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Conserved domains on  [gi|2556145065|ref|WP_303925172|]
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two-component regulator propeller domain-containing protein [Draconibacterium sediminis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
COG3292 super family cl27077
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
269-731 3.67e-15

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG3292:

Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 79.65  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 269 IASRDVVFIIDSNHSQIGRIDSYK-FNDRTVESIApksasVSADGSVWIADDKEvLVRY--YSENFEQ-TLPPGPINNDM 344
Cdd:COG3292    96 IGTDGGLSRYDPKTDKFTRYPLDPgLPNNSIRSIA-----EDSDGNIWVGTSNG-LYRYdpKTGKFKRfTLDGLPSNTIT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 345 YFVGAFNSEIWMTAGG----PNGYKGPVFQRFGNDGWTYFTDQTHPELRGFHNILAVEVDPRDpdHFFVASWGGGLLeyr 420
Cdd:COG3292   170 SLAEDADGNLWVDSDGnlwiGTDGNGLYRLDPNTGKFEHITHDPDPNSLSSNSIYSLFEDREG--NLWVGTYGGGLN--- 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 421 ndelveRYYNLNSPLETALPEQPNE-PFTRVGGMSFDSEGNLWI-----TNAecaHNLHKLTP-SGEWESFELPEIANRy 493
Cdd:COG3292   245 ------YLDPNNSKFKSYRHNDPNGlSGNSVRSIAEDSDGNLWIrlwigTYG---GGLFRLDPkTGKFKRYNPNGLPSN- 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 494 NVSDIIVNENDDKWMLIPGGHdAYVINKTGDQKKRLLVQTYFSNGtdniitpmhDVFSIAEDQNGAIWIGSGQGVAVYSS 573
Cdd:COG3292   315 SVYSILEDSDGNLWIGTSGGG-LYRYDPKTGKFTKFSEDNGLSNN---------FIRSILEDSDGNLWVGTNGGLYRLDP 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 574 PSRIWNSENFYATHPGLDLNdgiyhplleteTVTAIAVDGANRKWLGTQNSGVFLVSETGEaEVLHFTTENsPLLSNNIL 653
Cdd:COG3292   385 KTGKFTNFTHDPDKNGLSSN-----------YINSIFEDSDGRLWIGTDGGGLYRYDPKTG-KFKHFTTKD-GLPSNTIY 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 654 SIAINQKN---GEVFFGTDKGLISYQGEATGGADTYSNVYVYPNPVRETYDGPVTVAGLIENTDVKITDITGNLVYKTTS 730
Cdd:COG3292   452 SILEDDNGnlwNFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLS 531

                  .
gi 2556145065 731 F 731
Cdd:COG3292   532 L 532
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
269-731 3.67e-15

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 79.65  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 269 IASRDVVFIIDSNHSQIGRIDSYK-FNDRTVESIApksasVSADGSVWIADDKEvLVRY--YSENFEQ-TLPPGPINNDM 344
Cdd:COG3292    96 IGTDGGLSRYDPKTDKFTRYPLDPgLPNNSIRSIA-----EDSDGNIWVGTSNG-LYRYdpKTGKFKRfTLDGLPSNTIT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 345 YFVGAFNSEIWMTAGG----PNGYKGPVFQRFGNDGWTYFTDQTHPELRGFHNILAVEVDPRDpdHFFVASWGGGLLeyr 420
Cdd:COG3292   170 SLAEDADGNLWVDSDGnlwiGTDGNGLYRLDPNTGKFEHITHDPDPNSLSSNSIYSLFEDREG--NLWVGTYGGGLN--- 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 421 ndelveRYYNLNSPLETALPEQPNE-PFTRVGGMSFDSEGNLWI-----TNAecaHNLHKLTP-SGEWESFELPEIANRy 493
Cdd:COG3292   245 ------YLDPNNSKFKSYRHNDPNGlSGNSVRSIAEDSDGNLWIrlwigTYG---GGLFRLDPkTGKFKRYNPNGLPSN- 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 494 NVSDIIVNENDDKWMLIPGGHdAYVINKTGDQKKRLLVQTYFSNGtdniitpmhDVFSIAEDQNGAIWIGSGQGVAVYSS 573
Cdd:COG3292   315 SVYSILEDSDGNLWIGTSGGG-LYRYDPKTGKFTKFSEDNGLSNN---------FIRSILEDSDGNLWVGTNGGLYRLDP 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 574 PSRIWNSENFYATHPGLDLNdgiyhplleteTVTAIAVDGANRKWLGTQNSGVFLVSETGEaEVLHFTTENsPLLSNNIL 653
Cdd:COG3292   385 KTGKFTNFTHDPDKNGLSSN-----------YINSIFEDSDGRLWIGTDGGGLYRYDPKTG-KFKHFTTKD-GLPSNTIY 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 654 SIAINQKN---GEVFFGTDKGLISYQGEATGGADTYSNVYVYPNPVRETYDGPVTVAGLIENTDVKITDITGNLVYKTTS 730
Cdd:COG3292   452 SILEDDNGnlwNFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLS 531

