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Conserved domains on  [gi|1840172799|gb|QJR47771|]
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type VII secretion protein EsaA [Bacillus subtilis subsp. subtilis str. 168]

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
T7_esaA_Nterm TIGR03929
type VII secretion protein EsaA, N-terminal domain; Members of this family are associated with ...
 11-208 3.04e-74

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: 243.47  E-value: 3.04e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   11 LISAVIIILLLPVLFFRFIGDDPTKKAVNS--TRQIAVVNEDTGVLSDEvksdeedKSAQFGKEVAAVLGERPDYSWTVV 88
Cdd:TIGR03929    1 LIFLVLFIVLLPGLFFLAIGQNPKKQKTNQnaKMNIAVVNEDQGVSFDG-------KTYNFGASFVKAIERDNSQEWSVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   89 NRSAAETGLASKKYDAIVYIPSDFSKNILSYDKDHPQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMNKKMSALYWNFV 168
Cdd:TIGR03929   74 SRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASI 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1840172799  169 SQKVDNIRGEFDKIVNKESEFQNVMYNFYKPSSNDLAGEI 208
Cdd:TIGR03929  154 LQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF 193
PTZ00121 super family cl31754
MAEBL; Provisional
 210-626 8.78e-10

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 8.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  210 QQKDLIDELKKSMNEAQgTTKEKASTAEEAKNTLKEFIDTVERYKEYQENQKklllAAQDSTQQQIRTGLDAIQAQQ--- 286
Cdd:PTZ00121  1467 EEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK----AEEAKKADEAKKAEEAKKADEakk 1541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  287 -----KANQFSE----RMSGLATGIGQAKTQIGLTNLALNNAEKLRQNQVPLQEMGMKKIENDMFNAFLSRYKSQYEAIK 357
Cdd:PTZ00121  1542 aeekkKADELKKaeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  358 YQNLNQLQENigKNRLSLLKPKESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQR--DELKNVATEIKDISEGLKEPEQ 435
Cdd:PTZ00121  1622 AEELKKAEEE--KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKKAAEALKKEAE 1699

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  436 EKPTT-----PDAEEPSTDDSPNTEEPSNDIPTSD-DQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQ 509
Cdd:PTZ00121  1700 EAKKAeelkkKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  510 dtnTENTGTSKTDFSLIELADEN--DGSNQSDGLQGDGADGETDISGAKKRLNEAAIKLEEIENALQEKQEEhnnkLEKH 587
Cdd:PTZ00121  1780 ---VIEEELDEEDEKRRMEVDKKikDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA----FEKH 1852

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1840172799  588 IDELNQEIKELNKTVSKLNDQigdlTKKLVDFDNNVNDA 626
Cdd:PTZ00121  1853 KFNKNNENGEDGNKEADFNKE----KDLKEDDEEEIEEA 1887
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 555-737 3.55e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  555 AKKRLNEAAIKLEEIENALQEKQEEHNnKLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYRLIYNLE 634
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEEK-ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  635 DEIIQTLQSRGYIDQKEKLSSIFSSRIETDNISNLMkYYNSLNLYKSTLNDNL--DLGSLTIIKGEVIQEQDgNVQSVLA 712
Cdd:COG4942    104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELraDLAELAALRAELEAERA-ELEALLA 181

                          170       180
                   ....*....|....*....|....*
gi 1840172799  713 LTPEESASWEALKNNTMQTDEDINS 737
Cdd:COG4942    182 ELEEERAALEALKAERQKLLARLEK 206
 
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 ...
 11-208 3.04e-74

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: 243.47  E-value: 3.04e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   11 LISAVIIILLLPVLFFRFIGDDPTKKAVNS--TRQIAVVNEDTGVLSDEvksdeedKSAQFGKEVAAVLGERPDYSWTVV 88
Cdd:TIGR03929    1 LIFLVLFIVLLPGLFFLAIGQNPKKQKTNQnaKMNIAVVNEDQGVSFDG-------KTYNFGASFVKAIERDNSQEWSVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   89 NRSAAETGLASKKYDAIVYIPSDFSKNILSYDKDHPQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMNKKMSALYWNFV 168
Cdd:TIGR03929   74 SRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASI 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1840172799  169 SQKVDNIRGEFDKIVNKESEFQNVMYNFYKPSSNDLAGEI 208
Cdd:TIGR03929  154 LQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF 193
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
 5-169 3.25e-33

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


Pssm-ID: 441120  Cd Length: 225  Bit Score: 128.14  E-value: 3.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799    5 RKSLIKLIsAVIIILLLPVLFFRFIG---DDPTKKavNSTRQIAVVNEDTGVlsdevksDEEDKSAQFGKEVAAVLGERP 81
Cdd:COG1511      9 FKNKLALI-ALIALILVPLLYAGLYLwafWDPYGN--LDNLPVAVVNEDKGA-------TVDGKTVNLGDELVDELKDND 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   82 DYSWTVVNRSAAETGLASKKYDAIVYIPSDFSKNILSYDKDHPQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMNKKMS 161
Cdd:COG1511     79 SFDWQFVSEEEAEKGLKDGKYYAVIVIPEDFSANLASLLSDDPEKATITYYTNEANNYLASKITDTAATTVVDQVNSQVT 158


