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Conserved domains on  [gi|529016888|ref|WP_020924934|]
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MULTISPECIES: TIGR03752 family integrating conjugative element protein [Pseudomonadota]

Protein Classification

TIGR03752 family integrating conjugative element protein( domain architecture ID 11498765)

TIGR03752 family integrating conjugative element protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
conj_TIGR03752 TIGR03752
integrating conjugative element protein, PFL_4705 family; Members of this protein family are ...
 2-462 0e+00

integrating conjugative element protein, PFL_4705 family; Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida toluene catabolic TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition. [Mobile and extrachromosomal element functions, Plasmid functions]


:

Pssm-ID: 274765 [Multi-domain]  Cd Length: 472  Bit Score: 690.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888    2 RSNGLLKWLMIPVAILVLFAGIRLFSGGGGTAPPVADNGAQLTPEEMKALGIEGDTPRDTVATLVAQVKQLRTELQTALS 81
Cdd:TIGR03752   1 KSNKLLKVLVIPVILVVVLIGIKSFSGSGSPEPTSDTALAELSPEELKALGIEGDTPADTLRTLVAEVKELRKRLAKLIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   82 DNKSQREENQRLRQRENSIDQRINSALESERSNLRRDQEQAASARQQTEGLLADLQRRL-DSIGGRGGGHADLPVGLGLQ 160
Cdd:TIGR03752  81 ENEALKAENERLQKREQSIDQQIQQAVQSETQELTKEIEQLKSERQQLQGLIDQLQRRLaGVLTGPSGGGSDLPVGLGLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  161 GGDEAGME--GGVRWVEPDDAKPAEgRNGGRGASGGMSFPTSFGPAQSTLETTAETVANAG---ARAAGVKNAKPVYTVP 235
Cdd:TIGR03752 161 PGGGAQFEggGGVVWVEPQDALPTD-RNGNSGAPSKFSFPTSFDNALDRGKKALTRVTKGApsqSANSKEKKARPVYTIP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  236 TNSTLMGSVAMTALIGRVPIDGTVNDPYPFKVLVGPDNLTANGIDIPDVAGAVFSGTASGDWTLSCVRGQVRSITFVFND 315
Cdd:TIGR03752 240 ENSTLMGSVAMTALIGRVPIDGTVTDPYPFKVLIGPDNLTANGIELPDVAGAVVSGTASGDWTLSCVRGQVRSLTFVFND 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  316 GTIRTIPEDREGNQQNNQQ----RDGLGWISDPHGIPCVSGERRSNAQQYLGSQALITAAGAGVASLIESGSGRMSYVGS 391
Cdd:TIGR03752 320 GTIRTVPRPRNNSQTNGGDsgksNGGLGWISDPYGIPCISGERRTNAPQYLGTQALITAAGAGAAGLALAQSQNTTTVNA 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529016888  392 DGSI--GTVGITGQEAVGQILAGGVRDMSAWVNKLYGQAFAAVYVQPGAKVAVHLEKPLAIDFDPEGRKVDHR 462
Cdd:TIGR03752 400 GGGVtsGVTGDSGNYALGQALSGGVDEVADWVNKRYGQSFDAVYVPPGAQVAVHIDQELAIDYEPKGRKVDYG 472
 
Name Accession Description Interval E-value
conj_TIGR03752 TIGR03752
integrating conjugative element protein, PFL_4705 family; Members of this protein family are ...
 2-462 0e+00

