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Conserved domains on  [gi|1618853144|dbj|GDV91130|]
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cell envelope integrity inner membrane protein TolA [Escherichia coli]

Protein Classification

cell envelope integrity protein TolA( domain architecture ID 11484310)

cell envelope integrity protein TolA is part of the Tol-Pal system that plays a role in outer membrane invagination during cell division and is important for maintaining outer membrane integrity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1-399 5.53e-102

cell envelope integrity inner membrane protein TolA; Provisional


:

Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 307.50  E-value: 5.53e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144   1 MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGDGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQ 80
Cdd:PRK09510    1 MSKATEQNDKLKRAIIISVVLHIILFALLIWSSFDENIEASGGGGGGSVIDAVMVDPGAVVEQYNRQQQQQKSAKRAEEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  81 RKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAADAKKKAEAEAAKAAAEA 160
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 161 QKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADK 240
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 241 KAAAEKAAADKKAAAAKAAAEkaaaakaaaeaddIFGELSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAG 320
Cdd:PRK09510  241 AAAAKAAEKAAAAKAAAEVDD-------------LFGGLDSGKNAPKTGGGAKGNGAQGAGAGNGKKGGASGADIDQYAG 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1618853144 321 QIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFKP 399
Cdd:PRK09510  308 QIKSAIQSKFYDASSYAGKTCTLRIKLAPDGTLLDIKKEGGDPALCQAALAAAKTAKIPKPPSQEVYEKFKNAPLDFKP 386
 
Name Accession Description Interval E-value
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1-399 5.53e-102

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 307.50  E-value: 5.53e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144   1 MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGDGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQ 80
Cdd:PRK09510    1 MSKATEQNDKLKRAIIISVVLHIILFALLIWSSFDENIEASGGGGGGSVIDAVMVDPGAVVEQYNRQQQQQKSAKRAEEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  81 RKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAADAKKKAEAEAAKAAAEA 160
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 161 QKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADK 240
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 241 KAAAEKAAADKKAAAAKAAAEkaaaakaaaeaddIFGELSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAG 320
Cdd:PRK09510  241 AAAAKAAEKAAAAKAAAEVDD-------------LFGGLDSGKNAPKTGGGAKGNGAQGAGAGNGKKGGASGADIDQYAG 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1618853144 321 QIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFKP 399
Cdd:PRK09510  308 QIKSAIQSKFYDASSYAGKTCTLRIKLAPDGTLLDIKKEGGDPALCQAALAAAKTAKIPKPPSQEVYEKFKNAPLDFKP 386
TolA pfam06519
TolA C-terminal; This family consists of several bacterial TolA proteins as well as two ...
 305-397 8.63e-40

TolA C-terminal; This family consists of several bacterial TolA proteins as well as two eukaryotic proteins of unknown function. Tol proteins are involved in the translocation of group A colicins. Colicins are bacterial protein toxins, which are active against Escherichia coli and other related species (See pfam01024). TolA is anchored to the cytoplasmic membrane by a single membrane spanning segment near the N-terminus, leaving most of the protein exposed to the periplasm.


Pssm-ID: 399492 [Multi-domain]  Cd Length: 94  Bit Score: 136.79  E-value: 8.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 305 TKNNGASGADINNYAGQIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAA-LAAAKLAKIPKPPS 383
Cdd:pfam06519   1 AAGSGASGAEVDRYAGQIKQAIQSRFLKDDSFAGKTCRVRIKLAPDGTLISVKVEGGDPALCQAAkAAVAKTAKIPKPPS 80

                          90
                  ....*....|....
gi 1618853144 384 QAVYEVFKNAPLDF 397
Cdd:pfam06519  81 QDVYEKFKNINLDF 94
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 12-399 9.65e-39

