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Conserved domains on  [gi|1816261990|ref|WP_163353248|]
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type II secretion system F family protein [Desulfovibrio sp. JC010]

Protein Classification

type II secretion system F family protein( domain architecture ID 1001577)

type II secretion system (T2SS) F family protein similar to Thermus thermophilus PilC type IV pilus biogenesis protein and Vibrio Cholerae toxin coregulated pilus biosynthesis protein E (TcpE)

CATH:  1.20.81.30
Gene Ontology:  GO:0005886|GO:0016020
PubMed:  8438237|11266368

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PulF super family cl34272
Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, ...
13-281 2.27e-13

Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


The actual alignment was detected with superfamily member COG1459:

Pssm-ID: 441068 [Multi-domain]  Cd Length: 399  Bit Score: 70.53  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  13 LFFTQQvrirvyrkLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEALRGF---IPAEEAMLLQ 89
Cdd:COG1459    63 ALFTRQ--------LATLLRAGLPLLEALEILAEQTENPR--LRKVLADIREDVEEGASLSEALAKHpkvFPPLYVNMVR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  90 SGMESGKLHVSLELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLA--------ELSEPSRWvgsak 161
Cdd:COG1459   133 AGEASGNLDEVLERLADYLEKQEELRKKIKSALIYPAIVLVVAIGVVLFLLTFVVPQFAgifesfgaELPLLTRI----- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 162 tLYQVAGFVdSTFGTILLAGIVLLFLTSLATIKiwTGKIRVRFDGLppwsFYRL-IIGSLWL------F--TLSTLMKSG 232
Cdd:COG1459   208 -LIALSDFL-QNYWWLLLLGLVLLVVGFRRLLR--TPKGRLRLDRL----LLKLpVIGPLIRkaalarFarTLATLLSSG 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1816261990 233 IQLSQAMNDMLETPGsSPWLKERLNSIKAQLNLGKGIGEALDDSGYrFP 281
Cdd:COG1459   280 VPLLEALEIAAEVVG-NRVLREALEEARERVREGESLSEALEASGL-FP 326
 
Name Accession Description Interval E-value
PulF COG1459
Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, ...
13-281 2.27e-13

Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 441068 [Multi-domain]  Cd Length: 399  Bit Score: 70.53  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  13 LFFTQQvrirvyrkLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEALRGF---IPAEEAMLLQ 89
Cdd:COG1459    63 ALFTRQ--------LATLLRAGLPLLEALEILAEQTENPR--LRKVLADIREDVEEGASLSEALAKHpkvFPPLYVNMVR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  90 SGMESGKLHVSLELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLA--------ELSEPSRWvgsak 161
Cdd:COG1459   133 AGEASGNLDEVLERLADYLEKQEELRKKIKSALIYPAIVLVVAIGVVLFLLTFVVPQFAgifesfgaELPLLTRI----- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 162 tLYQVAGFVdSTFGTILLAGIVLLFLTSLATIKiwTGKIRVRFDGLppwsFYRL-IIGSLWL------F--TLSTLMKSG 232
Cdd:COG1459   208 -LIALSDFL-QNYWWLLLLGLVLLVVGFRRLLR--TPKGRLRLDRL----LLKLpVIGPLIRkaalarFarTLATLLSSG 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1816261990 233 IQLSQAMNDMLETPGsSPWLKERLNSIKAQLNLGKGIGEALDDSGYrFP 281
Cdd:COG1459   280 VPLLEALEIAAEVVG-NRVLREALEEARERVREGESLSEALEASGL-FP 326
GspF TIGR02120
type II secretion system protein F; This membrane protein is a component of the terminal ...
25-282 6.86e-07

