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Conserved domains on  [gi|672088871|ref|XP_008771830|]
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NF-kappa-B essential modulator isoform X5 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UBAN super family cl46991
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
252-338 2.30e-19

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


The actual alignment was detected with superfamily member cd09803:

Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 82.01  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 252 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQ 331
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80

                 ....*..
gi 672088871 332 REFNKLK 338
Cdd:cd09803   81 RENQELK 87
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
44-110 5.26e-17

NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.


:

Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 74.83  E-value: 5.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672088871   44 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 110
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
zf_C2H2_10 super family cl39752
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
387-412 1.18e-11

C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.


The actual alignment was detected with superfamily member pfam18414:

Pssm-ID: 436483  Cd Length: 26  Bit Score: 58.76  E-value: 1.18e-11
                          10        20
                  ....*....|....*....|....*.
gi 672088871  387 PDFCCPKCQYQAPDMDTLQIHVMECI 412
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-284 8.83e-10

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 129 KKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRM 205
Cdd:COG1196  350 EE-ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEE 428
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088871 206 QNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 284
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
252-338 2.30e-19

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 82.01  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 252 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQ 331
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80

                 ....*..
gi 672088871 332 REFNKLK 338
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
253-338 1.22e-17

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 77.72  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  253 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQR 332
Cdd:pfam16516  15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94

                  ....*.
gi 672088871  333 EFNKLK 338
Cdd:pfam16516  95 QNQQLK 100
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
44-110 5.26e-17

NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.


Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 74.83  E-value: 5.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672088871   44 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 110
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
387-412 1.18e-11

C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.


Pssm-ID: 436483  Cd Length: 26  Bit Score: 58.76  E-value: 1.18e-11
                          10        20
                  ....*....|....*....|....*.
gi 672088871  387 PDFCCPKCQYQAPDMDTLQIHVMECI 412
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-284 8.83e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 129 KKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRM 205
Cdd:COG1196  350 EE-ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEE 428
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088871 206 QNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 284
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-315 2.23e-08

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: 56.22  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   129 KkcqqvqmaedkasvkAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSvqvdQLRMQNQ 208
Cdd:TIGR02168  760 E---------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   209 SVEAALRMERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIV 288
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEE-------------------QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          250       260
                   ....*....|....*....|....*..
gi 672088871   289 METVPVLKAQADIYKADFQAERHAREK 315
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELES 908
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
135-234 5.34e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 45.71  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  135 QMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVEA 212
Cdd:PRK11448  146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQA 225
                          90       100
                  ....*....|....*....|....
gi 672088871  213 ALRMErqAASEEKRKL--AQLQAA 234
Cdd:PRK11448  226 AKRLE--LSEEETRILidQQLRKA 247
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
87-288 3.43e-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: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   87 REEKEFLMCKFQEARKLVERLSLEKLDLRRQR----EQALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLE 162
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELE 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  163 AATKERQTLEGRIRAVSEQVRQ---LESEREVLQQQHSVQVDQLRMQNQSV--EAALRMERQAASEEKRKLAQLQAAYHQ 237
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAEQEEArqREVRRLEEERAREMERVRLEEQERQQQ 461
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672088871  238 ---LFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELID---KLKEEAEQHKIV 288
Cdd:pfam17380 462 verLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEErkqAMIEEERKRKLL 518
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
252-338 2.30e-19

polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) is a regulatory subunit of the kinase complex IKK, which is involved in the activation of NF-kappaB via phosporylation of inhibitory IkappaBs. This mechanism requires the binding of NEMO to ubiquinated substrates. Binding is achieved via the UBAN motif (ubiquitin binding in ABIN and NEMO), which is described in this model. This region of NEMO has also been named CoZi (for coiled-coil 2 and leucine zipper). ABINs (A20-binding inhibitors of NF-kappaB) are sensors for ubiquitin that are involved in regulation of apoptosis, ABIN-1 is presumed to inhibit signalling via the NF-kappaB route. The UBAN motif is also found in optineurin, the product of a gene associated with glaucoma, which has been characterized as a negative regulator of NF-kappaB as well.


Pssm-ID: 197361 [Multi-domain]  Cd Length: 87  Bit Score: 82.01  E-value: 2.30e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 252 MQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQ 331
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80

                 ....*..
gi 672088871 332 REFNKLK 338
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
253-338 1.22e-17

Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a leucine-zipper domain associated with the CC2 coiled-coil region of NF-kappa-B essential modulator, NEMO. It plays a regulatory role, along with the very C-terminal zinc-finger; it contains a ubiquitin-binding domain (UBD) and represents one region that contributes to NEMO oligomerization. NEMO itself is an integral part of the IkappaB kinase complex and serves as a molecular switch via which the NF-kappaB signalling pathway is regulated.


Pssm-ID: 465155 [Multi-domain]  Cd Length: 100  Bit Score: 77.72  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  253 QLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQR 332
Cdd:pfam16516  15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94

                  ....*.
gi 672088871  333 EFNKLK 338
Cdd:pfam16516  95 QNQQLK 100
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
44-110 5.26e-17

NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK complex along with the catalytic IKKalpha and beta kinases. The IKK complex phosphorylates IkappaB targeting it for degradation which results in the release of NF-kappaB which initiates the inflammatory response, cell proliferation or cell differentiation. NEMO activates the IKK complex's activity by associating with the unphosphorylated IKK kinase C termini.The core domain of NEMO is a dimer which binds to two fragments of IKK.


Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 74.83  E-value: 5.26e-17
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 672088871   44 EQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLE 110
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
387-412 1.18e-11

C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin (optic neuropathy inducing protein) and NF-kappa-B essential modulator (NEMO) furthermore, it can be found in kinase TBK1, a member of the IKK (inhibitor of nuclear factor kappa-B kinase) family. The C-terminal region, which carries the zinc finger domain, constitutes the regulatory domain of NEMO, as it receives the activation signal from upstream molecules, and subsequently transmits this activation to the kinases bound to the N-terminal domain. The isolated NEMO zinc finger is thought to be involved in protein-protein rather than protein-DNA interaction.


Pssm-ID: 436483  Cd Length: 26  Bit Score: 58.76  E-value: 1.18e-11
                          10        20
                  ....*....|....*....|....*.
gi 672088871  387 PDFCCPKCQYQAPDMDTLQIHVMECI 412
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
49-284 8.83e-10

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 60.72  E-value: 8.83e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 129 KKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQ---QHSVQVDQLRM 205
Cdd:COG1196  350 EE-ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLErleRLEEELEELEE 428
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088871 206 QNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 284
Cdd:COG1196  429 ALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAA--LLEAALAELLEELAEAAARLLLLLEAEADYEG 505
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-273 1.56e-09

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 59.93  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   98 QEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQVQMAEDK-ASVKAQVTSLL---GELQESQSRLEAATKERQTLEG 173
Cdd:COG4913   627 AEAEERLEALEAELDALQERREALQRLAEYSWDEIDVASAEREiAELEAELERLDassDDLAALEEQLEELEAELEELEE 706
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  174 RIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmQ 253
Cdd:COG4913   707 ELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE--------R 774
                         170       180
                  ....*....|....*....|
gi 672088871  254 LEDLRQQLQQAEEALVAKQE 273
Cdd:COG4913   775 IDALRARLNRAEEELERAMR 794
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
113-319 1.18e-08

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: 56.31  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 113 DLRRQREQALEDLEHlkkcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVL 192
Cdd:COG4942   20 DAAAEAEAELEQLQQ----EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 193 QQQHSVQVDQLRMQnqsVEAALRMERQAASEEkrklaqlqaayhqLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQ 272
Cdd:COG4942   96 RAELEAQKEELAEL---LRALYRLGRQPPLAL-------------LLSPEDFLDAVRRLQYLKYLAPARREQAEELRADL 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 672088871 273 ELIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 319
Cdd:COG4942  160 AELAALRAELEAERAELEA---LLAELEEERAALEALKAERQKLLAR 203
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-315 2.23e-08

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: 56.22  E-value: 2.23e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   129 KkcqqvqmaedkasvkAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSvqvdQLRMQNQ 208
Cdd:TIGR02168  760 E---------------AEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT----LLNEEAA 820
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   209 SVEAALRMERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIV 288
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEE-------------------QIEELSEDIESLAAEIEELEELIEELESELEALLNE 881
                          250       260
                   ....*....|....*....|....*..
gi 672088871   289 METVPVLKAQADIYKADFQAERHAREK 315
Cdd:TIGR02168  882 RASLEEALALLRSELEELSEELRELES 908
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
96-286 4.03e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.33  E-value: 4.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  96 KFQEARKLVERLSLEKLDLRRQREQALEDLEHLKkcqqvqmaEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRI 175
Cdd:COG1196  219 KEELKELEAELLLLKLRELEAELEELEAELEELE--------AELEELEAELAELEAELEELRLELEELELELEEAQAEE 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 176 RAVSEQVRQLESEREVLQQQHSvQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLE 255
Cdd:COG1196  291 YELLAELARLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLE 369
                        170       180       190
                 ....*....|....*....|....*....|.
gi 672088871 256 DLRQQLQQAEEALVAKQELIDKLKEEAEQHK 286
Cdd:COG1196  370 AEAELAEAEEELEELAEELLEALRAAAELAA 400
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
49-309 1.00e-07

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 54.30  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEarklverLSLEKLDLRRQREQALEDLEHL 128
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREY---EGYE-------LLKEKEALERQKEAIERQLASL 249
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   129 KkcqqvqmaEDKASVKAQVTSLLGELQESQSRLEAATKERQTL-EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR-MQ 206
Cdd:TIGR02169  250 E--------EELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEdAE 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   207 NQSVEAALRMERQAASEE--KRKLAQLQAAYHQLFQDYDShikssKGMQLEDLRQQLQQAE-------EALVAKQELIDK 277
Cdd:TIGR02169  322 ERLAKLEAEIDKLLAEIEelEREIEEERKRRDKLTEEYAE-----LKEELEDLRAELEEVDkefaetrDELKDYREKLEK 396
                          250       260       270
                   ....*....|....*....|....*....|..
gi 672088871   278 LKEEAEQHKIVMETVPVLKAQADIYKADFQAE 309
Cdd:TIGR02169  397 LKREINELKRELDRLQEELQRLSEELADLNAA 428
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
97-284 1.82e-07

