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Conserved domains on  [gi|1309179805|gb|PKQ36917|]
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hypothetical protein CVT59_10545 [Actinobacteria bacterium HGW-Actinobacteria-1]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
DUF11 pfam01345
Domain of unknown function DUF11; A domain of unknown function found in multiple copies in ...
553-668 1.99e-12

Domain of unknown function DUF11; A domain of unknown function found in multiple copies in several archaebacterial proteins. Conserved N-terminal lysine and C-terminal asparagine with central asp/glu suggests that many of these domain may contain an isopeptide bond. In Methanothermobacter sp. CaT2, a DUF11-containing repeat hypothetical protein encoded by MTCT_1020 plays a key role as a membrane-bound adhesion protein in the aggregation of CaT2. DUF11-containing repeat domains are not involved in aggregation, but may be important for stabilizing the surface cell wall structures of CaT2.


:

Pssm-ID: 460168 [Multi-domain]  Cd Length: 114  Bit Score: 64.16  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 553 DLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIVDDFDE--RYVTVLDAAGGVVADGKItWTLaGPLAmADGPQT 630
Cdd:pfam01345   1 DLAITKTVDNTTPNVGDTVTFTITVTNNGPSDATGVVVTDTLPAglTFVSATASQGTYDSATGI-WTI-GSLA-VGASAT 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1309179805 631 ITYTVKVDStmptgTTNVDNTVVINHPD-DSNPDNNTDD 668
Cdd:pfam01345  78 LTITATVNT-----AGTITNTATVTSSTfDPNLSNNSAS 111
SdrD_B super family cl25441
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This ...
439-510 5.90e-10

SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold.


The actual alignment was detected with superfamily member pfam17210:

Pssm-ID: 435789 [Multi-domain]  Cd Length: 112  Bit Score: 57.22  E-value: 5.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179805 439 YKFNDLNGDGIWDEGEPGIEGWTIYLYRQVPQIVlndaptpepgfelyATTLTGADGSYHFSGVLPGTYYVA 510
Cdd:pfam17210   6 FVWEDANKNGIQDAGEPGISGVTVTLYDANGTVV--------------GTTTTDANGKYLFTNLAPGTYYVE 63
rne super family cl35953
ribonuclease E; Reviewed
40-129 6.05e-04

ribonuclease E; Reviewed


The actual alignment was detected with superfamily member PRK10811:

Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805   40 EPAKQAPEVVAPAEVAVPDPATEEVVAQPVADVVPEEPVVEVPASTET---------------VVSEEIAPVTAEVAVPV 104
Cdd:PRK10811   867 QPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETthpeviaapvteqpqVITESDVAVAQEVAEHA 946
                           90       100
                   ....*....|....*....|....*
gi 1309179805  105 AKATPTATTPTAIVSTSLVEPIVVP 129
Cdd:PRK10811   947 EPVVEPQDETADIEEAAETAEVVVA 971
ClfA super family cl34840
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
231-675 7.68e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


The actual alignment was detected with superfamily member COG4932:

Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 39.57  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 231 EPETGSITVVKfndLDGDGQKSeseptLDGWDFALTLPTGGMLTGTSGA--DGPGAVLFGELPAGTYSVDETAKPGWHNT 308
Cdd:COG4932   258 KYTKGSVTVTK---TDADTGEP-----LAGATFTLTDADGNTVVTTTVTvtDADGSYTFTDLPPGTYTVTETKAPAGYDL 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 309 TTLPMDVTLAEGEDKTVYVGNAEDPAEDFTKTF--ELTYNGDIP-AETTFRVHYTLGTppeevapaIVDGTWLDLVGTGP 385
Cdd:COG4932   330 DGEAVKVTITAGQTTTVTVTNGNNEVKTGSVTLtkVDADDGEAPlAGAEFTLTDADGT--------VVATITTDADGTAS 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 386 FSasvELPAG--TIIESVdwyAQRGLEqiLLGTTEGETLTEDITNSFTYNGDASGykfndlNGDGIWDEGEPGIEGWTIY 463
Cdd:COG4932   402 FK---GLAPGtyTLTETK---APEGYT--LDSTPITVTVTDGGTGAIDTITNERK------KGSVQVTKVDAPLAGATFT 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 464 LYRQVPQIV--LNDAPTPEPGFELYATTL--TGADGSYHFSGVLPGTYYVAEETregwdMTVGPEGTFVMVNDQPITGLI 539
Cdd:COG4932   468 LTDADGTVVtlTTDADLAGATFEADGKVVttTDASGKYTFKNLPPGTYTDAGGS-----ATVITDDTDGTVGDEATGTDP 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 540 FGNHEPFLPFTDIDLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIVDDFDERYVTVLDAAGGVVADGKITWTLA 619
Cdd:COG4932   543 EVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGVKTTKLTD 622
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179805 620 GPLAMADGPQTITYTVKVDSTMPTGTTNVDNTVVINHPDDSNPDNNTDDERVRVTV 675
Cdd:COG4932   623 TTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAF 678
 
