKLEMTVFENLKFWSEIY--------NSAETLYAAIHYFKLHDLLDEKCYSLSSGMQKIVAIARLIACQSDLWLLDE 149

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHS 482
Cdd:PRK13541  150 VETNLSKENRDLLNNLIVMKANSGGIVLLSSHL 182
PRK13549 PRK13549
xylose transporter ATP-binding subunit; Provisional
 290-492 5.85e-10

xylose transporter ATP-binding subunit; Provisional


Pssm-ID: 184134 [Multi-domain]  Cd Length: 506  Bit Score: 62.64  E-value: 5.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG-YATPT-TGSVTFEG-----HNIH-TEygslR 361
Cdd:PRK13549    6 LEMKNITKTFGGVKALDNVSLKVRAGEIVSLCGENGAGKSTLMKVLSGvYPHGTyEGEIIFEGeelqaSNIRdTE----R 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRIGMVPQDDVVHRQLTVNQALGYAAEL----RLPPDTSKAdRAQvvaQVLDELGLTKHGDTRVDKLSGGQRKRASVALE 437
Cdd:PRK13549   82 AGIAIIHQELALVKELSVLENIFLGNEItpggIMDYDAMYL-RAQ---KLLAQLKLDINPATPVGNLGLGQQQLVEIAKA 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQV 492
Cdd:PRK13549  158 LNKQARLLILDEPTASLTESETAVLLDIIRDLKAHGIACIYISHKLNEVkAISDTI 213
nikD PRK10418
nickel transporter ATP-binding protein NikD; Provisional
 301-498 5.85e-10

nickel transporter ATP-binding protein NikD; Provisional


Pssm-ID: 236688 [Multi-domain]  Cd Length: 254  Bit Score: 60.87  E-value: 5.85e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 301 DKNLLERVSLTARPGTLTAIIGGSGAGKT-----TLSRLIAGyATPTTGSVTFEGHNIHTEygSLRTR-IGMVPQD---- 370
Cdd:PRK10418   15 AQPLVHGVSLTLQRGRVLALVGGSGSGKSltcaaALGILPAG-VRQTAGRVLLDGKPVAPC--ALRGRkIATIMQNprsa 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 371 -----DVVHRQLTVNQALGyaaelrlppdtsKADRAQVVAQVLDELGLTKhgDTRVDKL-----SGGQRKRASVALELLT 440
Cdd:PRK10418   92 fnplhTMHTHARETCLALG------------KPADDATLTAALEAVGLEN--AARVLKLypfemSGGMLQRMMIALALLC 157

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 441 GPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLDVC-DQVLLMAPG 498
Cdd:PRK10418  158 EAPFIIADEPTTDLDVVAQARILDLLESIvQKRALGMLLVTHDMGVVARLaDDVAVMSHG 217
PLN03140 PLN03140
ABC transporter G family member; Provisional
 304-510 7.11e-10

ABC transporter G family member; Provisional


Pssm-ID: 215599 [Multi-domain]  Cd Length: 1470  Bit Score: 62.94  E-value: 7.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPT---TGSVTFEGHNIHtEYGSLRTRiGMVPQDDVVHRQLTVN 380
Cdd:PLN03140   180 ILKDASGIIKPSRMTLLLGPPSSGKTTLLLALAGKLDPSlkvSGEITYNGYRLN-EFVPRKTS-AYISQNDVHVGVMTVK 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  381 QALGYAA-------------EL-RLPPDTS-----------KADRAQVVAQ------VLDELGL-----TKHGDTRVDKL 424
Cdd:PLN03140   258 ETLDFSArcqgvgtrydllsELaRREKDAGifpeaevdlfmKATAMEGVKSslitdyTLKILGLdickdTIVGDEMIRGI 337

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  425 SGGQRKRASVAlELLTGPS-LLILDEPTSGLDPALDLQVMTMLRQ---LADAGRVVLVVTHSLTYLDVCDQVLLMAPgGK 500
Cdd:PLN03140   338 SGGQKKRVTTG-EMIVGPTkTLFMDEISTGLDSSTTYQIVKCLQQivhLTEATVLMSLLQPAPETFDLFDDIILLSE-GQ 415

                          250
                   ....*....|
gi 1184609190  501 TAYLGPPDQI 510
Cdd:PLN03140   416 IVYQGPRDHI 425
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 291-481 7.88e-10

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 61.95  E-value: 7.88e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG-----YATPTT------GSvtfeGHNIHteygS 359
Cdd:PRK10938  262 VLNNGVVSYNDRPILHNLSWQVNPGEHWQIVGPNGAGKSTLLSLITGdhpqgYSNDLTlfgrrrGS----GETIW----D 333

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 360 LRTRIGMVPQDdvVHRQLTVNQAL------GYAAELRLPPDTSkaDRAQVVA-QVLDELGLTKH-GDTRVDKLSGGQRKR 431
Cdd:PRK10938  334 IKKHIGYVSSS--LHLDYRVSTSVrnvilsGFFDSIGIYQAVS--DRQQKLAqQWLDILGIDKRtADAPFHSLSWGQQRL 409

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1184609190 432 ASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTH 481
Cdd:PRK10938  410 ALIVRALVKHPTLLILDEPLQGLDPLNRQLVRRFVDVLISEGETqLLFVSH 460
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
 205-274 1.19e-09

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 55.96  E-value: 1.19e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRV--GSAVLAEGDVVTIGNVDLVFTG 274
Cdd:cd22683    25 IGRSRSCDLVLSDPSISRFHAELRLEQNGINVIDNNSANGTFINGKRIkgKTYILKNGDIIVFGKCSFLIKY 96
PRK10938 PRK10938
putative molybdenum transport ATP-binding protein ModF; Provisional
 290-480 1.21e-09

putative molybdenum transport ATP-binding protein ModF; Provisional


Pssm-ID: 182852 [Multi-domain]  Cd Length: 490  Bit Score: 61.57  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGS----------VTFEG--HNIHTEY 357
Cdd:PRK10938    4 LQISQGTFRLSDTKTLQLPSLTLNAGDSWAFVGANGSGKSALARALAGELPLLSGErqsqfshitrLSFEQlqKLVSDEW 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 358 GSLRTRIGMVPQDDVvhrqltvnqalGYAAELRLPPDTSKADRAQVVAQvldELGLTKHGDTRVDKLSGGQRKRASVALE 437
Cdd:PRK10938   84 QRNNTDMLSPGEDDT-----------GRTTAEIIQDEVKDPARCEQLAQ---QFGITALLDRRFKYLSTGETRKTLLCQA 149

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 438 LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAG-RVVLVVT 480
Cdd:PRK10938  150 LMSEPDLLILDEPFDGLDVASRQQLAELLASLHQSGiTLVLVLN 193
GguA NF040905
sugar ABC transporter ATP-binding protein;
301-498 1.25e-09

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 61.34  E-value: 1.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG--YATPTTGSVTFEGHNIHTeygslRTrigmvpqddvVHRqlT 378
Cdd:NF040905  272 ERKVVDDVSLNVRRGEIVGIAGLMGAGRTELAMSVFGrsYGRNISGTVFKDGKEVDV-----ST----------VSD--A 334

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 379 VNQALGYAAE------LRLPPD----TSKADRAQVV-AQVLDELGLTKHG--------------DTRVDKLSGG-QRKra 432
Cdd:NF040905  335 IDAGLAYVTEdrkgygLNLIDDikrnITLANLGKVSrRGVIDENEEIKVAeeyrkkmniktpsvFQKVGNLSGGnQQK-- 412

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 433 sVALE--LLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:NF040905  413 -VVLSkwLFTDPDVLILDEPTRGIDVGAKYEIYTIINELAAEGKGVIVISSELpELLGMCDRIYVMNEG 480
PLN03130 PLN03130
ABC transporter C family member; Provisional
 298-498 1.43e-09

ABC transporter C family member; Provisional


Pssm-ID: 215595 [Multi-domain]  Cd Length: 1622  Bit Score: 62.06  E-value: 1.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  298 SIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTL-SRLIAGYATPTTGSVTfeghnihteygsLRTRIGMVPQDDVVHRQ 376
Cdd:PLN03130   626 SKAERPTLSNINLDVPVGSLVAIVGSTGEGKTSLiSAMLGELPPRSDASVV------------IRGTVAYVPQVSWIFNA 693

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  377 lTVNQALGYAAelrlPPDTSKADRAQVVAQVLDELGLTKHGD-----TRVDKLSGGQRKRASVALELLTGPSLLILDEPT 451
Cdd:PLN03130   694 -TVRDNILFGS----PFDPERYERAIDVTALQHDLDLLPGGDlteigERGVNISGGQKQRVSMARAVYSNSDVYIFDDPL 768

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1184609190  452 SGLDPALDLQVMT--MLRQLADAGRVvlVVTHSLTYLDVCDQVLLMAPG 498
Cdd:PLN03130   769 SALDAHVGRQVFDkcIKDELRGKTRV--LVTNQLHFLSQVDRIILVHEG 815
PRK15064 PRK15064
ABC transporter ATP-binding protein; Provisional
 290-455 1.44e-09

ABC transporter ATP-binding protein; Provisional


Pssm-ID: 237894 [Multi-domain]  Cd Length: 530  Bit Score: 61.45  E-value: 1.44e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFeghnihteygSLRTRIGMVPQ 369
Cdd:PRK15064  320 LEVENLTKGFDNGPLFKNLNLLLEAGERLAIIGENGVGKTTLLRTLVGELEPDSGTVKW----------SENANIGYYAQ 389

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DdvvHRQ-----LTVnqaLGYAAELRLPPDTSkadraQVVAQVLDELgLTKHGDTR--VDKLSGGQRKRASVALELLTGP 442
Cdd:PRK15064  390 D---HAYdfendLTL---FDWMSQWRQEGDDE-----QAVRGTLGRL-LFSQDDIKksVKVLSGGEKGRMLFGKLMMQKP 457

                         170
                  ....*....|...
gi 1184609190 443 SLLILDEPTSGLD 455
Cdd:PRK15064  458 NVLVMDEPTNHMD 470
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 296-498 1.48e-09

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 61.85  E-value: 1.48e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  296 NFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihteygslrtRIGMVPQ------ 369
Cdd:TIGR01271  433 NFSLYVTPVLKNISFKLEKGQLLAVAGSTGSGKSSLLMMIMGELEPSEGKIKHSG------------RISFSPQtswimp 500

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  370 ----DDVV-------HRQLTVNQALGYAAELRLPPDTSKAdraqvvaqVLDELGLTkhgdtrvdkLSGGQRKRASVALEL 438
Cdd:TIGR01271  501 gtikDNIIfglsydeYRYTSVIKACQLEEDIALFPEKDKT--------VLGEGGIT---------LSGGQRARISLARAV 563

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190  439 LTGPSLLILDEPTSGLDPALDLQVM--TMLRQLADAGRVvlVVTHSLTYLDVCDQVLLMAPG 498
Cdd:TIGR01271  564 YKDADLYLLDSPFTHLDVVTEKEIFesCLCKLMSNKTRI--LVTSKLEHLKKADKILLLHEG 623
FHA_GarA-like cd22720
forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation ...
 195-275 1.60e-09

forkhead associated (FHA) domain found in Mycobacterium tuberculosis glycogen accumulation regulator GarA and similar proteins; GarA is an FHA domain-containing protein involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent ON/OFF molecular switch that modulates the activities of KGD, GDH and GltB. Its FHA domain has dual specificity. It binds to both phosphorylated upstream partners, such as the kinases PknB and PknG, and nonphosphorylated downstream partners, such as the 2-oxoglutarate decarboxylase KGD. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438772 [Multi-domain]  Cd Length: 100  Bit Score: 55.78  E-value: 1.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 195 LEAPVTGAawiGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVFTG 274
Cdd:cd22720    21 LDQAITSA---GRHPDSDIFLDDVTVSRRHAEFRLENNEFNVVDVGSLNGTYVNREPVDSAVLANGDEVQIGKFRLVFLT 97


