NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|153792133|ref|NP_001093327|]
View 

NF-kappa-B essential modulator isoform a [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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) ...
 258-344 2.26e-18

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: 79.32  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 258 MQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQ 337
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 153792133 338 REYSKLK 344
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 6.19e-16

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: 71.74  E-value: 6.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792133   44 EQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLE 110
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-371 9.27e-12

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: 66.88  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  55 LEENQELRDAIRQSNQI--LRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQ 132
Cdd:COG1196  218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAA 212
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 213 LRMERQAASEEKRKLAQLQVAYHQLfQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhk 292
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-- 454

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792133 293 ivmetvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPA 371
Cdd:COG1196  455 --------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
zf_C2H2_10 super family cl39752
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 393-418 1.48e-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: 58.37  E-value: 1.48e-11
                          10        20
                  ....*....|....*....|....*.
gi 153792133  393 PDFCCPKCQYQAPDMDTLQIHVMECI 418
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 258-344 2.26e-18

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: 79.32  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 258 MQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQ 337
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 153792133 338 REYSKLK 344
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 259-344 6.91e-18

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: 78.49  E-value: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  259 QLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQR 338
Cdd:pfam16516  15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94


                  ....*.
gi 153792133  339 EYSKLK 344
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 6.19e-16

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: 71.74  E-value: 6.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792133   44 EQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLE 110
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-371 9.27e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  55 LEENQELRDAIRQSNQI--LRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQ 132
Cdd:COG1196  218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAA 212
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 213 LRMERQAASEEKRKLAQLQVAYHQLfQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhk 292
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-- 454

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792133 293 ivmetvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPA 371
Cdd:COG1196  455 --------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 393-418 1.48e-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: 58.37  E-value: 1.48e-11
                          10        20
                  ....*....|....*....|....*.
gi 153792133  393 PDFCCPKCQYQAPDMDTLQIHVMECI 418
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-321 4.56e-09

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: 58.53  E-value: 4.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    87 REEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKE 166
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   167 CQALEGRARAASEQARQLESEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIK 246
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792133   247 SSVVGSErkrgmQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREK 321
Cdd:TIGR02168  839 RLEDLEE-----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 133-233 2.13e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.79  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQ--GQSVE 210
Cdd:PRK11448  145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224

                          90       100
                  ....*....|....*....|....*
gi 153792133  211 AALRMErqAASEEKRKL--AQLQVA 233
Cdd:PRK11448  225 AAKRLE--LSEEETRILidQQLRKA 247
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 146-287 3.81e-04

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: 42.05  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  146 VTSLLGELQESQSRLEAATKECQALEGraraaseQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKR 225
Cdd:pfam09787  42 STALTLELEELRQERDLLREEIQKLRG-------QIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792133  226 KLAQLQVAYHQLFQEYDNHiKSSVVGSERKRGMQLEDLKQQL--------QQAE---------EALVAKQEVIDKLKEE 287
Cdd:pfam09787 115 ELERLQEELRYLEEELRRS-KATLQSRIKDREAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 139-323 5.27e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 42.51  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  139 KASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQ 218
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESR 1616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  219 AASEEKRKLAQ-LQV----AYHQ--LFQEYDNH--------IKSSVVGSERKRGMQLEDLKQQ----LQQAEEAlVAKQE 279
Cdd:NF012221 1617 AVTKELTTLAQgLDAldsqATYAgeSGDQWRNPfagglldrVQEQLDDAKKISGKQLADAKQRhvdnQQKVKDA-VAKSE 1695

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 153792133  280 VidkLKEEAEQHKivmetvpvLKAQADIYKADFQAERQAREKLA 323
Cdd:NF012221 1696 A---GVAQGEQNQ--------ANAEQDIDDAKADAEKRKDDALA 1728
 
Name Accession Description Interval E-value
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 258-344 2.26e-18

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: 79.32  E-value: 2.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 258 MQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQ 337
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 153792133 338 REYSKLK 344
Cdd:cd09803   81 RENQELK 87
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 259-344 6.91e-18

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: 78.49  E-value: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  259 QLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQR 338
Cdd:pfam16516  15 EIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHEEKEQLAAQLEYLQR 94


                  ....*.
gi 153792133  339 EYSKLK 344
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 6.19e-16

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: 71.74  E-value: 6.19e-16
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792133   44 EQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLE 110
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 55-371 9.27e-12

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.88  E-value: 9.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  55 LEENQELRDAIRQSNQI--LRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQ 132
Cdd:COG1196  218 LKEELKELEAELLLLKLreLEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAEL 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAA 212
Cdd:COG1196  298 ARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEA 377