                   ....*...
gi 1840172799  162 ALYWNFVS 169
Cdd:COG1511    159 ETYAETVS 166
PTZ00121 PTZ00121
MAEBL; Provisional
 210-626 8.78e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 8.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  210 QQKDLIDELKKSMNEAQgTTKEKASTAEEAKNTLKEFIDTVERYKEYQENQKklllAAQDSTQQQIRTGLDAIQAQQ--- 286
Cdd:PTZ00121  1467 EEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK----AEEAKKADEAKKAEEAKKADEakk 1541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  287 -----KANQFSE----RMSGLATGIGQAKTQIGLTNLALNNAEKLRQNQVPLQEMGMKKIENDMFNAFLSRYKSQYEAIK 357
Cdd:PTZ00121  1542 aeekkKADELKKaeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  358 YQNLNQLQENigKNRLSLLKPKESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQR--DELKNVATEIKDISEGLKEPEQ 435
Cdd:PTZ00121  1622 AEELKKAEEE--KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKKAAEALKKEAE 1699

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  436 EKPTT-----PDAEEPSTDDSPNTEEPSNDIPTSD-DQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQ 509
Cdd:PTZ00121  1700 EAKKAeelkkKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  510 dtnTENTGTSKTDFSLIELADEN--DGSNQSDGLQGDGADGETDISGAKKRLNEAAIKLEEIENALQEKQEEhnnkLEKH 587
Cdd:PTZ00121  1780 ---VIEEELDEEDEKRRMEVDKKikDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA----FEKH 1852

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1840172799  588 IDELNQEIKELNKTVSKLNDQigdlTKKLVDFDNNVNDA 626
Cdd:PTZ00121  1853 KFNKNNENGEDGNKEADFNKE----KDLKEDDEEEIEEA 1887
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-436 8.75e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 8.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  197 YKPSSNDLAGEIKQQKDLIDELKKSMNEAQGTTKEKASTAEEAKNTLKEFIDTVERYKEYQENQKKLLlaaqdstqQQIR 276
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------EELE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  277 TGLDAIQaQQKANQFSErMSGLATGIGQAKTQIGLTNLALNNAE-KLRQNQVPLQEMGMKKIEndmfnAFLSRYKSQYEA 355
Cdd:TIGR02169  744 EDLSSLE-QEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKLE-----EEVSRIEARLRE 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  356 IKyQNLNQLQEnigknRLSLLKPKESDEKEDGEDTSDNKDDTDKEdIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQ 435
Cdd:TIGR02169  817 IE-QKLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKE-IENLNGKKEELEEELEELEAALRDLESRLGDLKK 889


                   .
gi 1840172799  436 E 436
Cdd:TIGR02169  890 E 890
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 555-737 3.55e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  555 AKKRLNEAAIKLEEIENALQEKQEEHNnKLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYRLIYNLE 634
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEEK-ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  635 DEIIQTLQSRGYIDQKEKLSSIFSSRIETDNISNLMkYYNSLNLYKSTLNDNL--DLGSLTIIKGEVIQEQDgNVQSVLA 712
Cdd:COG4942    104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELraDLAELAALRAELEAERA-ELEALLA 181

                          170       180
                   ....*....|....*....|....*
gi 1840172799  713 LTPEESASWEALKNNTMQTDEDINS 737
Cdd:COG4942    182 ELEEERAALEALKAERQKLLARLEK 206
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-538 4.26e-06

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 51.06  E-value: 4.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   713 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 792

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDGSNQS 538
Cdd:NF033609   793 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNN 871
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-536 2.10e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.75  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   705 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 784

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDGSN 536
Cdd:NF033609   785 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSN 861
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-540 2.67e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   707 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDGSNQSD 539
Cdd:NF033609   787 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSES 866


                   .
gi 1840172799  540 G 540
Cdd:NF033609   867 G 867
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-551 3.65e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.98  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   691 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDfslieladeNDGSNQSD 539
Cdd:NF033609   771 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSD 841

                          170
                   ....*....|..
gi 1840172799  540 GLQGDGADGETD 551
Cdd:NF033609   842 SDSDSDSDSDSD 853
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 11-197 3.77e-05

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: 47.00  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   11 LISAVIIILLLPVLFFRFIGDDPTKKavnstrqIAVVNEDTGVLSDEVKsDEEDKSAQFgkevaavlgerpDYSWTVVNR 90
Cdd:pfam12698    8 LLLPILLILLLGLIFSNAVNDPEELP-------VAVVDEDNSSLSRQLV-RALEASPTV------------NLVQYVDSE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   91 SAAETGLASKKYDAIVYIPSDFSKNILSYdkdhpQKATLEFSIQDNLNAVNKEkVQRELEDAQKTMNKKMSALywnFVSQ 170
Cdd:pfam12698   68 EEAKEALKNGKIDGLLVIPKGFSKDLLKG-----ESATVTVYINSSNLLVSKL-ILNALQSLLQQLNASALVL---LLEA 138

                          170       180
                   ....*....|....*....|....*....
gi 1840172799  171 KVDNIRGEFDKIV--NKESEFQNVMYNFY 197
Cdd:pfam12698  139 LSTSAPIPVESTPlfNPQSGYAYYLVGLI 167
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-550 2.42e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.29  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDfslielaDENDGSNQSD 539
Cdd:NF033609   783 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSDSDSD 855