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 53.38  E-value: 1.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   97 FQEARKLVE------RLSLEKLDLRRQREqALEDLEhlKKCQQVQMAEDKASVKAQVTSLLgELQESQSRLEAATKERQT 170
Cdd:COG4913   224 FEAADALVEhfddleRAHEALEDAREQIE-LLEPIR--ELAERYAAARERLAELEYLRAAL-RLWFAQRRLELLEAELEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  171 LEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSK 250
Cdd:COG4913   300 LRAELARLEAELERLEARLDALREELDELEAQIRGNGGDRLEQLEREIERLERELEERERRRARLEALLAALGLPLPASA 379
                         170       180       190
                  ....*....|....*....|....*....|....
gi 672088871  251 GmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 284
Cdd:COG4913   380 E-EFAALRAEAAALLEALEEELEALEEALAEAEA 412
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
155-319 1.79e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  155 QESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV--QVDQLRMQNQSVEAA------LRMERQAASEEKR 226
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  227 KLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADF 306
Cdd:COG4913   686 DLAALEEQLEELEAELEELEE-----ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFAAALG 760
                         170
                  ....*....|....
gi 672088871  307 QA-ERHAREKLVER 319
Cdd:COG4913   761 DAvERELRENLEER 774
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
55-277 2.87e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 49.63  E-value: 2.87e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  55 LEENQELR-DAIRQSNQMLRERCEELLHfQVSQREEKeflMCKFQEARKLV-----ERLSLEKL-DLRRQREQALEDLEH 127
Cdd:COG3206  162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 128 LKKcQQVQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRM 205
Cdd:COG3206  238 AEA-RLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILA 316
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088871 206 Q-------NQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDshIKSSKGMQLEDLRQQLQQAEEALVAKQELIDK 277
Cdd:COG3206  317 SleaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVE--VARELYESLLQRLEEARLAEALTVGNVRVIDP 393
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-283 3.08e-06

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: 49.67  E-value: 3.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKL-------DLRRQREQA 121
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerlaNLERQLEEL 321
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   122 LEDLEHLKKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvd 201
Cdd:TIGR02168  322 EAQLEELES-KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQ------ 394
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   202 qlrmqnqsvEAALRMERQAASEEKRklaqlqaayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQELIDKLKEE 281
Cdd:TIGR02168  395 ---------IASLNNEIERLEARLE--------------------------RLEDRRERLQQEIEELLKKLEEAELKELQ 439

                   ..
gi 672088871   282 AE 283
Cdd:TIGR02168  440 AE 441
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
132-319 2.15e-05

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 46.36  E-value: 2.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 132 QQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVe 211
Cdd:COG3883   17 QIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERARAL- 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 212 aalrmerQAASEEKRKLAQL-----------QAAYHQLFQDYDSHIKSskgmQLEDLRQQLQQAEEALVAKQELIDKLKE 280
Cdd:COG3883   96 -------YRSGGSVSYLDVLlgsesfsdfldRLSALSKIADADADLLE----ELKADKAELEAKKAELEAKLAELEALKA 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 672088871 281 EAEQHKIVMETvpvLKAQADIYKADFQAERHAREKLVER 319
Cdd:COG3883  165 ELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAE 200
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
98-319 3.33e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.21  E-value: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    98 QEARKLVERLS-LEKLDlrRQREQALEDLEHLKkcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEG--- 173
Cdd:TIGR02169  153 VERRKIIDEIAgVAEFD--RKKEKALEELEEVE--ENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYEGyel 228
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   174 --RIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKG 251
Cdd:TIGR02169  229 lkEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLER 308
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 672088871   252 mQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQadiYKADFQAERHAREKLVER 319
Cdd:TIGR02169  309 -SIAEKERELEDAEERLAKLEAEIDKLLAEIEELEREIEEERKRRDK---LTEEYAELKEELEDLRAE 372
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
92-319 3.62e-05

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: 45.53  E-value: 3.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  92 FLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAatkerqtL 171
Cdd:COG4942   10 LLALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKK-EEKALLKQLAALERRIAALARRIRALEQELAA-------L 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 172 EGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKg 251
Cdd:COG4942   82 EAELAELEKEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEELRADLA- 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672088871 252 mQLEDLRQQLQQA----EEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVER 319
Cdd:COG4942  161 -ELAALRAELEAEraelEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIAR 231
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
51-283 4.66e-05

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 45.83  E-value: 4.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    51 LQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLrrqrEQALEDLEHLKK 130
Cdd:TIGR02169  714 ASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKL----EEALNDLEARLS 789
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   131 CQQVQMAEDKAS-VKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQS 209
Cdd:TIGR02169  790 HSRIPEIQAELSkLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEK----EIENLNGKKEE 865
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672088871   210 VEAALRmerqaasEEKRKLAQLQAAYHQLFQDYDSHIKsskgmQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 283
Cdd:TIGR02169  866 LEEELE-------ELEAALRDLESRLGDLKKERDELEA-----QLRELERKIEELEAQIEKKRKRLSELKAKLE 927
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
135-234 5.34e-05

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 45.71  E-value: 5.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  135 QMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQ--NQSVEA 212
Cdd:PRK11448  146 ALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQA 225
                          90       100
                  ....*....|....*....|....
gi 672088871  213 ALRMErqAASEEKRKL--AQLQAA 234
Cdd:PRK11448  226 AKRLE--LSEEETRILidQQLRKA 247
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-204 1.27e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEkeflmckfQEARKLVERLSLEKLDLRRQREQALEDLE 126
Cdd:COG4913   298 EELRAELARLEAELERLEARLDALREELDELEaqIRGNGGDRL--------EQLEREIERLERELEERERRRARLEALLA 369
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  127 HLKkcqqVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV---QVDQL 203
Cdd:COG4913   370 ALG----LPLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNipaRLLAL 445

