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Conserved domains on  [gi|446651616|ref|WP_000728962|]
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type VII secretion protein EsaA [Staphylococcus aureus]

Protein Classification

YhgE/Pip domain-containing protein( domain architecture ID 11445492)

YhgE/Pip (phage infection protein) domain-containing protein similar to the membrane protein EsaA of the Staphylococcus aureus ESS/Type VII secretion system, Bacillus subtilis ESX secretion system protein YueB, and uncharacterized protein YhgE

Gene Ontology:  GO:0016020

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
pip_yhgE_Nterm super family cl19580
YhgE/Pip N-terminal domain; This family contains the N-terminal domain of a family of multiple ...
44-208 1.02e-36

YhgE/Pip N-terminal domain; This family contains the N-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, TIGR03062, represents the conserved C-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.


The actual alignment was detected with superfamily member TIGR03929:

Pssm-ID: 354443 [Multi-domain]  Cd Length: 193  Bit Score: 137.16  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616    44 NKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKT 123
Cdd:TIGR03929   29 NQNAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEWSVVSRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKEN 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   124 PSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPIND 203
Cdd:TIGR03929  109 PEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASILQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSAN 188

                   ....*
gi 446651616   204 FPELF 208
Cdd:TIGR03929  189 LTNQF 193
SCP-1 super family cl30946
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
239-741 2.31e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


The actual alignment was detected with superfamily member pfam05483:

Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   239 DTFRVNTDYNVStlIEKQNSLFEE-----HNTAMD---KMLQDY-KSQKDSVELDNYINALKQMDSQIDQQSSMQDTGKE 309
Cdd:pfam05483  180 ETRQVYMDLNNN--IEKMILAFEElrvqaENARLEmhfKLKEDHeKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   310 EYKQTVKENLDK--------------LREIIQSQESPFSKgmIEDYRKQLTESLQDELANNKDLQDALNSI----KMNNA 371
Cdd:pfam05483  258 DLTFLLEESRDKanqleektklqdenLKELIEKKDHLTKE--LEDIKMSLQRSMSTQKALEEDLQIATKTIcqltEEKEA 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   372 QFAE-NLEKQLHDDIVKEPDTDTTFIYNMSKQDFIAAGLNED-------EANKYEAIVKEAKRYKNEYN-----LKKPLA 438
Cdd:pfam05483  336 QMEElNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDqlkiitmELQKKSSELEEMTKFKNNKEveleeLKKILA 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   439 EHINLTDYDNQVAQdtsslINDGVKVKRTETIksndinqltvatdphfnfegdIKINGKKYDIKDQSVQLDTSNKEYKVE 518
Cdd:pfam05483  416 EDEKLLDEKKQFEK-----IAEELKGKEQELI---------------------FLLQAREKEIHDLEIQLTAIKTSEEHY 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   519 VNGVAKLKKDAEKDFLKDKSmhlqlLFGQANRQDEPNDKKATSVVDVTLnhnldgrlskdalsqqlsalsRFDAHYKMYT 598
Cdd:pfam05483  470 LKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMTL---------------------ELKKHQEDII 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   599 DTKGREDKPFDNKRLIDMMVDQVINDMES----FKDDKVAVLHQIDSMEENSDKLIDDILNNKKNTTKNKEDISKLIDQL 674
Cdd:pfam05483  524 NCKKQEERMLKQIENLEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   675 ENVKKTFAEEPQEPKIDKGKN-------------------------DEFNTMSSNLDKEIS--RISEKstQLLSDTQESK 727
Cdd:pfam05483  604 ENKNKNIEELHQENKALKKKGsaenkqlnayeikvnklelelasakQKFEEIIDNYQKEIEdkKISEE--KLLEEVEKAK 681
                          570
                   ....*....|....
gi 446651616   728 SIADSVSGQLNQVD 741
Cdd:pfam05483  682 AIADEAVKLQKEID 695
ABC2_membrane_3 super family cl38365
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
774-999 3.25e-04

ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter family pfam01061.