integrating conjugative element protein, PFL_4705 family; Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida toluene catabolic TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274765 [Multi-domain]  Cd Length: 472  Bit Score: 690.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888    2 RSNGLLKWLMIPVAILVLFAGIRLFSGGGGTAPPVADNGAQLTPEEMKALGIEGDTPRDTVATLVAQVKQLRTELQTALS 81
Cdd:TIGR03752   1 KSNKLLKVLVIPVILVVVLIGIKSFSGSGSPEPTSDTALAELSPEELKALGIEGDTPADTLRTLVAEVKELRKRLAKLIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   82 DNKSQREENQRLRQRENSIDQRINSALESERSNLRRDQEQAASARQQTEGLLADLQRRL-DSIGGRGGGHADLPVGLGLQ 160
Cdd:TIGR03752  81 ENEALKAENERLQKREQSIDQQIQQAVQSETQELTKEIEQLKSERQQLQGLIDQLQRRLaGVLTGPSGGGSDLPVGLGLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  161 GGDEAGME--GGVRWVEPDDAKPAEgRNGGRGASGGMSFPTSFGPAQSTLETTAETVANAG---ARAAGVKNAKPVYTVP 235
Cdd:TIGR03752 161 PGGGAQFEggGGVVWVEPQDALPTD-RNGNSGAPSKFSFPTSFDNALDRGKKALTRVTKGApsqSANSKEKKARPVYTIP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  236 TNSTLMGSVAMTALIGRVPIDGTVNDPYPFKVLVGPDNLTANGIDIPDVAGAVFSGTASGDWTLSCVRGQVRSITFVFND 315
Cdd:TIGR03752 240 ENSTLMGSVAMTALIGRVPIDGTVTDPYPFKVLIGPDNLTANGIELPDVAGAVVSGTASGDWTLSCVRGQVRSLTFVFND 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  316 GTIRTIPEDREGNQQNNQQ----RDGLGWISDPHGIPCVSGERRSNAQQYLGSQALITAAGAGVASLIESGSGRMSYVGS 391
Cdd:TIGR03752 320 GTIRTVPRPRNNSQTNGGDsgksNGGLGWISDPYGIPCISGERRTNAPQYLGTQALITAAGAGAAGLALAQSQNTTTVNA 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529016888  392 DGSI--GTVGITGQEAVGQILAGGVRDMSAWVNKLYGQAFAAVYVQPGAKVAVHLEKPLAIDFDPEGRKVDHR 462
Cdd:TIGR03752 400 GGGVtsGVTGDSGNYALGQALSGGVDEVADWVNKRYGQSFDAVYVPPGAQVAVHIDQELAIDYEPKGRKVDYG 472
TraB cd16430
TraB is a homolog of VirB10 which forms part of core complex in Type IV secretion system (T4SS) ...
 233-451 7.16e-09

TraB is a homolog of VirB10 which forms part of core complex in Type IV secretion system (T4SS); This family contains TraB (VirB10 homolog) and a component of the type IV secretion system (T4SS), and similar proteins. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10, interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. TraB is localized similarly to related proteins in other systems, but unlike in other systems, Neisseria gonorrhoeae TraB does not require the presence of other T4SS components for proper localization. It has been shown to be expressed with TraK (VirB9 homolog) at low levels in wild-type cells, suggesting that gonococcal T4SS may be present in single copy per cell and the small amounts of these proteins are sufficient for DNA secretion.


Pssm-ID: 319756  Cd Length: 203  Bit Score: 55.59  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888 233 TVPTNSTLMGsVAMTALIGRVPIDGTvNDPYPFKVLVGPDNLTANGIDIpDVAGAVFSGTASGDWTLSCVRGQVRSITFV 312
Cdd:cd16430    1 YLPAGSFARA-VLLTGVDAPTGVQAQ-SNPVPVLLRIKDDAILPNGFRS-DLKGCFVLGSAYGDLSSERAYIRLESLSCI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888 313 FNDGTIRTIPedregnqqnnqqrdGLGWISDPHGIPCVSGERRSNAQQYLGsQALITAAGAGVASLIESGSGRMSYVGSD 392
Cdd:cd16430   78 RKDGKVIEVP--------------VKGYVVGEDGKAGIRGRVVSKQGQLLA-RALLAGFLSGLGQAFQQAATTTSTTSGL 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529016888 393 GSigTVGITGQEAVGQILAGGVRD----MSAWVNKLYGQAFAAVYVQPGAKVAVHLEKPLAID 451
Cdd:cd16430  143 GT--TQTIDPGDALKAGAGGGASSaldkLADYYLKLAEQMFPVIEVDAGREVDVVFTEGFSLE 203
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
59-143 6.82e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 6.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  59 RDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINsALESERSNLRRDQEQAASARQQTEGLLADLQR 138
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150