                  .
gi 2556145065 731 F 731
Cdd:COG3292   532 L 532
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
691-765 1.74e-05

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 43.37  E-value: 1.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2556145065 691 VYPNPVRETydgpVTV---AGLIENTDVKITDITGNLVYKTTSFGGQAVwdgKNLNGKRVKTGVYLVFCNDENGEETH 765
Cdd:pfam18962   1 IYPNPAKDV----LNIslkNSNSSNLNISIYDILGKLVKSNSKTNGNNT---KTIDVSNLSSGIYFVKINSGNGSTTK 71
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
691-770 1.44e-04

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 40.85  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 691 VYPNPVRETYDgpVTVAGLIENTDVKITDITGNLVYKTTSFGGQavwdgkNLNGKRVKTGVYLVfcNDENGEETHITKIL 770
Cdd:TIGR04183   1 IYPNPAKGTLI--IILLSSSGKVKVEIYDLSGKLVKKTTLNNSN------SIDLSNLSSGVYIV--KITTGNGTITKKII 70
T9SS_sortase NF033707
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the ...
688-753 1.13e-03

type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion.


Pssm-ID: 468145 [Multi-domain]  Cd Length: 1056  Bit Score: 42.54  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065  688 NVYVYPNPVRE------TYDGPvtvaglIENTDV--KITDITGNLVYK------TTSFGGQAV-WDGKNLNGKRVKTGVY 752
Cdd:NF033707   959 NVLNYPNPFVNytefwfEHNRP------GEPLDVqvQVFTVSGKLVWThnqtvtSTGFLSYTItWDGRDDFGDRLGKGVY 1032

                   .
gi 2556145065  753 L 753
Cdd:NF033707  1033 I 1033
 
Name Accession Description Interval E-value
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
269-731 3.67e-15