Name Accession Description Interval E-value
DUF11 pfam01345
Domain of unknown function DUF11; A domain of unknown function found in multiple copies in ...
553-668 1.99e-12

Domain of unknown function DUF11; A domain of unknown function found in multiple copies in several archaebacterial proteins. Conserved N-terminal lysine and C-terminal asparagine with central asp/glu suggests that many of these domain may contain an isopeptide bond. In Methanothermobacter sp. CaT2, a DUF11-containing repeat hypothetical protein encoded by MTCT_1020 plays a key role as a membrane-bound adhesion protein in the aggregation of CaT2. DUF11-containing repeat domains are not involved in aggregation, but may be important for stabilizing the surface cell wall structures of CaT2.


Pssm-ID: 460168 [Multi-domain]  Cd Length: 114  Bit Score: 64.16  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 553 DLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIVDDFDE--RYVTVLDAAGGVVADGKItWTLaGPLAmADGPQT 630
Cdd:pfam01345   1 DLAITKTVDNTTPNVGDTVTFTITVTNNGPSDATGVVVTDTLPAglTFVSATASQGTYDSATGI-WTI-GSLA-VGASAT 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1309179805 631 ITYTVKVDStmptgTTNVDNTVVINHPD-DSNPDNNTDD 668
Cdd:pfam01345  78 LTITATVNT-----AGTITNTATVTSSTfDPNLSNNSAS 111
SdrD_B pfam17210
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This ...
439-510 5.90e-10

SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold.


Pssm-ID: 435789 [Multi-domain]  Cd Length: 112  Bit Score: 57.22  E-value: 5.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179805 439 YKFNDLNGDGIWDEGEPGIEGWTIYLYRQVPQIVlndaptpepgfelyATTLTGADGSYHFSGVLPGTYYVA 510
Cdd:pfam17210   6 FVWEDANKNGIQDAGEPGISGVTVTLYDANGTVV--------------GTTTTDANGKYLFTNLAPGTYYVE 63
MJ0795 COG1361
S-layer protein MJ0795, predicted component of type IV pili-like system [General function ...
552-708 2.63e-06

S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 440972 [Multi-domain]  Cd Length: 409  Bit Score: 50.46  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 552 IDLAITKaaDVATAAPGATITYTLTYRNLGETEATNftivddfderyVTV-LDAAGGVVADGKiTWTLaGPLAmADGPQT 630
Cdd:COG1361   270 ADFEVEN--VESTITAGETVTITITVTNTGNETAKN-----------VVArLSADDPLSSLDD-EAFI-GDLA-PGESAT 333
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179805 631 ITYTVKVDSTMPTGTTNVdnTVVINHPDDSNPDNNTDDERVRVTVQGEPflPFTGGEALLLVSAAILSAGVGALLRRR 708
Cdd:COG1361   334 VTFTVSASSDATPGTYPI--TVTIRYDDDDGNTQLSDTITVPVEVTEPS--SGGLLTVLAIIIGLLIVAVGGYLYRRR 407
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
556-655 3.18e-04