type II secretion system protein F; This membrane protein is a component of the terminal branch complex of the general secretion pathway (GSP), also known as the"Type II" secretion pathway. The GSP transports proteins (generally virulence-associated cell wall hydrolases) across the outer membrase of the bacterial cell. Transport across the inner membrane is often, but not exclusively handled by the Sec system. This model was constructed from the broader subfamily model, pfam00482 which includes components of pilin complexes (PilC) as well as other related genes. GspF is nearly always gene clustered with other GSP subunits. Some genes from Xylella and Xanthomonas strains score below the trusted cutoff due to excessive divergence from the family such that a sequence from Deinococcus which does not appear to be GspF scores higher. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273980 [Multi-domain]  Cd Length: 399  Bit Score: 50.79  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  25 RKLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEAL----RGFIPAEEAMLlQSGMESGKLHVS 100
Cdd:TIGR02120  68 RQLATLLGAGLPLEEALAALLEQAEKPR--LKSVLAAIRSRVLEGKSLADALaqhpRDFPPLYRALV-AAGEASGALDAV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 101 LELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLAELSEPSRWVGSAKT--LYQVAGFVDStFGTIL 178
Cdd:TIGR02120 145 LERLADYLEERQALRSKITTALIYPAVLTVVAIGVVIFLLAYVVPKVVEQFAHMKQTLPLLTraLIALSDFLRS-WGWAL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 179 LAGIVLLFLTSLATIKiwTGKIRVRFD----GLPPW-SFYRLIIGSLWLFTLSTLMKSGIQLSQAMNDMLETPGSSPwLK 253
Cdd:TIGR02120 224 LAALAALVVLFRRLLR--DPAFRLRFDrrllRLPVIgRLVRGLNTARFARTLSILLSSGVPLLRALQIARETLTNRA-LR 300
                         250       260
                  ....*....|....*....|....*....
gi 1816261990 254 ERLNSIKAQLNLGKGIGEALDDSGyRFPA 282
Cdd:TIGR02120 301 AAVEDAAARVREGGSLSRALRATG-LFPP 328
T4P_ComGB NF041012
competence type IV pilus assembly protein ComGB; Members of this family occur in Gram-positive ...
20-278 1.04e-06

competence type IV pilus assembly protein ComGB; Members of this family occur in Gram-positive bacteria as part of a type IV pilus system used for DNA binding and uptake when species such as Streptococcus pneumoniae or Bacilus subtilis are in a competent state for natural transformation. Members of this family, typically called ComGB (second protein of the ComG operon), belong more broadly to the family of GspF, part of type 2 secretion systems (T2SS) in Gram-negative bacteria.


Pssm-ID: 468941 [Multi-domain]  Cd Length: 333  Bit Score: 49.78  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  20 RIRVYRKLAAMTRHGILMADAVSYIEeryaKQRNLLSPV-LSEVSARINSGDSIHEALR--GFiPAEEAMLLQSGMESGK 96
Cdd:NF041012    3 QAKFLQRLGELLESGFSLSEALEFLL----RQLPKKSKEyLQKILEGLKEGASLSEILKqlGF-SDEIVTQIYFAEKHGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  97 LHVSLELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLAELSEPSRWVGSAKTlyQVAGFVDSTFGT 176
Cdd:NF041012   78 LAETLKEIAEYLKRKEKQKKKLIKVLQYPLLLLLFLILILLGLRQYLLPQFEQLYSSMNVMLSSFT--NLLTLFIQHLPL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 177 ILLAGIVLLFLTSLATIKIWTGK---IRVRFDGLPPW--SFYRLIIGSLWLFTLSTLMKSGIQLSQAMNDMLETPgSSPW 251
Cdd:NF041012  156 IILGFLLLLLLLFLIYIFYFKKLsplKQIKFLSKIPLigSLYKLYLTYYFARELGNLLKQGLSLQQILQLMQEQK-SDPF 234
                         250       260
                  ....*....|....*....|....*..
gi 1816261990 252 LKERLNSIKAQLNLGKGIGEALDDSGY 278
Cdd:NF041012  235 LQELAKRLEERLLKGESLEQILKKYPF 261
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
208-313 1.03e-04

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatases 5 and 13; This subgroup of enzymatically inactive phosphatase domains of myotubularins consists of MTMR5, also known as SET binding factor 1 (SBF1) and MTMR13, also known as SET binding factor 2 (SBF2), and similar domains. Beside the pseudophosphatase domain, they contain a variety of other domains, including a DENN and a PH-like domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR5 and MTMR13 are pseudophosphatases that lack the catalytic cysteine in their catalytic pocket. Mutations in MTMR13 causes Charcot-Marie-Tooth type 4B2, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR2. Mutations in the MTMR5 gene cause Charcot-Marie-tooth disease type 4B3. MTMR5 and MTMR13 interact with MTMR2 and stimulate its phosphatase activity.