                  .
gi 1184609190 275 G 275
Cdd:cd22720    98 G 98
FHA_EmbR-like cd22669
forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional ...
 192-267 2.35e-09

forkhead associated (FHA) domain found in Mycobacterium tuberculosis transcriptional regulatory protein EmbR and similar proteins; EmbR is a transcriptional regulator of the embCAB operon encoding cell wall arabinosyltransferases (EmbC, -A, and -B), and is phosphorylated by the cognate mycobacterial serine/threonine protein kinase PknH. It interacts with RNA polymerase and possesses a phosphorylation-dependent ATPase activity. EmbR contains a regulatory C-terminal forkhead-associated (FHA) domain, which mediates binding to a threonine-phosphorylated site in PknH. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438721 [Multi-domain]  Cd Length: 89  Bit Score: 55.12  E-value: 2.35e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 192 SGKLEAPVTGAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRV-GSAVLAEGDVVTIGN 267
Cdd:cd22669     7 SGRGYPLQAAATRIGRLHDNDIVLDSANVSRHHAVIVDTGTNYVINDLRSSNGVHVQHERIrSAVTLNDGDHIRICD 83
ABCC_CFTR1 cd03291
ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The ...
 296-503 2.48e-09

ATP-binding cassette domain of the cystic fibrosis transmembrane regulator, subfamily C; The CFTR subfamily domain 1. The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits, or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213258 [Multi-domain]  Cd Length: 282  Bit Score: 59.10  E-value: 2.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 296 NFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihteygslrtRIGMVPQ------ 369
Cdd:cd03291    44 NLCLVGAPVLKNINLKIEKGEMLAITGSTGSGKTSLLMLILGELEPSEGKIKHSG------------RISFSSQfswimp 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 ----DDVV-------HRQLTVNQALGYAAELRLPPDTSKAdraqvvaqVLDELGLTkhgdtrvdkLSGGQRKRASVALEL 438
Cdd:cd03291   112 gtikENIIfgvsydeYRYKSVVKACQLEEDITKFPEKDNT--------VLGEGGIT---------LSGGQRARISLARAV 174

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVM--TMLRQLADAGRVvlVVTHSLTYLDVCDQVLLMAPGGKTAY 503
Cdd:cd03291   175 YKDADLYLLDSPFGYLDVFTEKEIFesCVCKLMANKTRI--LVTSKMEHLKKADKILILHEGSSYFY 239
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 196-272 3.00e-09

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 54.57  E-value: 3.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 196 EAPVTGAAW-IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGS--AVLAEGDVVTIGNVDLVF 272
Cdd:pfam16697  11 EFPLEGGRYrIGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGSGNGTLVNGQRVTElgIALRPGDRIELGQTEFCL 90
ABC2_perm_RbbA NF033858
ribosome-associated ATPase/putative transporter RbbA;
291-456 3.29e-09

ribosome-associated ATPase/putative transporter RbbA;


Pssm-ID: 468210 [Multi-domain]  Cd Length: 907  Bit Score: 60.52  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 291 EVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI----HTEygSLRTRIGM 366
Cdd:NF033858    3 RLEGVSHRYGKTVALDDVSLDIPAGCMVGLIGPDGVGKSSLLSLIAGARKIQQGRVEVLGGDMadarHRR--AVCPRIAY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 367 VPQddvvhrqltvnqALG---YaaelrlpPDTS---------------KADRAQVVAQVLDELGLTKHGDTRVDKLSGGQ 428
Cdd:NF033858   81 MPQ------------GLGknlY-------PTLSvfenldffgrlfgqdAAERRRRIDELLRATGLAPFADRPAGKLSGGM 141

                         170       180
                  ....*....|....*....|....*...
gi 1184609190 429 RKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:NF033858  142 KQKLGLCCALIHDPDLLILDEPTTGVDP 169
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 290-481 3.99e-09

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 60.18  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTfeghnihteygslrtrigmvpq 369
Cdd:PRK10636  313 LKMEKVSAGYGDRIILDSIKLNLVPGSRIGLLGRNGAGKSTLIKLLAGELAPVSGEIG---------------------- 370

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 ddvvhrqLTVNQALGYAAELRLppDTSKADRA----------QVVAQVL-DELG-LTKHGDTRVD---KLSGGQRKRASV 434
Cdd:PRK10636  371 -------LAKGIKLGYFAQHQL--EFLRADESplqhlarlapQELEQKLrDYLGgFGFQGDKVTEetrRFSGGEKARLVL 441

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1184609190 435 ALELLTGPSLLILDEPTSGLDpaLDL-QVMTmlRQLADAGRVVLVVTH 481
Cdd:PRK10636  442 ALIVWQRPNLLLLDEPTNHLD--LDMrQALT--EALIDFEGALVVVSH 485
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 205-267 1.07e-08

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 53.11  E-value: 1.07e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIR--VGSAVLAEGDVVTIGN 267
Cdd:cd22680    25 IGRDPENVIVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNDFKriKGPAKLHPNDIIKLGR 89
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 204-265 1.10e-08

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 53.39  E-value: 1.10e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 204 WIGRSLDNDVVVHDVLASRHHAFL-------TATPVgTEIRDAhSINGTFVNGIRVG---SAVLAEGDVVTI 265
Cdd:cd22670    25 TIGRSPSCDIVINDPFVSRTHCRIysvqfdeSSAPL-VYVEDL-SSNGTYLNGKLIGrnnTVLLSDGDVIEI 94
dppD PRK11022
dipeptide transporter ATP-binding subunit; Provisional
 290-498 1.44e-08

dipeptide transporter ATP-binding subunit; Provisional


Pssm-ID: 182906 [Multi-domain]  Cd Length: 326  Bit Score: 57.44  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVREVNFSIGDKNL----LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGY----ATPTTGSVTFEGHNIHTEYGSLR 361
Cdd:PRK11022    4 LNVDKLSVHFGDESApfraVDRISYSVKQGEVVGIVGESGSGKSVSSLAIMGLidypGRVMAEKLEFNGQDLQRISEKER 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 362 TRI-----GMVPQDDVVhrQLTVNQALGYA--AELRLPPDTSKADRAQVVAQVLDELGLTKhGDTRVD----KLSGGQRK 430
Cdd:PRK11022   84 RNLvgaevAMIFQDPMT--SLNPCYTVGFQimEAIKVHQGGNKKTRRQRAIDLLNQVGIPD-PASRLDvyphQLSGGMSQ 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 431 RASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLV-VTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK11022  161 RVMIAMAIACRPKLLIADEPTTALDVTIQAQIIELLLELQQKENMALVlITHDLALVaEAAHKIIVMYAG 230
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 301-496 1.47e-08

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 58.89  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  301 DKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTF-EGHNIH-TEYGSLRTRIGMVPQDDVVHRQLT 378
Cdd:PTZ00265   397 DVEIYKDLNFTLTEGKTYAFVGESGCGKSTILKLIERLYDPTEGDIIInDSHNLKdINLKWWRSKIGVVSQDPLLFSNSI 476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  379 VNQ---ALGYAAELRLPPDTSKAD--------------RAQV------VAQVLDELGLTK-------------------- 415
Cdd:PTZ00265   477 KNNikySLYSLKDLEALSNYYNEDgndsqenknkrnscRAKCagdlndMSNTTDSNELIEmrknyqtikdsevvdvskkv 556

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  416 --HG---------DTRV----DKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVV 479
Cdd:PTZ00265   557 liHDfvsalpdkyETLVgsnaSKLSGGQKQRISIARAIIRNPKILILDEATSSLDNKSEYLVQKTINNLkGNENRITIII 636

                          250
                   ....*....|....*..
gi 1184609190  480 THSLTYLDVCDQVLLMA 496
Cdd:PTZ00265   637 AHRLSTIRYANTIFVLS 653
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 22-91 1.85e-08

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 53.13  E-value: 1.85e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190  22 PGRDVVVGS--DVRADLRVAHPL-VARAHLLLRF-DKGRWVAVDNHSLNGVFLNGQRVP---AVDIQDGQSVNIGKP 91
Cdd:cd22663    19 DGKEVTVGRglGVTYQLVSTCPLmISRNHCVLKKnDEGQWTIKDNKSLNGVWVNGERIEplkPYPLNEGDLIQLGVP 95
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 300-506 1.96e-08

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: 58.42  E-value: 1.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihteygslrtRIGMVPQDDVVHR-QLT 378
Cdd:TIGR00957  649 DLPPTLNGITFSIPEGALVAVVGQVGCGKSSLLSALLAEMDKVEGHVHMKG------------SVAYVPQQAWIQNdSLR 716

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  379 VNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDkLSGGQRKRASVALELLTGPSLLILDEPTSGLDPAL 458
Cdd:TIGR00957  717 ENILFGKALNEKYYQQVLEACALLPDLEILPSGDRTEIGEKGVN-LSGGQKQRVSLARAVYSNADIYLFDDPLSAVDAHV 795

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190  459 DLQV-------MTMLrqladAGRVVLVVTHSLTYLDVCDQVLLMApGGKTAYLGP 506
Cdd:TIGR00957  796 GKHIfehvigpEGVL-----KNKTRILVTHGISYLPQVDVIIVMS-GGKISEMGS 844
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 424-504 1.98e-08

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 58.30  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  424 LSGGQRKRASVALELLTG---PSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAP--G 498
Cdd:PRK00635   810 LSGGEIQRLKLAYELLAPskkPTLYVLDEPTTGLHTHDIKALIYVLQSLTHQGHTVVIIEHNMHVVKVADYVLELGPegG 889


                   ....*.
gi 1184609190  499 GKTAYL 504
Cdd:PRK00635   890 NLGGYL 895
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 190-279 2.07e-08

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 52.47  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 190 LGSGKLEAPVT-GAAWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAV-LAEGDVVTIGn 267
Cdd:cd22668     6 DDGSGRVYQLReGSNIIGRGSDADFRLPDTGVSRRHAEIRWDGQVAHLTDLGSTNGTTVNNAPVTPEWrLADGDVITLG- 84

                          90
                  ....*....|..
gi 1184609190 268 vdlvfTGGILVR 279
Cdd:cd22668    85 -----HSEIIVR 91
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 205-267 3.02e-08

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 51.83  E-value: 3.02e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGT-EIRDAHSINGTFVNGIRV-GSAVLAEGDVVTIGN 267
Cdd:cd22673    25 FGRDLSCDIRIQLPGVSREHCRIEVDENGKaYLENLSTTNPTLVNGKAIeKSAELKDGDVITIGG 89
Yop-YscD_cpl pfam16697
Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain ...
 22-75 3.14e-08

Inner membrane component of T3SS, cytoplasmic domain; Yop-YscD-cpl is the cytoplasmic domain of Yop proteins like YscD from Proteobacteria. YscD forms part of the inner membrane component of the bacterial type III secretion injectosome apparatus.


Pssm-ID: 465238 [Multi-domain]  Cd Length: 94  Bit Score: 51.88  E-value: 3.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1184609190  22 PGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRV 75
Cdd:pfam16697  15 EGGRYRIGSDPDCDIVLSDKEVSRVHLKLEVDDEGWRLDDLGSGNGTLVNGQRV 68
ABCC_CFTR2 cd03289
ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator ...
 288-503 4.22e-08

ATP-binding cassette domain 2 of CFTR,subfamily C; The cystic fibrosis transmembrane regulator (CFTR), the product of the gene mutated in patients with cystic fibrosis, has adapted the ABC transporter structural motif to form a tightly regulated anion channel at the apical surface of many epithelia. Use of the term assembly of a functional ion channel implies the coming together of subunits or at least smaller not-yet functional components of the active whole. In fact, on the basis of current knowledge only the CFTR polypeptide itself is required to form an ATP- and protein kinase A-dependent low-conductance chloride channel of the type present in the apical membrane of many epithelial cells. CFTR displays the typical organization (IM-ABC)2 and carries a characteristic hydrophilic R-domain that separates IM1-ABC1 from IM2-ABC2.