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 213 LRMERQAASEEKRKLAQLQVAYHQLfQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhk 292
Cdd:COG1196  378 EEELEELAEELLEALRAAAELAAQL-EELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL-- 454

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792133 293 ivmetvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQAPLPPA 371
Cdd:COG1196  455 --------EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGA 525
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 393-418 1.48e-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: 58.37  E-value: 1.48e-11
                          10        20
                  ....*....|....*....|....*.
gi 153792133  393 PDFCCPKCQYQAPDMDTLQIHVMECI 418
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 49-290 1.73e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHL 128
Cdd:COG1196  270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEA 349

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 129 KRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHsvqvDQLRMQGQS 208
Cdd:COG1196  350 EEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERL----ERLEEELEE 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 209 VEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSVvgSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEA 288
Cdd:COG1196  426 LEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA--ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY 503


                 ..
gi 153792133 289 EQ 290
Cdd:COG1196  504 EG 505
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-321 4.56e-09

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: 58.53  E-value: 4.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    87 REEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKE 166
Cdd:TIGR02168  683 EEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAE 762

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   167 CQALEGRARAASEQARQLESEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIK 246
Cdd:TIGR02168  763 IEELEERLEEAEEELAEAEAEIEELEA----QIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATER 838

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792133   247 SSVVGSErkrgmQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREK 321
Cdd:TIGR02168  839 RLEDLEE-----QIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELES 908
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-323 1.68e-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: 56.99  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHL 128
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQL 794

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   129 KRCQQQMAEDKASVKAQVTSLLGELQESQSRLE-------AATKECQALEGRARAASEQARQLESEREALQQQhsvqvdq 201
Cdd:TIGR02168  795 KEELKALREALDELRAELTLLNEEAANLRERLEslerriaATERRLEDLEEQIEELSEDIESLAAEIEELEEL------- 867

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   202 lrmqgqsvEAALRMERQAASEEKrklAQLQVAYHQLFQEYDNhiKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEV- 280
Cdd:TIGR02168  868 --------IEELESELEALLNER---ASLEEALALLRSELEE--LSEELRELESKRSELRRELEELREKLAQLELRLEGl 934

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 153792133   281 ---IDKLKEE-AEQHKIVMETVPVLKAQADIYKADFQAE-RQAREKLA 323
Cdd:TIGR02168  935 evrIDNLQERlSEEYSLTLEEAEALENKIEDDEEEARRRlKRLENKIK 982
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 49-363 3.06e-08

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: 55.84  E-value: 3.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEF----LMCKFQEARKLVERLGLEKLDLKRQKEQALRE 124
Cdd:TIGR02169  180 EEVEENIERLDLIIDEKRQQLERLRREREKAERYQALLKEKREYegyeLLKEKEALERQKEAIERQLASLEEELEKLTEE 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   125 VEHL-KRC---QQQMAEDKASVKA-------QVTSLLGELQESQSRLEAATKECqalEGRARAASEQARQLESEREALQQ 193
Cdd:TIGR02169  260 ISELeKRLeeiEQLLEELNKKIKDlgeeeqlRVKEKIGELEAEIASLERSIAEK---ERELEDAEERLAKLEAEIDKLLA 336

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   194 QHS----------VQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYD--NHIKSSVVGSERKRGMQLE 261
Cdd:TIGR02169  337 EIEelereieeerKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEklKREINELKRELDRLQEELQ 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   262 DLKQQLQQAEEALVAKQEVIDKLKEEAEQhkiVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYS 341
Cdd:TIGR02169  417 RLSEELADLNAAIAGIEAKINELEEEKED---KALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEKELSKLQRELA 493

                          330       340
                   ....*....|....*....|..
gi 153792133   342 KLKASCQESARIEDMRKRHVEV 363
Cdd:TIGR02169  494 EAEAQARASEERVRGGRAVEEV 515
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 117-382 3.14e-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: 55.16  E-value: 3.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 117 QKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHS 196
Cdd:COG4942   21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELE 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 197 VQVDQLRmqgqsveaalrmerqaaseekrklAQLQVAYHQLFQEYDNHIKSSVVGSERKRGMQ-LEDLKQQLQQAEEALV 275
Cdd:COG4942  101 AQKEELA------------------------ELLRALYRLGRQPPLALLLSPEDFLDAVRRLQyLKYLAPARREQAEELR 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 276 AKQEVIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREysKLKASCQESARIED 355
Cdd:COG4942  157 ADLAELAALRAELEAERAELEA---LLAELEEERAALEALKAERQKLLARLEKELAELAAELAE--LQQEAEELEALIAR 231