                 ....*
gi 529016888 139 RLDSI 143
Cdd:COG4372  151 ELKEL 155
RNase_Y_N pfam12072
RNase Y N-terminal region;
68-145 2.79e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 44.88  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   68 QVKQLRTELQTALSD--NKSQREENqRLRQRENSIDQRINS------ALESERSNLRRDQEQAASARQQTEGLLADLQRR 139
Cdd:pfam12072  61 EIHKLRAEAERELKErrNELQRQER-RLLQKEETLDRKDESlekkeeSLEKKEKELEAQQQQLEEKEEELEELIEEQRQE 139


                  ....*.
gi 529016888  140 LDSIGG 145
Cdd:pfam12072 140 LERISG 145
PRK12704 PRK12704
phosphodiesterase; Provisional
 68-145 4.70e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  68 QVKQLRTELQTALSD--NKSQREENqRLRQRENSIDQRINSA------LESERSNLRRDQEQAASARQQTEGLLADLQRR 139
Cdd:PRK12704  65 EIHKLRNEFEKELRErrNELQKLEK-RLLQKEENLDRKLELLekreeeLEKKEKELEQKQQELEKKEEELEELIEEQLQE 143


                 ....*.
gi 529016888 140 LDSIGG 145
Cdd:PRK12704 144 LERISG 149
 
Name Accession Description Interval E-value
conj_TIGR03752 TIGR03752
integrating conjugative element protein, PFL_4705 family; Members of this protein family are ...
 2-462 0e+00

integrating conjugative element protein, PFL_4705 family; Members of this protein family are found occasionally on plasmids such as the Pseudomonas putida toluene catabolic TOL plasmid pWWO_p085. Usually, however, they are found on the bacterial main chromosome in regions flanked by markers of conjugative transfer and/or transposition. [Mobile and extrachromosomal element functions, Plasmid functions]


Pssm-ID: 274765 [Multi-domain]  Cd Length: 472  Bit Score: 690.61  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888    2 RSNGLLKWLMIPVAILVLFAGIRLFSGGGGTAPPVADNGAQLTPEEMKALGIEGDTPRDTVATLVAQVKQLRTELQTALS 81
Cdd:TIGR03752   1 KSNKLLKVLVIPVILVVVLIGIKSFSGSGSPEPTSDTALAELSPEELKALGIEGDTPADTLRTLVAEVKELRKRLAKLIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   82 DNKSQREENQRLRQRENSIDQRINSALESERSNLRRDQEQAASARQQTEGLLADLQRRL-DSIGGRGGGHADLPVGLGLQ 160
Cdd:TIGR03752  81 ENEALKAENERLQKREQSIDQQIQQAVQSETQELTKEIEQLKSERQQLQGLIDQLQRRLaGVLTGPSGGGSDLPVGLGLD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  161 GGDEAGME--GGVRWVEPDDAKPAEgRNGGRGASGGMSFPTSFGPAQSTLETTAETVANAG---ARAAGVKNAKPVYTVP 235
Cdd:TIGR03752 161 PGGGAQFEggGGVVWVEPQDALPTD-RNGNSGAPSKFSFPTSFDNALDRGKKALTRVTKGApsqSANSKEKKARPVYTIP 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  236 TNSTLMGSVAMTALIGRVPIDGTVNDPYPFKVLVGPDNLTANGIDIPDVAGAVFSGTASGDWTLSCVRGQVRSITFVFND 315
Cdd:TIGR03752 240 ENSTLMGSVAMTALIGRVPIDGTVTDPYPFKVLIGPDNLTANGIELPDVAGAVVSGTASGDWTLSCVRGQVRSLTFVFND 319