Pssm-ID: 213256 [Multi-domain]  Cd Length: 275  Bit Score: 55.25  E-value: 4.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 288 GGLEVRE--VNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLS----RLIAgyatpTTGSVTFEGHNIHT-EYGSL 360
Cdd:cd03289     1 GQMTVKDltAKYTEGGNAVLENISFSISPGQRVGLLGRTGSGKSTLLsaflRLLN-----TEGDIQIDGVSWNSvPLQKW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 361 RTRIGMVPQDDVVhrqltvnqalgYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKL-----------SGGQR 429
Cdd:cd03289    76 RKAFGVIPQKVFI-----------FSGTFRKNLDPYGKWSDEEIWKVAEEVGLKSVIEQFPGQLdfvlvdggcvlSHGHK 144

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190 430 KRASVALELLTGPSLLILDEPTSGLDPaLDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPGGKTAY 503
Cdd:cd03289   145 QLMCLARSVLSKAKILLLDEPSAHLDP-ITYQVIRKTLKQAFADCTVILSEHRIEAMLECQRFLVIEENKVRQY 217
araG PRK11288
L-arabinose ABC transporter ATP-binding protein AraG;
304-498 5.03e-08

L-arabinose ABC transporter ATP-binding protein AraG;


Pssm-ID: 183077 [Multi-domain]  Cd Length: 501  Bit Score: 56.46  E-value: 5.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhteygSLRTrigmvPQDDVvhrqltvnqal 383
Cdd:PRK11288  268 LREPISFSVRAGEIVGLFGLVGAGRSELMKLLYGATRRTAGQVYLDGKPI-----DIRS-----PRDAI----------- 326

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 384 gyAAELRLPPDTSKADRAQVVAQVLDELGL--------------------------------TKHGDTRVDKLSGGQRKR 431
Cdd:PRK11288  327 --RAGIMLCPEDRKAEGIIPVHSVADNINIsarrhhlragclinnrweaenadrfirslnikTPSREQLIMNLSGGNQQK 404

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 432 ASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLT-YLDVCDQVLLMAPG 498
Cdd:PRK11288  405 AILGRWLSEDMKVILLDEPTRGIDVGAKHEIYNVIYELAAQGVAVLFVSSDLPeVLGVADRIVVMREG 472
uvra TIGR00630
excinuclease ABC, A subunit; This family is a member of the ABC transporter superfamily of ...
 358-510 5.96e-08

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: 56.56  E-value: 5.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 358 GSLRTRIGMVPQDDVVhrQLTVNQALGYAAELRLPPDtskadRAQVVAQVLDE---------------LGLTKHGDTrvd 422
Cdd:TIGR00630 419 EALAVTVGGKSIADVS--ELSIREAHEFFNQLTLTPE-----EKKIAEEVLKEirerlgflidvgldyLSLSRAAGT--- 488

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 423 kLSGGQRKRASVALEL---LTGpSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAP-- 497
Cdd:TIGR00630 489 -LSGGEAQRIRLATQIgsgLTG-VLYVLDEPSIGLHQRDNRRLINTLKRLRDLGNTLIVVEHDEDTIRAADYVIDIGPga 566

                         170
                  ....*....|....*.
gi 1184609190 498 ---GGKTAYLGPPDQI 510
Cdd:TIGR00630 567 gehGGEVVASGTPEEI 582
PRK10636 PRK10636
putative ABC transporter ATP-binding protein; Provisional
 300-493 6.33e-08

putative ABC transporter ATP-binding protein; Provisional


Pssm-ID: 236729 [Multi-domain]  Cd Length: 638  Bit Score: 56.33  E-value: 6.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 300 GDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHN----IHTEYGSL-RTRIGMVPQDDVVH 374
Cdd:PRK10636   12 GVRVLLDNATATINPGQKVGLVGKNGCGKSTLLALLKNEISADGGSYTFPGNWqlawVNQETPALpQPALEYVIDGDREY 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQL--TVNQAL----GYA-AELRLPPDTSKA----DRAqvvAQVLDELGLTKHGDTR-VDKLSGGQRKRASVALELLTGP 442
Cdd:PRK10636   92 RQLeaQLHDANerndGHAiATIHGKLDAIDAwtirSRA---ASLLHGLGFSNEQLERpVSDFSGGWRMRLNLAQALICRS 168

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 443 SLLILDEPTSGLDpaLDlQVMTMLRQLADAGRVVLVVTHSLTYLD-VCDQVL 493
Cdd:PRK10636  169 DLLLLDEPTNHLD--LD-AVIWLEKWLKSYQGTLILISHDRDFLDpIVDKII 217
PRK11147 PRK11147
ABC transporter ATPase component; Reviewed
 298-455 8.96e-08

ABC transporter ATPase component; Reviewed


Pssm-ID: 236861 [Multi-domain]  Cd Length: 635  Bit Score: 55.73  E-value: 8.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 298 SIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhteygslrtrIGMVPQDDVVHRQL 377
Cdd:PRK11147   12 SFSDAPLLDNAELHIEDNERVCLVGRNGAGKSTLMKILNGEVLLDDGRIIYEQDLI----------VARLQQDPPRNVEG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 378 TV----NQALGYAAE--------LRL----PPDTSKADRAQV---------------VAQVLDELGLtkHGDTRVDKLSG 426
Cdd:PRK11147   82 TVydfvAEGIEEQAEylkryhdiSHLvetdPSEKNLNELAKLqeqldhhnlwqlenrINEVLAQLGL--DPDAALSSLSG 159

                         170       180
                  ....*....|....*....|....*....
gi 1184609190 427 GQRKRASVALELLTGPSLLILDEPTSGLD 455
Cdd:PRK11147  160 GWLRKAALGRALVSNPDVLLLDEPTNHLD 188
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 205-252 9.60e-08

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 49.10  E-value: 9.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1184609190  205 IGR-SLDNDVVVHDVLASRHHAFLTATP-VGTEIRDAHSINGTFVNGIRV 252
Cdd:smart00240   3 IGRsSEDCDIQLDGPSISRRHAVIVYDGgGRFYLIDLGSTNGTFVNGKRI 52
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 205-266 1.02e-07

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 50.38  E-value: 1.02e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRV-GSAVLAEGDVVTIG 266
Cdd:cd22693    22 IGRADDNDLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGNRVtQPVVVQPGDTIRIG 84
ABC_Class2 cd03227
ATP-binding cassette domain of non-transporter proteins; ABC-type Class 2 contains systems ...
 382-481 1.09e-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: 52.36  E-value: 1.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 382 ALGYAAELRLPPDTSKAD--RAQVVAQVldELGLTkhgdTRVDKLSGGQRKRASVALEL----LTGPSLLILDEPTSGLD 455
Cdd:cd03227    40 AIGLALGGAQSATRRRSGvkAGCIVAAV--SAELI----FTRLQLSGGEKELSALALILalasLKPRPLYILDEIDRGLD 113

                          90       100
                  ....*....|....*....|....*.
gi 1184609190 456 PALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:cd03227   114 PRDGQALAEAILEHLVKGAQVIVITH 139
hmuV PRK13547
heme ABC transporter ATP-binding protein;
304-481 1.64e-07

heme ABC transporter ATP-binding protein;


Pssm-ID: 184132 [Multi-domain]  Cd Length: 272  Bit Score: 53.68  E-value: 1.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPT--------TGSVTFEGHNIHT-EYGSLRTRIGMVPQDDVVH 374
Cdd:PRK13547   16 ILRDLSLRIEPGRVTALLGRNGAGKSTLLKALAGDLTGGgaprgarvTGDVTLNGEPLAAiDAPRLARLRAVLPQAAQPA 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVNQ--ALGYAAELRLPPDTSKADRaQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALEL---------LTGPS 443
Cdd:PRK13547   96 FAFSAREivLLGRYPHARRAGALTHRDG-EIAWQALALAGATALVGRDVTTLSGGELARVQFARVLaqlwpphdaAQPPR 174

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1184609190 444 LLILDEPTSGLDPALDLQVMTMLRQLADAGRV-VLVVTH 481
Cdd:PRK13547  175 YLLLDEPTAALDLAHQHRLLDTVRRLARDWNLgVLAIVH 213
MRP_assoc_pro TIGR00957
multi drug resistance-associated protein (MRP); This model describes multi drug ...
 304-510 2.30e-07

multi drug resistance-associated protein (MRP); This model describes multi drug resistance-associated protein (MRP) in eukaryotes. The multidrug resistance-associated protein is an integral membrane protein that causes multidrug resistance when overexpressed in mammalian cells. It belongs to ABC transporter superfamily. The protein topology and function was experimentally demonstrated by epitope tagging and immunofluorescence. Insertion of tags in the critical regions associated with drug efflux, abrogated its function. The C-terminal domain seem to highly conserved. [Transport and binding proteins, Other]


Pssm-ID: 188098 [Multi-domain]  Cd Length: 1522  Bit Score: 54.95  E-value: 2.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYG--SLRTRIGMVPQDDVVhrqltvnq 381
Cdd:TIGR00957 1301 VLRHINVTIHGGEKVGIVGRTGAGKSSLTLGLFRINESAEGEIIIDGLNI-AKIGlhDLRFKITIIPQDPVL-------- 1371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  382 algYAAELR--LPPDTSKADRAQVVAQVLDEL---------GLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:TIGR00957 1372 ---FSGSLRmnLDPFSQYSDEEVWWALELAHLktfvsalpdKLDHECAEGGENLSVGQRQLVCLARALLRKTKILVLDEA 1448

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190  451 TSGLDPALDLQVMTMLR-QLADAgrVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGPPDQI 510
Cdd:TIGR00957 1449 TAAVDLETDNLIQSTIRtQFEDC--TVLTIAHRLNTIMDYTRVIVLDKGEVAEFGAPSNLL 1507
tagH PRK13545
teichoic acids export protein ATP-binding subunit; Provisional
 305-484 2.38e-07

teichoic acids export protein ATP-binding subunit; Provisional


Pssm-ID: 184130 [Multi-domain]  Cd Length: 549  Bit Score: 54.13  E-value: 2.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTEYGSlrtriGMvpqddvvHRQLTVNQALg 384
Cdd:PRK13545   40 LNNISFEVPEGEIVGIIGLNGSGKSTLSNLIAGVTMPNKGTVDIKGSAALIAISS-----GL-------NGQLTGIENI- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 385 yaaELR-LPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVM 463
Cdd:PRK13545  107 ---ELKgLMMGLTKEKIKEIIPEIIEFADIGKFIYQPVKTYSSGMKSRLGFAISVHINPDILVIDEALSVGDQTFTKKCL 183

                         170       180
                  ....*....|....*....|.
gi 1184609190 464 TMLRQLADAGRVVLVVTHSLT 484
Cdd:PRK13545  184 DKMNEFKEQGKTIFFISHSLS 204
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 407-507 2.58e-07

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 54.83  E-value: 2.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  407 VLDELGLTKHGDTR-VDKLSGGQRKRASVALELltGPSLL----ILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:PRK00635   459 ILIDLGLPYLTPERaLATLSGGEQERTALAKHL--GAELIgityILDEPSIGLHPQDTHKLINVIKKLRDQGNTVLLVEH 536

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1184609190  482 SLTYLDVCDQVLLMAP-----GGKTAYLGPP 507
Cdd:PRK00635   537 DEQMISLADRIIDIGPgagifGGEVLFNGSP 567
ABC_UvrA_I cd03270
ATP-binding cassette domain I of the excision repair protein UvrA; Nucleotide excision repair ...
 408-498 3.28e-07

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: 51.87  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 408 LDELGLTKHGDTrvdkLSGGQRKRASVALEL---LTGpSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLT 484
Cdd:cd03270   126 LGYLTLSRSAPT----LSGGEAQRIRLATQIgsgLTG-VLYVLDEPSIGLHPRDNDRLIETLKRLRDLGNTVLVVEHDED 200