The actual alignment was detected with superfamily member pfam12698:

Pssm-ID: 463674 [Multi-domain]  Cd Length: 345  Bit Score: 43.92  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   774 LFAKEFKKVLQNSKDGDRQNQALKAFMSNPVQKKNLENVLANNGNTDVISPTLFVLLMYLLSMITAYIFYSyERAKGQMN 853
Cdd:pfam12698  115 LILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVE-EKESRIKE 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   854 FIKDDYSSKNHLWN-NVITSGVIGttgLVEGLIVGLIAMNkFHVLAGYRAKFILMVILTMMVFVLInTYLL-------RQ 925
Cdd:pfam12698  194 RLLVSGVSPLQYWLgKILGDFLVG---LLQLLIILLLLFG-IGIPFGNLGLLLLLFLLYGLAYIAL-GYLLgslfknsED 268
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446651616   926 VKSIGMFLMIAALGLYFVA--MNNLKAAGQGVTnKISPLSYIDNMFFNYLNAEH--PIGLALVILTVLVIIGFVLNMF 999
Cdd:pfam12698  269 AQSIIGIVILLLSGFFGGLfpLEDPPSFLQWIF-SIIPFFSPIDGLLRLIYGDSlwEIAPSLIILLLFAVVLLLLALL 345
 
Name Accession Description Interval E-value
T7_esaA_Nterm TIGR03929
type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with ...
44-208 1.02e-36

type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This model represents the conserved N-terminal domain.


Pssm-ID: 274861 [Multi-domain]  Cd Length: 193  Bit Score: 137.16  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616    44 NKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKT 123
Cdd:TIGR03929   29 NQNAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEWSVVSRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKEN 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   124 PSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPIND 203
Cdd:TIGR03929  109 PEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASILQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSAN 188

                   ....*
gi 446651616   204 FPELF 208
Cdd:TIGR03929  189 LTNQF 193
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
44-168 2.28e-29

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 441120  Cd Length: 225  Bit Score: 116.97  E-value: 2.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   44 NKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKT 123
Cdd:COG1511    41 GNLDNLPVAVVNEDKGATVDGKTVNLGDELVDELKDNDSFDWQFVSEEEAEKGLKDGKYYAVIVIPEDFSANLASLLSDD 120
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446651616  124 PSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSI 168
Cdd:COG1511   121 PEKATITYYTNEANNYLASKITDTAATTVVDQVNSQVTETYAETV 165
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
239-741 2.31e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   239 DTFRVNTDYNVStlIEKQNSLFEE-----HNTAMD---KMLQDY-KSQKDSVELDNYINALKQMDSQIDQQSSMQDTGKE 309
Cdd:pfam05483  180 ETRQVYMDLNNN--IEKMILAFEElrvqaENARLEmhfKLKEDHeKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   310 EYKQTVKENLDK--------------LREIIQSQESPFSKgmIEDYRKQLTESLQDELANNKDLQDALNSI----KMNNA 371
Cdd:pfam05483  258 DLTFLLEESRDKanqleektklqdenLKELIEKKDHLTKE--LEDIKMSLQRSMSTQKALEEDLQIATKTIcqltEEKEA 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   372 QFAE-NLEKQLHDDIVKEPDTDTTFIYNMSKQDFIAAGLNED-------EANKYEAIVKEAKRYKNEYN-----LKKPLA 438
Cdd:pfam05483  336 QMEElNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDqlkiitmELQKKSSELEEMTKFKNNKEveleeLKKILA 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   439 EHINLTDYDNQVAQdtsslINDGVKVKRTETIksndinqltvatdphfnfegdIKINGKKYDIKDQSVQLDTSNKEYKVE 518
Cdd:pfam05483  416 EDEKLLDEKKQFEK-----IAEELKGKEQELI---------------------FLLQAREKEIHDLEIQLTAIKTSEEHY 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   519 VNGVAKLKKDAEKDFLKDKSmhlqlLFGQANRQDEPNDKKATSVVDVTLnhnldgrlskdalsqqlsalsRFDAHYKMYT 598
Cdd:pfam05483  470 LKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMTL---------------------ELKKHQEDII 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   599 DTKGREDKPFDNKRLIDMMVDQVINDMES----FKDDKVAVLHQIDSMEENSDKLIDDILNNKKNTTKNKEDISKLIDQL 674
Cdd:pfam05483  524 NCKKQEERMLKQIENLEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   675 ENVKKTFAEEPQEPKIDKGKN-------------------------DEFNTMSSNLDKEIS--RISEKstQLLSDTQESK 727
Cdd:pfam05483  604 ENKNKNIEELHQENKALKKKGsaenkqlnayeikvnklelelasakQKFEEIIDNYQKEIEdkKISEE--KLLEEVEKAK 681
                          570
                   ....*....|....
gi 446651616   728 SIADSVSGQLNQVD 741
Cdd:pfam05483  682 AIADEAVKLQKEID 695
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
774-999 3.25e-04