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 141.91  E-value: 9.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  12 KRAIIISAVLHVILFAALIWSSFDENIEASAGGGdGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQRKMKEQQAAEE 91
Cdd:TIGR02794   1 RRAFLLSLLLHILLLGLLILGSLYHSVKPEPGGG-AEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  92 LREKQAAEQERLKQLeKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAA-DAKKKAEAEAAKAAAEAQKKAEAAAAA 170
Cdd:TIGR02794  80 AEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeAKAKAEAEAERKAKEEAAKQAEEEAKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 171 LKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADKKAAAEKAAAd 250
Cdd:TIGR02794 159 KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDI- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 251 kkaaaakaaaekaaaakaaaeaddifGELSSGKNAPKTGGGAKgnnaspagsgntknnGASGADINNYAGQIKSAIESKF 330
Cdd:TIGR02794 238 --------------------------FGLASGSNAEKQGGARG---------------AAAGSEVDKYAAIIQQAIQQNL 276

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 331 YDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALA-AAKLAKIPKPPSQAVYEVFKNAPLDFKP 399
Cdd:TIGR02794 277 YDDPSFRGKTCRLRIRLAPDGTLLSVTKSSGDPALCQAALAaVAKAAKLPMPPSDPVYEEFKNINLTFKP 346
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-128 8.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 8.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1618853144  61 VEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAE 128
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 59-129 4.91e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.71  E-value: 4.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1618853144  59 AVVEQYkrMQSQESSAK---RSDEQRKMKEQQAAEELREKQAAEQERlkQLEKERLAAQEQKKQAEEAAKQAEL 129
Cdd:cd16269   170 EVLQEF--LQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQER--KLLEEQQRELEQKLEDQERSYEEHL 239
 
Name Accession Description Interval E-value
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 1-399 5.53e-102

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 307.50  E-value: 5.53e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144   1 MSKATEQNDKLKRAIIISAVLHVILFAALIWSSFDENIEASAGGGDGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQ 80
Cdd:PRK09510    1 MSKATEQNDKLKRAIIISVVLHIILFALLIWSSFDENIEASGGGGGGSVIDAVMVDPGAVVEQYNRQQQQQKSAKRAEEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  81 RKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAADAKKKAEAEAAKAAAEA 160
Cdd:PRK09510   81 RKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAALKQKQAEEAAAKAAAAAKAKAEAEAKRAAAAA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 161 QKKAEAAAAALKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADK 240
Cdd:PRK09510  161 KKAAAEAKKKAEAEAAKKAAAEAKKKAEAEAAAKAAAEAKKKAEAEAKKKAAAEAKKKAAAEAKAAAAKAAAEAKAAAEK 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 241 KAAAEKAAADKKAAAAKAAAEkaaaakaaaeaddIFGELSSGKNAPKTGGGAKGNNASPAGSGNTKNNGASGADINNYAG 320
Cdd:PRK09510  241 AAAAKAAEKAAAAKAAAEVDD-------------LFGGLDSGKNAPKTGGGAKGNGAQGAGAGNGKKGGASGADIDQYAG 307

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1618853144 321 QIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALAAAKLAKIPKPPSQAVYEVFKNAPLDFKP 399
Cdd:PRK09510  308 QIKSAIQSKFYDASSYAGKTCTLRIKLAPDGTLLDIKKEGGDPALCQAALAAAKTAKIPKPPSQEVYEKFKNAPLDFKP 386
TolA pfam06519
TolA C-terminal; This family consists of several bacterial TolA proteins as well as two ...
 305-397 8.63e-40

TolA C-terminal; This family consists of several bacterial TolA proteins as well as two eukaryotic proteins of unknown function. Tol proteins are involved in the translocation of group A colicins. Colicins are bacterial protein toxins, which are active against Escherichia coli and other related species (See pfam01024). TolA is anchored to the cytoplasmic membrane by a single membrane spanning segment near the N-terminus, leaving most of the protein exposed to the periplasm.