                          90
                  ....*....|....
gi 1184609190 485 YLDVCDQVLLMAPG 498
Cdd:cd03270   201 TIRAADHVIDIGPG 214
PRK10982 PRK10982
galactose/methyl galaxtoside transporter ATP-binding protein; Provisional
 290-498 3.60e-07

galactose/methyl galaxtoside transporter ATP-binding protein; Provisional


Pssm-ID: 182880 [Multi-domain]  Cd Length: 491  Bit Score: 53.58  E-value: 3.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 290 LEVRevNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI--HTEYGSLRTRIGMV 367
Cdd:PRK10982  251 LEVR--NLTSLRQPSIRDVSFDLHKGEILGIAGLVGAKRTDIVETLFGIREKSAGTITLHGKKInnHNANEAINHGFALV 328

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 368 PQD----------DVVHRQLTVN-----QALGYAAELRLPPDTSkadraqvvaQVLDELGL-TKHGDTRVDKLSGGQRKR 431
Cdd:PRK10982  329 TEErrstgiyaylDIGFNSLISNirnykNKVGLLDNSRMKSDTQ---------WVIDSMRVkTPGHRTQIGSLSGGNQQK 399

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 432 ASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSL-TYLDVCDQVLLMAPG 498
Cdd:PRK10982  400 VIIGRWLLTQPEILMLDEPTRGIDVGAKFEIYQLIAELAKKDKGIIIISSEMpELLGITDRILVMSNG 467
FHA_TCF19 cd22685
forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar ...
 205-266 3.68e-07

forkhead associated (FHA) domain found in transcription factor 19 (TCF-19) and similar proteins; TCF-19, also called transcription factor SC1, was identified as a putative trans-activating factor with expression beginning at the late G1-S boundary in dividing cells. It also functions as a novel islet factor necessary for proliferation and survival in the INS-1 beta cell line. It plays an important role in susceptibility to both Type 1 Diabetes Mellitus (T1DM) and Type 2 Diabetes Mellitus (T2DM); it has been suggested that it may positively impact beta cell mass under conditions of beta cell stress and increased insulin demand. TCF-19 contains an N-terminal fork head association domain (FHA), a proline rich region, and a C-terminal plant homeodomain (PHD) finger. The FHA domain may serve as a nuclear signaling domain or as a phosphoprotein binding domain. The proline rich region is a common characteristic of trans-activating factors. The PHD finger may allow TCF-19 to interact with chromatin via methylated histone H3.


Pssm-ID: 438737 [Multi-domain]  Cd Length: 130  Bit Score: 49.72  E-value: 3.68e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 205 IGR-SLDNDVV----VHDVLASRHHAFLTATPVGTE-----IRDaHSINGTFVNGIRVGSAV---LAEGDVVTIG 266
Cdd:cd22685    32 IGRnPEVCDVFlcssQHPNLISREHAEIHAERDGNGnwkvlIED-RSTNGTYVNDVRLQDGQrreLSDGDTITFG 105
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
424-510 3.88e-07

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 53.88  E-value: 3.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 424 LSGG--QR-KRASvalELL---TGPSLLILDEPTSGLDPAlDLQV-MTMLRQLADAGRVVLVVTHSltyLDV---CDQVL 493
Cdd:COG0178   827 LSGGeaQRvKLAS---ELSkrsTGKTLYILDEPTTGLHFH-DIRKlLEVLHRLVDKGNTVVVIEHN---LDViktADWII 899

                          90       100
                  ....*....|....*....|..
gi 1184609190 494 LMAP-----GGKTAYLGPPDQI 510
Cdd:COG0178   900 DLGPeggdgGGEIVAEGTPEEV 921
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 622-824 4.03e-07

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 52.78  E-value: 4.03e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 622 QILTLTSVAAVFMGTALTIRDLIGER--AIFRREQAVGLSTGAYLAAKLAVFCVFAVVQAAIVTVIVLvgkgaptQPAVL 699
Cdd:pfam12698 162 YLVGLILMIIILIGAAIIAVSIVEEKesRIKERLLVSGVSPLQYWLGKILGDFLVGLLQLLIILLLLF-------GIGIP 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 700 LGNPSFeLFVTIAAMCVASAVLGLVLSSLARSSEQIMPLLVVSLMLQLVLAGGMVPVTG-RIFLDQLSWLLPSrwgyaAS 778
Cdd:pfam12698 235 FGNLGL-LLLLFLLYGLAYIALGYLLGSLFKNSEDAQSIIGIVILLLSGFFGGLFPLEDpPSFLQWIFSIIPF-----FS 308

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1184609190 779 ASTVNVRLLVPGSLVQQdshwahtpaawLLDMGMLVALSVLYAAIV 824
Cdd:pfam12698 309 PIDGLLRLIYGDSLWEI-----------APSLIILLLFAVVLLLLA 343
PTZ00243 PTZ00243
ABC transporter; Provisional
 304-507 4.61e-07

ABC transporter; Provisional


Pssm-ID: 240327 [Multi-domain]  Cd Length: 1560  Bit Score: 54.01  E-value: 4.61e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIHTeYG--SLRTRIGMVPQDDVVhrqltvnq 381
Cdd:PTZ00243  1325 VLRGVSFRIAPREKVGIVGRTGSGKSTLLLTFMRMVEVCGGEIRVNGREIGA-YGlrELRRQFSMIPQDPVL-------- 1395

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  382 algYAAELRLPPDT-SKADRAQVVAqVLDELGLTKHG-------DTRV----DKLSGGQRKRASVALELLTGPSLLIL-D 448
Cdd:PTZ00243  1396 ---FDGTVRQNVDPfLEASSAEVWA-ALELVGLRERVasesegiDSRVleggSNYSVGQRQLMCMARALLKKGSGFILmD 1471

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190  449 EPTSGLDPALDLQVMTMLRQlADAGRVVLVVTHSLTYLDVCDQVLLMaPGGKTAYLGPP 507
Cdd:PTZ00243  1472 EATANIDPALDRQIQATVMS-AFSAYTVITIAHRLHTVAQYDKIIVM-DHGAVAEMGSP 1528
PRK10261 PRK10261
glutathione transporter ATP-binding protein; Provisional
 254-498 5.54e-07

glutathione transporter ATP-binding protein; Provisional


Pssm-ID: 182342 [Multi-domain]  Cd Length: 623  Bit Score: 53.32  E-value: 5.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 254 SAVLAEGDVVTIGNVDLVFTGgilvRRQEVAArtggleVREVNFSIgdknllervsltaRPGTLTAIIGGSGAGKT---- 329
Cdd:PRK10261    4 SDELDARDVLAVENLNIAFMQ----EQQKIAA------VRNLSFSL-------------QRGETLAIVGESGSGKSvtal 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 330 TLSRLIAGyatpttgsvtfEGHNIHTEYGSLRTR----------------------IGMVPQDDV--VHRQLTVNQALgy 385
Cdd:PRK10261   61 ALMRLLEQ-----------AGGLVQCDKMLLRRRsrqvielseqsaaqmrhvrgadMAMIFQEPMtsLNPVFTVGEQI-- 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 386 AAELRLPPDTSKADRAQVVAQVLDE---------LGLTKHgdtrvdKLSGGQRKRASVALELLTGPSLLILDEPTSGLDP 456
Cdd:PRK10261  128 AESIRLHQGASREEAMVEAKRMLDQvripeaqtiLSRYPH------QLSGGMRQRVMIAMALSCRPAVLIADEPTTALDV 201

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 457 ALDLQVMTMLRQL-ADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK10261  202 TIQAQILQLIKVLqKEMSMGVIFITHDMGVVaEIADRVLVMYQG 245
PRK10762 PRK10762
D-ribose transporter ATP binding protein; Provisional
 305-498 6.92e-07

D-ribose transporter ATP binding protein; Provisional


Pssm-ID: 236755 [Multi-domain]  Cd Length: 501  Bit Score: 52.70  E-value: 6.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYG---SLRTRIGMVPQDDVVHRQLTV-- 379
Cdd:PRK10762   20 LSGAALNVYPGRVMALVGENGAGKSTMMKVLTGIYTRDAGSILYLGKEV-TFNGpksSQEAGIGIIHQELNLIPQLTIae 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 380 NQALGyaaelRLPPDT----------SKADRaqvvaqVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDE 449
Cdd:PRK10762   99 NIFLG-----REFVNRfgridwkkmyAEADK------LLARLNLRFSSDKLVGELSIGEQQMVEIAKVLSFESKVIIMDE 167

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 450 PTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYL-DVCDQVLLMAPG 498
Cdd:PRK10762  168 PTDALTDTETESLFRVIRELKSQGRGIVYISHRLKEIfEICDDVTVFRDG 217
PLN03232 PLN03232
ABC transporter C family member; Provisional
 304-506 7.94e-07

ABC transporter C family member; Provisional


Pssm-ID: 215640 [Multi-domain]  Cd Length: 1495  Bit Score: 53.06  E-value: 7.94e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  304 LLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNIhTEYG--SLRTRIGMVPQDDVVhrqltvnq 381
Cdd:PLN03232  1251 VLHGLSFFVSPSEKVGVVGRTGAGKSSMLNALFRIVELEKGRIMIDDCDV-AKFGltDLRRVLSIIPQSPVL-------- 1321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  382 algYAAELR--LPPDTSKAD----RAQVVAQVLDELGLTKHG-DTRV----DKLSGGQRKRASVALELLTGPSLLILDEP 450
Cdd:PLN03232  1322 ---FSGTVRfnIDPFSEHNDadlwEALERAHIKDVIDRNPFGlDAEVseggENFSVGQRQLLSLARALLRRSKILVLDEA 1398

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190  451 TSGLDPALDLQVMTMLRQLADAGrVVLVVTHSLTYLDVCDQVLLMAPGGKTAYLGP 506
Cdd:PLN03232  1399 TASVDVRTDSLIQRTIREEFKSC-TMLVIAHRLNTIIDCDKILVLSSGQVLEYDSP 1453
FHA_RAD53-like_rpt2 cd22690
second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine ...
 203-265 8.12e-07

second forkhead associated (FHA) domain found in Saccharomyces cerevisiae Serine/threonine-protein kinase RAD53 and similar proteins; RAD53, also called CHEK2 homolog, or serine-protein kinase 1 (Spk1), is a nuclear protein kinase that phosphorylates proteins on serine, threonine, and tyrosine. It controls S-phase checkpoint as well as G1 and G2 DNA damage checkpoints and prevents entry into anaphase and mitotic exit after DNA damage via regulation of the Polo kinase CDC5. It may be involved in the phosphorylation of RPH1. RAD53 contains two FHA domains. This model corresponds to the second one. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438742 [Multi-domain]  Cd Length: 105  Bit Score: 48.06  E-value: 8.12e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 203 AWIGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAH----SINGTFVNGIRVGSAV---LAEGDVVTI 265
Cdd:cd22690    21 TFIGRSKDCDEEITDPRISKHHCIITRKRSGKGLDDVYvtdtSTNGTFINNNRLGKGSqslLQDGDEIVL 90
PLN03073 PLN03073
ABC transporter F family; Provisional
 302-481 9.92e-07

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 52.55  E-value: 9.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARpgtlTAIIGGSGAGKTTLSRLIAGYATPTTGSVtfeghnihteYGSLRTRIGMVPQDDVVHRQLTVNQ 381
Cdd:PLN03073  526 KNLNFGIDLDSR----IAMVGPNGIGKSTILKLISGELQPSSGTV----------FRSAKVRMAVFSQHHVDGLDLSSNP 591

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 382 ALgYAAELrLPPDTSKADRAQvvaqvLDELGLTkhGDTRVD---KLSGGQRKRASVALELLTGPSLLILDEPTSGLDpaL 458
Cdd:PLN03073  592 LL-YMMRC-FPGVPEQKLRAH-----LGSFGVT--GNLALQpmyTLSGGQKSRVAFAKITFKKPHILLLDEPSNHLD--L 660