                        250       260
                 ....*....|....*....|....*..
gi 153792133 356 MRKRHVEVSQAPLPPAPAYLSSPLALP 382
Cdd:COG4942  232 LEAEAAAAAERTPAAGFAALKGKLPWP 258
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 39-322 4.27e-07

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: 52.37  E-value: 4.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    39 LHLPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERLGLEKL------ 112
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQilrerl 311

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   113 -DLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREAL 191
Cdd:TIGR02168  312 aNLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   192 QQQhsvqvdqlrmqgqsvEAALRMERQAASEEKRKLaqlqvayhqlfqeydnhikssvvgsERKRGMQLEDLKQQLQQAE 271
Cdd:TIGR02168  392 ELQ---------------IASLNNEIERLEARLERL-------------------------EDRRERLQQEIEELLKKLE 431

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 153792133   272 EAlvAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKADFQAERQAREKL 322
Cdd:TIGR02168  432 EA--ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAA 480
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
101-360 7.25e-06

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 48.37  E-value: 7.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  101 RKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAqvtslLGELQESQSRLEAATKECQALEGRARAASEQ 180
Cdd:COG4913   210 DDFVREYMLEEPDTFEAADALVEHFDDLERAHEALEDAREQIEL-----LEPIRELAERYAAARERLAELEYLRAALRLW 284

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  181 ARQLesEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQlfqeydnhikssvVGSERkrgmqL 260
Cdd:COG4913   285 FAQR--RLELLEA----ELEELRAELARLEAELERLEARLDALREELDELEAQIRG-------------NGGDR-----L 340

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  261 EDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKI-VMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQRE 339
Cdd:COG4913   341 EQLEREIERLERELEERERRRARLEALLAALGLpLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRE 420

                         250       260
                  ....*....|....*....|.
gi 153792133  340 YSKLKascqesARIEDMRKRH 360
Cdd:COG4913   421 LRELE------AEIASLERRK 435
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
98-279 1.38e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 47.60  E-value: 1.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   98 QEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDK---------ASVKAQVTSLL---GELQESQSRLEAATK 165
Cdd:COG4913   620 AELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvasaereiAELEAELERLDassDDLAALEEQLEELEA 699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  166 ECQALEGRARAASEQARQLESEREALQQqhsvQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNhi 245
Cdd:COG4913   700 ELEELEEELDELKGEIGRLEKELEQAEE----ELDELQDRLEAAEDLARLELRALLEERFAAALGDAVERELRENLEE-- 773

                         170       180       190
                  ....*....|....*....|....*....|....
gi 153792133  246 kssvvgserkrgmQLEDLKQQLQQAEEALVAKQE 279
Cdd:COG4913   774 -------------RIDALRARLNRAEEELERAMR 794
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
154-323 2.01e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  154 QESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSV--QVDQLRMQGQSVEAA------LRMERQAASEEKR 225
Cdd:COG4913   606 FDNRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREAlqRLAEYSWDEIDVASAereiaeLEAELERLDASSD 685

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  226 KLAQLQVAYHQLFQEYDNHIKssvvgserkrgmQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQA 305
Cdd:COG4913   686 DLAALEEQLEELEAELEELEE------------ELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753

                         170
                  ....*....|....*....
gi 153792133  306 DIYKADFQA-ERQAREKLA 323
Cdd:COG4913   754 RFAAALGDAvERELRENLE 772
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 104-360 3.22e-05

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: 46.20  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   104 VERLGLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQ 183
Cdd:TIGR02168  234 LEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLAN 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   184 LESEREALQQQH-----------------SVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNHIK 246
Cdd:TIGR02168  314 LERQLEELEAQLeeleskldelaeelaelEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL 393

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   247 SsvVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVMETVPVLKAQADIYKadfqAERQAREKLAEKK 326
Cdd:TIGR02168  394 Q--IASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQE----ELERLEEALEELR 467

                          250       260       270
                   ....*....|....*....|....*....|....
gi 153792133   327 ELLQEQLEQLQREYSKLKASCQESARIEDMRKRH 360
Cdd:TIGR02168  468 EELEEAEQALDAAERELAQLQARLDSLERLQENL 501
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 49-290 5.04e-05

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: 45.82  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    49 ETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVErlgleklDLKRQKEQALREVEHL 128
Cdd:TIGR02168  785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE-------DLEEQIEELSEDIESL 857