                  .
gi 672088871  204 R 204
Cdd:COG4913   446 R 446
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
45-233 2.37e-04

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: 43.51  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    45 QGTPETLQRCLEENQELRDAIRQSNQMLRERCEELlhfqvsqREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALED 124
Cdd:TIGR02168  315 ERQLEELEAQLEELESKLDELAEELAELEEKLEEL-------KEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   125 LEHLKKCQQVQMAEdKASVKAQVTSLLGELQESQSRLEAATKERQtlEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLR 204
Cdd:TIGR02168  388 VAQLELQIASLNNE-IERLEARLERLEDRRERLQQEIEELLKKLE--EAELKELQAELEELEEELEELQEELERLEEALE 464
                          170       180
                   ....*....|....*....|....*....
gi 672088871   205 MQNQSVEAALRMERQAASEEKRKLAQLQA 233
Cdd:TIGR02168  465 ELREELEEAEQALDAAERELAQLQARLDS 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
48-284 3.07e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.07e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    48 PETLQRCLEENQELRDAIRQSNQMLRERC----EELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQaLE 123
Cdd:TIGR02169  261 SELEKRLEEIEQLLEELNKKIKDLGEEEQlrvkEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAE-IE 339
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   124 DLEHlkkcQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqVDQL 203
Cdd:TIGR02169  340 ELER----EIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRE----LDRL 411
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   204 RMQNQSVEAALRMERQAASEEKRKLAQLQAAyhqlfqdydshiKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAE 283
Cdd:TIGR02169  412 QEELQRLSEELADLNAAIAGIEAKINELEEE------------KEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYD 479

                   .
gi 672088871   284 Q 284
Cdd:TIGR02169  480 R 480
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
70-325 3.29e-04

chromosome segregation protein SMC, primarily archaeal 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. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.29e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    70 QMLRERCEEL---LHFQVSQREEKEFLM----CKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQvQMAEDKAS 142
Cdd:TIGR02169  677 QRLRERLEGLkreLSSLQSELRRIENRLdelsQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLS-SLEQEIEN 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   143 VKAQVTSLLGELQESQSRLEAATKERQTLEGRIRavSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAAS 222
Cdd:TIGR02169  756 VKSELKELEARIEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEK 833
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   223 EEKRKLAQLQAAYHQlfqdydshiKSSKGMQLEDLRQQL----QQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQ 298
Cdd:TIGR02169  834 EIQELQEQRIDLKEQ---------IKSIEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKERDELEAQLRELERK 904
                          250       260
                   ....*....|....*....|....*..
gi 672088871   299 ADIYKADFQAERHAREKLVERKELLQE 325
Cdd:TIGR02169  905 IEELEAQIEKKRKRLSELKAKLEALEE 931
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
103-291 3.53e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.83  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 103 LVERLSLEKLDLRRQREQALE-DLEHLKKC-QQVQMAEDKasvKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSE 180
Cdd:COG4717   47 LLERLEKEADELFKPQGRKPElNLKELKELeEELKEAEEK---EEEYAELQEELEELEEELEELEAELEELREELEKLEK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 181 QVRQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLE 255
Cdd:COG4717  124 LLQLLPLYQELEALEAELaelpeRLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAE-ELE 202
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 672088871 256 DLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMET 291
Cdd:COG4717  203 ELQQRLAELEEELEEAQEELEELEEELEQLENELEA 238
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
80-319 5.55e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.33  E-value: 5.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  80 LHFQVSQREEKEfLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKkcqqvQMAEDKASVKAQVTSLLGELQESQS 159
Cdd:PRK02224 192 LKAQIEEKEEKD-LHERLNGLESELAELDEEIERYEEQREQARETRDEAD-----EVLEEHEERREELETLEAEIEDLRE 265
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 160 RLEAATKERQTLEGRIRAVSEQVRQLESEREVL----------QQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLA 229
Cdd:PRK02224 266 TIAETEREREELAEEVRDLRERLEELEEERDDLlaeaglddadAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAE 345
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 230 QLQAAYHQLFQDYDshiksSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAE 309
Cdd:PRK02224 346 SLREDADDLEERAE-----ELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDAPVDLGNAEDFLEELREE 420
                        250
                 ....*....|.
gi 672088871 310 R-HAREKLVER 319
Cdd:PRK02224 421 RdELREREAEL 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
114-338 5.72e-04

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: 42.35  E-value: 5.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   114 LRRQREQAL------EDLEHLkkcqqvqmaeDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLES 187
Cdd:TIGR02168  205 LERQAEKAErykelkAELREL----------ELALLVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRL 274
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   188 EREVLQQQhsVQVDQLRMQNQSVEAAlRMERQAAsEEKRKLAQLQAAYHQLfQDYDSHIKSSKGMQLEDLRQQLQQAEEA 267
Cdd:TIGR02168  275 EVSELEEE--IEELQKELYALANEIS-RLEQQKQ-ILRERLANLERQLEEL-EAQLEELESKLDELAEELAELEEKLEEL 349
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672088871   268 LVAKQELIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERHAREKLVERKELLQEQLEQLQREFNKLK 338
Cdd:TIGR02168  350 KEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQ 420
PRK09039 PRK09039
peptidoglycan -binding protein;
140-287 6.29e-04