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: 43.92  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   774 LFAKEFKKVLQNSKDGDRQNQALKAFMSNPVQKKNLENVLANNGNTDVISPTLFVLLMYLLSMITAYIFYSyERAKGQMN 853
Cdd:pfam12698  115 LILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVE-EKESRIKE 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   854 FIKDDYSSKNHLWN-NVITSGVIGttgLVEGLIVGLIAMNkFHVLAGYRAKFILMVILTMMVFVLInTYLL-------RQ 925
Cdd:pfam12698  194 RLLVSGVSPLQYWLgKILGDFLVG---LLQLLIILLLLFG-IGIPFGNLGLLLLLFLLYGLAYIAL-GYLLgslfknsED 268
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446651616   926 VKSIGMFLMIAALGLYFVA--MNNLKAAGQGVTnKISPLSYIDNMFFNYLNAEH--PIGLALVILTVLVIIGFVLNMF 999
Cdd:pfam12698  269 AQSIIGIVILLLSGFFGGLfpLEDPPSFLQWIF-SIIPFFSPIDGLLRLIYGDSlwEIAPSLIILLLFAVVLLLLALL 345
iSH2_PIK3R1 cd12924
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
249-381 7.32e-04

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.


Pssm-ID: 214017 [Multi-domain]  Cd Length: 161  Bit Score: 41.22  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616  249 VSTLIEKQNSLFEEHNTAMDKMLQDYKSQKDSVELD-NYINALKQMDSQIDQQSSMQDTGKEEYKQTVKE--NLDKLREI 325
Cdd:cd12924     6 VGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKrTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKRegNEKEIQRI 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446651616  326 IQSQESPFSK-GMIEDYRKQLTESLQDELANNKDLQDALNSIKMNNAQFAENLEKQL 381
Cdd:cd12924    86 MHNYEKLKSRiSEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYL 142
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
43-198 7.39e-04