                          170
                   ....*....|.
gi 1840172799  540 GLQGDGADGET 550
Cdd:NF033609   856 SESDSNSDSES 866
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-520 4.06e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDElknvateikdiseglkepEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   769 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------------------DSDSDSDSDSDSDSDSDSDSDSDSDS 830

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSK 520
Cdd:NF033609   831 DSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAK 891
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 549-738 1.51e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  549 ETDISGAKKRLNEAAIKLEEIENALQEKQEEHnNKLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLvdfdnnvNDAYR 628
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKEL-------YALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  629 LIYNLEDEIIqtlqsrgyidqkeklssIFSSRIETDNISNLMKYYNSLNLYKSTLNDNLDLGSLtiikGEVIQEQDGNVQ 708
Cdd:TIGR02168  296 EISRLEQQKQ-----------------ILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELE 354

                          170       180       190
                   ....*....|....*....|....*....|
gi 1840172799  709 SVLALTPEESASWEALKNNTMQTDEDINSF 738
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETL 384
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 546-632 1.59e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  546 ADGETDISGAKKRLNEAAIKLEEIENALQEKQEEHNNKLEKhIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVND 625
Cdd:COG3883     12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE-YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90


                   ....*..
gi 1840172799  626 AYRLIYN 632
Cdd:COG3883     91 RARALYR 97
 
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 ...
 11-208 3.04e-74

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: 243.47  E-value: 3.04e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   11 LISAVIIILLLPVLFFRFIGDDPTKKAVNS--TRQIAVVNEDTGVLSDEvksdeedKSAQFGKEVAAVLGERPDYSWTVV 88
Cdd:TIGR03929    1 LIFLVLFIVLLPGLFFLAIGQNPKKQKTNQnaKMNIAVVNEDQGVSFDG-------KTYNFGASFVKAIERDNSQEWSVV 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   89 NRSAAETGLASKKYDAIVYIPSDFSKNILSYDKDHPQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMNKKMSALYWNFV 168
Cdd:TIGR03929   74 SRGAAENGLKNNTYDAVVYIPSDFSKKVLSVNKENPEKATIQYKVNANGNAVLKEEAQREAEDILNDFNSQMSDLYWASI 153

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1840172799  169 SQKVDNIRGEFDKIVNKESEFQNVMYNFYKPSSNDLAGEI 208
Cdd:TIGR03929  154 LQNLQTAQDNVQAIVNKEAEFQSTYYKNYLPSSANLTNQF 193
YhgE COG1511
Uncharacterized membrane protein YhgE, phage infection protein (PIP) family [Function unknown]; ...
 5-169 3.25e-33

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


Pssm-ID: 441120  Cd Length: 225  Bit Score: 128.14  E-value: 3.25e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799    5 RKSLIKLIsAVIIILLLPVLFFRFIG---DDPTKKavNSTRQIAVVNEDTGVlsdevksDEEDKSAQFGKEVAAVLGERP 81
Cdd:COG1511      9 FKNKLALI-ALIALILVPLLYAGLYLwafWDPYGN--LDNLPVAVVNEDKGA-------TVDGKTVNLGDELVDELKDND 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   82 DYSWTVVNRSAAETGLASKKYDAIVYIPSDFSKNILSYDKDHPQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMNKKMS 161
Cdd:COG1511     79 SFDWQFVSEEEAEKGLKDGKYYAVIVIPEDFSANLASLLSDDPEKATITYYTNEANNYLASKITDTAATTVVDQVNSQVT 158


                   ....*...
gi 1840172799  162 ALYWNFVS 169
Cdd:COG1511    159 ETYAETVS 166
pip_yhgE_Nterm TIGR03061
YhgE/Pip N-terminal domain; This family contains the N-terminal domain of a family of multiple ...
 5-164 2.61e-19

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: 86.10  E-value: 2.61e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799    5 RKSLIKLIsAVIIILLLPVLF-FRFIGD--DPTKKavnsTRQI--AVVNEDTGVLSDevksdeeDKSAQFGKEVAAVLGE 79
Cdd:TIGR03061    7 RKNKLLRI-ALIAIMLIPLLYgGLFLWAfwDPYGN----LDNLpvAVVNEDKGATYD-------GKTLNAGDDLVKELKK 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   80 RPDYSWTVVNRSAAETGLASKKYDAIVYIPSDFSKNILSYDKDHPQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMNKK 159
Cdd:TIGR03061   75 NDDLDWHFVSAKEAEKGLADGKYYMVITIPEDFSENATSLLDDQPKKAQLIYKTNDANNYIASQIAESAAEKVKTSVSKS 154


                   ....*
gi 1840172799  160 MSALY 164
Cdd:TIGR03061  155 ITETY 159
PTZ00121 PTZ00121
MAEBL; Provisional
 210-626 8.78e-10