Pssm-ID: 350382 [Multi-domain]  Cd Length: 274  Bit Score: 43.51  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 208 PPWSFYRLIIGSLWLFTLSTLMksgiQLSQAMNDMLETPGSSPWLK-ERLNSIKAQLNlgkGIGEALDDSGYRfpaqtii 286
Cdd:cd14534   157 PEQSFLKAVEDSEWLQQLQCLM----QLSGAVVDLLDVQGSSVLLClEDGWDVTTQVS---SLSQLLLDPYYR------- 222
                          90       100
                  ....*....|....*....|....*..
gi 1816261990 287 edlriysTLPGFdaRLhLIAEEWLAEG 313
Cdd:cd14534   223 -------TLEGF--RV-LVEKEWLAFG 239
T2SSF pfam00482
Type II secretion system (T2SS), protein F; The original family covered both the regions found ...
24-125 3.76e-04

Type II secretion system (T2SS), protein F; The original family covered both the regions found by the current model. The splitting of the family has allowed the related FlaJ_arch (archaeal FlaJ family) to be merged with it. Proteins with this domain in form a platform for the machiney of the Type II secretion system, as well as the Type 4 pili and the archaeal flagella. This domain seems to show some similarity to PF00664 but this may just be due to similarities in the TM helices (personal obs: C Yeats).


Pssm-ID: 425708 [Multi-domain]  Cd Length: 119  Bit Score: 39.63  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  24 YRKLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEALR----GFIPAEEAMLLQSGMESGKLHV 99
Cdd:pfam00482   2 LRQLATLLRAGLPLVEALEILAEEAENGP--LREELRRIAERVREGGSLSEALArtpsSVFPPLLVALIAAGESGGNLAE 79
                          90       100
                  ....*....|....*....|....*.
gi 1816261990 100 SLELCVKLIKARLKIVNSMWKALSYP 125
Cdd:pfam00482  80 VLERLADYLEEERELRRKIKAALLYP 105
 
Name Accession Description Interval E-value
PulF COG1459
Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, ...
13-281 2.27e-13

Type II secretory pathway, component PulF [Cell motility, Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 441068 [Multi-domain]  Cd Length: 399  Bit Score: 70.53  E-value: 2.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  13 LFFTQQvrirvyrkLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEALRGF---IPAEEAMLLQ 89
Cdd:COG1459    63 ALFTRQ--------LATLLRAGLPLLEALEILAEQTENPR--LRKVLADIREDVEEGASLSEALAKHpkvFPPLYVNMVR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  90 SGMESGKLHVSLELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLA--------ELSEPSRWvgsak 161
Cdd:COG1459   133 AGEASGNLDEVLERLADYLEKQEELRKKIKSALIYPAIVLVVAIGVVLFLLTFVVPQFAgifesfgaELPLLTRI----- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 162 tLYQVAGFVdSTFGTILLAGIVLLFLTSLATIKiwTGKIRVRFDGLppwsFYRL-IIGSLWL------F--TLSTLMKSG 232
Cdd:COG1459   208 -LIALSDFL-QNYWWLLLLGLVLLVVGFRRLLR--TPKGRLRLDRL----LLKLpVIGPLIRkaalarFarTLATLLSSG 279
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1816261990 233 IQLSQAMNDMLETPGsSPWLKERLNSIKAQLNLGKGIGEALDDSGYrFP 281
Cdd:COG1459   280 VPLLEALEIAAEVVG-NRVLREALEEARERVREGESLSEALEASGL-FP 326
GspF TIGR02120
type II secretion system protein F; This membrane protein is a component of the terminal ...
25-282 6.86e-07

type II secretion system protein F; This membrane protein is a component of the terminal branch complex of the general secretion pathway (GSP), also known as the"Type II" secretion pathway. The GSP transports proteins (generally virulence-associated cell wall hydrolases) across the outer membrase of the bacterial cell. Transport across the inner membrane is often, but not exclusively handled by the Sec system. This model was constructed from the broader subfamily model, pfam00482 which includes components of pilin complexes (PilC) as well as other related genes. GspF is nearly always gene clustered with other GSP subunits. Some genes from Xylella and Xanthomonas strains score below the trusted cutoff due to excessive divergence from the family such that a sequence from Deinococcus which does not appear to be GspF scores higher. [Protein fate, Protein and peptide secretion and trafficking]