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 41.49  E-value: 6.29e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 140 KASVKAQVTSLLGELQESQSrLEAATKerQTLEGRIRAVSEQVRQLESEREVLQQQH---SVQVDQLRMQNQSVEAALRM 216
Cdd:PRK09039  51 KDSALDRLNSQIAELADLLS-LERQGN--QDLQDSVANLRASLSAAEAERSRLQALLaelAGAGAAAEGRAGELAQELDS 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 672088871 217 ERQAASEEKRKLAQLQAayhqlfqdydshiksskgmQLEDLRQQLQQAEEALVAKQElidklKEEAEQHKI 287
Cdd:PRK09039 128 EKQVSARALAQVELLNQ-------------------QIAALRRQLAALEAALDASEK-----RDRESQAKI 174
PTZ00121 PTZ00121
MAEBL; Provisional
56-290 1.05e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   56 EENQELRDAiRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKCQQVQ 135
Cdd:PTZ00121 1575 DKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELK 1653
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  136 MAEDKASVKAQvtSLLGELQESQSRLEAATKErqtlEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQsVEAALR 215
Cdd:PTZ00121 1654 KAEEENKIKAA--EEAKKAEEDKKKAEEAKKA----EEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEE-LKKAEE 1726
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672088871  216 MERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQElidkLKEEAEQHKIVME 290
Cdd:PTZ00121 1727 ENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEE----LDEEDEKRRMEVD 1797
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
144-296 1.14e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 41.00  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 144 KAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRMQNQSVEAALRMERQAASE 223
Cdd:COG2433  384 ELIEKELPEEEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEA----ELEEKDERIERLERELSEARSEERR 459
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672088871 224 EKRKlaqlqaayhqlfqdyDSHIKSSKGMqLEDLRQQLQQAEEALvakQELIDKLKEEAEQHKIVM--ETVPVLK 296
Cdd:COG2433  460 EIRK---------------DREISRLDRE-IERLERELEEERERI---EELKRKLERLKELWKLEHsgELVPVKV 515
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
49-234 1.17e-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: 41.20  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    49 ETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQ-------REQA 121
Cdd:TIGR02168  326 EELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQiaslnneIERL 405
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   122 LEDLEHLKKCQQVQMAEDKASVKAQVTSllgELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVD 201
Cdd:TIGR02168  406 EARLERLEDRRERLQQEIEELLKKLEEA---ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAER 482
                          170       180       190
                   ....*....|....*....|....*....|...
gi 672088871   202 QLRMQNQSVEAALRMERQAASEEKRKLAQLQAA 234
Cdd:TIGR02168  483 ELAQLQARLDSLERLQENLEGFSEGVKALLKNQ 515
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
41-304 1.22e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 41.10  E-value: 1.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  41 LPSEQGTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREE-KEFLMCKFQEARKLVERLSLEKLDLRRQRE 119
Cdd:COG5185  245 LEDLAQTSDKLEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENtKEKIAEYTKSIDIKKATESLEEQLAAAEAE 324
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 120 QALEDlehlkkcqqvQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEG--RIRAVSEQVR----QLESEREVLQ 193
Cdd:COG5185  325 QELEE----------SKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDsfkdTIESTKESLD 394
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 194 QQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKS-SKGMQLEDLRQQLQQAEEALVAKQ 272
Cdd:COG5185  395 EIPQNQRGYAQEILATLEDTLKAADRQIEELQRQIEQATSSNEEVSKLLNELISElNKVMREADEESQSRLEEAYDEINR 474
                        250       260       270
                 ....*....|....*....|....*....|..
gi 672088871 273 ELIDKLKEEAEQHKIVMETVPVLKAQADIYKA 304
Cdd:COG5185  475 SVRSKKEDLNEELTQIESRVSTLKATLEKLRA 506
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
52-274 1.24e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 41.11  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    52 QRCLEENQELRDAIRQSNQMLRERCEELLhfQVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHLKKC 131
Cdd:TIGR00618  307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   132 QQ-VQMAEDKASVKAQVTSllgELQESQSRLEAATKERQTLEGRIrAVSEQVRQLESEREVLQQQHSVQVDQLRMQNqsv 210
Cdd:TIGR00618  385 QQqKTTLTQKLQSLCKELD---ILQREQATIDTRTSAFRDLQGQL-AHAKKQQELQQRYAELCAAAITCTAQCEKLE--- 457
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 672088871   211 EAALRMERQAASEEKRKLAQLQAAyhqlfqdydsHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 274
Cdd:TIGR00618  458 KIHLQESAQSLKEREQQLQTKEQI----------HLQETRKKAVVLARLLELQEEPCPLCGSCI 511
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
49-266 1.79e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 1.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   49 ETLQRCLEENQELRDAIRQSNQMLRErceelLHFQVSQREEKeflmckFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:COG4913   664 ASAEREIAELEAELERLDASSDDLAA-----LEEQLEELEAE------LEELEEELDELKGEIGRLEKELEQAEEELDEL 732
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  129 KkcQQVQMAEDKASVkaQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHsVQVDQLRMQNQ 208
Cdd:COG4913   733 Q--DRLEAAEDLARL--ELRALLEERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAF-NREWPAETADL 807
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 672088871  209 SVEAAlrmerqAASEEKRKLAQLQA----AYHQLFQDYdshIKSSKGMQLEDLRQQLQQAEE 266
Cdd:COG4913   808 DADLE------SLPEYLALLDRLEEdglpEYEERFKEL---LNENSIEFVADLLSKLRRAIR 860
PRK12704 PRK12704
phosphodiesterase; Provisional
217-286 1.85e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.53  E-value: 1.85e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 217 ERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGmQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 286
Cdd:PRK12704  48 KKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRN-ELQKLEKRLLQKEENLDRKLELLEKREEELEKKE 116
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
49-229 2.39e-03