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 63.24  E-value: 8.78e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  210 QQKDLIDELKKSMNEAQgTTKEKASTAEEAKNTLKEFIDTVERYKEYQENQKklllAAQDSTQQQIRTGLDAIQAQQ--- 286
Cdd:PTZ00121  1467 EEAKKADEAKKKAEEAK-KADEAKKKAEEAKKKADEAKKAAEAKKKADEAKK----AEEAKKADEAKKAEEAKKADEakk 1541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  287 -----KANQFSE----RMSGLATGIGQAKTQIGLTNLALNNAEKLRQNQVPLQEMGMKKIENDMFNAFLSRYKSQYEAIK 357
Cdd:PTZ00121  1542 aeekkKADELKKaeelKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIK 1621

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  358 YQNLNQLQENigKNRLSLLKPKESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQR--DELKNVATEIKDISEGLKEPEQ 435
Cdd:PTZ00121  1622 AEELKKAEEE--KKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKkaEEAKKAEEDEKKAAEALKKEAE 1699

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  436 EKPTT-----PDAEEPSTDDSPNTEEPSNDIPTSD-DQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQ 509
Cdd:PTZ00121  1700 EAKKAeelkkKEAEEKKKAEELKKAEEENKIKAEEaKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEA 1779

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  510 dtnTENTGTSKTDFSLIELADEN--DGSNQSDGLQGDGADGETDISGAKKRLNEAAIKLEEIENALQEKQEEhnnkLEKH 587
Cdd:PTZ00121  1780 ---VIEEELDEEDEKRRMEVDKKikDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEVADSKNMQLEEADA----FEKH 1852

                          410       420       430
                   ....*....|....*....|....*....|....*....
gi 1840172799  588 IDELNQEIKELNKTVSKLNDQigdlTKKLVDFDNNVNDA 626
Cdd:PTZ00121  1853 KFNKNNENGEDGNKEADFNKE----KDLKEDDEEEIEEA 1887
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 197-436 8.75e-07

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 53.15  E-value: 8.75e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  197 YKPSSNDLAGEIKQQKDLIDELKKSMNEAQGTTKEKASTAEEAKNTLKEFIDTVERYKEYQENQKKLLlaaqdstqQQIR 276
Cdd:TIGR02169  672 EPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERL--------EELE 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  277 TGLDAIQaQQKANQFSErMSGLATGIGQAKTQIGLTNLALNNAE-KLRQNQVPLQEMGMKKIEndmfnAFLSRYKSQYEA 355
Cdd:TIGR02169  744 EDLSSLE-QEIENVKSE-LKELEARIEELEEDLHKLEEALNDLEaRLSHSRIPEIQAELSKLE-----EEVSRIEARLRE 816

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  356 IKyQNLNQLQEnigknRLSLLKPKESDEKEDGEDTSDNKDDTDKEdIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQ 435
Cdd:TIGR02169  817 IE-QKLNRLTL-----EKEYLEKEIQELQEQRIDLKEQIKSIEKE-IENLNGKKEELEEELEELEAALRDLESRLGDLKK 889


                   .
gi 1840172799  436 E 436
Cdd:TIGR02169  890 E 890
2A1904 TIGR00927
K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying ...
 381-594 1.39e-06

K+-dependent Na+/Ca+ exchanger; [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273344 [Multi-domain]  Cd Length: 1096  Bit Score: 52.69  E-value: 1.39e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  381 SDEKEDGEDTSDNKDDTDKE-DIEDIKLDLEKQRDElKNVATEIKDISEGlKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:TIGR00927  677 GENESEGEIPAERKGEQEGEgEIEAKEADHKGETEA-EEVEHEGETEAEG-TEDEGEIETGEEGEEVEDEGEGEAEGKHE 754

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNG-----SQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDG 534
Cdd:TIGR00927  755 VETEGDRKETEHEGETEAEGKEDEDegeiqAGEDGEMKGDEGAEGKVEHEGETEAGEKDEHEGQSETQADDTEVKDETGE 834

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  535 SNQSDGLQGDGADGETDISGAKKrlNEAAIKLEEIENALQEKQEEHNNKLEKHIDELNQE 594
Cdd:TIGR00927  835 QELNAENQGEAKQDEKGVDGGGG--SDGGDSEEEEEEEEEEEEEEEEEEEEEEEEEENEE 892
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 555-737 3.55e-06

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 50.53  E-value: 3.55e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  555 AKKRLNEAAIKLEEIENALQEKQEEHNnKLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYRLIYNLE 634
Cdd:COG4942     25 AEAELEQLQQEIAELEKELAALKKEEK-ALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  635 DEIIQTLQSRGYIDQKEKLSSIFSSRIETDNISNLMkYYNSLNLYKSTLNDNL--DLGSLTIIKGEVIQEQDgNVQSVLA 712
Cdd:COG4942    104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQ-YLKYLAPARREQAEELraDLAELAALRAELEAERA-ELEALLA 181

                          170       180
                   ....*....|....*....|....*
gi 1840172799  713 LTPEESASWEALKNNTMQTDEDINS 737
Cdd:COG4942    182 ELEEERAALEALKAERQKLLARLEK 206
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-538 4.26e-06

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 51.06  E-value: 4.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   713 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 792

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDGSNQS 538
Cdd:NF033609   793 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNN 871
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
333-629 7.61e-06