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   129 KRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHS---VQVDQLRMQ 205
Cdd:TIGR02168  858 AAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAqleLRLEGLEVR 937

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   206 GQSVEAALRMERQ-----AASEEKRKLAQLQVAYHQLFQ-----------------EYDnhikssvvgSERKRgmqLEDL 263
Cdd:TIGR02168  938 IDNLQERLSEEYSltleeAEALENKIEDDEEEARRRLKRlenkikelgpvnlaaieEYE---------ELKER---YDFL 1005

                          250       260
                   ....*....|....*....|....*..
gi 153792133   264 KQQLQQAEEALVAKQEVIDKLKEEAEQ 290
Cdd:TIGR02168 1006 TAQKEDLTEAKETLEEAIEEIDREARE 1032
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
55-196 1.13e-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: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   55 LEENQELRDAIR-----QSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVERL-------GLEKLD-LKRQKEQA 121
Cdd:COG4913   271 LAELEYLRAALRlwfaqRRLELLEAELEELRAELARLEAELERLEARLDALREELDELeaqirgnGGDRLEqLEREIERL 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  122 LREVEHLKRCQQQMAE-----------DKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREA 190
Cdd:COG4913   351 ERELEERERRRARLEAllaalglplpaSAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIAS 430


                  ....*.
gi 153792133  191 LQQQHS 196
Cdd:COG4913   431 LERRKS 436
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 52-356 1.21e-04

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: 44.57  E-value: 1.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    52 QRCLEENQELRDAIRQSNQILRERCEELLhfQASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEHLKRC 131
Cdd:TIGR00618  307 QQAQRIHTELQSKMRSRAKLLMKRAAHVK--QQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   132 QQQMAEDKASVKAqVTSLLGELQESQSRLEAATKECQALEGRaRAASEQARQLESEREALQQQHSVQVDQLRMQGqsvEA 211
Cdd:TIGR00618  385 QQQKTTLTQKLQS-LCKELDILQREQATIDTRTSAFRDLQGQ-LAHAKKQQELQQRYAELCAAAITCTAQCEKLE---KI 459

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   212 ALRMERQAASEEKRKLAQLQVaYHQLFQEYDN---HIKSSVVGSERKRGMQLEDLKQQLQQAEEaLVAKQEVIDKLKEEA 288
Cdd:TIGR00618  460 HLQESAQSLKEREQQLQTKEQ-IHLQETRKKAvvlARLLELQEEPCPLCGSCIHPNPARQDIDN-PGPLTRRMQRGEQTY 537

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 153792133   289 EQHKIVMETV----PVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDM 356
Cdd:TIGR00618  538 AQLETSEEDVyhqlTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRLQDLTEKLSEAEDM 609
hsdR PRK11448
type I restriction enzyme EcoKI subunit R; Provisional
 133-233 2.13e-04

type I restriction enzyme EcoKI subunit R; Provisional


Pssm-ID: 236912 [Multi-domain]  Cd Length: 1123  Bit Score: 43.79  E-value: 2.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  133 QQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQ--GQSVE 210
Cdd:PRK11448  145 HALQQEVLTLKQQLELQAREKAQSQALAEAQQQELVALEGLAAELEEKQQELEAQLEQLQEKAAETSQERKQKrkEITDQ 224

                          90       100
                  ....*....|....*....|....*
gi 153792133  211 AALRMErqAASEEKRKL--AQLQVA 233
Cdd:PRK11448  225 AAKRLE--LSEEETRILidQQLRKA 247
PTZ00121 PTZ00121
MAEBL; Provisional
 59-362 2.16e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   59 QELRDAIRQSNQILRERCEELLHFQASQREEKEFLMCKFQEARKLVErlGLEKLDLKRQKEQALREVEHLKRCQQQMAED 138
Cdd:PTZ00121 1428 EEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKADEAKKKAEEAKKKADEAKKA 1505

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  139 KASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQ 218
Cdd:PTZ00121 1506 AEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEE 1585

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  219 AASEEKRKLAQLQVAYH--------QLFQEYDNHIKSSVVGSERKRGMQLEDLK----QQLQQAEEalVAKQEVIDKLKE 286
Cdd:PTZ00121 1586 AKKAEEARIEEVMKLYEeekkmkaeEAKKAEEAKIKAEELKKAEEEKKKVEQLKkkeaEEKKKAEE--LKKAEEENKIKA 1663