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: 39.75  E-value: 2.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  49 ETLQRCLEENQELRDAIRQSNQMLRERCEELL--HFQVSQREEKEFLMcKFQEARKLVERLSLEKLDLRRQREQALEDLE 126
Cdd:COG4942   79 AALEAELAELEKEIAELRAELEAQKEELAELLraLYRLGRQPPLALLL-SPEDFLDAVRRLQYLKYLAPARREQAEELRA 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 127 HLKKCQQVQMAEDKAsvKAQVTSLLGELQESQSRLEAATKERQT----LEGRIRAVSEQVRQLESEREVLQQQHSvqvdq 202
Cdd:COG4942  158 DLAELAALRAELEAE--RAELEALLAELEEERAALEALKAERQKllarLEKELAELAAELAELQQEAEELEALIA----- 230
                        170       180
                 ....*....|....*....|....*..
gi 672088871 203 lRMQNQSVEAALRMERQAASEEKRKLA 229
Cdd:COG4942  231 -RLEAEAAAAAERTPAAGFAALKGKLP 256
PRK12704 PRK12704
phosphodiesterase; Provisional
154-289 2.69e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 39.76  E-value: 2.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 154 LQESQSRLEAATKERqtlegrIRAVSEQVRQL--ESEREVLQQQHSVQVDQLRMQNQsvEAALRMERQAASEEKRKLAQL 231
Cdd:PRK12704  44 LEEAKKEAEAIKKEA------LLEAKEEIHKLrnEFEKELRERRNELQKLEKRLLQK--EENLDRKLELLEKREEELEKK 115
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 672088871 232 QAAYHQLFQDYDSHIKSSKGMQLEdLRQQLQQ-----AEEAlvaKQELIDKLKEEAEQHKIVM 289
Cdd:PRK12704 116 EKELEQKQQELEKKEEELEELIEE-QLQELERisgltAEEA---KEILLEKVEEEARHEAAVL 174
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
46-284 2.74e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 444066 [Multi-domain]  Cd Length: 594  Bit Score: 39.94  E-value: 2.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  46 GTPETLQRCLEENQELRDAIRQSNQMLRERCEELLHFQVSQREEKEFlmcKFQEARKLVERLSLEkldlrrqREQALEDL 125
Cdd:COG5185  272 ENAESSKRLNENANNLIKQFENTKEKIAEYTKSIDIKKATESLEEQL---AAAEAEQELEESKRE-------TETGIQNL 341
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 126 EHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRlEAATKERQTLEGRIRAVSEQVR-QLESEREVLQ----------Q 194
Cdd:COG5185  342 TAEIEQGQESLTENLEAIKEEIENIVGEVELSKSS-EELDSFKDTIESTKESLDEIPQnQRGYAQEILAtledtlkaadR 420
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 195 QHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQEL 274
Cdd:COG5185  421 QIEELQRQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDLNEELTQIESRVSTLKAT 500
                        250
                 ....*....|
gi 672088871 275 IDKLKEEAEQ 284
Cdd:COG5185  501 LEKLRAKLER 510
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
87-288 3.43e-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: 3.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   87 REEKEFLMCKFQEARKLVERLSLEKLDLRRQR----EQALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLE 162
Cdd:pfam17380 302 RQEKEEKAREVERRRKLEEAEKARQAEMDRQAaiyaEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELE 381
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  163 AATKERQTLEGRIRAVSEQVRQ---LESEREVLQQQHSVQVDQLRMQNQSV--EAALRMERQAASEEKRKLAQLQAAYHQ 237
Cdd:pfam17380 382 RLQMERQQKNERVRQELEAARKvkiLEEERQRKIQQQKVEMEQIRAEQEEArqREVRRLEEERAREMERVRLEEQERQQQ 461
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 672088871  238 ---LFQDYDSHIKSSKGMQLEDLRQQLQQAEEALVAKQELID---KLKEEAEQHKIV 288
Cdd:pfam17380 462 verLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEErkqAMIEEERKRKLL 518
PRK09039 PRK09039
peptidoglycan -binding protein;
120-234 3.71e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 120 QALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLE--SER-----EVL 192
Cdd:PRK09039  63 AELADLLSLERQGNQDLQDSVANLRASLSAAEAERSRLQALLAELAGAGAAAEGRAGELAQELDSEKqvSARalaqvELL 142
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 672088871 193 QQQhsvqVDQLRMQNQSVEAALRmerqaASEEKRKLAQLQAA 234
Cdd:PRK09039 143 NQQ----IAALRRQLAALEAALD-----ASEKRDRESQAKIA 175