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  316 GTIRTIPEDREGNQQNNQQ----RDGLGWISDPHGIPCVSGERRSNAQQYLGSQALITAAGAGVASLIESGSGRMSYVGS 391
Cdd:TIGR03752 320 GTIRTVPRPRNNSQTNGGDsgksNGGLGWISDPYGIPCISGERRTNAPQYLGTQALITAAGAGAAGLALAQSQNTTTVNA 399

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529016888  392 DGSI--GTVGITGQEAVGQILAGGVRDMSAWVNKLYGQAFAAVYVQPGAKVAVHLEKPLAIDFDPEGRKVDHR 462
Cdd:TIGR03752 400 GGGVtsGVTGDSGNYALGQALSGGVDEVADWVNKRYGQSFDAVYVPPGAQVAVHIDQELAIDYEPKGRKVDYG 472
TraB cd16430
TraB is a homolog of VirB10 which forms part of core complex in Type IV secretion system (T4SS) ...
 233-451 7.16e-09

TraB is a homolog of VirB10 which forms part of core complex in Type IV secretion system (T4SS); This family contains TraB (VirB10 homolog) and a component of the type IV secretion system (T4SS), and similar proteins. T4S system is employed by pathogenic bacteria to export virulence DNAs and/or proteins directly from the bacterial cytoplasm into the host cell. It forms a large multiprotein complex consisting of 12 proteins termed VirB1-11 and VirD4. VirB10, interacts with VirB7 and VirB9, forming the membrane-spanning 'core complex' (CC), around which all other components assemble. The CC is inserted in both the outer and inner membranes, playing a fundamental role as a scaffold for the rest of the T4SS components and actively participating in T4S substrate transfer through the bacterial envelope via conformational changes regulating channel opening and closing. TraB is localized similarly to related proteins in other systems, but unlike in other systems, Neisseria gonorrhoeae TraB does not require the presence of other T4SS components for proper localization. It has been shown to be expressed with TraK (VirB9 homolog) at low levels in wild-type cells, suggesting that gonococcal T4SS may be present in single copy per cell and the small amounts of these proteins are sufficient for DNA secretion.


Pssm-ID: 319756  Cd Length: 203  Bit Score: 55.59  E-value: 7.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888 233 TVPTNSTLMGsVAMTALIGRVPIDGTvNDPYPFKVLVGPDNLTANGIDIpDVAGAVFSGTASGDWTLSCVRGQVRSITFV 312
Cdd:cd16430    1 YLPAGSFARA-VLLTGVDAPTGVQAQ-SNPVPVLLRIKDDAILPNGFRS-DLKGCFVLGSAYGDLSSERAYIRLESLSCI 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888 313 FNDGTIRTIPedregnqqnnqqrdGLGWISDPHGIPCVSGERRSNAQQYLGsQALITAAGAGVASLIESGSGRMSYVGSD 392
Cdd:cd16430   78 RKDGKVIEVP--------------VKGYVVGEDGKAGIRGRVVSKQGQLLA-RALLAGFLSGLGQAFQQAATTTSTTSGL 142

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 529016888 393 GSigTVGITGQEAVGQILAGGVRD----MSAWVNKLYGQAFAAVYVQPGAKVAVHLEKPLAID 451
Cdd:cd16430  143 GT--TQTIDPGDALKAGAGGGASSaldkLADYYLKLAEQMFPVIEVDAGREVDVVFTEGFSLE 203
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
59-143 6.82e-07

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.44  E-value: 6.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  59 RDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINsALESERSNLRRDQEQAASARQQTEGLLADLQR 138
Cdd:COG4372   72 RSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELE-ELQKERQDLEQQRKQLEAQIAELQSEIAEREE 150