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 153792133  287 EAEQHKIVMEtvpvlKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKAScQESARIEDMRKRHVE 362
Cdd:PTZ00121 1664 AEEAKKAEED-----KKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKA-EELKKAEEENKIKAE 1733
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
55-283 3.05e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.08  E-value: 3.05e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  55 LEENQELR-DAIRQSNQILRERCEELLHfQASQREEKeflMCKFQEARKLV-----ERLGLEKL-DLKRQKEQALREVEH 127
Cdd:COG3206  162 LEQNLELRrEEARKALEFLEEQLPELRK-ELEEAEAA---LEEFRQKNGLVdlseeAKLLLQQLsELESQLAEARAELAE 237

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 128 LKRCQQQMAEDKASVKAQVTSLLG--ELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQ 205
Cdd:COG3206  238 AEARLAALRAQLGSGPDALPELLQspVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRILAS 317

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 206 -------GQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQEYDNhikssvvgsERKRGMQLEDLKQQLQQAEEALVAKQ 278
Cdd:COG3206  318 leaeleaLQAREASLQAQLAQLEARLAELPELEAELRRLEREVEV---------ARELYESLLQRLEEARLAEALTVGNV 388


                 ....*
gi 153792133 279 EVIDK 283
Cdd:COG3206  389 RVIDP 393
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 146-287 3.81e-04

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: 42.05  E-value: 3.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  146 VTSLLGELQESQSRLEAATKECQALEGraraaseQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKR 225
Cdd:pfam09787  42 STALTLELEELRQERDLLREEIQKLRG-------QIQQLRTELQELEAQQQEEAESSREQLQELEEQLATERSARREAEA 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 153792133  226 KLAQLQVAYHQLFQEYDNHiKSSVVGSERKRGMQLEDLKQQL--------QQAE---------EALVAKQEVIDKLKEE 287
Cdd:pfam09787 115 ELERLQEELRYLEEELRRS-KATLQSRIKDREAEIEKLRNQLtsksqsssSQSElenrlhqltETLIQKQTMLEALSTE 192
PTZ00121 PTZ00121
MAEBL; Provisional
 44-362 4.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.82  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   44 EQGAPETLQRCLEENQELRDAIRQSNQiLRERCEELLHfQASQREEKEFLMCKFQEARKLVErlGLEKLDLKRQKEQALR 123
Cdd:PTZ00121 1389 EKKKADEAKKKAEEDKKKADELKKAAA-AKKKADEAKK-KAEEKKKADEAKKKAEEAKKADE--AKKKAEEAKKAEEAKK 1464

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  124 EVEHLKRCQQ--QMAEDKA---SVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQ 198
Cdd:PTZ00121 1465 KAEEAKKADEakKKAEEAKkadEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEE 1544

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  199 V---DQLRMQGQSVEAA-LRMERQAASEEKRKLAQLQVAyHQLFQEYDNHIKSSVVGSERKRGMQLEDLK---------Q 265
Cdd:PTZ00121 1545 KkkaDELKKAEELKKAEeKKKAEEAKKAEEDKNMALRKA-EEAKKAEEARIEEVMKLYEEEKKMKAEEAKkaeeakikaE 1623

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  266 QLQQAEEALVAKQEVIDKLKEE---AEQHKIVMETVPVLKAQAdiyKADFQAERQAREKLAEKKELLQEQLEQLQREysk 342
Cdd:PTZ00121 1624 ELKKAEEEKKKVEQLKKKEAEEkkkAEELKKAEEENKIKAAEE---AKKAEEDKKKAEEAKKAEEDEKKAAEALKKE--- 1697

                         330       340
                  ....*....|....*....|
gi 153792133  343 lkasCQESARIEDMRKRHVE 362
Cdd:PTZ00121 1698 ----AEEAKKAEELKKKEAE 1713
HEC1 COG5185
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...
 51-310 4.11e-04

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: 42.64  E-value: 4.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  51 LQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEflmckfQEARKLVERLGLEKldLKRQKEQALREVEHLKR 130
Cdd:COG5185  255 LEKLVEQNTDLRLEKLGENAESSKRLNENANNLIKQFENTK------EKIAEYTKSIDIKK--ATESLEEQLAAAEAEQE 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 131 CQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEG--RARAASEQARQLESEREALQQQHSVQVDQLRMQGQS 208
Cdd:COG5185  327 LEESKRETETGIQNLTAEIEQGQESLTENLEAIKEEIENIVGevELSKSSEELDSFKDTIESTKESLDEIPQNQRGYAQE 406