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 50.04  E-value: 7.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  333 GMKKIENDMFNAfLSRYKSQYEAIKYQNLNQlqenigknRLSLLKPKESDEKEDGEDTSDNKDDTD--KEDIEDIKLDLE 410
Cdd:PRK02224   177 GVERVLSDQRGS-LDQLKAQIEEKEEKDLHE--------RLNGLESELAELDEEIERYEEQREQARetRDEADEVLEEHE 247

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  411 KQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEpsndiptsddqptnEDTGSSEEGTQDNGSQNDVQ 490
Cdd:PRK02224   248 ERREELETLEAEIEDLRETIAETEREREELAEEVRDLRERLEELEE--------------ERDDLLAEAGLDDADAEAVE 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  491 TNIETGQKHQESSKNVPEQdTNTENTGTSKTDFSLIELADENDGsnQSDGLQGDGADGETDISGAKKRLNEAAIKLEEIE 570
Cdd:PRK02224   314 ARREELEDRDEELRDRLEE-CRVAAQAHNEEAESLREDADDLEE--RAEELREEAAELESELEEAREAVEDRREEIEELE 390

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1840172799  571 NALQEKQEEHNNkLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYRL 629
Cdd:PRK02224   391 EEIEELRERFGD-APVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEAL 448
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-536 2.10e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.75  E-value: 2.10e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   705 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 784

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDGSN 536
Cdd:NF033609   785 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSN 861
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-540 2.67e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 48.37  E-value: 2.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   707 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 786

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDFSLIELADENDGSNQSD 539
Cdd:NF033609   787 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSES 866


                   .
gi 1840172799  540 G 540
Cdd:NF033609   867 G 867
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-551 3.65e-05

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 47.98  E-value: 3.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   691 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 770

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDfslieladeNDGSNQSD 539
Cdd:NF033609   771 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD---------SDSDSDSD 841

                          170
                   ....*....|..
gi 1840172799  540 GLQGDGADGETD 551
Cdd:NF033609   842 SDSDSDSDSDSD 853
ABC2_membrane_3 pfam12698
ABC-2 family transporter protein; This family is related to the ABC-2 membrane transporter ...
 11-197 3.77e-05

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: 47.00  E-value: 3.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   11 LISAVIIILLLPVLFFRFIGDDPTKKavnstrqIAVVNEDTGVLSDEVKsDEEDKSAQFgkevaavlgerpDYSWTVVNR 90
Cdd:pfam12698    8 LLLPILLILLLGLIFSNAVNDPEELP-------VAVVDEDNSSLSRQLV-RALEASPTV------------NLVQYVDSE 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   91 SAAETGLASKKYDAIVYIPSDFSKNILSYdkdhpQKATLEFSIQDNLNAVNKEkVQRELEDAQKTMNKKMSALywnFVSQ 170
Cdd:pfam12698   68 EEAKEALKNGKIDGLLVIPKGFSKDLLKG-----ESATVTVYINSSNLLVSKL-ILNALQSLLQQLNASALVL---LLEA 138

                          170       180
                   ....*....|....*....|....*....
gi 1840172799  171 KVDNIRGEFDKIV--NKESEFQNVMYNFY 197
Cdd:pfam12698  139 LSTSAPIPVESTPlfNPQSGYAYYLVGLI 167
PHA03169 PHA03169
hypothetical protein; Provisional
 378-507 4.03e-05

hypothetical protein; Provisional


Pssm-ID: 223003 [Multi-domain]  Cd Length: 413  Bit Score: 47.27  E-value: 4.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  378 PKESDEKEDGEDTSDNKDDTDKEDIEDiKLDLEKQRDELKnvateikdisEGLKEPEQEKPTTPDAEEPSTDDSPNTE-- 455
Cdd:PHA03169   141 PSHPGPHEPAPPESHNPSPNQQPSSFL-QPSHEDSPEEPE----------PPTSEPEPDSPGPPQSETPTSSPPPQSPpd 209

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840172799  456 ---EPSNDIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIET------GQKHQESSKNVP 507
Cdd:PHA03169   210 epgEPQSPTPQQAPSPNTQQAVEHEDEPTEPEREGPPFPGHRShsytvvGWKPSTRPGGVP 270
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 347-616 4.81e-05

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 47.76  E-value: 4.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  347 SRYKSQYEaiKYQNLNQLQENIGKNRLSLLKPKESDEKEDGEDTSDNKDDTDK-----EDIEDIKLDLEKQRDELKNVAT 421
Cdd:TIGR02169  667 LFSRSEPA--ELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKigeieKEIEQLEQEEEKLKERLEELEE 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  422 EIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSNDIPTS-DDQPTNEDTGSSEEgtqdngsqndvqtnIETGQKHQ 500
Cdd:TIGR02169  745 DLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARlSHSRIPEIQAELSK--------------LEEEVSRI 810

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  501 ESSKNVPEQDTNTENTgtsktdfsLIELADEndgsnQSDGLQGDGADGETDISGAKKRLNEAAIKLEEIENALQEKQ--- 577
Cdd:TIGR02169  811 EARLREIEQKLNRLTL--------EKEYLEK-----EIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEaal 877