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 41.10  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 556 ITK---AADVATAAPGATITYTLTYRN-LGETEATNFTIVDDFDERyvtvLDAAGG--VVADGK---------------I 614
Cdd:TIGR04226   5 ITKkvnDKDDADVNIGDEVTYTITTTVpADIADYKSFVITDTLDDG----LTYKGSvkVTVDGKtltvdtdytvtdgqtV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1309179805 615 TWTL--AGPLAMADGPQTITYTVKVDSTMPTGTTNvDNTVVIN 655
Cdd:TIGR04226  81 TVTFtdAGLKKLAGKKITVTYTAKVKEGAVLGKGI-PNTATLT 122
rne PRK10811
ribonuclease E; Reviewed
40-129 6.05e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805   40 EPAKQAPEVVAPAEVAVPDPATEEVVAQPVADVVPEEPVVEVPASTET---------------VVSEEIAPVTAEVAVPV 104
Cdd:PRK10811   867 QPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETthpeviaapvteqpqVITESDVAVAQEVAEHA 946
                           90       100
                   ....*....|....*....|....*
gi 1309179805  105 AKATPTATTPTAIVSTSLVEPIVVP 129
Cdd:PRK10811   947 EPVVEPQDETADIEEAAETAEVVVA 971
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
231-675 7.68e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 39.57  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 231 EPETGSITVVKfndLDGDGQKSeseptLDGWDFALTLPTGGMLTGTSGA--DGPGAVLFGELPAGTYSVDETAKPGWHNT 308
Cdd:COG4932   258 KYTKGSVTVTK---TDADTGEP-----LAGATFTLTDADGNTVVTTTVTvtDADGSYTFTDLPPGTYTVTETKAPAGYDL 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 309 TTLPMDVTLAEGEDKTVYVGNAEDPAEDFTKTF--ELTYNGDIP-AETTFRVHYTLGTppeevapaIVDGTWLDLVGTGP 385
Cdd:COG4932   330 DGEAVKVTITAGQTTTVTVTNGNNEVKTGSVTLtkVDADDGEAPlAGAEFTLTDADGT--------VVATITTDADGTAS 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 386 FSasvELPAG--TIIESVdwyAQRGLEqiLLGTTEGETLTEDITNSFTYNGDASGykfndlNGDGIWDEGEPGIEGWTIY 463
Cdd:COG4932   402 FK---GLAPGtyTLTETK---APEGYT--LDSTPITVTVTDGGTGAIDTITNERK------KGSVQVTKVDAPLAGATFT 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 464 LYRQVPQIV--LNDAPTPEPGFELYATTL--TGADGSYHFSGVLPGTYYVAEETregwdMTVGPEGTFVMVNDQPITGLI 539
Cdd:COG4932   468 LTDADGTVVtlTTDADLAGATFEADGKVVttTDASGKYTFKNLPPGTYTDAGGS-----ATVITDDTDGTVGDEATGTDP 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 540 FGNHEPFLPFTDIDLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIVDDFDERYVTVLDAAGGVVADGKITWTLA 619
Cdd:COG4932   543 EVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGVKTTKLTD 622
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179805 620 GPLAMADGPQTITYTVKVDSTMPTGTTNVDNTVVINHPDDSNPDNNTDDERVRVTV 675
Cdd:COG4932   623 TTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAF 678
 
Name Accession Description Interval E-value
DUF11 pfam01345
Domain of unknown function DUF11; A domain of unknown function found in multiple copies in ...
553-668 1.99e-12

Domain of unknown function DUF11; A domain of unknown function found in multiple copies in several archaebacterial proteins. Conserved N-terminal lysine and C-terminal asparagine with central asp/glu suggests that many of these domain may contain an isopeptide bond. In Methanothermobacter sp. CaT2, a DUF11-containing repeat hypothetical protein encoded by MTCT_1020 plays a key role as a membrane-bound adhesion protein in the aggregation of CaT2. DUF11-containing repeat domains are not involved in aggregation, but may be important for stabilizing the surface cell wall structures of CaT2.