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 209 VEAALrmeRQAASEEKRKLAQLQVAYHQLFQEYDNHIKSSV-VGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEE 287
Cdd:COG5185  407 ILATL---EDTLKAADRQIEELQRQIEQATSSNEEVSKLLNeLISELNKVMREADEESQSRLEEAYDEINRSVRSKKEDL 483

                        250       260
                 ....*....|....*....|...
gi 153792133 288 AEQHKIVMETVPVLKAQADIYKA 310
Cdd:COG5185  484 NEELTQIESRVSTLKATLEKLRA 506
PTZ00121 PTZ00121
MAEBL; Provisional
 83-359 4.98e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   83 QASQREEKEflmcKFQEARKLVErlgLEKLDLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQS-RLE 161
Cdd:PTZ00121 1538 EAKKAEEKK----KADELKKAEE---LKKAEEKKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKmKAE 1610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  162 AATKECQAlegraRAASEQARQLESEREALQQ------QHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAyh 235
Cdd:PTZ00121 1611 EAKKAEEA-----KIKAEELKKAEEEKKKVEQlkkkeaEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA-- 1683

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  236 qlfqEYDNHIKSSVVGSERKRGMQLEDLKQQlqQAEEALVAKQevidkLKEEAEQHKIVMETVPvLKAQADIYKAD-FQA 314
Cdd:PTZ00121 1684 ----EEDEKKAAEALKKEAEEAKKAEELKKK--EAEEKKKAEE-----LKKAEEENKIKAEEAK-KEAEEDKKKAEeAKK 1751

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 153792133  315 ERQAREKLAEKKELLQEQLEQLQREYsklKASCQESARIEDMRKR 359
Cdd:PTZ00121 1752 DEEEKKKIAHLKKEEEKKAEEIRKEK---EAVIEEELDEEDEKRR 1793
MARTX_Nterm NF012221
MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model ...
 139-323 5.27e-04

MARTX multifunctional-autoprocessing repeats-in-toxin holotoxin N-terminal region; This model describes the N-terminal 1900 amino acids of MARTX family multifunctional-autoprocessing repeats-in-toxin holotoxins, which contain both repeat regions that facilitate their entry into eukaryotic target cells, and multiple effector domains.


Pssm-ID: 467957 [Multi-domain]  Cd Length: 1848  Bit Score: 42.51  E-value: 5.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  139 KASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQ 218
Cdd:NF012221 1537 TSESSQQADAVSKHAKQDDAAQNALADKERAEADRQRLEQEKQQQLAAISGSQSQLESTDQNALETNGQAQRDAILEESR 1616

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  219 AASEEKRKLAQ-LQV----AYHQ--LFQEYDNH--------IKSSVVGSERKRGMQLEDLKQQ----LQQAEEAlVAKQE 279
Cdd:NF012221 1617 AVTKELTTLAQgLDAldsqATYAgeSGDQWRNPfagglldrVQEQLDDAKKISGKQLADAKQRhvdnQQKVKDA-VAKSE 1695

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 153792133  280 VidkLKEEAEQHKivmetvpvLKAQADIYKADFQAERQAREKLA 323
Cdd:NF012221 1696 A---GVAQGEQNQ--------ANAEQDIDDAKADAEKRKDDALA 1728
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 120-352 5.98e-04

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 41.74  E-value: 5.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 120 QALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQV 199
Cdd:COG3883   13 FADPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELGERA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 200 DQLRMQGQSVEAalrmerqaaseekrkLAQLQVAyhQLFQEYDNHIK--SSVVGSERKRGMQLEDLKQQLQQAEEALVAK 277
Cdd:COG3883   93 RALYRSGGSVSY---------------LDVLLGS--ESFSDFLDRLSalSKIADADADLLEELKADKAELEAKKAELEAK 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792133 278 QEVIDKLKEEAEQHKIVMETvpvLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESAR 352
Cdd:COG3883  156 LAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAA 227
PTZ00121 PTZ00121
MAEBL; Provisional
 83-358 6.29e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 6.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   83 QASQREEKEFLMCKFQEARKLVErlglekldLKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEA 162
Cdd:PTZ00121 1297 KAEEKKKADEAKKKAEEAKKADE--------AKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEA 1368

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  163 ATKECQALEGRARAASEQARQLESEREALQ--QQHSVQVDQLRMQGQSVEAALRMERQAasEEKRKLAQLQVAyhqlfqe 240
Cdd:PTZ00121 1369 AEKKKEEAKKKADAAKKKAEEKKKADEAKKkaEEDKKKADELKKAAAAKKKADEAKKKA--EEKKKADEAKKK------- 1439