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: 43.15  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616    43 SNKNNKIHIAIVNEDqpttyngkKVELGQAFIKRLANEK--NYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLD 120
Cdd:pfam12698   26 VNDPEELPVAVVDED--------NSSLSRQLVRALEASPtvNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGE 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446651616   121 AKTPSKISLqyktavGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNlhnaqKNVGAIMTREHGVNSKFSNYLL 198
Cdd:pfam12698   98 SATVTVYIN------SSNLLVSKLILNALQSLLQQLNASALVLLLEALSTS-----APIPVESTPLFNPQSGYAYYLV 164
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
143-731 4.31e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.19  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   143 KNTEKVVSNVLNDFNK--NLVEIYLTSI--IDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPINdFPELFTDTLVNSISA 218
Cdd:TIGR01612  761 KNKEKELSNKINDYAKekDELNKYKSKIseIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIS-IKEDEIFKIINEMKF 839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   219 NKDitKWFQTYNKSLLSANSDTFRVNTDY-NVSTLIEK-QNSLFEEHNTAMDKMLQDYKS----QKDSVELD-NYINALK 291
Cdd:TIGR01612  840 MKD--DFLNKVDKFINFENNCKEKIDSEHeQFAELTNKiKAEISDDKLNDYEKKFNDSKSlineINKSIEEEyQNINTLK 917
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   292 QMDSQIDQQSSMQDTGKE------EYKQTVKENLDKLRE---IIQSQESPFSKGMIE---DYRKQLTE-SLQDELANNKD 358
Cdd:TIGR01612  918 KVDEYIKICENTKESIEKfhnkqnILKEILNKNIDTIKEsnlIEKSYKDKFDNTLIDkinELDKAFKDaSLNDYEAKNNE 997
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   359 LQDALNSIKMNNA---------QFAENlEKQLHDDIVKEPDTDT----------TFIYNMSKQDFIAAGLNEDEANKyeA 419
Cdd:TIGR01612  998 LIKYFNDLKANLGknkenmlyhQFDEK-EKATNDIEQKIEDANKnipnieiaihTSIYNIIDEIEKEIGKNIELLNK--E 1074
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   420 IVKEAKRYKNEYNLKKPLAEHINLTDYdnqVAQDTSSLINDGVKVKrtetiksNDINQLTVATDPHFNFEGDIKINGKKY 499
Cdd:TIGR01612 1075 ILEEAEINITNFNEIKEKLKHYNFDDF---GKEENIKYADEINKIK-------DDIKNLDQKIDHHIKALEEIKKKSENY 1144
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   500 dikdqsvqldtsNKEYKVEVNgvaKLKKDAEKDFLKDKSmhlqllfgqanrqDEPNDKKATSVVDVTLNHNLdgrlsKDA 579
Cdd:TIGR01612 1145 ------------IDEIKAQIN---DLEDVADKAISNDDP-------------EEIEKKIENIVTKIDKKKNI-----YDE 1191
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   580 LSQQLSALSRFDAHYKMYTDTKGredkpfdnkrlIDMMVDQVINDMesfkddkvaVLHQIDSMEENSDKLIddilnnkkn 659
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEEVKG-----------INLSYGKNLGKL---------FLEKIDEEKKKSEHMI--------- 1242
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   660 ttknkEDISKLIDQLENVKKTFAEEPQEPKIDKGKNDEFNTM-------------SSNLDKEISRISEKSTQLLSDTQES 726
Cdd:TIGR01612 1243 -----KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFnishdddkdhhiiSKKHDENISDIREKSLKIIEDFSEE 1317

                   ....*
gi 446651616   727 KSIAD 731
Cdd:TIGR01612 1318 SDIND 1322
MFS_YajR_like cd17472
Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux ...
884-996 9.55e-03

Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli inner membrane transport protein YajR and some uncharacterized multidrug-efflux transporters. YajR is a putative proton-driven major facilitator superfamily (MFS) transporter found in many gram-negative bacteria. Unlike most MFS transporters, YajR contains a C-terminal, cytosolic YAM domain, which may play an essential role for the proper functioning of the transporter. YajR-like transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341025 [Multi-domain]  Cd Length: 371  Bit Score: 39.51  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616  884 LIVGLIAMNKFHVLA-GYRAKFILMVILTMMVFVlinTYLLRQVKSIGMFLMIAALGLYFVAMNNLKAAGQGVTNKISPL 962
Cdd:cd17472   239 ILIGFILMVPFVIYAeKKGKMKQVFVSSILLIAV---GFLLLLFAATSLWLLIIGLIIFFIGFNLLEALLPSLVSKIAPK 315
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446651616  963 SY------IDNMF---------------FNYLNAEHPIGLALVILTVLVIIGFVL 996
Cdd:cd17472   316 EYrgtamgIYNTSqflgsflggalggllWGLLGYSSVFLTILILALLWLLVSFLL 370
 
Name Accession Description Interval E-value
T7_esaA_Nterm TIGR03929
type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with ...
44-208 1.02e-36

type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with type VII secretion of WXG100 family targets in the Firmicutes, but not in the Actinobacteria. This model represents the conserved N-terminal domain.