                         170       180
                  ....*....|....*....|...
gi 1184609190 459 DlQVMTMLRQLADAGRVVLVVTH 481
Cdd:PLN03073  661 D-AVEALIQGLVLFQGGVLMVSH 682
CFTR_protein TIGR01271
cystic fibrosis transmembrane conductor regulator (CFTR); The model describes the cystis ...
 295-495 1.34e-06

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


Pssm-ID: 273530 [Multi-domain]  Cd Length: 1490  Bit Score: 52.22  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  295 VNFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATpTTGSVTFEGHNIHT-EYGSLRTRIGMVPQDDVV 373
Cdd:TIGR01271 1225 AKYTEAGRAVLQDLSFSVEGGQRVGLLGRTGSGKSTLLSALLRLLS-TEGEIQIDGVSWNSvTLQTWRKAFGVIPQKVFI 1303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  374 hrqltvnqalgYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTRVDKL-----------SGGQRKRASVALELLTGP 442
Cdd:TIGR01271 1304 -----------FSGTFRKNLDPYEQWSDEEIWKVAEEVGLKSVIEQFPDKLdfvlvdggyvlSNGHKQLMCLARSILSKA 1372

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1184609190  443 SLLILDEPTSGLDPaLDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLM 495
Cdd:TIGR01271 1373 KILLLDEPSAHLDP-VTLQIIRKTLKQSFSNCTVILSEHRVEALLECQQFLVI 1424
FHA_OdhI-like cd22721
forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate ...
 206-272 1.35e-06

forkhead associated (FHA) domain found in Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI) and similar proteins; OdhI is an essential component of the PknG signaling pathway. It regulates glutamate production under biotin non-limiting conditions. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438773 [Multi-domain]  Cd Length: 102  Bit Score: 47.39  E-value: 1.35e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 206 GRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAVLAEGDVVTIGNVDLVF 272
Cdd:cd22721    34 GRHPESDIFLDDVTVSRRHAEFRINEGEFEVVDVGSLNGTYVNREPRNAQVMQTGDEIQIGKFRLVF 100
PTZ00265 PTZ00265
multidrug resistance protein (mdr1); Provisional
 267-494 1.57e-06

multidrug resistance protein (mdr1); Provisional


Pssm-ID: 240339 [Multi-domain]  Cd Length: 1466  Bit Score: 51.95  E-value: 1.57e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  267 NVDLVFTGGILVRRQEVAarTGGLEVREVNFS-IGDKN--LLERVSLTARPGTLTAIIGGSGAGKTTLSRLI-------- 335
Cdd:PTZ00265  1145 NIDVRDNGGIRIKNKNDI--KGKIEIMDVNFRyISRPNvpIYKDLTFSCDSKKTTAIVGETGSGKSTVMSLLmrfydlkn 1222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  336 -----------------------------------------AGYATPTT-----GSVTFEGHNIhTEYG--SLRTRIGMV 367
Cdd:PTZ00265  1223 dhhivfknehtndmtneqdyqgdeeqnvgmknvnefsltkeGGSGEDSTvfknsGKILLDGVDI-CDYNlkDLRNLFSIV 1301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  368 PQDDVVHrQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELglTKHGDTRV----DKLSGGQRKRASVALELLTGPS 443
Cdd:PTZ00265  1302 SQEPMLF-NMSIYENIKFGKEDATREDVKRACKFAAIDEFIESL--PNKYDTNVgpygKSLSGGQKQRIAIARALLREPK 1378

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190  444 LLILDEPTSGLDPALDLQVMTMLRQLAD-AGRVVLVVTHSLTYLDVCDQVLL 494
Cdd:PTZ00265  1379 ILLLDEATSSLDSNSEKLIEKTIVDIKDkADKTIITIAHRIASIKRSDKIVV 1430
FHA_RNF8 cd22663
forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; ...
 205-266 1.88e-06

forkhead associated (FHA) domain found in RING finger protein 8 (RNF8) and similar proteins; RNF8 is a telomere-associated E3 ubiquitin-protein ligase that plays an important role in DNA double-strand break (DSB) repair via histone ubiquitination. It is localized in the nucleus and interacts with class III E2s (UBE2E2, UbcH6, and UBE2E3), but not with other E2s (UbcH5, UbcH7, UbcH10, hCdc34, and hBendless). It recruits UBC13 for lysine 63-based self polyubiquitylation. Its deficiency causes neuronal pathology and cognitive decline, and its loss results in neuron degeneration. RNF8, together with RNF168, catalyzes a series of ubiquitylation events on substrates such as H2A and H2AX, with the H2AK13/15 ubiquitylation being particularly important for recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of DSBs. Specially, RNF8 mediates the ubiquitination of gammaH2AX, and recruits 53BP1 and BRCA1 to DNA damage sites which promotes DNA damage response (DDR) and inhibits chromosomal instability. Moreover, RNF8 interacts with retinoid X receptor alpha (RXR alpha) and enhances its transcription-stimulating activity. It also regulates the rate of exit from mitosis and cytokinesis. RNF8 contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438715 [Multi-domain]  Cd Length: 110  Bit Score: 47.35  E-value: 1.88e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190 205 IGRSLD--NDVVVHDVLA-SRHHAFLTATPVGT-EIRDAHSINGTFVNGIRVGSA---VLAEGDVVTIG 266
Cdd:cd22663    25 VGRGLGvtYQLVSTCPLMiSRNHCVLKKNDEGQwTIKDNKSLNGVWVNGERIEPLkpyPLNEGDLIQLG 93
FHA smart00240
Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear ...
 26-75 2.01e-06

Forkhead associated domain; Found in eukaryotic and prokaryotic proteins. Putative nuclear signalling domain.


Pssm-ID: 214578 [Multi-domain]  Cd Length: 52  Bit Score: 45.25  E-value: 2.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1184609190   26 VVVG-SDVRADLRVAHPLVARAHLLLRFDKG-RWVAVDNHSLNGVFLNGQRV 75
Cdd:smart00240   1 VTIGrSSEDCDIQLDGPSISRRHAVIVYDGGgRFYLIDLGSTNGTFVNGKRI 52
FHA_GarA_OdhI-like cd22684
forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium ...
 26-90 2.18e-06

forkhead associated (FHA) domain found in Mycobacterium tuberculosis GarA, Corynebacterium glutamicum OdhI and similar proteins; This family includes Mycobacterium tuberculosis glycogen accumulation regulator GarA and Corynebacterium glutamicum oxoglutarate dehydrogenase inhibitor (OdhI). GarA is involved in the regulation of glutamate metabolism. It acts as a phosphorylation-dependent molecular switch that modulates the activities of Kgd, Gdh and GltB. GarA binds to Kgd, Gdh, GltB, PknB, and the N-terminal region of PknG via its FHA domain. OdhI is an essential component of the PknG signaling pathway. It can inhibit the activity of 2-oxoglutarate dehydrogenase only when it is unphosphorylated. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438736 [Multi-domain]  Cd Length: 94  Bit Score: 46.61  E-value: 2.18e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190  26 VVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVPAVDIQDGQSVNIGK 90
Cdd:cd22684    23 TTAGRHPESDIFLDDVTVSRRHAEFRRAEGGFVVRDVGSLNGTYVNRERIDSAVLRNGDEVQIGK 87
PLN03073 PLN03073
ABC transporter F family; Provisional
 296-508 2.18e-06

ABC transporter F family; Provisional


Pssm-ID: 215558 [Multi-domain]  Cd Length: 718  Bit Score: 51.40  E-value: 2.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 296 NFSIGDKNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYAT---PTTGSVtfeghnIHTE---YGSLRTRIGMVPQ 369
Cdd:PLN03073  184 SISVGGRDLIVDASVTLAFGRHYGLVGRNGTGKTTFLRYMAMHAIdgiPKNCQI------LHVEqevVGDDTTALQCVLN 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 370 DDVVHRQLTVNQALGYAAELRLPPDTSKAD---------RAQVVAQVLDEL---------------------GLTKHGDT 419
Cdd:PLN03073  258 TDIERTQLLEEEAQLVAQQRELEFETETGKgkgankdgvDKDAVSQRLEEIykrlelidaytaearaasilaGLSFTPEM 337

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 420 RVDK---LSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLAdagRVVLVVTHSLTYLD-VCDQVLLM 495
Cdd:PLN03073  338 QVKAtktFSGGWRMRIALARALFIEPDLLLLDEPTNHLDLHAVLWLETYLLKWP---KTFIVVSHAREFLNtVVTDILHL 414

                         250
                  ....*....|...
gi 1184609190 496 APGGKTAYLGPPD 508
Cdd:PLN03073  415 HGQKLVTYKGDYD 427
ABCC_SUR2 cd03288
ATP-binding cassette domain 2 of the sulfonylurea receptor SUR; The SUR domain 2. The ...
 302-498 2.21e-06

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


Pssm-ID: 213255 [Multi-domain]  Cd Length: 257  Bit Score: 49.91  E-value: 2.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 302 KNLLERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGHNI-----HTeygsLRTRIGMVPQDDVVhrq 376
Cdd:cd03288    34 KPVLKHVKAYIKPGQKVGICGRTGSGKSSLSLAFFRMVDIFDGKIVIDGIDIsklplHT----LRSRLSIILQDPIL--- 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 377 ltvnqalgYAAELRL---PPDTSKADR---AQVVAQV----------LDELgLTKHGDTrvdkLSGGQRKRASVALELLT 440
Cdd:cd03288   107 --------FSGSIRFnldPECKCTDDRlweALEIAQLknmvkslpggLDAV-VTEGGEN----FSVGQRQLFCLARAFVR 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 441 GPSLLILDEPTSGLDPALD--LQVMTMlrqLADAGRVVLVVTHSLTYLDVCDQVLLMAPG 498
Cdd:cd03288   174 KSSILIMDEATASIDMATEniLQKVVM---TAFADRTVVTIAHRVSTILDADLVLVLSRG 230
SapD COG4170
ABC-type antimicrobial peptide export system, ATPase component SapD [Defense mechanisms];
305-510 2.54e-06

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


Pssm-ID: 443330 [Multi-domain]  Cd Length: 331  Bit Score: 50.29  E-value: 2.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGyATPTTGSVT---FEGHNIHTEYGSLRTR-------IGMVPQDDVvh 374
Cdd:COG4170    23 VDRVSLTLNEGEIRGLVGESGSGKSLIAKAICG-ITKDNWHVTadrFRWNGIDLLKLSPRERrkiigreIAMIFQEPS-- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVNQALGYAAELRLPPDTSKA-------DRAQVVAQVLDELGLTKHGDTRVD---KLSGGQRKRASVALELLTGPSL 444
Cdd:COG4170   100 SCLDPSAKIGDQLIEAIPSWTFKGkwwqrfkWRKKRAIELLHRVGIKDHKDIMNSyphELTEGECQKVMIAMAIANQPRL 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQLAD-AGRVVLVVTHSLTYL-DVCDQVLLMApGGKTAYLGPPDQI 510
Cdd:COG4170   180 LIADEPTNAMESTTQAQIFRLLARLNQlQGTSILLISHDLESIsQWADTITVLY-CGQTVESGPTEQI 246
PRK13546 PRK13546
teichoic acids export ABC transporter ATP-binding subunit TagH;
305-483 2.87e-06

teichoic acids export ABC transporter ATP-binding subunit TagH;


Pssm-ID: 184131 [Multi-domain]  Cd Length: 264  Bit Score: 49.81  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVTFEGhnihtEYGSLRTRIGMVPQ----DDVVHRQLtvn 380
Cdd:PRK13546   40 LDDISLKAYEGDVIGLVGINGSGKSTLSNIIGGSLSPTVGKVDRNG-----EVSVIAISAGLSGQltgiENIEFKML--- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 qALGYAaelrlpPDTSKADRAQVVAqvLDELGLTKHgdTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDL 460
Cdd:PRK13546  112 -CMGFK------RKEIKAMTPKIIE--FSELGEFIY--QPVKKYSSGMRAKLGFSINITVNPDILVIDEALSVGDQTFAQ 180