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  241 ydnhikssvvGSERKRGMQLEDLKQQLQQAEEALVAKQEV--IDKLKEEAEQHKIVMETVPvlKAQADIYKADFQAERQA 318
Cdd:PTZ00121 1440 ----------AEEAKKADEAKKKAEEAKKAEEAKKKAEEAkkADEAKKKAEEAKKADEAKK--KAEEAKKKADEAKKAAE 1507

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 153792133  319 REKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRK 358
Cdd:PTZ00121 1508 AKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKK 1547
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 45-292 8.26e-04

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: 41.88  E-value: 8.26e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    45 QGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEF--LMCKFQEARKLVERLGL--EKLDLKRQKEQ 120
Cdd:TIGR00618  215 DTYHERKQVLEKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLkqLRARIEELRAQEAVLEEtqERINRARKAAP 294

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   121 ALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRL--EAATKECQALEGRARAASEQARQLESE----REALQQQ 194
Cdd:TIGR00618  295 LAAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVkqQSSIEEQRRLLQTLHSQEIHIRDAHEVatsiREISCQQ 374

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   195 HSVQvDQLRMQGQSVEAALRMErQAASEEKRKLAQLQVAYHQLFQEYDN------HIKSSVVGSERKRGMQLEDLKQQLQ 268
Cdd:TIGR00618  375 HTLT-QHIHTLQQQKTTLTQKL-QSLCKELDILQREQATIDTRTSAFRDlqgqlaHAKKQQELQQRYAELCAAAITCTAQ 452

                          250       260
                   ....*....|....*....|....
gi 153792133   269 QAEEALVAKQEVIDKLKEEAEQHK 292
Cdd:TIGR00618  453 CEKLEKIHLQESAQSLKEREQQLQ 476
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 56-366 9.00e-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: 41.59  E-value: 9.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    56 EENQELRDAIrQSNQILRERCEELLHFQASQREEKEFLMckfQEARKLVERLGLEKLDLKRQKEQALREVEHLKRCQQQM 135
Cdd:TIGR02169  674 AELQRLRERL-EGLKRELSSLQSELRRIENRLDELSQEL---SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSL 749

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   136 AEDKASVKAQVTSLLGELQESQSRLEAATKECQALEgrARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRM 215
Cdd:TIGR02169  750 EQEIENVKSELKELEARIEELEEDLHKLEEALNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   216 ERQAASEEKRKLAQLQvayhqlfqEYDNHIKSsvvgserkRGMQLEDLKQQL----QQAEEALVAKQEVIDKLKEEAEQH 291
Cdd:TIGR02169  828 KEYLEKEIQELQEQRI--------DLKEQIKS--------IEKEIENLNGKKeeleEELEELEAALRDLESRLGDLKKER 891

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 153792133   292 KIVMETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDMRKRHVEVSQA 366
Cdd:TIGR02169  892 DELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEE 966
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 48-230 9.99e-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: 41.58  E-value: 9.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    48 PETLQRCLEENQelrdairQSNQILRERCEELlhfqasqREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEH 127
Cdd:TIGR02168  318 LEELEAQLEELE-------SKLDELAEELAEL-------EEKLEELKEELESLEAELEELEAELEELESRLEELEEQLET 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   128 LKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQAL-----EGRARAASEQARQLESEREALQQQHSVQVDQL 202
Cdd:TIGR02168  384 LRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELlkkleEAELKELQAELEELEEELEELQEELERLEEAL 463

                          170       180
                   ....*....|....*....|....*...
gi 153792133   203 RMQGQSVEAALRMERQAASEEKRKLAQL 230
Cdd:TIGR02168  464 EELREELEEAEQALDAAERELAQLQARL 491
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 56-354 1.57e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 41.11  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    56 EENQELRDAIRQSNQILRERCEELLHFQASQREEKEflmckfqearklvERLGLEKLDLKRQKEQALREVEHLKRCQQQM 135
Cdd:pfam02463  173 EALKKLIEETENLAELIIDLEELKLQELKLKEQAKK-------------ALEYYQLKEKLELEEEYLLYLDYLKLNEERI 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   136 AEDKasvkaQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVDQLRMQGQSVEAALRM 215
Cdd:pfam02463  240 DLLQ-----ELLRDEQEEIESSKQEIEKEEEKLAQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEE 314

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   216 ERQAASEEKRKLAQLQVAYHQLFQEYDNHIKSsvvgSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQHKIVM 295
Cdd:pfam02463  315 KLKESEKEKKKAEKELKKEKEEIEELEKELKE----LEIKREAEEEEEEELEKLQEKLEQLEEELLAKKKLESERLSSAA 390