Pssm-ID: 274861 [Multi-domain]  Cd Length: 193  Bit Score: 137.16  E-value: 1.02e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616    44 NKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKT 123
Cdd:TIGR03929   29 NQNAKMNIAVVNEDQGVSFDGKTYNFGASFVKAIERDNSQEWSVVSRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKEN 108
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   124 PSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPIND 203
Cdd:TIGR03929  109 PEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASILQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSAN 188

                   ....*
gi 446651616   204 FPELF 208
Cdd:TIGR03929  189 LTNQF 193
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
44-168 2.28e-29

Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown];


Pssm-ID: 441120  Cd Length: 225  Bit Score: 116.97  E-value: 2.28e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   44 NKNNKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKT 123
Cdd:COG1511    41 GNLDNLPVAVVNEDKGATVDGKTVNLGDELVDELKDNDSFDWQFVSEEEAEKGLKDGKYYAVIVIPEDFSANLASLLSDD 120
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 446651616  124 PSKISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSI 168
Cdd:COG1511   121 PEKATITYYTNEANNYLASKITDTAATTVVDQVNSQVTETYAETV 165
pip_yhgE_Nterm TIGR03061
YhgE/Pip N-terminal domain; This family contains the N-terminal domain of a family of multiple ...
47-168 3.35e-21

YhgE/Pip N-terminal domain; This family contains the N-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, TIGR03062, represents the conserved C-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: 274413 [Multi-domain]  Cd Length: 164  Bit Score: 91.50  E-value: 3.35e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616    47 NKIHIAIVNEDQPTTYNGKKVELGQAFIKRLANEKNYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLDAKTPSK 126
Cdd:TIGR03061   42 DNLPVAVVNEDKGATYDGKTLNAGDDLVKELKKNDDLDWHFVSAKEAEKGLADGKYYMVITIPEDFSENATSLLDDQPKK 121
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 446651616   127 ISLQYKTAVGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSI 168
Cdd:TIGR03061  122 AQLIYKTNDANNYIASQIAESAAEKVKTSVSKSITETYAETI 163
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
239-741 2.31e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.10  E-value: 2.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   239 DTFRVNTDYNVStlIEKQNSLFEE-----HNTAMD---KMLQDY-KSQKDSVELDNYINALKQMDSQIDQQSSMQDTGKE 309
Cdd:pfam05483  180 ETRQVYMDLNNN--IEKMILAFEElrvqaENARLEmhfKLKEDHeKIQHLEEEYKKEINDKEKQVSLLLIQITEKENKMK 257
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   310 EYKQTVKENLDK--------------LREIIQSQESPFSKgmIEDYRKQLTESLQDELANNKDLQDALNSI----KMNNA 371
Cdd:pfam05483  258 DLTFLLEESRDKanqleektklqdenLKELIEKKDHLTKE--LEDIKMSLQRSMSTQKALEEDLQIATKTIcqltEEKEA 335
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   372 QFAE-NLEKQLHDDIVKEPDTDTTFIYNMSKQDFIAAGLNED-------EANKYEAIVKEAKRYKNEYN-----LKKPLA 438
Cdd:pfam05483  336 QMEElNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDqlkiitmELQKKSSELEEMTKFKNNKEveleeLKKILA 415
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   439 EHINLTDYDNQVAQdtsslINDGVKVKRTETIksndinqltvatdphfnfegdIKINGKKYDIKDQSVQLDTSNKEYKVE 518
Cdd:pfam05483  416 EDEKLLDEKKQFEK-----IAEELKGKEQELI---------------------FLLQAREKEIHDLEIQLTAIKTSEEHY 469
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   519 VNGVAKLKKDAEKDFLKDKSmhlqlLFGQANRQDEPNDKKATSVVDVTLnhnldgrlskdalsqqlsalsRFDAHYKMYT 598
Cdd:pfam05483  470 LKEVEDLKTELEKEKLKNIE-----LTAHCDKLLLENKELTQEASDMTL---------------------ELKKHQEDII 523
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   599 DTKGREDKPFDNKRLIDMMVDQVINDMES----FKDDKVAVLHQIDSMEENSDKLIDDILNNKKNTTKNKEDISKLIDQL 674
Cdd:pfam05483  524 NCKKQEERMLKQIENLEEKEMNLRDELESvreeFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQI 603
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   675 ENVKKTFAEEPQEPKIDKGKN-------------------------DEFNTMSSNLDKEIS--RISEKstQLLSDTQESK 727
Cdd:pfam05483  604 ENKNKNIEELHQENKALKKKGsaenkqlnayeikvnklelelasakQKFEEIIDNYQKEIEdkKISEE--KLLEEVEKAK 681
                          570
                   ....*....|....
gi 446651616   728 SIADSVSGQLNQVD 741
Cdd:pfam05483  682 AIADEAVKLQKEID 695
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
774-999 3.25e-04