PTZ00121 PTZ00121
MAEBL; Provisional
59-356 3.97e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.74  E-value: 3.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   59 QELRDAIRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVErlslekldLRRQREQALEDLEHLKKCQQVQMAE 138
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--------AKKKAEEAKKADEAKKKAEEAKKKA 1499
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  139 DKASVKAQVTSLLGELQESQSRLEA-----ATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAA 213
Cdd:PTZ00121 1500 DEAKKAAEAKKKADEAKKAEEAKKAdeakkAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMA 1579
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  214 LRMERQAASEEKRKLAQLQAAYHQlfqdyDSHIKSSKGMQLEDLR---QQLQQAEEALVAKQELIDKLKEE---AEQHKI 287
Cdd:PTZ00121 1580 LRKAEEAKKAEEARIEEVMKLYEE-----EKKMKAEEAKKAEEAKikaEELKKAEEEKKKVEQLKKKEAEEkkkAEELKK 1654
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088871  288 VMETVPVLKAQadiykadfqaERHAREKLVERKELLQEQLEQLQREFNKLKVGCHESARIEDMRKRHVE 356
Cdd:PTZ00121 1655 AEEENKIKAAE----------EAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAE 1713
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
133-287 4.55e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 39.42  E-value: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 133 QVQMAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQhsvqvdqlrmQNQSVEA 212
Cdd:PRK00409 508 KKLIGEDKEKLNELIASLEELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEE----------AEKEAQQ 577
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 672088871 213 ALRMERQAASEEKRKLAQLQAAYHqlfqdydSHIKSSkgmQLEDLRQQLQQAEEALVAKqelidKLKEEAEQHKI 287
Cdd:PRK00409 578 AIKEAKKEADEIIKELRQLQKGGY-------ASVKAH---ELIEARKRLNKANEKKEKK-----KKKQKEKQEEL 637
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
51-288 4.61e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 4.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  51 LQRCLEENQELRDAIRQsnqmLRERCEELlhfqvsqREEKEFLMCKFQEARKLVE--RLSLEKLD-----LRRQREQALE 123
Cdd:PRK02224 337 AQAHNEEAESLREDADD----LEERAEEL-------REEAAELESELEEAREAVEdrREEIEELEeeieeLRERFGDAPV 405
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 124 DLEHLKKCQQvQMAEDKASVKAQVTSLLGELQESQSRLEAATKER---------QTLEG-----RIRAVSEQVRQLESER 189
Cdd:PRK02224 406 DLGNAEDFLE-ELREERDELREREAELEATLRTARERVEEAEALLeagkcpecgQPVEGsphveTIEEDRERVEELEAEL 484
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 190 EVLQQQHSVQVDQLRMQNQSVEAALRMERqaaSEEKRKLAQlqaayhQLFQDYDSHIKsSKGMQLEDLRQQLQQAEEALV 269
Cdd:PRK02224 485 EDLEEEVEEVEERLERAEDLVEAEDRIER---LEERREDLE------ELIAERRETIE-EKRERAEELRERAAELEAEAE 554
                        250
                 ....*....|....*....
gi 672088871 270 AKQELIDKLKEEAEQHKIV 288
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREE 573
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
83-272 4.66e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 39.33  E-value: 4.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871    83 QVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL----------KKCQQVQMAEDKASVKAQVTSLLG 152
Cdd:pfam15921  305 QEQARNQNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKQlvlanselteARTERDQFSQESGNLDDQLQKLLA 384
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   153 ELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESErevlqqqhsvqVDQLRMQNQSVEAALR-MERQAASEEKRKLAQL 231
Cdd:pfam15921  385 DLHKREKELSLEKEQNKRLWDRDTGNSITIDHLRRE-----------LDDRNMEVQRLEALLKaMKSECQGQMERQMAAI 453
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 672088871   232 QAAYHQLFQdydshiKSSKGMQLEDLRQQLQQAEEALVAKQ 272
Cdd:pfam15921  454 QGKNESLEK------VSSLTAQLESTKEMLRKVVEELTAKK 488
KpsE COG3524
Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];
97-295 4.85e-03