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 79.65  E-value: 3.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 269 IASRDVVFIIDSNHSQIGRIDSYK-FNDRTVESIApksasVSADGSVWIADDKEvLVRY--YSENFEQ-TLPPGPINNDM 344
Cdd:COG3292    96 IGTDGGLSRYDPKTDKFTRYPLDPgLPNNSIRSIA-----EDSDGNIWVGTSNG-LYRYdpKTGKFKRfTLDGLPSNTIT 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 345 YFVGAFNSEIWMTAGG----PNGYKGPVFQRFGNDGWTYFTDQTHPELRGFHNILAVEVDPRDpdHFFVASWGGGLLeyr 420
Cdd:COG3292   170 SLAEDADGNLWVDSDGnlwiGTDGNGLYRLDPNTGKFEHITHDPDPNSLSSNSIYSLFEDREG--NLWVGTYGGGLN--- 244
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 421 ndelveRYYNLNSPLETALPEQPNE-PFTRVGGMSFDSEGNLWI-----TNAecaHNLHKLTP-SGEWESFELPEIANRy 493
Cdd:COG3292   245 ------YLDPNNSKFKSYRHNDPNGlSGNSVRSIAEDSDGNLWIrlwigTYG---GGLFRLDPkTGKFKRYNPNGLPSN- 314
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 494 NVSDIIVNENDDKWMLIPGGHdAYVINKTGDQKKRLLVQTYFSNGtdniitpmhDVFSIAEDQNGAIWIGSGQGVAVYSS 573
Cdd:COG3292   315 SVYSILEDSDGNLWIGTSGGG-LYRYDPKTGKFTKFSEDNGLSNN---------FIRSILEDSDGNLWVGTNGGLYRLDP 384
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 574 PSRIWNSENFYATHPGLDLNdgiyhplleteTVTAIAVDGANRKWLGTQNSGVFLVSETGEaEVLHFTTENsPLLSNNIL 653
Cdd:COG3292   385 KTGKFTNFTHDPDKNGLSSN-----------YINSIFEDSDGRLWIGTDGGGLYRYDPKTG-KFKHFTTKD-GLPSNTIY 451
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 654 SIAINQKN---GEVFFGTDKGLISYQGEATGGADTYSNVYVYPNPVRETYDGPVTVAGLIENTDVKITDITGNLVYKTTS 730
Cdd:COG3292   452 SILEDDNGnlwNFNSASNLGLLSLLGGLLGGLNLGNAIKLPLSNLGLLLTLLLLGINLSLVRSLISLLTLLLLALLLLLS 531

                  .
gi 2556145065 731 F 731
Cdd:COG3292   532 L 532
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
289-678 4.92e-12

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 69.63  E-value: 4.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 289 DSYKFNDRTVESIApksasVSADGSVWIADDKEvLVRY--YSENFEQ-TLPPGPINNDMY-FVGAFNSEIWM-TAGGPNG 363
Cdd:COG3292    74 DPNSLPSNYIRALL-----EDSDGRLWIGTDGG-LSRYdpKTDKFTRyPLDPGLPNNSIRsIAEDSDGNIWVgTSNGLYR 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 364 YKgpvfqrFGNDGWTYFTDQTHPelrgFHNILAVEVDPR------DPDHFFVASWGGGLLEYRNDELVERYYNlNSPLET 437
Cdd:COG3292   148 YD------PKTGKFKRFTLDGLP----SNTITSLAEDADgnlwvdSDGNLWIGTDGNGLYRLDPNTGKFEHIT-HDPDPN 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 438 ALPEqpnepfTRVGGMSFDSEGNLWI-TNAecaHNLHKLTPSgeWESFELPEIANRYNVSDIIVN---ENDDK--WMLIP 511
Cdd:COG3292   217 SLSS------NSIYSLFEDREGNLWVgTYG---GGLNYLDPN--NSKFKSYRHNDPNGLSGNSVRsiaEDSDGnlWIRLW 285
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 512 GGHDA---YVINKTGDQKKRLLVQTYFSNgtdniitpmhDVFSIAEDQNGAIWIGS-GQGVAVYSSPSRIWNSenfYATH 587
Cdd:COG3292   286 IGTYGgglFRLDPKTGKFKRYNPNGLPSN----------SVYSILEDSDGNLWIGTsGGGLYRYDPKTGKFTK---FSED 352
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 588 PGLDLNDgiyhplletetVTAIAVDGANRKWLGTQNSGVFLVSETGEAEVLHFTTENSPLLSNNILSIAINqKNGEVFFG 667
Cdd:COG3292   353 NGLSNNF-----------IRSILEDSDGNLWVGTNGGLYRLDPKTGKFTNFTHDPDKNGLSSNYINSIFED-SDGRLWIG 420
                         410
                  ....*....|..
gi 2556145065 668 TD-KGLISYQGE 678
Cdd:COG3292   421 TDgGGLYRYDPK 432
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
31-520 1.86e-10