Pssm-ID: 273980 [Multi-domain]  Cd Length: 399  Bit Score: 50.79  E-value: 6.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  25 RKLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEAL----RGFIPAEEAMLlQSGMESGKLHVS 100
Cdd:TIGR02120  68 RQLATLLGAGLPLEEALAALLEQAEKPR--LKSVLAAIRSRVLEGKSLADALaqhpRDFPPLYRALV-AAGEASGALDAV 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 101 LELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLAELSEPSRWVGSAKT--LYQVAGFVDStFGTIL 178
Cdd:TIGR02120 145 LERLADYLEERQALRSKITTALIYPAVLTVVAIGVVIFLLAYVVPKVVEQFAHMKQTLPLLTraLIALSDFLRS-WGWAL 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 179 LAGIVLLFLTSLATIKiwTGKIRVRFD----GLPPW-SFYRLIIGSLWLFTLSTLMKSGIQLSQAMNDMLETPGSSPwLK 253
Cdd:TIGR02120 224 LAALAALVVLFRRLLR--DPAFRLRFDrrllRLPVIgRLVRGLNTARFARTLSILLSSGVPLLRALQIARETLTNRA-LR 300
                         250       260
                  ....*....|....*....|....*....
gi 1816261990 254 ERLNSIKAQLNLGKGIGEALDDSGyRFPA 282
Cdd:TIGR02120 301 AAVEDAAARVREGGSLSRALRATG-LFPP 328
T4P_ComGB NF041012
competence type IV pilus assembly protein ComGB; Members of this family occur in Gram-positive ...
20-278 1.04e-06

competence type IV pilus assembly protein ComGB; Members of this family occur in Gram-positive bacteria as part of a type IV pilus system used for DNA binding and uptake when species such as Streptococcus pneumoniae or Bacilus subtilis are in a competent state for natural transformation. Members of this family, typically called ComGB (second protein of the ComG operon), belong more broadly to the family of GspF, part of type 2 secretion systems (T2SS) in Gram-negative bacteria.


Pssm-ID: 468941 [Multi-domain]  Cd Length: 333  Bit Score: 49.78  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  20 RIRVYRKLAAMTRHGILMADAVSYIEeryaKQRNLLSPV-LSEVSARINSGDSIHEALR--GFiPAEEAMLLQSGMESGK 96
Cdd:NF041012    3 QAKFLQRLGELLESGFSLSEALEFLL----RQLPKKSKEyLQKILEGLKEGASLSEILKqlGF-SDEIVTQIYFAEKHGN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  97 LHVSLELCVKLIKARLKIVNSMWKALSYPVILVLALIALLLVLSRYVVPKLAELSEPSRWVGSAKTlyQVAGFVDSTFGT 176
Cdd:NF041012   78 LAETLKEIAEYLKRKEKQKKKLIKVLQYPLLLLLFLILILLGLRQYLLPQFEQLYSSMNVMLSSFT--NLLTLFIQHLPL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 177 ILLAGIVLLFLTSLATIKIWTGK---IRVRFDGLPPW--SFYRLIIGSLWLFTLSTLMKSGIQLSQAMNDMLETPgSSPW 251
Cdd:NF041012  156 IILGFLLLLLLLFLIYIFYFKKLsplKQIKFLSKIPLigSLYKLYLTYYFARELGNLLKQGLSLQQILQLMQEQK-SDPF 234
                         250       260
                  ....*....|....*....|....*..
gi 1816261990 252 LKERLNSIKAQLNLGKGIGEALDDSGY 278
Cdd:NF041012  235 LQELAKRLEERLLKGESLEQILKKYPF 261
PTP-MTMR5-like cd14534
protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related ...
208-313 1.03e-04