                 ....*
gi 529016888 139 RLDSI 143
Cdd:COG4372  151 ELKEL 155
RNase_Y_N pfam12072
RNase Y N-terminal region;
68-145 2.79e-05

RNase Y N-terminal region;


Pssm-ID: 463456 [Multi-domain]  Cd Length: 201  Bit Score: 44.88  E-value: 2.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   68 QVKQLRTELQTALSD--NKSQREENqRLRQRENSIDQRINS------ALESERSNLRRDQEQAASARQQTEGLLADLQRR 139
Cdd:pfam12072  61 EIHKLRAEAERELKErrNELQRQER-RLLQKEETLDRKDESlekkeeSLEKKEKELEAQQQQLEEKEEELEELIEEQRQE 139


                  ....*.
gi 529016888  140 LDSIGG 145
Cdd:pfam12072 140 LERISG 145
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
62-138 7.24e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.89  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  62 VATLVAQVKQLRTEL---QTALSDNKSQREE-NQRLRQRENSIdQRINSALESERSNLRRDQEQAASARQQTEGLLADLQ 137
Cdd:COG4372   47 LEQLREELEQAREELeqlEEELEQARSELEQlEEELEELNEQL-QAAQAELAQAQEELESLQEEAEELQEELEELQKERQ 125


                 .
gi 529016888 138 R 138
Cdd:COG4372  126 D 126
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 60-108 8.37e-05

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 40.71  E-value: 8.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 529016888   60 DTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINSAL 108
Cdd:pfam06005  18 DTIALLQMENEELKEENEELKEEANELEEENQQLKQERNQWQERIRGLL 66
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 59-139 3.30e-04

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: 42.83  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  59 RDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINSALESERSNLRRDQEQAASARQQTEGLLADLQR 138
Cdd:COG4942  159 LAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238


                 .
gi 529016888 139 R 139
Cdd:COG4942  239 A 239
ADIP pfam11559
Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at ...
 62-120 3.43e-04

Afadin- and alpha -actinin-Binding; This family is found in mammals where it is localized at cell-cell adherens junctions, and in Sch. pombe and other fungi where it anchors spindle-pole bodies to spindle microtubules. It is a coiled-coil structure, and in pombe, it is required for anchoring the minus end of spindle microtubules to the centrosome equivalent, the spindle-pole body. The name ADIP derives from the family being composed of Afadin- and alpha -Actinin-Binding Proteins localized at Cell-Cell Adherens Junctions.


Pssm-ID: 463295 [Multi-domain]  Cd Length: 151  Bit Score: 40.76  E-value: 3.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 529016888   62 VATLVAQVKQLRTELQTALSDNKSQREENQRLRqreNSIDQRINSALESERsnlRRDQE 120
Cdd:pfam11559  89 LALLQAKERQLEKKLKTLEQKLKNEKEELQRLK---NALQQIKTQFAHEVK---KRDRE 141
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 37-130 4.56e-04

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 41.90  E-value: 4.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   37 ADNGAQLTPEEMKALGIEgdtprdtVATLVAQVKQLRTELQ--TALSD-NKSQREEnqrLRQRENSIDQRINsALESERS 113
Cdd:pfam12795 140 APPGEPLSEAQRWALQAE-------LAALKAQIDMLEQELLsnNNRQDlLKARRDL---LTLRIQRLEQQLQ-ALQELLN 208

                          90
                  ....*....|....*..
gi 529016888  114 NLRRDQEQAASARQQTE 130
Cdd:pfam12795 209 EKRLQEAEQAVAQTEQL 225
PRK12704 PRK12704
phosphodiesterase; Provisional
 68-145 4.70e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.46  E-value: 4.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  68 QVKQLRTELQTALSD--NKSQREENqRLRQRENSIDQRINSA------LESERSNLRRDQEQAASARQQTEGLLADLQRR 139
Cdd:PRK12704  65 EIHKLRNEFEKELRErrNELQKLEK-RLLQKEENLDRKLELLekreeeLEKKEKELEQKQQELEKKEEELEELIEEQLQE 143