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 64.63  E-value: 1.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065  31 LSYNKASKIAVSPD-KVFCVTEGGLFYYDLEDNSVNKFGGAIQLSDFGVSTIAYSEQSQVLVIAYSNsnidLLYDDGEVV 109
Cdd:COG3292    78 LPSNYIRALLEDSDgRLWIGTDGGLSRYDPKTDKFTRYPLDPGLPNNSIRSIAEDSDGNIWVGTSNG----LYRYDPKTG 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 110 NLSDIKRKTIAGNKvVNNISFSENEAYLA----------CGFGIVVLDLDRQEVKdTYYIGDGGSSLEVNDI----ETDN 175
Cdd:COG3292   154 KFKRFTLDGLPSNT-ITSLAEDADGNLWVdsdgnlwigtDGNGLYRLDPNTGKFE-HITHDPDPNSLSSNSIyslfEDRE 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 176 NSIFAAT-NQGIYRADknePNLANFANWIHVDdiphPDGIFNHLVYhggSVianfsagewYQDEmymlNNGVWepynpeI 254
Cdd:COG3292   232 GNLWVGTyGGGLNYLD---PNNSKFKSYRHND----PNGLSGNSVR---SI---------AEDS----DGNLW------I 282
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 255 RFAFDLQSNGnylsiasrdvVFIIDSNHSQIGRIDSYKFNDRTVESIAPKSasvsaDGSVWIADDKEVLVRYYSEN--FE 332
Cdd:COG3292   283 RLWIGTYGGG----------LFRLDPKTGKFKRYNPNGLPSNSVYSILEDS-----DGNLWIGTSGGGLYRYDPKTgkFT 347
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 333 QTLPPGPINNDMYFVGAFNSE--IWM-TAGGPNGYKGpvfqrfGNDGWTYFTDQTHPELRGFHNILAVEVDPRdpDHFFV 409
Cdd:COG3292   348 KFSEDNGLSNNFIRSILEDSDgnLWVgTNGGLYRLDP------KTGKFTNFTHDPDKNGLSSNYINSIFEDSD--GRLWI 419
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 410 ASWGGGLLEYRNDELVERYYNLNSPLetalpeqpnePFTRVGGMSFDSEGNLWITNAECAHNLHKLTPSGEWESFELPEI 489
Cdd:COG3292   420 GTDGGGLYRYDPKTGKFKHFTTKDGL----------PSNTIYSILEDDNGNLWNFNSASNLGLLSLLGGLLGGLNLGNAI 489
                         490       500       510
                  ....*....|....*....|....*....|.
gi 2556145065 490 ANRYNVSDIIVNENDDKWMLIPGGHDAYVIN 520
Cdd:COG3292   490 KLPLSNLGLLLTLLLLGINLSLVRSLISLLT 520
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
269-487 9.56e-08

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 54.26  E-value: 9.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 269 IASRDVVFIIDSNHSQIGRIDSykfNDRTVESIAPKSAS------VSADGSVWIADDKEVLVRYY---SENFEQTLPPGP 339
Cdd:COG4257    24 VDPDGAVWFTDQGGGRIGRLDP---ATGEFTEYPLGGGSgphgiaVDPDGNLWFTDNGNNRIGRIdpkTGEITTFALPGG 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 340 INN----------DMYFVGAFNSEIWM---------TAGGPNGYKGPVFQRFGNDGWTYFTDqthpelRGFHNILAVEVD 400
Cdd:COG4257   101 GSNphgiafdpdgNLWFTDQGGNRIGRldpatgevtEFPLPTGGAGPYGIAVDPDGNLWVTD------FGANAIGRIDPD 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 401 ---------------PR----DPD-HFFVASWGGGLLeYR---NDELVERYynlnspletALPEQPNEPFtrvgGMSFDS 457
Cdd:COG4257   175 tgtlteyalptpgagPRglavDPDgNLWVADTGSGRI-GRfdpKTGTVTEY---------PLPGGGARPY----GVAVDG 240
                         250       260       270
                  ....*....|....*....|....*....|
gi 2556145065 458 EGNLWITNAEcAHNLHKLTPSGEWESFELP 487
Cdd:COG4257   241 DGRVWFAESG-ANRIVRFDPDTELTEYVLP 269
COG3292 COG3292
Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];
549-697 2.89e-06