Pssm-ID: 399492 [Multi-domain]  Cd Length: 94  Bit Score: 136.79  E-value: 8.63e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 305 TKNNGASGADINNYAGQIKSAIESKFYDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAA-LAAAKLAKIPKPPS 383
Cdd:pfam06519   1 AAGSGASGAEVDRYAGQIKQAIQSRFLKDDSFAGKTCRVRIKLAPDGTLISVKVEGGDPALCQAAkAAVAKTAKIPKPPS 80

                          90
                  ....*....|....
gi 1618853144 384 QAVYEVFKNAPLDF 397
Cdd:pfam06519  81 QDVYEKFKNINLDF 94
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 12-399 9.65e-39

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 141.91  E-value: 9.65e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  12 KRAIIISAVLHVILFAALIWSSFDENIEASAGGGdGSSIDAVMVDSGAVVEQYKRMQSQESSAKRSDEQRKMKEQQAAEE 91
Cdd:TIGR02794   1 RRAFLLSLLLHILLLGLLILGSLYHSVKPEPGGG-AEIIQAVLVDPGAVAQQANRIQQQKKPAAKKEQERQKKLEQQAEE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  92 LREKQAAEQERLKQLeKERLAAQEQKKQAEEAAKQAELKQKQAEEAAAKAAA-DAKKKAEAEAAKAAAEAQKKAEAAAAA 170
Cdd:TIGR02794  80 AEKQRAAEQARQKEL-EQRAAAEKAAKQAEQAAKQAEEKQKQAEEAKAKQAAeAKAKAEAEAERKAKEEAAKQAEEEAKA 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 171 LKKKAEAAEAAAAEARKKAATEAAEKAKAEAEKKAAAEKAAADKKAAAEKAAADKKAAEKAAAEKAAADKKAAAEKAAAd 250
Cdd:TIGR02794 159 KAAAEAKKKAEEAKKKAEAEAKAKAEAEAKAKAEEAKAKAEAAKAKAAAEAAAKAEAEAAAAAAAEAERKADEAELGDI- 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 251 kkaaaakaaaekaaaakaaaeaddifGELSSGKNAPKTGGGAKgnnaspagsgntknnGASGADINNYAGQIKSAIESKF 330
Cdd:TIGR02794 238 --------------------------FGLASGSNAEKQGGARG---------------AAAGSEVDKYAAIIQQAIQQNL 276

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144 331 YDASSYAGKTCTLRIKLAPDGMLLDIKPEGGDPALCQAALA-AAKLAKIPKPPSQAVYEVFKNAPLDFKP 399
Cdd:TIGR02794 277 YDDPSFRGKTCRLRIRLAPDGTLLSVTKSSGDPALCQAALAaVAKAAKLPMPPSDPVYEEFKNINLTFKP 346
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 80-128 6.24e-04

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.02  E-value: 6.24e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1618853144  80 QRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAE 128
Cdd:pfam05672  20 RRQAREQREREEQERLEKEEEERLRKEELRRRAEEERARREEEARRLEE 68
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 61-128 8.35e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 8.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1618853144  61 VEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAE 128
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAE 364
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 68-129 1.20e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.20e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1618853144  68 QSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAEL 129
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 62-128 1.41e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 1.41e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1618853144  62 EQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAE 128
Cdd:COG1196   368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELE 434
CCDC47 pfam07946
PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of ...
 76-127 2.27e-03

PAT complex subunit CCDC47; This family represents CCDC47 proteins which are a component of the PAT complex, an endoplasmic reticulum (ER)-resident membrane multiprotein complex that facilitates multi-pass membrane proteins insertion into membranes. The PAT complex, formed by CCDC47 and Asterix proteins, acts as an intramembrane chaperone by directly interacting with nascent transmembrane domains (TMDs), releasing its substrates upon correct folding, and is needed for optimal biogenesis of multi-pass membrane proteins. CCDC47 is required to maintain the stability of Asterix. CCDC47 is associated with various membrane-associated processes and is component of a ribosome-associated ER translocon complex involved in multi-pass membrane protein transport into the ER membrane and biogenesis. It is also involved in the regulation of calcium ion homeostasis in the ER, being also required for proper protein degradation via the ERAD (ER-associated degradation) pathway.