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: 43.92  E-value: 3.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   774 LFAKEFKKVLQNSKDGDRQNQALKAFMSNPVQKKNLENVLANNGNTDVISPTLFVLLMYLLSMITAYIFYSyERAKGQMN 853
Cdd:pfam12698  115 LILNALQSLLQQLNASALVLLLEALSTSAPIPVESTPLFNPQSGYAYYLVGLILMIIILIGAAIIAVSIVE-EKESRIKE 193
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   854 FIKDDYSSKNHLWN-NVITSGVIGttgLVEGLIVGLIAMNkFHVLAGYRAKFILMVILTMMVFVLInTYLL-------RQ 925
Cdd:pfam12698  194 RLLVSGVSPLQYWLgKILGDFLVG---LLQLLIILLLLFG-IGIPFGNLGLLLLLFLLYGLAYIAL-GYLLgslfknsED 268
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446651616   926 VKSIGMFLMIAALGLYFVA--MNNLKAAGQGVTnKISPLSYIDNMFFNYLNAEH--PIGLALVILTVLVIIGFVLNMF 999
Cdd:pfam12698  269 AQSIIGIVILLLSGFFGGLfpLEDPPSFLQWIF-SIIPFFSPIDGLLRLIYGDSlwEIAPSLIILLLFAVVLLLLALL 345
iSH2_PIK3R1 cd12924
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
249-381 7.32e-04

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunit 1, PIK3R1, also called p85alpha; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In addition, p85alpha, also called PIK3R1, contains N-terminal SH3 and GAP domains. p85alpha carry functions independent of its PI3K regulatory role. It can independently stimulate signaling pathways involved in cytoskeletal rearrangements. Insulin-sensitive tissues express splice variants of the PIK3R1 gene, p50alpha and p55alpha, which may play important roles in insulin signaling during lipid and glucose metabolism. Mice deficient with PIK3R1 die perinatally, indicating its importance in development.


Pssm-ID: 214017 [Multi-domain]  Cd Length: 161  Bit Score: 41.22  E-value: 7.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616  249 VSTLIEKQNSLFEEHNTAMDKMLQDYKSQKDSVELD-NYINALKQMDSQIDQQSSMQDTGKEEYKQTVKE--NLDKLREI 325
Cdd:cd12924     6 VGKKLHEYNTQFQEKSREYDRLYEEYTRTSQEIQMKrTAIEAFNETIKIFEEQCQTQERYSKEYIEKFKRegNEKEIQRI 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 446651616  326 IQSQESPFSK-GMIEDYRKQLTESLQDELANNKDLQDALNSIKMNNAQFAENLEKQL 381
Cdd:cd12924    86 MHNYEKLKSRiSEIVDSRRRLEEDLKKQAAEYREIDKRMNSIKPDLIQLRKTRDQYL 142
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
43-198 7.39e-04

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: 43.15  E-value: 7.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616    43 SNKNNKIHIAIVNEDqpttyngkKVELGQAFIKRLANEK--NYKFETVTRNVAESGLKNGGYQVMIVIPENFSKLAMQLD 120
Cdd:pfam12698   26 VNDPEELPVAVVDED--------NSSLSRQLVRALEASPtvNLVQYVDSEEEAKEALKNGKIDGLLVIPKGFSKDLLKGE 97
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446651616   121 AKTPSKISLqyktavGQKEEVAKNTEKVVSNVLNDFNKNLVEIYLTSIIDNlhnaqKNVGAIMTREHGVNSKFSNYLL 198
Cdd:pfam12698   98 SATVTVYIN------SSNLLVSKLILNALQSLLQQLNASALVLLLEALSTS-----APIPVESTPLFNPQSGYAYYLV 164
iSH2_PI3K_IA_R cd12923
Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory ...
251-367 1.99e-03