protein tyrosine phosphatase-like pseudophosphatase domain of myotubularin related phosphoinositide phosphatases 5 and 13; This subgroup of enzymatically inactive phosphatase domains of myotubularins consists of MTMR5, also known as SET binding factor 1 (SBF1) and MTMR13, also known as SET binding factor 2 (SBF2), and similar domains. Beside the pseudophosphatase domain, they contain a variety of other domains, including a DENN and a PH-like domain. In general, myotubularins are a unique subgroup of protein tyrosine phosphatases that use inositol phospholipids, rather than phosphoproteins, as substrates. MTMR5 and MTMR13 are pseudophosphatases that lack the catalytic cysteine in their catalytic pocket. Mutations in MTMR13 causes Charcot-Marie-Tooth type 4B2, a severe childhood-onset neuromuscular disorder, characterized by demyelination and redundant loops of myelin known as myelin outfoldings, a similar phenotype as mutations in MTMR2. Mutations in the MTMR5 gene cause Charcot-Marie-tooth disease type 4B3. MTMR5 and MTMR13 interact with MTMR2 and stimulate its phosphatase activity.


Pssm-ID: 350382 [Multi-domain]  Cd Length: 274  Bit Score: 43.51  E-value: 1.03e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 208 PPWSFYRLIIGSLWLFTLSTLMksgiQLSQAMNDMLETPGSSPWLK-ERLNSIKAQLNlgkGIGEALDDSGYRfpaqtii 286
Cdd:cd14534   157 PEQSFLKAVEDSEWLQQLQCLM----QLSGAVVDLLDVQGSSVLLClEDGWDVTTQVS---SLSQLLLDPYYR------- 222
                          90       100
                  ....*....|....*....|....*..
gi 1816261990 287 edlriysTLPGFdaRLhLIAEEWLAEG 313
Cdd:cd14534   223 -------TLEGF--RV-LVEKEWLAFG 239
T2SSF pfam00482
Type II secretion system (T2SS), protein F; The original family covered both the regions found ...
24-125 3.76e-04

Type II secretion system (T2SS), protein F; The original family covered both the regions found by the current model. The splitting of the family has allowed the related FlaJ_arch (archaeal FlaJ family) to be merged with it. Proteins with this domain in form a platform for the machiney of the Type II secretion system, as well as the Type 4 pili and the archaeal flagella. This domain seems to show some similarity to PF00664 but this may just be due to similarities in the TM helices (personal obs: C Yeats).


Pssm-ID: 425708 [Multi-domain]  Cd Length: 119  Bit Score: 39.63  E-value: 3.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990  24 YRKLAAMTRHGILMADAVSYIEERYAKQRnlLSPVLSEVSARINSGDSIHEALR----GFIPAEEAMLLQSGMESGKLHV 99
Cdd:pfam00482   2 LRQLATLLRAGLPLVEALEILAEEAENGP--LREELRRIAERVREGGSLSEALArtpsSVFPPLLVALIAAGESGGNLAE 79
                          90       100
                  ....*....|....*....|....*.
gi 1816261990 100 SLELCVKLIKARLKIVNSMWKALSYP 125
Cdd:pfam00482  80 VLERLADYLEEERELRRKIKAALLYP 105
T2SSF pfam00482
Type II secretion system (T2SS), protein F; The original family covered both the regions found ...
221-321 4.50e-03

Type II secretion system (T2SS), protein F; The original family covered both the regions found by the current model. The splitting of the family has allowed the related FlaJ_arch (archaeal FlaJ family) to be merged with it. Proteins with this domain in form a platform for the machiney of the Type II secretion system, as well as the Type 4 pili and the archaeal flagella. This domain seems to show some similarity to PF00664 but this may just be due to similarities in the TM helices (personal obs: C Yeats).


Pssm-ID: 425708 [Multi-domain]  Cd Length: 119  Bit Score: 36.54  E-value: 4.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1816261990 221 WLFTLSTLMKSGIQLSQAMNDMLETpGSSPWLKERLNSIKAQLNLGKGIGEALDDSGYRFPAQTIIEDLRIYSTLPGFDA 300
Cdd:pfam00482   1 FLRQLATLLRAGLPLVEALEILAEE-AENGPLREELRRIAERVREGGSLSEALARTPSSVFPPLLVALIAAGESGGNLAE 79
                          90       100
                  ....*....|....*....|.
gi 1816261990 301 RLHLIAEEWLAEGMETIKTQA 321
Cdd:pfam00482  80 VLERLADYLEEERELRRKIKA 100
 
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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