                 ....*.
gi 529016888 140 LDSIGG 145
Cdd:PRK12704 144 LERISG 149
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
62-147 7.17e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 7.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   62 VATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQrinsaLESERSNLRRDQEQAASARQQTEGLLADLQRRLD 141
Cdd:COG4913   663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEE-----LEEELDELKGEIGRLEKELEQAEEELDELQDRLE 737


                  ....*.
gi 529016888  142 SIGGRG 147
Cdd:COG4913   738 AAEDLA 743
ZapB pfam06005
Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is ...
 68-137 7.34e-04

Cell division protein ZapB; ZapB is a non-essential, abundant cell division factor that is required for proper Z-ring formation.


Pssm-ID: 428718 [Multi-domain]  Cd Length: 71  Bit Score: 38.02  E-value: 7.34e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   68 QVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINsALESERSNLRRDQEQaasARQQTEGLLADLQ 137
Cdd:pfam06005   5 LLEQLETKIQAAVDTIALLQMENEELKEENEELKEEAN-ELEEENQQLKQERNQ---WQERIRGLLGKLD 70
CALCOCO1 pfam07888
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ...
 66-153 1.11e-03

Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are similar to the coiled-coil transcriptional coactivator protein coexpressed by Mus musculus (CoCoA/CALCOCO1). This protein binds to a highly conserved N-terminal domain of p160 coactivators, such as GRIP1, and thus enhances transcriptional activation by a number of nuclear receptors. CALCOCO1 has a central coiled-coil region with three leucine zipper motifs, which is required for its interaction with GRIP1 and may regulate the autonomous transcriptional activation activity of the C-terminal region.


Pssm-ID: 462303 [Multi-domain]  Cd Length: 488  Bit Score: 41.42  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   66 VAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINSA------LESERSNLRRDQEQAASARQQTEGLLADLQrr 139
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAhrkeaeNEALLEELRSLQERLNASERKVEGLGEELS-- 261

                          90
                  ....*....|....
gi 529016888  140 lDSIGGRGGGHADL 153
Cdd:pfam07888 262 -SMAAQRDRTQAEL 274
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
59-146 1.23e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.44  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   59 RDTVATLVAQVKQLR--TELQTALSDNKSQREENQRLR---------QRENSIDQRInSALESERSNLRRDQEQAASARQ 127
Cdd:COG4913   241 HEALEDAREQIELLEpiRELAERYAAARERLAELEYLRaalrlwfaqRRLELLEAEL-EELRAELARLEAELERLEARLD 319

                          90
                  ....*....|....*....
gi 529016888  128 QTEGLLADLQRRLDSIGGR 146
Cdd:COG4913   320 ALREELDELEAQIRGNGGD 338
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 59-142 1.25e-03

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 41.26  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   59 RDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRInSALESERSNLRRDQEQAASARQQteglLADLQR 138
Cdd:pfam05557 103 REVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKA-SEAEQLRQNLEKQQSSLAEAEQR----IKELEF 177


                  ....
gi 529016888  139 RLDS 142
Cdd:pfam05557 178 EIQS 181
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 47-143 1.30e-03

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 40.90  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   47 EMKALGIEGDTPRDTVATLVAQVKQLRTELQ----TALSDNKSQREENQRLRQR---ENSIDQRINSALESERSNLRRDQ 119
Cdd:pfam09787  48 ELEELRQERDLLREEIQKLRGQIQQLRTELQeleaQQQEEAESSREQLQELEEQlatERSARREAEAELERLQEELRYLE 127