Pssm-ID: 460168 [Multi-domain]  Cd Length: 114  Bit Score: 64.16  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 553 DLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIVDDFDE--RYVTVLDAAGGVVADGKItWTLaGPLAmADGPQT 630
Cdd:pfam01345   1 DLAITKTVDNTTPNVGDTVTFTITVTNNGPSDATGVVVTDTLPAglTFVSATASQGTYDSATGI-WTI-GSLA-VGASAT 77
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1309179805 631 ITYTVKVDStmptgTTNVDNTVVINHPD-DSNPDNNTDD 668
Cdd:pfam01345  78 LTITATVNT-----AGTITNTATVTSSTfDPNLSNNSAS 111
SdrD_B pfam17210
SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This ...
439-510 5.90e-10

SdrD B-like domain; This family corresponds to the B-like domain from the SdrD protein. This domain has three calcium binding sites within a greek key beta sandwich fold.


Pssm-ID: 435789 [Multi-domain]  Cd Length: 112  Bit Score: 57.22  E-value: 5.90e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179805 439 YKFNDLNGDGIWDEGEPGIEGWTIYLYRQVPQIVlndaptpepgfelyATTLTGADGSYHFSGVLPGTYYVA 510
Cdd:pfam17210   6 FVWEDANKNGIQDAGEPGISGVTVTLYDANGTVV--------------GTTTTDANGKYLFTNLAPGTYYVE 63
MJ0795 COG1361
S-layer protein MJ0795, predicted component of type IV pili-like system [General function ...
552-708 2.63e-06

S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 440972 [Multi-domain]  Cd Length: 409  Bit Score: 50.46  E-value: 2.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 552 IDLAITKaaDVATAAPGATITYTLTYRNLGETEATNftivddfderyVTV-LDAAGGVVADGKiTWTLaGPLAmADGPQT 630
Cdd:COG1361   270 ADFEVEN--VESTITAGETVTITITVTNTGNETAKN-----------VVArLSADDPLSSLDD-EAFI-GDLA-PGESAT 333
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1309179805 631 ITYTVKVDSTMPTGTTNVdnTVVINHPDDSNPDNNTDDERVRVTVQGEPflPFTGGEALLLVSAAILSAGVGALLRRR 708
Cdd:COG1361   334 VTFTVSASSDATPGTYPI--TVTIRYDDDDGNTQLSDTITVPVEVTEPS--SGGLLTVLAIIIGLLIVAVGGYLYRRR 407
MJ0795 COG1361
S-layer protein MJ0795, predicted component of type IV pili-like system [General function ...
553-679 3.74e-05

S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 440972 [Multi-domain]  Cd Length: 409  Bit Score: 46.61  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 553 DLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIV------------DDFDERYVTVLDAAGGVVADGKITWTLaG 620
Cdd:COG1361   137 RFEVVSVTSPDSLTPGDTGTLTLTIKNTGTGTAKNVTVTltspsgdltdlePGPRPATNVVVVLSSPVSPVGSNSVAL-G 215
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1309179805 621 PLAmADGPQTITYTVKVDSTMPTGTTNVDNTVVInhpDDSNPDNNTDDERVRVTVQGEP 679
Cdd:COG1361   216 TLE-PGESATFTFKVDVSEDAEPGPYPLPLTVTY---RDEDGDTYSDTVTIGVYVAPKA 270
RrgB_K2N_iso_D2 TIGR04226
fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, ...
556-655 3.18e-04

fimbrial isopeptide formation D2 domain; The Streptococcus Pneumoniae pilus backbone protein, RrgB, has three tandem domains with Lys-to-Asn isopeptide bonds, but these three regions are extremely divergent in sequence. This model represents the homology domain family of the D2 domain. It occurs just once in many surface proteins but up to twenty times in some pilin subunit proteins. Three of every four members have the typical Gram-positive C-terminal motif, LPXTG, although in many cases this motif may be involved in pilin subunit cross-linking rather than cell wall attachment. Proteins with this domain include fimbrial proteins with lectin-like adhesion functions, and the majority of characterized members are involved in surface adhesion to host structures.