Capsule polysaccharide export protein KpsE/RkpR [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442746 [Multi-domain]  Cd Length: 370  Bit Score: 38.68  E-value: 4.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  97 FQEARKLVERLSlekldlRRQREQALEDLEhlkkcQQVQMAEDKA-----------------SVKAQVTSLLGELQESQS 159
Cdd:COG3524  160 LAESEELVNQLS------ERAREDAVRFAE-----EEVERAEERLrdareallafrnrngilDPEATAEALLQLIATLEG 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 160 RLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQqhsvQVDQLRmqnqsveaalrmERQAASEEKRKLAQLQAAYhqlf 239
Cdd:COG3524  229 QLAELEAELAALRSYLSPNSPQVRQLRRRIAALEK----QIAAER------------ARLTGASGGDSLASLLAEY---- 288
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 672088871 240 qdydshiksskgmqlEDLRQQLQQAEEALVAKQELIDKLKEEAEQHKIVMETV--PVL 295
Cdd:COG3524  289 ---------------ERLELEREFAEKAYTSALAALEQARIEAARQQRYLAVIvqPTL 331
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
156-281 4.90e-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: 38.59  E-value: 4.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  156 ESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQAAY 235
Cdd:pfam09787  44 ALTLELEELRQERDLLREEIQKLRGQIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEAELERLQEEL 123
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 672088871  236 HQLFQDYDSHIKSSKG------MQLEDLRQQL--------QQAE---------EALVAKQELIDKLKEE 281
Cdd:pfam09787 124 RYLEEELRRSKATLQSrikdreAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
22-226 5.52e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 5.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  22 EDQDMLGEESSLGKPAMLHLPSEQGTPETLQRCLEENQELRDAIRQSNQM-LRERCEELLH-FQVSQREEKEFLMCKFQE 99
Cdd:COG4717  317 EEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLEeLEQEIAALLAeAGVEDEEELRAALEQAEE 396
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 100 ARKLVERLSLEKLDLRRQREQALEDLEhlkkcqqvqmAEDKASVKAQVTSLLGELQESQSRLEAATKERQTLEGRIRAV- 178
Cdd:COG4717  397 YQELKEELEELEEQLEELLGELEELLE----------ALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLe 466
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 672088871 179 -SEQVRQLESEREVLQQQHSVQVDQlRMQNQSVEAALRMERQAASEEKR 226
Cdd:COG4717  467 eDGELAELLQELEELKAELRELAEE-WAALKLALELLEEAREEYREERL 514
PTZ00121 PTZ00121
MAEBL; Provisional
96-315 5.65e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 39.35  E-value: 5.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871   96 KFQEARKLverlSLEKLDLRRQREQALEDLEHLKKCQQVQMAEDKASVKAQVTSLLGELQESQSRLEAATK--------E 167
Cdd:PTZ00121 1099 KAEEAKKT----ETGKAEEARKAEEAKKKAEDARKAEEARKAEDARKAEEARKAEDAKRVEIARKAEDARKaeearkaeD 1174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  168 RQTLEGRIRAV----------------------SEQVRQLESEREVLQQQHSVQVDQLRMQNQSVEAALRMERQAASEEK 225
Cdd:PTZ00121 1175 AKKAEAARKAEevrkaeelrkaedarkaeaarkAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEI 1254
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  226 RKLAQLQAAYhqlFQDYDSHIKSSKGMQLEDLR--QQLQQAEEALVAKQ-ELIDKLKEEAEQHKIVMETVPvlKAQADIY 302
Cdd:PTZ00121 1255 RKFEEARMAH---FARRQAAIKAEEARKADELKkaEEKKKADEAKKAEEkKKADEAKKKAEEAKKADEAKK--KAEEAKK 1329
                         250
                  ....*....|...
gi 672088871  303 KADfQAERHAREK 315
Cdd:PTZ00121 1330 KAD-AAKKKAEEA 1341
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
65-270 5.82e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  65 IRQSNQMLRERCEELLHFQVSQREEKEFLMCKFQEARKLVERlslekldLRRQREQALEDLEHLKKCQQVQMAEDKasvK 144
Cdd:COG4717   65 KPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEE-------LEAELEELREELEKLEKLLQLLPLYQE---L 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 145 AQVTSLLGELQESQSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV----QVDQLRMQNQSVEAALRMERQA 220
Cdd:COG4717  135 EALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLateeELQDLAEELEELQQRLAELEEE 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 672088871 221 ASEEKRKLAQLQAAYHQLfqdydshiksSKGMQLEDLRQQLQQAEEALVA 270
Cdd:COG4717  215 LEEAQEELEELEEELEQL----------ENELEAAALEERLKEARLLLLI 254
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
49-284 6.51e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 38.87  E-value: 6.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  49 ETLQRCLEENQELRDAirqsnqmlrERCEEllhfqVSQREEKEFLMCKFQEARKLVERLSLEKLDLRRQREQALEDLEHL 128
Cdd:PRK02224 436 RTARERVEEAEALLEA---------GKCPE-----CGQPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 129 KkcqqvqmaedkasvkaqvtsllgELQESQSRLEAATKERQTLEGRIravSEQVRQLESEREVLQQQHSvQVDQLRMQNQ 208
Cdd:PRK02224 502 E-----------------------DLVEAEDRIERLEERREDLEELI---AERRETIEEKRERAEELRE-RAAELEAEAE 554
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 672088871 209 SVEAALRMERQAASEEKRKLAQLQAAYHQLFQDYDShiksskgmqLEDLRQQLQQAEEALVAKQELIDKLKEEAEQ 284
Cdd:PRK02224 555 EKREAAAEAEEEAEEAREEVAELNSKLAELKERIES---------LERIRTLLAAIADAEDEIERLREKREALAEL 621
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
167-286 7.74e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871  167 ERQTLEGRIRAVSEQVRQLES-EREVLQQQHsvQVDQLRmqnQSVEAALRmeRQAASEEKRKLAQLQAAYHQLFqdyDSH 245
Cdd:COG4913   219 EEPDTFEAADALVEHFDDLERaHEALEDARE--QIELLE---PIRELAER--YAAARERLAELEYLRAALRLWF---AQR 288
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 672088871  246 IKSSKGMQLEDLRQQLQQAEEALVAKQELIDKLKEEAEQHK 286
Cdd:COG4913   289 RLELLEAELEELRAELARLEAELERLEARLDALREELDELE 329
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
158-337 7.81e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 38.46  E-value: 7.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 158 QSRLEAATKERQTLEGRIRAVSEQVRQLESEREVLQQQHSV-----QVDQLRMQNQSVEAALRMERQAASEEKRKLAQLQ 232
Cdd:COG3206  167 ELRREEARKALEFLEEQLPELRKELEEAEAALEEFRQKNGLvdlseEAKLLLQQLSELESQLAEARAELAEAEARLAALR 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 672088871 233 AayhQLFQDYDSHIKSSKGMQLEDLRQQLQQAEealvakQELIDKLKEEAEQHKIVMEtvpvLKAQADIYKADFQAE--- 309
Cdd:COG3206  247 A---QLGSGPDALPELLQSPVIQQLRAQLAELE------AELAELSARYTPNHPDVIA----LRAQIAALRAQLQQEaqr 313
                        170       180       190
                 ....*....|....*....|....*....|...
gi 672088871 310 -----RHAREKLVERKELLQEQLEQLQREFNKL 337
Cdd:COG3206  314 ilaslEAELEALQAREASLQAQLAQLEARLAEL 346
 
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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