Inter-Src homology 2 (iSH2) helical domain of Class IA Phosphoinositide 3-kinase Regulatory subunits; PI3Ks catalyze the transfer of the gamma-phosphoryl group from ATP to the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives. They play an important role in a variety of fundamental cellular processes, including cell motility, the Ras pathway, vesicle trafficking and secretion, immune cell activation, and apoptosis. They are classified according to their substrate specificity, regulation, and domain structure. Class IA PI3Ks are heterodimers of a p110 catalytic (C) subunit and a p85-related regulatory (R) subunit. The R subunit down-regulates PI3K basal activity, stabilizes the C subunit, and plays a role in the activation downstream of tyrosine kinases. All R subunits contain two SH2 domains that flank an intervening helical domain (iSH2), which binds to the N-terminal adaptor-binding domain (ABD) of the catalytic subunit. In vertebrates, there are three genes (PIK3R1, PIK3R2, and PIK3R3) that encode for different Class IA PI3K R subunits.


Pssm-ID: 214016 [Multi-domain]  Cd Length: 152  Bit Score: 39.90  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616  251 TLIEKQN---SLFEEHNTAMDKMlqDYKSQKdsveLDNYINALKQMDSQIDQQSSMQDTGKEEYKQTVKENLDKLREIIQ 327
Cdd:cd12923    16 EYLDKSReydELYEKYNKLSQEI--QLKRQA----LEAFEEAVKMFEEQLRTQEKFQKEAQPHEKQRLMENNELLKSRLK 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 446651616  328 sqespfskgMIEDYRKQLTESLQDELANNKDLQDALNSIK 367
Cdd:cd12923    90 ---------ELEESKEQLEEDLRKQVAYNRELEREMNSLK 120
EzrA pfam06160
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ...
254-380 2.25e-03

Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.


Pssm-ID: 428797 [Multi-domain]  Cd Length: 542  Bit Score: 41.76  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   254 EKQNSLFEEHN-----TAMDKMLQDYKSQKDSVELDNYINALKQMDSQIDQqssMQDTGKEEY--KQTVKENLDKLREII 326
Cdd:pfam06160  224 EEEGYALEHLNvdkeiQQLEEQLEENLALLENLELDEAEEALEEIEERIDQ---LYDLLEKEVdaKKYVEKNLPEIEDYL 300
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 446651616   327 QSQESPFSKGMIEDYRKQLTESLQ-DELANNKDLQDALNSIKMNNAQFAENLEKQ 380
Cdd:pfam06160  301 EHAEEQNKELKEELERVQQSYTLNeNELERVRGLEKQLEELEKRYDEIVERLEEK 355
235kDa-fam TIGR01612
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ...
143-731 4.31e-03

reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.