Pssm-ID: 462322  Cd Length: 323  Bit Score: 39.86  E-value: 2.27e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1618853144  76 RSDEQ---RKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAE-EAAKQA 127
Cdd:pfam07946 266 REEEIekiKKAAEEERAEEAQEKKEEAKKKEREEKLAKLSPEEQRKYEEkERKKEQ 321
Radial_spoke_3 pfam06098
Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) ...
 50-126 3.40e-03

Radial spoke protein 3; This family consists of several radial spoke protein 3 (RSP3) sequences. Eukaryotic cilia and flagella present in diverse types of cells perform motile, sensory, and developmental functions in organizms from protists to humans. They are centred by precisely organized, microtubule-based structures, the axonemes. The axoneme consists of two central singlet microtubules, called the central pair, and nine outer doublet microtubules. These structures are well-conserved during evolution. The outer doublet microtubules, each composed of A and B sub-fibres, are connected to each other by nexin links, while the central pair is held at the centre of the axoneme by radial spokes. The radial spokes are T-shaped structures extending from the A-tubule of each outer doublet microtubule to the centre of the axoneme. Radial spoke protein 3 (RSP3), is present at the proximal end of the spoke stalk and helps in anchoring the radial spoke to the outer doublet. It is thought that radial spokes regulate the activity of inner arm dynein through protein phosphorylation and dephosphorylation.


Pssm-ID: 461827  Cd Length: 286  Bit Score: 39.16  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  50 IDAVMVdsGAVVEQYKRMQSQEssakrsDEQRKMKEQQAA-EELREKQAAEQERL------KQLEKERLAAQ--EQKKQA 120
Cdd:pfam06098 133 ILEVLV--GKTLEQALLEVLEE------EELANLREQQRAfEELRNAELAEVQRLeeqerrLREEKERRIAQqrEALKKE 204


                  ....*.
gi 1618853144 121 EEAAKQ 126
Cdd:pfam06098 205 KETAEK 210
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 61-129 3.61e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 39.72  E-value: 3.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1618853144  61 VEQYKRMQSQESSAKRSDEQRKMKEQQAAEELR-EKQA---AEQERL---KQLEKERLaAQEQKKQAEEAAKQAEL 129
Cdd:pfam17380 296 MEQERLRQEKEEKAREVERRRKLEEAEKARQAEmDRQAaiyAEQERMameRERELERI-RQEERKRELERIRQEEI 370
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 75-128 3.93e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 37.19  E-value: 3.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1618853144  75 KRSDEQRKMKEQQAAEELREKQAAEQER---LKQLEKER--LAAQEQKKQAEEAAKQAE 128
Cdd:pfam17675  33 KKLEKETPEELEELEKELEKLEKEEEELlqeLEELEKEReeLDAELEALEEELEALDEE 91
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 62-126 4.11e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.16  E-value: 4.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1618853144  62 EQYKRMQSQESSAKRSDE-QRKMKEQQAAEELREKQAAEQERLKQL-EKERLAAQEQKKQAEEAAKQ 126
Cdd:pfam15709 426 EEFRRKLQELQRKKQQEEaERAEAEKQRQKELEMQLAEEQKRLMEMaEEERLEYQRQKQEAEEKARL 492
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 60-127 4.25e-03

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 39.55  E-value: 4.25e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1618853144   60 VVEQYKRMQSQESSAKRSDEQRKMKEQQAAEeLREKQAAEQERLKQLEKERLAA-QEQKKQAEEAAKQA 127
Cdd:PRK11448   158 LELQAREKAQSQALAEAQQQELVALEGLAAE-LEEKQQELEAQLEQLQEKAAETsQERKQKRKEITDQA 225
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 63-129 4.85e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 39.16  E-value: 4.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  63 QYKRMQSQESSAKRSDEQRKMKEQQAAEE---------------LREKQAAEQERLKQLEKERLAAQEQKKQA-EEAAKQ 126
Cdd:pfam15709 436 QRKKQQEEAERAEAEKQRQKELEMQLAEEqkrlmemaeeerleyQRQKQEAEEKARLEAEERRQKEEEAARLAlEEAMKQ 515