Pssm-ID: 275067 [Multi-domain]  Cd Length: 124  Bit Score: 41.10  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 556 ITK---AADVATAAPGATITYTLTYRN-LGETEATNFTIVDDFDERyvtvLDAAGG--VVADGK---------------I 614
Cdd:TIGR04226   5 ITKkvnDKDDADVNIGDEVTYTITTTVpADIADYKSFVITDTLDDG----LTYKGSvkVTVDGKtltvdtdytvtdgqtV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1309179805 615 TWTL--AGPLAMADGPQTITYTVKVDSTMPTGTTNvDNTVVIN 655
Cdd:TIGR04226  81 TVTFtdAGLKKLAGKKITVTYTAKVKEGAVLGKGI-PNTATLT 122
rne PRK10811
ribonuclease E; Reviewed
40-129 6.05e-04

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 43.10  E-value: 6.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805   40 EPAKQAPEVVAPAEVAVPDPATEEVVAQPVADVVPEEPVVEVPASTET---------------VVSEEIAPVTAEVAVPV 104
Cdd:PRK10811   867 QPVVAEVPVAAAVEPVVSAPVVEAVAEVVEEPVVVAEPQPEEVVVVETthpeviaapvteqpqVITESDVAVAQEVAEHA 946
                           90       100
                   ....*....|....*....|....*
gi 1309179805  105 AKATPTATTPTAIVSTSLVEPIVVP 129
Cdd:PRK10811   947 EPVVEPQDETADIEEAAETAEVVVA 971
rne PRK10811
ribonuclease E; Reviewed
40-106 1.20e-03

ribonuclease E; Reviewed


Pssm-ID: 236766 [Multi-domain]  Cd Length: 1068  Bit Score: 42.33  E-value: 1.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1309179805   40 EPAKQAPEVVAPAEVAVPDPATEEvvAQPVADVVPEEPVVEVPASTE-------TVVSEEIAPVTAEVAVPVAK 106
Cdd:PRK10811   922 APVTEQPQVITESDVAVAQEVAEH--AEPVVEPQDETADIEEAAETAevvvaepEVVAQPAAPVVAEVAAEVET 993
COG4719 COG4719
Uncharacterized conserved protein, UCP014979 family [Function unknown];
561-611 2.02e-03

Uncharacterized conserved protein, UCP014979 family [Function unknown];


Pssm-ID: 443754  Cd Length: 167  Bit Score: 39.64  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1309179805 561 DVATAAPGATITYTLTYRNLGETEATNFTIVDDFDERYVTVLDAAGGVVAD 611
Cdd:COG4719    55 PAATVVPGDVLRYTLTYRNTGDRPATGLVITNPIPEGTIYVLASATGLGAT 105
MJ0795 COG1361
S-layer protein MJ0795, predicted component of type IV pili-like system [General function ...
564-681 2.33e-03

S-layer protein MJ0795, predicted component of type IV pili-like system [General function prediction only];


Pssm-ID: 440972 [Multi-domain]  Cd Length: 409  Bit Score: 40.83  E-value: 2.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 564 TAAPGATITYTLTYRNLGETEATNFTIVDDFDE--RYVTVLDAAGGVVADGKitwtlagplamadgPQTITYTVKVDSTM 641
Cdd:COG1361    35 EVAPGEEVTLTVTITNDGTLTARNVTVELEGDYpfEVKSGEQSVGGSLPPGQ--------------SVTVTFTVTVPEDA 100
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1309179805 642 PTGTTNVDntVVINHPDDSNPDNNTDDERVRVTVQGEPFL 681
Cdd:COG1361   101 EPGTYPIP--VTVSYSYGYTDRTETETYTVTVKVEGEPRF 138
B_ant_repeat TIGR01451
conserved repeat domain; This model represents the conserved region of about 53 amino acids ...
558-592 2.65e-03

conserved repeat domain; This model represents the conserved region of about 53 amino acids shared between regions, usually repeated, of proteins from a small number of phylogenetically distant prokaryotes. Examples include a 132-residue region found repeated in three of the five longest proteins of Bacillus anthracis, a 131-residue repeat in a cell wall-anchored protein of Enterococcus faecalis, and a 120-residue repeat in Methanobacterium thermoautotrophicum. A similar region is found in some Chlamydial outer membrane proteins.