Periplasmic ligand-binding sensor domain [Signal transduction mechanisms];


Pssm-ID: 442521 [Multi-domain]  Cd Length: 924  Bit Score: 51.14  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 549 VFSIAEDQNGAIWIGSGQGVAVYsspsriwNSENFYATHPGLDLNDGIYHPlleteTVTAIAVDGANRKWLGTQNsGVFL 628
Cdd:COG3292    38 VNSIAQDSDGFLWIGTEDGLNRY-------DGYEFKVFRHDPGDPNSLPSN-----YIRALLEDSDGRLWIGTDG-GLSR 104
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2556145065 629 VSetGEAEVLHFTTENSPLLSNNILSIAINqKNGEVFFGTDKGLISYQgEATGGADTYSNVYVYPNPVR 697
Cdd:COG3292   105 YD--PKTDKFTRYPLDPGLPNNSIRSIAED-SDGNIWVGTSNGLYRYD-PKTGKFKRFTLDGLPSNTIT 169
Vgb COG4257
Streptogramin lyase [Defense mechanisms];
436-629 7.68e-06

Streptogramin lyase [Defense mechanisms];


Pssm-ID: 443399 [Multi-domain]  Cd Length: 270  Bit Score: 48.48  E-value: 7.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 436 ETALPEQPNEPFtrvgGMSFDSEGNLWITNAEcAHNLHKLTP-SGEWESFELPeiANRYNVSDIIVNENDDKWMLIPGGH 514
Cdd:COG4257    94 TFALPGGGSNPH----GIAFDPDGNLWFTDQG-GNRIGRLDPaTGEVTEFPLP--TGGAGPYGIAVDPDGNLWVTDFGAN 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 515 DAYVIN-KTGDqkkrllVQTYfsngtdNIITPMHDVFSIAEDQNGAIWI---GSGQgVAVYSSPSRIWnsenfyATHPgl 590
Cdd:COG4257   167 AIGRIDpDTGT------LTEY------ALPTPGAGPRGLAVDPDGNLWVadtGSGR-IGRFDPKTGTV------TEYP-- 225
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2556145065 591 dLNDGIYHPlletetvTAIAVDGANRKWLGTQNSGVFLV 629
Cdd:COG4257   226 -LPGGGARP-------YGVAVDGDGRVWFAESGANRIVR 256
Por_Secre_tail pfam18962
Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
691-765 1.74e-05

Secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber have on average twenty or more copies of this C-terminal domain, associated with sorting to the outer membrane and covalent modification. This domain targets proteins to type IX secretion systems and is secreted then cleaved off by a C-terminal signal peptidease. Based on similarity to other families it is likely that this domain adopts an immunoglobulin like fold.


Pssm-ID: 436869 [Multi-domain]  Cd Length: 75  Bit Score: 43.37  E-value: 1.74e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2556145065 691 VYPNPVRETydgpVTV---AGLIENTDVKITDITGNLVYKTTSFGGQAVwdgKNLNGKRVKTGVYLVFCNDENGEETH 765
Cdd:pfam18962   1 IYPNPAKDV----LNIslkNSNSSNLNISIYDILGKLVKSNSKTNGNNT---KTIDVSNLSSGIYFVKINSGNGSTTK 71
Por_Secre_tail TIGR04183
Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, ...
691-770 1.44e-04

Por secretion system C-terminal sorting domain; Species that include Porphyromonas gingivalis, Fibrobacter succinogenes, Flavobacterium johnsoniae, Cytophaga hutchinsonii, Gramella forsetii, Prevotella intermedia, and Salinibacter ruber average twenty or more copies of a C-terminal domain, represented by this model, associated with sorting to the outer membrane and covalent modification.