Pssm-ID: 130673 [Multi-domain]  Cd Length: 2757  Bit Score: 41.19  E-value: 4.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   143 KNTEKVVSNVLNDFNK--NLVEIYLTSI--IDNLHNAQKNVGAIMTREHGVNSKFSNYLLNPINdFPELFTDTLVNSISA 218
Cdd:TIGR01612  761 KNKEKELSNKINDYAKekDELNKYKSKIseIKNHYNDQINIDNIKDEDAKQNYDKSKEYIKTIS-IKEDEIFKIINEMKF 839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   219 NKDitKWFQTYNKSLLSANSDTFRVNTDY-NVSTLIEK-QNSLFEEHNTAMDKMLQDYKS----QKDSVELD-NYINALK 291
Cdd:TIGR01612  840 MKD--DFLNKVDKFINFENNCKEKIDSEHeQFAELTNKiKAEISDDKLNDYEKKFNDSKSlineINKSIEEEyQNINTLK 917
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   292 QMDSQIDQQSSMQDTGKE------EYKQTVKENLDKLRE---IIQSQESPFSKGMIE---DYRKQLTE-SLQDELANNKD 358
Cdd:TIGR01612  918 KVDEYIKICENTKESIEKfhnkqnILKEILNKNIDTIKEsnlIEKSYKDKFDNTLIDkinELDKAFKDaSLNDYEAKNNE 997
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   359 LQDALNSIKMNNA---------QFAENlEKQLHDDIVKEPDTDT----------TFIYNMSKQDFIAAGLNEDEANKyeA 419
Cdd:TIGR01612  998 LIKYFNDLKANLGknkenmlyhQFDEK-EKATNDIEQKIEDANKnipnieiaihTSIYNIIDEIEKEIGKNIELLNK--E 1074
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   420 IVKEAKRYKNEYNLKKPLAEHINLTDYdnqVAQDTSSLINDGVKVKrtetiksNDINQLTVATDPHFNFEGDIKINGKKY 499
Cdd:TIGR01612 1075 ILEEAEINITNFNEIKEKLKHYNFDDF---GKEENIKYADEINKIK-------DDIKNLDQKIDHHIKALEEIKKKSENY 1144
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   500 dikdqsvqldtsNKEYKVEVNgvaKLKKDAEKDFLKDKSmhlqllfgqanrqDEPNDKKATSVVDVTLNHNLdgrlsKDA 579
Cdd:TIGR01612 1145 ------------IDEIKAQIN---DLEDVADKAISNDDP-------------EEIEKKIENIVTKIDKKKNI-----YDE 1191
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   580 LSQQLSALSRFDAHYKMYTDTKGredkpfdnkrlIDMMVDQVINDMesfkddkvaVLHQIDSMEENSDKLIddilnnkkn 659
Cdd:TIGR01612 1192 IKKLLNEIAEIEKDKTSLEEVKG-----------INLSYGKNLGKL---------FLEKIDEEKKKSEHMI--------- 1242
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616   660 ttknkEDISKLIDQLENVKKTFAEEPQEPKIDKGKNDEFNTM-------------SSNLDKEISRISEKSTQLLSDTQES 726
Cdd:TIGR01612 1243 -----KAMEAYIEDLDEIKEKSPEIENEMGIEMDIKAEMETFnishdddkdhhiiSKKHDENISDIREKSLKIIEDFSEE 1317

                   ....*
gi 446651616   727 KSIAD 731
Cdd:TIGR01612 1318 SDIND 1322
MFS_YajR_like cd17472
Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux ...
884-996 9.55e-03

Escherichia coli inner membrane transport protein YajR and similar multidrug-efflux transporters of the Major Facilitator Superfamily; This family is composed of Escherichia coli inner membrane transport protein YajR and some uncharacterized multidrug-efflux transporters. YajR is a putative proton-driven major facilitator superfamily (MFS) transporter found in many gram-negative bacteria. Unlike most MFS transporters, YajR contains a C-terminal, cytosolic YAM domain, which may play an essential role for the proper functioning of the transporter. YajR-like transporters belong to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement.


Pssm-ID: 341025 [Multi-domain]  Cd Length: 371  Bit Score: 39.51  E-value: 9.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446651616  884 LIVGLIAMNKFHVLA-GYRAKFILMVILTMMVFVlinTYLLRQVKSIGMFLMIAALGLYFVAMNNLKAAGQGVTNKISPL 962
Cdd:cd17472   239 ILIGFILMVPFVIYAeKKGKMKQVFVSSILLIAV---GFLLLLFAATSLWLLIIGLIIFFIGFNLLEALLPSLVSKIAPK 315
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 446651616  963 SY------IDNMF---------------FNYLNAEHPIGLALVILTVLVIIGFVL 996
Cdd:cd17472   316 EYrgtamgIYNTSqflgsflggalggllWGLLGYSSVFLTILILALLWLLVSFLL 370
 
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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