Pssm-ID: 273634 [Multi-domain]  Cd Length: 53  Bit Score: 36.44  E-value: 2.65e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1309179805 558 KAADVATAAPGATITYTLTYRNLGETEATNFTIVD 592
Cdd:TIGR01451   1 KTVDKTVATIGDTITYTITVTNNGNVPATNVVVTD 35
isopep_sspB_C2 TIGR04228
adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 ...
561-613 5.64e-03

adhesin isopeptide-forming domain, sspB-C2 type; This domain has a conserved Lys (position 3 in seed alignment) and Asn at 177 that form an intramolecular isopeptide bond. The Asp (or Glu) at position 59


Pssm-ID: 275068 [Multi-domain]  Cd Length: 173  Bit Score: 38.43  E-value: 5.64e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1309179805 561 DVATAAPGATITYTLT-----YRNLG---ETEATNFTIVDDFDERYVTVLDAAGGVV-ADGK 613
Cdd:TIGR04228  14 DGKTVLPGSTNYYRLTwdlsqYKGIKaskEAIAKGFGYVDDYDEEALTVDQDKITITdSNGK 75
ClfA COG4932
Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing ...
231-675 7.68e-03

Clumping factor A-related surface protein, MSCRAMM (microbial surface components recognizing adhesive matrix molecules) family, DEv-IgG fold [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 443959 [Multi-domain]  Cd Length: 689  Bit Score: 39.57  E-value: 7.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 231 EPETGSITVVKfndLDGDGQKSeseptLDGWDFALTLPTGGMLTGTSGA--DGPGAVLFGELPAGTYSVDETAKPGWHNT 308
Cdd:COG4932   258 KYTKGSVTVTK---TDADTGEP-----LAGATFTLTDADGNTVVTTTVTvtDADGSYTFTDLPPGTYTVTETKAPAGYDL 329
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 309 TTLPMDVTLAEGEDKTVYVGNAEDPAEDFTKTF--ELTYNGDIP-AETTFRVHYTLGTppeevapaIVDGTWLDLVGTGP 385
Cdd:COG4932   330 DGEAVKVTITAGQTTTVTVTNGNNEVKTGSVTLtkVDADDGEAPlAGAEFTLTDADGT--------VVATITTDADGTAS 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 386 FSasvELPAG--TIIESVdwyAQRGLEqiLLGTTEGETLTEDITNSFTYNGDASGykfndlNGDGIWDEGEPGIEGWTIY 463
Cdd:COG4932   402 FK---GLAPGtyTLTETK---APEGYT--LDSTPITVTVTDGGTGAIDTITNERK------KGSVQVTKVDAPLAGATFT 467
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 464 LYRQVPQIV--LNDAPTPEPGFELYATTL--TGADGSYHFSGVLPGTYYVAEETregwdMTVGPEGTFVMVNDQPITGLI 539
Cdd:COG4932   468 LTDADGTVVtlTTDADLAGATFEADGKVVttTDASGKYTFKNLPPGTYTDAGGS-----ATVITDDTDGTVGDEATGTDP 542
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1309179805 540 FGNHEPFLPFTDIDLAITKAADVATAAPGATITYTLTYRNLGETEATNFTIVDDFDERYVTVLDAAGGVVADGKITWTLA 619
Cdd:COG4932   543 EVTVTGKSTTTTPDVALLTNLGTTEDALTSLAKTGDEVGKGLTLTTTTTVDTLDTNATEKTETVTVTAQLIGVKTTKLTD 622
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1309179805 620 GPLAMADGPQTITYTVKVDSTMPTGTTNVDNTVVINHPDDSNPDNNTDDERVRVTV 675
Cdd:COG4932   623 TTDPKGGTVEEATTTGGTANTGKTGTDLTDDTTVTSTTNTATSVEDTTDVDNKDAF 678
 
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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