Pssm-ID: 275036 [Multi-domain]  Cd Length: 72  Bit Score: 40.85  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065 691 VYPNPVRETYDgpVTVAGLIENTDVKITDITGNLVYKTTSFGGQavwdgkNLNGKRVKTGVYLVfcNDENGEETHITKIL 770
Cdd:TIGR04183   1 IYPNPAKGTLI--IILLSSSGKVKVEIYDLSGKLVKKTTLNNSN------SIDLSNLSSGVYIV--KITTGNGTITKKII 70
FLgD_tudor pfam13861
FlgD Tudor-like domain; This domain has a tudor domain-like beta barrel fold. It is found in ...
704-752 3.47e-04

FlgD Tudor-like domain; This domain has a tudor domain-like beta barrel fold. It is found in the FlgD protein the flagellar hook capping protein. The structure for this domain shows that it contains a nested Ig-like domain within it. However in some firmicute proteins this inserted domain is absent such as Q67K21.


Pssm-ID: 433533  Cd Length: 136  Bit Score: 41.43  E-value: 3.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2556145065 704 VTVAGLIENTDVKITDITGNLVyKTTSFGGQA------VWDGKNLNGKRVKTGVY 752
Cdd:pfam13861  33 VELPSAADNVTVTIYDSSGQVV-RTIDLGAQAagnvsfTWDGKDSDGNQLPDGTY 86
T9SS_sortase NF033707
type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the ...
688-753 1.13e-03

type IX secretion system sortase PorU; PorU, part of type IX secretion systems (T9SS), is the protease responsible for both removing the C-terminal sorting signal found in substrates and for its replacement by anionic LPS, through which most T9SS substrates become attached to the cell surface after secretion.


Pssm-ID: 468145 [Multi-domain]  Cd Length: 1056  Bit Score: 42.54  E-value: 1.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2556145065  688 NVYVYPNPVRE------TYDGPvtvaglIENTDV--KITDITGNLVYK------TTSFGGQAV-WDGKNLNGKRVKTGVY 752
Cdd:NF033707   959 NVLNYPNPFVNytefwfEHNRP------GEPLDVqvQVFTVSGKLVWThnqtvtSTGFLSYTItWDGRDDFGDRLGKGVY 1032

                   .
gi 2556145065  753 L 753
Cdd:NF033707  1033 I 1033
FlgD_ig pfam13860
FlgD Ig-like domain; This domains has an immunoglobulin like beta sandwich fold. It is found ...
704-754 4.34e-03

FlgD Ig-like domain; This domains has an immunoglobulin like beta sandwich fold. It is found in the FlgD protein the flagellar hook capping protein. THe structure for this domain shows that it is inserted within a TUDOR like beta barrel domain.


Pssm-ID: 433532 [Multi-domain]  Cd Length: 78  Bit Score: 36.56  E-value: 4.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2556145065 704 VTVAGLIENTDVKITDITGNLVyKTTSFGGQA------VWDGKNLNGKRVKTGVYLV 754
Cdd:pfam13860  16 LTLPSPADSVTVTIYDAAGQLV-RTIDLGAQSagdvsfTWDGTDDDGNKLADGTYTF 71
FlgD COG1843
Flagellar hook-capping protein FlgD [Cell motility];
698-754 4.73e-03

Flagellar hook-capping protein FlgD [Cell motility];


Pssm-ID: 441448 [Multi-domain]  Cd Length: 223  Bit Score: 39.22  E-value: 4.73e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2556145065 698 ETYDGPVTVAGLIENTDVKITDITGNLVyKTTSFGGQA------VWDGKNLNGKRVKTGVYLV 754
Cdd:COG1843   110 GSASGGFELPSAADSVTVTITDANGNVV-RTIDLGAQSagvhtfTWDGTDDDGNALPDGTYTF 171
 
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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