                         170       180
                  ....*....|....*....|...
gi 1184609190 461 QVMTMLRQLADAGRVVLVVTHSL 483
Cdd:PRK13546  181 KCLDKIYEFKEQNKTIFFVSHNL 203
FHA_DUN1-like cd22683
forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein ...
 23-90 2.89e-06

forkhead associated (FHA) domain found in Saccharomyces cerevisiae DNA damage response protein kinase DUN1 and similar proteins; DUN1 is a protein kinase that controls the DNA damage response in yeast. It phosphorylates SML1 on serine residues and cooperates with the PAN deadenylation complex in the regulation of RAD5 mRNA levels and cell survival in response to replicational stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438735 [Multi-domain]  Cd Length: 96  Bit Score: 46.33  E-value: 2.89e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1184609190  23 GRDVV-VGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRV--PAVDIQDGQSVNIGK 90
Cdd:cd22683    19 NRNVTtIGRSRSCDLVLSDPSISRFHAELRLEQNGINVIDNNSANGTFINGKRIkgKTYILKNGDIIVFGK 89
uvrA PRK00349
excinuclease ABC subunit UvrA;
424-510 3.05e-06

excinuclease ABC subunit UvrA;


Pssm-ID: 234734 [Multi-domain]  Cd Length: 943  Bit Score: 50.84  E-value: 3.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 424 LSGGQRKRASVALELL---TGPSLLILDEPTSGLDPAlDL-QVMTMLRQLADAGRVVLVVTHSltyLDV---CDQVLLMA 496
Cdd:PRK00349  831 LSGGEAQRVKLAKELSkrsTGKTLYILDEPTTGLHFE-DIrKLLEVLHRLVDKGNTVVVIEHN---LDViktADWIIDLG 906

                          90
                  ....*....|....*....
gi 1184609190 497 P-----GGKTAYLGPPDQI 510
Cdd:PRK00349  907 PeggdgGGEIVATGTPEEV 925
GguA NF040905
sugar ABC transporter ATP-binding protein;
305-483 5.13e-06

sugar ABC transporter ATP-binding protein;


Pssm-ID: 468840 [Multi-domain]  Cd Length: 500  Bit Score: 49.79  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAG-YATPT-TGSVTFEGHniHTEYGSLRT--RIGMVpqddVVHRQLTVN 380
Cdd:NF040905   17 LDDVNLSVREGEIHALCGENGAGKSTLMKVLSGvYPHGSyEGEILFDGE--VCRFKDIRDseALGIV----IIHQELALI 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 381 QALGYAAELRLPPDTSKA---DRAQV---VAQVLDELGLTKHGDTRVDKLSGGQRKRASVALELLTGPSLLILDEPTSGL 454
Cdd:NF040905   91 PYLSIAENIFLGNERAKRgviDWNETnrrARELLAKVGLDESPDTLVTDIGVGKQQLVEIAKALSKDVKLLILDEPTAAL 170

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1184609190 455 ---DPA--LDLqvmtmLRQLADAGRVVLVVTHSL 483
Cdd:NF040905  171 neeDSAalLDL-----LLELKAQGITSIIISHKL 199
FHA_DgcB-like cd22682
forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB ...
 24-89 1.13e-05

forkhead associated (FHA) domain found in Bdellovibrio bacteriovorus GGDEF domain protein DgcB and similar proteins; DgcB is a GGDEF enzyme that produces cyclic-di-GMP in response to an unknown stimulus. It appends the C-terminal GGDEF enzymatic domain with an N-terminal forkhead-associated (FHA) domain that acts as a consensus phosphopeptide sensor. The GGDEF and sensory FHA domains form an asymmetrical dimer.


Pssm-ID: 438734 [Multi-domain]  Cd Length: 96  Bit Score: 44.83  E-value: 1.13e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190  24 RDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVP---AVDIQDGQSVNIG 89
Cdd:cd22682    20 STIVIGRSVESQVQIDDDSVSRYHAKLAVNPSAVSIIDLGSTNGTIVNGKKIPklaSCDLQNGDQIKIG 88
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 314-487 1.13e-05

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


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 46.21  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  314 PGTLTAIIGGSGAGKTTLSRLIAGYATPTTGSVtfeghnihteygslrtrigmvpqddvvhrqltvnqalgyaaeLRLPP 393
Cdd:smart00382   1 PGEVILIVGPPGSGKTTLARALARELGPPGGGV------------------------------------------IYIDG 38

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  394 DTSKADRAQVVAQVLdelgltkhgdTRVDKLSGGQRKRASVALELL--TGPSLLILDEPTSGLDPALDLQVM------TM 465
Cdd:smart00382  39 EDILEEVLDQLLLII----------VGGKKASGSGELRLRLALALArkLKPDVLILDEITSLLDAEQEALLLlleelrLL 108

                          170       180
                   ....*....|....*....|..
gi 1184609190  466 LRQLADAGRVVLVVTHSLTYLD 487
Cdd:smart00382 109 LLLKSEKNLTVILTTNDEKDLG 130
ABC_RNaseL_inhibitor cd03222
ATP-binding cassette domain of RNase L inhibitor; The ABC ATPase RNase L inhibitor (RLI) is a ...
 423-506 1.19e-05

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: 46.41  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 423 KLSGGQRKRASVALELLTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAG-RVVLVVTHSLTYLD-VCDQVLLM--APG 498
Cdd:cd03222    71 DLSGGELQRVAIAAALLRNATFYLFDEPSAYLDIEQRLNAARAIRRLSEEGkKTALVVEHDLAVLDyLSDRIHVFegEPG 150


                  ....*...
gi 1184609190 499 GKTAYLGP 506
Cdd:cd03222   151 VYGIASQP 158
AAA_21 pfam13304
AAA domain, putative AbiEii toxin, Type IV TA system; Several members are annotated as being ...
 375-487 1.22e-05

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: 48.15  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVNQALGYAAELRLPPDTSKADRAQVVAQVLDELGLTKHGDTR---VDKLSGGQRK---RASVALELLTGPSLLILD 448
Cdd:pfam13304 185 LQRLVRGLKLADLNLSDLGEGIEKSLLVDDRLRERGLILLENGGGGelpAFELSDGTKRllaLLAALLSALPKGGLLLID 264

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1184609190 449 EPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLD 487
Cdd:pfam13304 265 EPESGLHPKLLRRLLELLKELSRNGAQLILTTHSPLLLD 303
ABC_Rad50 cd03240
ATP-binding cassette domain of Rad50; The catalytic domains of Rad50 are similar to the ...
 317-481 1.76e-05

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


Pssm-ID: 213207 [Multi-domain]  Cd Length: 204  Bit Score: 46.45  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 317 LTAIIGGSGAGKTTLSRLIAgYATpttgsvtfeghnihteYGSLRTRigmvpQDDVVH-RQLTVNQALGYAAELRLppdT 395
Cdd:cd03240    24 LTLIVGQNGAGKTTIIEALK-YAL----------------TGELPPN-----SKGGAHdPKLIREGEVRAQVKLAF---E 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 396 SKADRAQVVAQ---VLDELGLTKHGDTR------VDKLSGGQRKRASVAL-----ELLTGP-SLLILDEPTSGLDPA-LD 459
Cdd:cd03240    79 NANGKKYTITRslaILENVIFCHQGESNwplldmRGRCSGGEKVLASLIIrlalaETFGSNcGILALDEPTTNLDEEnIE 158

                         170       180
                  ....*....|....*....|...
gi 1184609190 460 LQVMTMLR-QLADAGRVVLVVTH 481
Cdd:cd03240   159 ESLAEIIEeRKSQKNFQLIVITH 181
FHA_NBN cd22667
forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also ...
 205-266 2.61e-05

forkhead associated (FHA) domain found in nibrin and similar proteins; Nibrin (NBN), also called cell cycle regulatory protein p95, or Nijmegen breakage syndrome protein 1 (NBS1), is a novel DNA double-strand break repair protein that is mutated in Nijmegen breakage syndrome. It is a component of the MRE11-RAD50-NBN (MRN complex) which plays a critical role in the cellular response to DNA damage and the maintenance of chromosome integrity. Nibrin modulates the DNA damage signal sensing by recruiting PI3/PI4-kinase family members ATM, ATR, and probably DNA-dependent protein kinase catalytic subunit (DNA-PKcs) to the DNA damage sites and activating their functions. It can also recruit MRE11 and RAD50 to the proximity of DSBs by an interaction with the histone H2AX. Nibrin also functions in telomere length maintenance by generating the 3' overhang which serves as a primer for telomerase dependent telomere elongation. Nibrin is a major player in the control of intra-S-phase checkpoint. This subfamily also includes Schizosaccharomyces pombe DNA repair and telomere maintenance protein Nbs1 and Arabidopsis thaliana AtNbs1. SpNbs1 is an FHA domain-containing protein required for DNA damage repair and S-phase DNA damage checkpoint. It is involved in telomere length maintenance and maintenance of chromatin structure. AtNbs1 is a component of MRN complex. It also functions in the very early stages of meiosis. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438719 [Multi-domain]  Cd Length: 108  Bit Score: 43.85  E-value: 2.61e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGT-----------EIRDaHSINGTFVNGIRV---GSAVLAEGDVVTIG 266
Cdd:cd22667    24 VGRKDCDIIIVDDSSISRKHATLTVLHPEAnlsdpdtrpelTLKD-LSKYGTFVNGEKLkggSEVTLKDGDVITFG 98
PRK15093 PRK15093
peptide ABC transporter ATP-binding protein SapD;
305-510 3.12e-05

peptide ABC transporter ATP-binding protein SapD;


Pssm-ID: 185049 [Multi-domain]  Cd Length: 330  Bit Score: 47.10  E-value: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 305 LERVSLTARPGTLTAIIGGSGAGKTTLSRLIAGyATPTTGSVT---FEGHNIHTEYGSLRTR-------IGMVPQDDvvH 374
Cdd:PRK15093   23 VDRVSMTLTEGEIRGLVGESGSGKSLIAKAICG-VTKDNWRVTadrMRFDDIDLLRLSPRERrklvghnVSMIFQEP--Q 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 375 RQLTVNQALGYAAELRLPPDTSKADRAQVVA-------QVLDELGLTKHGDTRVD---KLSGGQRKRASVALELLTGPSL 444
Cdd:PRK15093  100 SCLDPSERVGRQLMQNIPGWTYKGRWWQRFGwrkrraiELLHRVGIKDHKDAMRSfpyELTEGECQKVMIAIALANQPRL 179

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190 445 LILDEPTSGLDPALDLQVMTMLRQL-ADAGRVVLVVTHSLTYLD-VCDQVLLMApGGKTAYLGPPDQI 510
Cdd:PRK15093  180 LIADEPTNAMEPTTQAQIFRLLTRLnQNNNTTILLISHDLQMLSqWADKINVLY-CGQTVETAPSKEL 246
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
 205-266 4.16e-05

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 43.22  E-value: 4.16e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFL-----TATPVGTEIRD-----AHSINGTFVNGIRVGSAVLAEGDVVTIG 266
Cdd:cd22697    22 IGRHPGNDIQIPSQQISRRHATLrrkinPNLDISFWIIDgdlegAESLNGLWVNGERILQHELVNGDEIALG 93
pip_yhgE_Cterm TIGR03062
YhgE/Pip C-terminal domain; This family contains the C-terminal domain of a family of multiple ...
 631-770 4.43e-05

YhgE/Pip C-terminal domain; This family contains the C-terminal domain of a family of multiple membrane-spanning proteins of Gram-positive bacteria. One member was shown to be a host protein essential for phage infection, so many members of this family are called "phage infection protein". A separate model, TIGR03061, represents the conserved N-terminal domain. The domains are separated by regions highly variable in both length and sequence, often containing extended heptad repeats as described in model TIGR03057.