                          90       100
                  ....*....|....*....|....
gi 529016888  120 EQAASARQQTEGLLADLQRRLDSI 143
Cdd:pfam09787 128 EELRRSKATLQSRIKDREAEIEKL 151
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
67-143 1.82e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.91  E-value: 1.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  67 AQVKQLRTELQTAlsdnKSQREENQRLRQRENSIDQRINsALESERSNLRRDQEQAASA---------RQQTEGLLADLQ 137
Cdd:COG4717   71 KELKELEEELKEA----EEKEEEYAELQEELEELEEELE-ELEAELEELREELEKLEKLlqllplyqeLEALEAELAELP 145


                 ....*.
gi 529016888 138 RRLDSI 143
Cdd:COG4717  146 ERLEEL 151
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 69-137 2.17e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 40.29  E-value: 2.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 529016888   69 VKQLRTELQTA--LSDNKSQREENQRLRQRENSIDQRINSALESERSN-LRRDQEQAASARQQTEGLLADLQ 137
Cdd:pfam13868   8 LRELNSKLLAAkcNKERDAQIAEKKRIKAEEKEEERRLDEMMEEERERaLEEEEEKEEERKEERKRYRQELE 79
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-141 2.61e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.31  E-value: 2.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  59 RDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRInSALESERSNLRRDQEQAASARQQTEGLLADLQR 138
Cdd:COG1196  252 EAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL-ARLEQDIARLEERRRELEERLEELEEELAELEE 330


                 ...
gi 529016888 139 RLD 141
Cdd:COG1196  331 ELE 333
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
46-145 3.58e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  46 EEMKALGIEGDTPRDTVATLVAQVKQLRtELQTALSDNKSQREENQRLRQRENSIDQRINSALESERSNLRRDQEqaasa 125
Cdd:COG4717  323 ELLAALGLPPDLSPEELLELLDRIEELQ-ELLREAEELEEELQLEELEQEIAALLAEAGVEDEEELRAALEQAEE----- 396

                         90       100
                 ....*....|....*....|
gi 529016888 126 RQQTEGLLADLQRRLDSIGG 145
Cdd:COG4717  397 YQELKEELEELEEQLEELLG 416
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 46-141 3.96e-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: 40.04  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888    46 EEMKALGIEGDTPRDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRINSA------LESERSNLRRDQ 119
Cdd:TIGR02168  691 EKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLskelteLEAEIEELEERL 770

                           90       100
                   ....*....|....*....|..
gi 529016888   120 EQAASARQQTEGLLADLQRRLD 141
Cdd:TIGR02168  771 EEAEEELAEAEAEIEELEAQIE 792
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 59-146 4.44e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 39.28  E-value: 4.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888   59 RDTVATLVAQVKQLRTELQTALSDNKSQREENQRLRQRENSIDQRInSALESERSNLRRD---------------QEQAA 123
Cdd:pfam19220 110 RIELRDKTAQAEALERQLAAETEQNRALEEENKALREEAQAAEKAL-QRAEGELATARERlalleqenrrlqalsEEQAA 188

                          90       100
                  ....*....|....*....|....*....
gi 529016888  124 -----SAR-QQTEGLLADLQRRLDSIGGR 146
Cdd:pfam19220 189 elaelTRRlAELETQLDATRARLRALEGQ 217
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
46-143 5.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 529016888  46 EEMKALGIEGDTPRDTVATLVAQVKQLRTELQtALSDNKSQREENQRLRQRE-NSIDQRINSaLESERSNLRRDQEQ--A 122
Cdd:COG4372  101 EELESLQEEAEELQEELEELQKERQDLEQQRK-QLEAQIAELQSEIAEREEElKELEEQLES-LQEELAALEQELQAlsE 178

                         90       100
                 ....*....|....*....|.
gi 529016888 123 ASARQQTEGLLADLQRRLDSI 143
Cdd:COG4372  179 AEAEQALDELLKEANRNAEKE 199
 
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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