                  ...
gi 1618853144 127 AEL 129
Cdd:pfam15709 516 AQE 518
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 59-129 4.91e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 38.71  E-value: 4.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1618853144  59 AVVEQYkrMQSQESSAK---RSDEQRKMKEQQAAEELREKQAAEQERlkQLEKERLAAQEQKKQAEEAAKQAEL 129
Cdd:cd16269   170 EVLQEF--LQSKEAEAEailQADQALTEKEKEIEAERAKAEAAEQER--KLLEEQQRELEQKLEDQERSYEEHL 239
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 62-128 5.29e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 38.78  E-value: 5.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  62 EQYKRMQSQESSAKRSDEQRKMKEQQAAEELR-EKQAAEQERLKQLEKER------LAAQE----------------QKK 118
Cdd:pfam15709 359 EQRRLQQEQLERAEKMREELELEQQRRFEEIRlRKQRLEEERQRQEEEERkqrlqlQAAQErarqqqeefrrklqelQRK 438

                          90
                  ....*....|
gi 1618853144 119 QAEEAAKQAE 128
Cdd:pfam15709 439 KQQEEAERAE 448
CCDC34 pfam13904
Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several ...
 73-129 5.35e-03

Coiled-coil domain-containing protein 3; This family is found in eukaryotes; it has several conserved tryptophan residues. The function is not known.


Pssm-ID: 464032 [Multi-domain]  Cd Length: 221  Bit Score: 38.15  E-value: 5.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1618853144  73 SAKRsdEQRKmKEQQAAEELREKQAAEQERLKQLEKERL------AAQEQKKQAEEAAKQAEL 129
Cdd:pfam13904  62 AAKQ--RQRQ-KELQAQKEEREKEEQEAELRKRLAKEKYqewlqrKARQQTKKREESHKQKAA 121
bZIP_2 pfam07716
Basic region leucine zipper;
65-109 7.56e-03

Basic region leucine zipper;


Pssm-ID: 462244 [Multi-domain]  Cd Length: 51  Bit Score: 34.50  E-value: 7.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1618853144  65 KRMQSQESsAKRSDEQRKMKEQQAAEE---LREKQAAEQERLKQLEKE 109
Cdd:pfam07716   5 RRRKNNEA-AKRSREKKKQKEEELEERvkeLERENAQLRQKVEQLEKE 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 59-129 8.84e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 8.84e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1618853144  59 AVVEQYKRMQSQESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAEL 129
Cdd:COG1196   253 AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 66-126 9.01e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 36.56  E-value: 9.01e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1618853144  66 RMQSQESSAKRSDEQRKMKEQQ---AAEELREKQAAEQERLKQLEKERLAAqeQKKQAEEAAKQ 126
Cdd:pfam05672  56 RARREEEARRLEEERRREEEERqrkAEEEAEEREQREQEEQERLQKQKEEA--EAKAREEAERQ 117
PTZ00121 PTZ00121
MAEBL; Provisional
 71-129 9.52e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 9.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1618853144   71 ESSAKRSDEQRKMKEQQAAEELREK--QAAEQERLKQLEKERLAAQEQKKQAEEAAKQAEL 129
Cdd:PTZ00121  1428 EEKKKADEAKKKAEEAKKADEAKKKaeEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEA 1488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 70-129 9.72e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.38  E-value: 9.72e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1618853144  70 QESSAKRSDEQRKMKEQQAAEELREKQAAEQERLKQLEKERLAAQEQKKQAEEAAKQAEL 129
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452
 
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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