Pssm-ID: 274414 [Multi-domain]  Cd Length: 208  Bit Score: 45.26  E-value: 4.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 631 AVFMGtALTIRDLIgeRAIFRREQAVGLSTGAYLAAKLAVFCVFAVVQAAIVTVIVLVGKGA-PTQPAVLLGnpsfelFV 709
Cdd:TIGR03062  33 ALFVG-ALVLNLIF--PPLSRRALPKSARSWRIALAKLLPGGLIGVIQAIILYGVLILALGLdPAHPPATFG------FA 103

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1184609190 710 TIAAMCVASAVLGLV--LSSLARsseqimPLLVVSLMLQLVLAGGMVPV--TGRiFLDQLSWLLP 770
Cdd:TIGR03062 104 ILTSLTFMAIIQFLValFGSVGR------FLALVLLVLQLGSSGGTFPIelLPA-FFQAIHPFLP 161
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 205-267 5.14e-05

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 46.68  E-value: 5.14e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 205 IGRSLDNDVVVHD----VlaSRHHAFLTATPVGTEIRDaHSINGTFVNGIRV-----GSAVLAEGDVVTIGN 267
Cdd:COG3456    30 IGRSADCDWVLPDpdrsV--SRRHAEIRFRDGAFCLTD-LSTNGTFLNGSDHplgpgRPVRLRDGDRLRIGD 98
COG3456 COG3456
Predicted component of the type VI protein secretion system, contains a FHA domain [Signal ...
 22-183 5.61e-05

Predicted component of the type VI protein secretion system, contains a FHA domain [Signal transduction mechanisms, Intracellular trafficking, secretion, and vesicular transport];


Pssm-ID: 442679 [Multi-domain]  Cd Length: 402  Bit Score: 46.29  E-value: 5.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHP--LVARAHLLLRFDKGRWVAVDnHSLNGVFLNGQRVPA-----VDIQDGQSVNIgkpdGP 94
Cdd:COG3456    24 GRGGGTIGRSADCDWVLPDPdrSVSRRHAEIRFRDGAFCLTD-LSTNGTFLNGSDHPLgpgrpVRLRDGDRLRI----GD 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  95 L-ITFHVGQHQGTVGLLP----------PTETLPTIVAPSGPLPVRPRGPAPRPPAPSRDETPRTDAIP--IIPP--GGP 159
Cdd:COG3456    99 YeIRVEISGEDEGADDPLaaapepavssPSNLSDTEAAPDAALAFSFSLDPLEALDEAATEAPATADDPpsLLPEdwLPS 178

                         170       180
                  ....*....|....*....|....
gi 1184609190 160 ASPAAQEENPPTQIGVSGEIAEFP 183
Cdd:COG3456   179 AAPVADEAAAQAIDQLPSAAAPAP 202
UvrA COG0178
Excinuclease UvrABC ATPase subunit [Replication, recombination and repair];
345-510 6.36e-05

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


Pssm-ID: 439948 [Multi-domain]  Cd Length: 941  Bit Score: 46.56  E-value: 6.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 345 SVTFEGHNIHteygslrtrigmvpqdDVVhrQLTVNQALGYAAELRLPPDtskadRAQVVAQVLDE-------------- 410
Cdd:COG0178   419 AVKIGGKNIA----------------ELT--ALSIDEALEFFENLELTER-----EAEIAERILKEirsrlgflvdvgld 475

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 411 -LGLTKHGDTrvdkLSGG--QRKRasvaleL-------LTGpSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVT 480
Cdd:COG0178   476 yLTLDRSAGT----LSGGeaQRIR------LatqigsgLVG-VLYVLDEPSIGLHQRDNDRLIETLKRLRDLGNTVIVVE 544

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1184609190 481 HsltylD-----VCDQVLLMAP-----GGKTAYLGPPDQI 510
Cdd:COG0178   545 H-----DedtirAADYIIDIGPgagehGGEVVAQGTPEEI 579
FHA_FhaA-like cd22668
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 22-89 7.86e-05

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaA and similar proteins; FhaA regulates cell growth and peptidoglycan synthesis by binding to MviN. It may inhibit the late stages of peptidoglycan synthesis. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438720 [Multi-domain]  Cd Length: 91  Bit Score: 42.07  E-value: 7.86e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190  22 PGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRV-PAVDIQDGQSVNIG 89
Cdd:cd22668    16 REGSNIIGRGSDADFRLPDTGVSRRHAEIRWDGQVAHLTDLGSTNGTTVNNAPVtPEWRLADGDVITLG 84
FHA_EspA-like cd22698
forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA ...
 28-89 1.10e-04

forkhead associated (FHA) domain found in Myxococcus xanthus EspA and similar proteins; EspA is a histidine protein kinase with a fork head-associated (FHA) domain at the N-terminus and a receiver domain at the C-terminus. It functions as an inhibitor of sporulation during early fruiting body development while cells are aggregating into raised mounds. EspA is part of a two-component signal transduction system that regulates the timing of sporulation initiation. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438750 [Multi-domain]  Cd Length: 93  Bit Score: 41.63  E-value: 1.10e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190  28 VGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVPAVDIQDGQSVNIG 89
Cdd:cd22698    25 IGRSSNNDIRLNDHSVSRHHARIVRQGDKCNLTDLGSTNGTFLNGIRVGTHELKHGDRIQLG 86
FHA_ArnA-like cd22680
forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing ...
 23-90 1.15e-04

forkhead associated (FHA) domain found in Sulfolobus Acidocaldarius FHA domain-containing protein ArnA and similar proteins; ArnA is an FHA domain-containing protein from Sulfolobus acidocaldarius that was shown to strongly interact with ArnB, a von Willebrand domain-containing protein. They act synergistically and negatively to modulate motility. ArnA is involved in regulating archaella expression in S. acidocaldarius. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438732 [Multi-domain]  Cd Length: 96  Bit Score: 41.94  E-value: 1.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  23 GRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLN-GQRV-PAVDIQDGQSVNIGK 90
Cdd:cd22680    20 FSSVSIGRDPENVIVIPDPFVSRNHARITVDSNEIYIEDLGSTNGTFVNdFKRIkGPAKLHPNDIIKLGR 89
ABC_sbcCD cd03279
ATP-binding cassette domain of sbcCD; SbcCD and other Mre11/Rad50 (MR) complexes are ...
 317-481 1.42e-04

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


Pssm-ID: 213246 [Multi-domain]  Cd Length: 213  Bit Score: 43.80  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 317 LTAIIGGSGAGKTTLSRLIAgYA----TPTTGSVTFEGHNIHTEYGSLR----TRIGmvPQDDVVHRQLTVNQalgyaae 388
Cdd:cd03279    30 LFLICGPTGAGKSTILDAIT-YAlygkTPRYGRQENLRSVFAPGEDTAEvsftFQLG--GKKYRVERSRGLDY------- 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 389 lrlppDTSKadRAQVVAQ-VLDELgLTKHgdtrVDKLSGGQRKRASVALEL--------LTGPSL--LILDEPTSGLDPA 457
Cdd:cd03279   100 -----DQFT--RIVLLPQgEFDRF-LARP----VSTLSGGETFLASLSLALalsevlqnRGGARLeaLFIDEGFGTLDPE 167

                         170       180
                  ....*....|....*....|....
gi 1184609190 458 LDLQVMTMLRQLADAGRVVLVVTH 481
Cdd:cd03279   168 ALEAVATALELIRTENRMVGVISH 191
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 205-266 1.49e-04

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 42.02  E-value: 1.49e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEI--RDAHSINGTFVNGIRVGSAV---LAEGDVVTIG 266
Cdd:cd22691    33 VGRHPDCDIVLDHPSISRFHLEIRIIPSRRKItlTDLSSVHGTWVNGQRIEPGVpveLEEGDTVRLG 99
FHA_PP2C70-like cd22678
forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 ...
 197-266 1.55e-04

forkhead associated (FHA) domain found in Arabidopsis thaliana protein phosphatase 2C 70 (AtPP2C70) and similar proteins; AtPP2C70, also called kinase-associated protein phosphatase, or protein ROOT ATTENUATED GROWTH 1, dephosphorylates the serine/threonine receptor-like kinase RLK5. It may function as a signaling component in a pathway involving RLK5. It acts as a negative regulator of the CLAVATA1 signaling in plant development by binding and dephosphorylating CLAVATA1. It is also a component of a signaling pathway which mediates adaptation to NaCl stress. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438730 [Multi-domain]  Cd Length: 102  Bit Score: 41.58  E-value: 1.55e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 197 APVTGAA-WIGRSLDNDVVVHDVLASRHHAFLTATPVGT--EIRDAHSINGTFVNG----IRVGSAVLAEGDVVTIG 266
Cdd:cd22678    18 QPGTRLPlTIGRIQRGDIALKDDEVSGKHARIEWNSTGSkwELVDLGSLNGTLVNGesisPNGRPVVLSSGDVITLG 94
FHA_Rv1747-like_rpt2 cd22737
second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ...
 8-89 2.32e-04

second forkhead associated (FHA) domain found in Mycobacterium tuberculosis ABC transporter ATP-binding/permease protein Rv1747 and similar proteins; Rv1747 is a putative ATP-binding cassette (ABC) transporter involved in the translocation of an unknown substrate across the membrane. It is required for normal virulent infection by M. tuberculosis. Rv1747 has a cytoplasmic regulatory module consisting of two pThr-interacting forkhead-associated (FHA) domains connected by a conformationally disordered linker with two phospho-acceptor threonines (pThr). Recruitment and phosphorylation of Rv1747 depend on the interaction between its two non-redundant FHA domains and the autophosphorylated form of serine/threonine protein kinase PknF. This model corresponds to the second FHA domain, which has a circularly permuted FHA domain fold with a conserved pThr-binding interface.


Pssm-ID: 439356 [Multi-domain]  Cd Length: 93  Bit Score: 40.94  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190   8 VLTVRSQRWEGNFAPGRdVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRVPAVDIQDGQSVN 87
Cdd:cd22737     6 ITRPDGDTLTFELPPQA-VRIGRASDNDIVIPEGSVSRHHATLVPTPGGTQIRDLRSTNGTFVNGLRVDAALLHDGDVVT 84