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1840172799  578 ----EEHNN------KLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKL 616
Cdd:TIGR02169  878 rdleSRLGDlkkerdELEAQLRELERKIEELEAQIEKKRKRLSELKAKL 926
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 133-436 1.69e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 45.82  E-value: 1.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  133 IQDNLNAVNK---------EKVQR--ELEDAQKTMNKKMSALYWNFVSQKVDNIRGEFDKIVNKESEfqnvmynfykpss 201
Cdd:TIGR02168  191 LEDILNELERqlkslerqaEKAERykELKAELRELELALLVLRLEELREELEELQEELKEAEEELEE------------- 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  202 ndLAGEIKQQKDLIDELKKSMNEAQgttkEKASTAEEAKNTLKEFIDTVERYKEYQENQKKLLLAAQDSTQQQIRtglda 281
Cdd:TIGR02168  258 --LTAELQELEEKLEELRLEVSELE----EEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLE----- 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  282 iQAQQKANQFSERMSGLATGIGQAKTQIGLTNLALNNAEKLRQNqvplQEMGMKKIENDMfNAFLSRYKSQYEAIKYQNl 361
Cdd:TIGR02168  327 -ELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE----LESRLEELEEQL-ETLRSKVAQLELQIASLN- 399

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840172799  362 NQLQEN-IGKNRLSLLKPKESDEKED-GEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQE 436
Cdd:TIGR02168  400 NEIERLeARLERLEDRRERLQQEIEElLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQA 476
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-550 2.42e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 45.29  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   703 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS 782

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSKTDfslielaDENDGSNQSD 539
Cdd:NF033609   783 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSD-------SDSDSDSDSD 855

                          170
                   ....*....|.
gi 1840172799  540 GLQGDGADGET 550
Cdd:NF033609   856 SESDSNSDSES 866
NatB COG1668
ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ...
 11-157 2.42e-04

ABC-type Na+ efflux pump, permease component NatB [Energy production and conversion, Inorganic ion transport and metabolism];


Pssm-ID: 441274 [Multi-domain]  Cd Length: 402  Bit Score: 44.90  E-value: 2.42e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   11 LISAVIIILLLPVLFFrfIGDDPTKKAVNSTRQIAVVNED-TGVLSDEVKSDEEDKsaqfgkevaavlgerpDYSWTVVN 89
Cdd:COG1668     22 LISTLLLPLLLVPLLG--LGMLFMSGNDDEPLKVAVVDESgAPALAEALKEAAVNF----------------EVVPEVAD 83

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1840172799   90 RSAAETGLASKKYDAIVYIPSDFSKNilsydkdhpQKATLEFSIQDNLNAVNKEKVQRELEDAQKTMN 157
Cdd:COG1668     84 EEEAEAAVEDGEIDAVLVIPEDFSLE---------NPATVELYSDSSPDSSAVSRLESALSQALLALR 142
PTZ00341 PTZ00341
Ring-infected erythrocyte surface antigen; Provisional
 141-501 3.75e-04

Ring-infected erythrocyte surface antigen; Provisional


Pssm-ID: 173534 [Multi-domain]  Cd Length: 1136  Bit Score: 44.78  E-value: 3.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  141 NKEKVQRELEdaQKTMNKKMSALYWNfvsQKVDNIRGEFdkiVNKESEFQNVMYNFYKPSSNDLAG---------EIKQQ 211
Cdd:PTZ00341   766 KPKKAAKKLE--QRSKANKEELANEN---NKLMNILKEY---FGNNEQINSITYNFENINLNEDNEngskkildlNHKDQ 837

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  212 KDLIDELKK-----SMNEAQGTTKEKAS-----------TAEEAKNTLKEFIDTVERYKEYQENQKKLLLAAQDSTQQQI 275
Cdd:PTZ00341   838 KEIFEEIISyivdiSLSDIENTAKNAAEqilsdegldekKLKKRAESLKKLANAIEKYAGGGKKDKKAKKKDAKDLSGNI 917

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  276 RTGLDAIQAQQKaNQFSERMSGLatgigQAKTQIGLTNLALNNAEKLRQNQVP--LQEMGMKKIENDMFNAFLSRYKSQY 353
Cdd:PTZ00341   918 AHEINLINKELK-NQNENVPEHL-----KEHAEANIEEDAEENVEEDAEENVEenVEENVEENVEENVEENVEENVEENV 991

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  354 EAIKYQNLNQ-LQENIGKN-RLSLLKPKESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDElkNVATEIKDISEGLK 431
Cdd:PTZ00341   992 EENVEENVEEnIEENVEENvEENIEENVEEYDEENVEEVEENVEEYDEENVEEIEENAEENVEE--NIEENIEEYDEENV 1069

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  432 EpEQEKPTTPDAEEPSTDdspNTEEPSNDIPTSDDQPTNEDtgsSEEGTQDNGSQNDVQTNIETGQKHQE 501
Cdd:PTZ00341  1070 E-EIEENIEENIEENVEE---NVEENVEEIEENVEENVEEN---AEENAEENAEENAEEYDDENPEEHNE 1132
MSCRAMM_ClfA NF033609
MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial ...
 380-520 4.06e-04

MSCRAMM family adhesin clumping factor ClfA; Clumping factor A is an MSCRAMM (Microbial Surface Components Recognizing Adhesive Matrix Molecules). It is heavily studied in Staphylococcus aureus both for its biological role in adhesion and for its potential for vaccination. Features of the sequence, but also of other MSCRAMM adhesins, include a long run of Ser-Asp dipeptide repeats and a C-terminal cell wall anchoring LPXTG motif.