                  ..
gi 1184609190  88 IG 89
Cdd:cd22737    85 IG 86
FHA_PS1-like cd22691
forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) ...
 19-89 2.59e-04

forkhead associated (FHA) domain found in Arabidopsis thaliana Protein PARALLEL SPINDLE 1 (PS1) and similar proteins; PS1 is an FHA domain-containing protein required for normal spindle orientation at male meiosis II and normal formation of tetrad of microspores. It is not involved in female meiosis. Mutations in PS1 lead to the production of diploid pollen grains. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438743 [Multi-domain]  Cd Length: 113  Bit Score: 41.25  E-value: 2.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1184609190  19 NFAPGRDVVVGSDVRADLRVAHPLVARAHLLLRFDKGR--WVAVDNHSLNGVFLNGQRVPA---VDIQDGQSVNIG 89
Cdd:cd22691    24 KSEEEDILVVGRHPDCDIVLDHPSISRFHLEIRIIPSRrkITLTDLSSVHGTWVNGQRIEPgvpVELEEGDTVRLG 99
FHA_MDC1 cd22665
forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) ...
 205-272 2.78e-04

forkhead associated (FHA) domain found in mediator of DNA damage checkpoint protein 1 (MDC1) and similar proteins; MDC1, also called nuclear factor with BRCT domains 1 (NFBD1), is a nuclear chromatin-associated protein that is required for checkpoint mediated cell cycle arrest in response to DNA damage within both the S and G2/M phases of the cell cycle. It directly binds phosphorylated histone H2AX to regulate cellular responses to DNA double-strand breaks. MDC1 contains a forkhead-associated (FHA) domain and two BRCT domains, as well as an internal 41-amino acid repeat sequence. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438717 [Multi-domain]  Cd Length: 97  Bit Score: 40.68  E-value: 2.78e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFLTATPVGTEIRDAHSINGTFVN-GIRVGSAV---LAEGDVVTIGNVDLVF 272
Cdd:cd22665    25 IGRDPSCSVVLPDKSVSKQHACIEVDGGTHLIEDLGSTNGTRIGnKVRLKPNVryeLIDGDLLLFGDVKCQY 96
FHA_SLMAP cd22679
forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and ...
 198-271 2.80e-04

forkhead associated (FHA) domain found in sarcolemmal membrane-associated protein (SLMAP) and similar proteins; SLMAP, also called sarcolemmal-associated protein (SLAP), is a tail-anchored protein involved in fundamental cellular processes, such as myoblast fusion, cell cycle progression, and chromosomal inheritance. It is a cardiac membrane protein that plays an important role in E-C coupling and the adrenergic response of the heart. Overexpression of the SLMAP gene has been associated with diabetes and endothelial dysfunction of macro- and micro-blood vessels. SLMAP contains an N-terminal FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438731 [Multi-domain]  Cd Length: 126  Bit Score: 41.48  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 198 PVTGAAWIGRSL-------DNDVVVHDVLaSRHHAFLTATPVGTEIRDAHSINGTFVNGIRVGSAV-------LAEGDVV 263
Cdd:cd22679    21 VLDEPVKIGRSVararpaaNNAIFDCKVL-SRNHALLWYDDGKFYLQDTKSSNGTFVNNQRLSKGSeesepreLHSGDIV 99


                  ....*...
gi 1184609190 264 TIGnVDLV 271
Cdd:cd22679   100 QFG-VDVV 106
ABC2_membrane_2 pfam12679
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 568-773 2.81e-04

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family.


Pssm-ID: 403774 [Multi-domain]  Cd Length: 281  Bit Score: 43.54  E-value: 2.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 568 TIARRQVRLVVSDRAYFVFLALLpFVLGALSL--------------TVPGNTGFGIASPTSGTPDESAQILTLTSVAAVF 633
Cdd:pfam12679   2 AIAKKEFRDSIRSRRFWALTVLL-PLLVALAFyldyggslpqgakqIVELLLAFEYVSAASALDEADDTDIDITAFLIPV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 634 MGTALTIRDLIGERA--IFRREQAVGLSTGAYLAAKLAVFCVFAVVQAAIVTVIVLVGKGAPtqpAVLLGNPSFELFVTI 711
Cdd:pfam12679  81 IAALLGADAIAGERErgTIELLLSLPVSRSEILLGKFIGRLAIGLILAVALLAGVLLALAIT---LALGDPLDLGDLLLL 157

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190 712 AAMCVASAV------LGLVLSSLARSSEQ-----IMPLLVVSLMLQLVLAGGMVPVTGRIF----LDQLSWLLPSRW 773
Cdd:pfam12679 158 VAASVLLALalvflsIGLLLSSVARSTRTaaaiaLGLFFVLAILWPIVLYGLAELLAGPAPpqelLDFLLFLNPTSP 234
FHA_FhaB-like cd22693
forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing ...
 35-90 3.05e-04

forkhead associated (FHA) domain found in Mycobacterium tuberculosis FHA domain-containing protein FhaB and similar proteins; FhaB, also called FtsZ-interacting protein A (FipA), is a putative virulence factor involved in regulating cell shape. It can interact with polyketide-associated protein PapA5, a putative membrane protein involved in the biosynthesis of virulence enhancing lipids. FhaB regulates growth and cell division. It is probably required for divisomal protein assembly under oxidative stress. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438745 [Multi-domain]  Cd Length: 91  Bit Score: 40.36  E-value: 3.05e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1184609190  35 DLRVAHPLVARAHLLLRFDKGRWVAVDNHSLNGVFLNGQRV-PAVDIQDGQSVNIGK 90
Cdd:cd22693    29 DLVLSDDFVSSRHARIYLQGSSWYLEDLGSTNGTFVNGNRVtQPVVVQPGDTIRIGA 85
FHA_Ki67 cd22673
forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar ...
 24-90 3.46e-04

forkhead associated (FHA) domain found in proliferation marker protein Ki-67 and similar proteins; Ki-67, also called antigen identified by monoclonal antibody Ki-67, antigen KI-67, or antigen Ki67, acts as a biological surfactant to disperse mitotic chromosomes. It is required to maintain individual mitotic chromosomes dispersed in the cytoplasm following nuclear envelope disassembly. Ki-67 binds DNA with a preference for supercoiled DNA and AT-rich DNA. It may also play a role in chromatin organization. Ki-67 contains an FHA domain at its N-terminus. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438725 [Multi-domain]  Cd Length: 95  Bit Score: 40.27  E-value: 3.46e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1184609190  24 RDVVVGSDVRADLRVAHPLVARAHLLLRFDKGRWVAVDNHS-LNGVFLNGQRVPA-VDIQDGQSVNIGK 90
Cdd:cd22673    21 KSCTFGRDLSCDIRIQLPGVSREHCRIEVDENGKAYLENLStTNPTLVNGKAIEKsAELKDGDVITIGG 89
FHA_VPS64-like cd22695
forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein ...
 221-266 6.74e-04

forkhead associated (FHA) domain found in Saccharomyces cerevisiae vacuolar protein sorting-associated protein 64 (VPS64) and similar proteins; This subfamily includes VPS64 (also called factor arrest protein 9 or FAR9) and factor arrest protein 10 (FAR10), which participate in the control of the re-entry into the cell cycle following pheromone treatment. VPS64 is also involved in vacuolar protein sorting. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438747 [Multi-domain]  Cd Length: 133  Bit Score: 40.75  E-value: 6.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1184609190 221 SRHHAFLTATPVGTE--IRDAHSINGTFVNGIRVG--SAVLAEGDVVTIG 266
Cdd:cd22695    66 SRNHACLSCDPTTGKvyIRDLKSSNGTFVNGQKIRqnDVELKVGDEVDLG 115
PRK00635 PRK00635
excinuclease ABC subunit A; Provisional
 442-510 1.90e-03

excinuclease ABC subunit A; Provisional


Pssm-ID: 234806 [Multi-domain]  Cd Length: 1809  Bit Score: 42.12  E-value: 1.90e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1184609190  442 PSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHSLTYLDVCDQVLLMAPG-----GKTAYLGPPDQI 510
Cdd:PRK00635  1721 PTLFLLDEIATSLDNQQKSALLVQLRTLVSLGHSVIYIDHDPALLKQADYLIEMGPGsgktgGKILFSGPPKDI 1794
FHA_Slr1951-like cd22697
forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar ...
 28-89 2.41e-03

forkhead associated (FHA) domain found in Synechocystis sp. Slr1951 protein and similar proteins; This subfamily corresponds to a group of uncharacterized FHA domain-containing proteins which show high sequence similarity with Synechocystis sp. protein Slr1951 and protein Sll1895. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438749 [Multi-domain]  Cd Length: 102  Bit Score: 38.21  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190  28 VGSDVRADLRVAHPLVARAHLLLR------FDKGRWVAVD----NHSLNGVFLNGQRVPAVDIQDGQSVNIG 89
Cdd:cd22697    22 IGRHPGNDIQIPSQQISRRHATLRrkinpnLDISFWIIDGdlegAESLNGLWVNGERILQHELVNGDEIALG 93
COG3910 COG3910
Predicted ATPase [General function prediction only];
439-482 3.13e-03

Predicted ATPase [General function prediction only];


Pssm-ID: 443116 [Multi-domain]  Cd Length: 239  Bit Score: 40.13  E-value: 3.13e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1184609190 439 LTGPSLLILDEPTSGLDPALDLQVMTMLRQLADAGRVVLVVTHS 482
Cdd:COG3910   150 FRGNGLYLLDEPEAALSPSRQLALLALIHDLVREGSQFIIATHS 193
VI_FHA TIGR03354
type VI secretion system FHA domain protein; Members of this protein family are FHA ...
 205-281 5.73e-03

type VI secretion system FHA domain protein; Members of this protein family are FHA (forkhead-associated) domain-containing proteins that are part of type VI secretion loci in a considerable number of bacteria, most of which are known pathogens. Species include Pseudomonas aeruginosa PAO1, Aeromonas hydrophila, Yersinia pestis, Burkholderia mallei, etc. [Protein fate, Protein and peptide secretion and trafficking, Cellular processes, Pathogenesis]


Pssm-ID: 274537 [Multi-domain]  Cd Length: 396  Bit Score: 40.05  E-value: 5.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190 205 IGRSLDNDVVVHD--VLASRHHAFLTATPVGTEIRDaHSINGTFVNG----IRVG-SAVLAEGDVVTIGNVDL-VFTGGI 276
Cdd:TIGR03354  28 IGRSEDCDWVLPDpeRHVSGRHARIRYRDGAYLLTD-LSTNGVFLNGsgspLGRGnPVRLEQGDRLRLGDYEIrVSLGDP 106


                  ....*
gi 1184609190 277 LVRRQ 281
Cdd:TIGR03354 107 LVSRQ 111
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 205-267 7.05e-03

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 36.77  E-value: 7.05e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1184609190 205 IGRSLDNDVVVHDVLASRHHAFL------TATPVGTEIRDAHSINGTFVNGIRVGSAV---LAEGDVVTIGN 267
Cdd:cd22677    26 FGRLPGCDVVLEHPSISRYHAVLqyrgdaDDHDGGFYLYDLGSTHGTFLNKQRIPPKQyyrLRVGHVLKFGG 97
FHA_MEK1-like cd22670
forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine ...
 22-75 8.05e-03

forkhead associated (FHA) domain found in Saccharomyces cerevisiae meiosis-specific serine/threonine-protein kinase MEK1 and similar proteins; MEK1 (EC 2.7.11.1), also known as MRE4, is a meiosis-specific protein kinase required for chromosome synapsis and meiotic recombination. The recruitment and activation of MEK1 require the phosphorylation of the chromosome axis protein Hop1 at Thr318 (pT318), which is necessary for recognition by the MEK1 FHA domain. The FHA domain is a small phosphopeptide recognition module.


Pssm-ID: 438722 [Multi-domain]  Cd Length: 105  Bit Score: 36.82  E-value: 8.05e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1184609190  22 PGRDVVVGSDVRADLRVAHPLVARAHLLL---RFDKGRWVAV---DNhSLNGVFLNGQRV 75
Cdd:cd22670    20 KNQVITIGRSPSCDIVINDPFVSRTHCRIysvQFDESSAPLVyveDL-SSNGTYLNGKLI 78
FHA_Kanadaptin cd22677
forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also ...
 26-77 9.61e-03

forkhead associated (FHA) domain found in kanadaptin and similar proteins; Kanadaptin, also called human lung cancer oncogene 3 protein (HLC-3), kidney anion exchanger adapter protein, or solute carrier family 4 anion exchanger member 1 adapter protein (SLC4A1AP), is a nuclear protein widely expressed in mammalian tissues. It was originally isolated as a kidney Cl-/HCO3- anion exchanger 1 (kAE1)-binding protein. It is a highly mobile nucleocytoplasmic shuttling and multilocalizing protein. Its role in mammalian cells remains unclear. It contains an FHA domain, which is a small phosphopeptide recognition module.


Pssm-ID: 438729 [Multi-domain]  Cd Length: 106  Bit Score: 36.38  E-value: 9.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1184609190  26 VVVGSDVRADLRVAHPLVARAHLLLRFD------KGRWVAVDNHSLNGVFLNGQRVPA 77
Cdd:cd22677    24 YVFGRLPGCDVVLEHPSISRYHAVLQYRgdaddhDGGFYLYDLGSTHGTFLNKQRIPP 81
 
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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