Pssm-ID: 468110 [Multi-domain]  Cd Length: 934  Bit Score: 44.51  E-value: 4.06e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  380 ESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDElknvateikdiseglkepEQEKPTTPDAEEPSTDDSPNTEEPSN 459
Cdd:NF033609   769 DSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDSDS------------------DSDSDSDSDSDSDSDSDSDSDSDSDS 830

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840172799  460 DIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQESSKNVPEQDTNTENTGTSK 520
Cdd:NF033609   831 DSDSDSDSDSDSDSDSDSDSDSDSDSESDSNSDSESGSNNNVVPPNSPKNGTNASNKNEAK 891
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
 385-491 1.00e-03

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.04  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  385 EDGEdTSDNKDDTDKEDIEdikldlekqRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPNTEEPSNDIPTS 464
Cdd:PRK13108   355 RDGE-STPAVEETSEADIE---------REQPGDLAGQAPAAHQVDAEAASAAPEEPAALASEAHDETEPEVPEKAAPIP 424

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1840172799  465 D----DQPTNEDTGSSEEGTQDNGSQNDVQT 491
Cdd:PRK13108   425 DpakpDELAVAGPGDDPAEPDGIRRQDDFSS 455
PRK09418 PRK09418
bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;
407-516 1.02e-03

bifunctional 2',3'-cyclic-nucleotide 2'-phosphodiesterase/3'-nucleotidase;


Pssm-ID: 236504 [Multi-domain]  Cd Length: 780  Bit Score: 43.16  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  407 LDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDAEEPSTDDSPN---TEEPSN-DIPTSDDQPTNEDTGSSEEGTQD 482
Cdd:PRK09418   650 IDITKKNDDDKETGGENPTTPPTGEGDNGENPTTPPTGEGNNGENPTtppTGEGNNgGNPTTPSTDEGNNAGSGQTTTDN 729

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1840172799  483 ngsQNDVQTNIETGQKHQessKNVPEQDTNTENT 516
Cdd:PRK09418   730 ---QNSKETTTVSENKEE---RDLPKTGTSVAST 757
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 549-738 1.51e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  549 ETDISGAKKRLNEAAIKLEEIENALQEKQEEHnNKLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLvdfdnnvNDAYR 628
Cdd:TIGR02168  224 ELELALLVLRLEELREELEELQEELKEAEEEL-EELTAELQELEEKLEELRLEVSELEEEIEELQKEL-------YALAN 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  629 LIYNLEDEIIqtlqsrgyidqkeklssIFSSRIETDNISNLMKYYNSLNLYKSTLNDNLDLGSLtiikGEVIQEQDGNVQ 708
Cdd:TIGR02168  296 EISRLEQQKQ-----------------ILRERLANLERQLEELEAQLEELESKLDELAEELAEL----EEKLEELKEELE 354

                          170       180       190
                   ....*....|....*....|....*....|
gi 1840172799  709 SVLALTPEESASWEALKNNTMQTDEDINSF 738
Cdd:TIGR02168  355 SLEAELEELEAELEELESRLEELEEQLETL 384
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 546-632 1.59e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 42.12  E-value: 1.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  546 ADGETDISGAKKRLNEAAIKLEEIENALQEKQEEHNNKLEKhIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVND 625
Cdd:COG3883     12 AFADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEE-YNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGE 90


                   ....*..
gi 1840172799  626 AYRLIYN 632
Cdd:COG3883     91 RARALYR 97
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 583-660 2.42e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.68  E-value: 2.42e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840172799  583 KLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYRLIYNLEDEiIQTLQSRgyIDQ-KEKLSSIFSSR 660
Cdd:COG1579     14 ELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELE-IEEVEAR--IKKyEEQLGNVRNNK 89
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 549-616 3.41e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 40.29  E-value: 3.41e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840172799  549 ETDISGAKKRLNEAAIKLEEIENALQEKQEEHNN---KLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKL 616
Cdd:COG1579    102 KRRISDLEDEILELMERIEELEEELAELEAELAEleaELEEKKAELDEELAELEAELEELEAEREELAAKI 172
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 50-432 3.62e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 3.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799   50 DTGVLSDEVKSDEEDKSAqfgkeVAAVLGERPDYswTVVNRSAA-----------ETG------LASKKYDAIVYIPSDF 112
Cdd:TIGR02168  521 ILGVLSELISVDEGYEAA-----IEAALGGRLQA--VVVENLNAakkaiaflkqnELGrvtflpLDSIKGTEIQGNDREI 593

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  113 SKNI---LSYDKDHPQKAT-LEFSIQDNLNAVnkeKVQRELEDAQKtMNKKMSAlYWNFVSQKVDNIRGEFdKIVNKESE 188
Cdd:TIGR02168  594 LKNIegfLGVAKDLVKFDPkLRKALSYLLGGV---LVVDDLDNALE-LAKKLRP-GYRIVTLDGDLVRPGG-VITGGSAK 667

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  189 FQNVMYNfYKPSSNDLAGEIKQQKDLIDELKKSMNEAQGT------------------------TKEKASTAEEAKNTLK 244
Cdd:TIGR02168  668 TNSSILE-RRREIEELEEKIEELEEKIAELEKALAELRKEleeleeeleqlrkeleelsrqisaLRKDLARLEAEVEQLE 746

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  245 EFIDTVERYKEYQENQKKLLLAAQDSTQQQIRTGLDAIQA-QQKANQFSERMSGLATGIGQAKTQIGLTNLALNNAEKLR 323
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEElEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERL 826

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  324 QNQvpLQEMGMKKIENDMFNaflsryksqyeaikyQNLNQLQENIGKNRLSLLKPKES-DEKEDGEDTSDNKDDTDKEDI 402
Cdd:TIGR02168  827 ESL--ERRIAATERRLEDLE---------------EQIEELSEDIESLAAEIEELEELiEELESELEALLNERASLEEAL 889

                          410       420       430
                   ....*....|....*....|....*....|
gi 1840172799  403 EDIKLDLEKQRDELKNVATEIKDISEGLKE 432
Cdd:TIGR02168  890 ALLRSELEELSEELRELESKRSELRRELEE 919
PTZ00121 PTZ00121
MAEBL; Provisional
 210-615 4.07e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 4.07e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  210 QQKDLIDELKKSMNEAQgTTKEKASTAEEAKNTLKEFIDTVERYKEYQENQKKLLLAAQDSTQQQIRTGLDAIQAQQKAN 289
Cdd:PTZ00121  1299 EEKKKADEAKKKAEEAK-KADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAK 1377

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  290 QFSERMSGLATGIGQAKTqigltnlALNNAEKLRQNQVPLQEMGMKKIENDMFNaflsryKSQYEAIKYQNLNQLQENig 369
Cdd:PTZ00121  1378 KKADAAKKKAEEKKKADE-------AKKKAEEDKKKADELKKAAAAKKKADEAK------KKAEEKKKADEAKKKAEE-- 1442

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  370 KNRLSLLKpKESDEKEDGEDTSDNKDDTDKEDIEDIKLDLEKQRDELKNVATEIKDISEGLKEPEQEKPTTPDA----EE 445
Cdd:PTZ00121  1443 AKKADEAK-KKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAkkaeEA 1521

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  446 PSTDDSPNTEEP--------------SNDIPTSDDQPTNEDTGSSEEGTQDNGSQNDVQTNIETGQKHQEssKNVPEQDT 511
Cdd:PTZ00121  1522 KKADEAKKAEEAkkadeakkaeekkkADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEE--ARIEEVMK 1599

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  512 NTENTGTSKTDfsliELADENDGSNQSDGLQGDGADgetdisgAKKRLNEAAIKLEEIENALQEKQEEHNNKLEKhiDEL 591
Cdd:PTZ00121  1600 LYEEEKKMKAE----EAKKAEEAKIKAEELKKAEEE-------KKKVEQLKKKEAEEKKKAEELKKAEEENKIKA--AEE 1666

                          410       420
                   ....*....|....*....|....
gi 1840172799  592 NQEIKELNKTVSKLNDQIGDLTKK 615
Cdd:PTZ00121  1667 AKKAEEDKKKAEEAKKAEEDEKKA 1690
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 549-640 4.91e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 4.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  549 ETDISGAKKRLNEAAIKLEEIENALQEKQEEHNNkLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYR 628
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLET-LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLK 428

                           90
                   ....*....|..
gi 1840172799  629 LIYNLEDEIIQT 640
Cdd:TIGR02168  429 KLEEAELKELQA 440
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 556-689 4.96e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 40.77  E-value: 4.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  556 KKRLNEAAIKLEEIENALQEKQEEHNNkLEKHIDELNQEIKELNKTVSKLNDQIGDLTKKLVDFDNNVNDAYRLIYNLED 635
Cdd:TIGR04523   46 KNELKNKEKELKNLDKNLNKDEEKINN-SNNKIKILEQQIKDLNDKLKKNKDKINKLNSDLSKINSEIKNDKEQKNKLEV 124

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1840172799  636 EIIQTLQSrgyIDQKEKLSSIFSSRI--ETDNISNLMKYYNSLNLYKSTLNDNLDL 689
Cdd:TIGR04523  125 ELNKLEKQ---KKENKKNIDKFLTEIkkKEKELEKLNNKYNDLKKQKEELENELNL 177
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 536-665 5.90e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.82  E-value: 5.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840172799  536 NQSDGLQGDGADGETDISGAKKRLNEAAIKLEEIENALQEKQEEHNNKLEKHIDELNQEIKELNKTVSKLNDQIGDLTKK 615
Cdd:TIGR02169  244 RQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEER 323

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1840172799  616 LVDFDNNVNDAYRLIYNLEDEiIQTLQSRgyidqKEKLSSIFSSRIETDN 665
Cdd:TIGR02169  324 LAKLEAEIDKLLAEIEELERE-IEEERKR-----RDKLTEEYAELKEELE 367
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 537-612 7.61e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.81  E-value: 7.61e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840172799  537 QSDGLQGDGADGETDISGAKKRLNEAAIKLEEIENALQEKQEEhNNKLEKHIDELNQEIKELNKTVSKLNDQIGDL 612
Cdd:COG3883     17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAE-LEALQAEIDKLQAEIAEAEAEIEERREELGER 91
 
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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