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 153792133   296 ETVPVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIE 354
Cdd:pfam02463  391 KLKEEELELKSEEEKEAQLLLELARQLEDLLKEEKKEELEILEEEEESIELKQGKLTEE 449
CusB_dom_1 pfam00529
Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli ...
 153-316 2.04e-03

Cation efflux system protein CusB domain 1; The cation efflux system protein CusB from E. coli can be divided into four different domains, the first three domains of the protein are mostly beta-strands and the fourth forms an all alpha-helical domain. This entry represents the first beta-domain (domain 1) of CusB and it is formed by the N and C-terminal ends of the polypeptide (residues 89-102 and 324-385). CusB is part of the copper-transporting efflux system CusCFBA. This domain can also be found in other membrane-fusion proteins, such as HlyD, MdtN, MdtE and AaeA. HlyD is a component of the prototypical alpha-haemolysin (HlyA) bacterial type I secretion system, along with the other components HlyB and TolC. HlyD is anchored in the cytoplasmic membrane by a single transmembrane domain and has a large periplasmic domain within the carboxy-terminal 100 amino acids, HlyB and HlyD form a stable complex that binds the recombinant protein bearing a C-terminal HlyA signal sequence and ATP in the cytoplasm. HlyD, HlyB and TolC combine to form the three-component ABC transporter complex that forms a trans-membrane channel or pore through which HlyA can be transferred directly to the extracellular medium. Cutinase has been shown to be transported effectively through this pore.


Pssm-ID: 425733 [Multi-domain]  Cd Length: 322  Bit Score: 40.10  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  153 LQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHsvqvDQLRMQGQSVEAALrmerqAASEEKRKLAQLQV 232
Cdd:pfam00529  56 YQAALDSAEAQLAKAQAQVARLQAELDRLQALESELAISRQDY----DGATAQLRAAQAAV-----KAAQAQLAQAQIDL 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  233 AYHQLFQEYDNHIKSSVVGSERKRGMQLEDLKQQLQQAEEALVAKQEVIDKLKEEAEQhKIVMETVPVLKAQADIYKADF 312
Cdd:pfam00529 127 ARRRVLAPIGGISRESLVTAGALVAQAQANLLATVAQLDQIYVQITQSAAENQAEVRS-ELSGAQLQIAEAEAELKLAKL 205


                  ....
gi 153792133  313 QAER 316
Cdd:pfam00529 206 DLER 209
PTZ00491 PTZ00491
major vault protein; Provisional
 117-234 2.60e-03

major vault protein; Provisional


Pssm-ID: 240439 [Multi-domain]  Cd Length: 850  Bit Score: 40.00  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 117 QKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLgelqesqsRLEAATKECQAlEGRARAASEQarqlESEREALQQQHS 196
Cdd:PTZ00491 669 RHQAELLEQEARGRLERQKMHDKAKAEEQRTKLL--------ELQAESAAVES-SGQSRAEALA----EAEARLIEAEAE 735

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 153792133 197 VQVDQLRMQGQSVEAA-----LRMERQAASEEKRKLAQLQVAY 234
Cdd:PTZ00491 736 VEQAELRAKALRIEAEaelekLRKRQELELEYEQAQNELEIAK 778
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 51-194 3.46e-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: 39.65  E-value: 3.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    51 LQRCLEENQELRDAIRQSNQILRERCEELLHFQ---ASQREEKEFLMCKFQEARKLVERLGLEKLDLKRQKEQALREVEH 127
Cdd:TIGR02168  353 LESLEAELEELEAELEELESRLEELEEQLETLRskvAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEE 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 153792133   128 LKRCQQQMaeDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQ 194
Cdd:TIGR02168  433 AELKELQA--ELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERL 497
PRK09039 PRK09039
peptidoglycan -binding protein;
139-233 3.53e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 39.18  E-value: 3.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133 139 KASVKAQVTSLLGELQESQ---SRLEAATKEcqaLEGRARAASEQARQLESEREALQQQHS----------VQVDQLRMQ 205
Cdd:PRK09039  76 NQDLQDSVANLRASLSAAEaerSRLQALLAE---LAGAGAAAEGRAGELAQELDSEKQVSAralaqvellnQQIAALRRQ 152

                         90       100
                 ....*....|....*....|....*...
gi 153792133 206 GQSVEAALRmerqaASEEKRKLAQLQVA 233
Cdd:PRK09039 153 LAALEAALD-----ASEKRDRESQAKIA 175
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 41-225 6.94e-03

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: 38.90  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    41 LPSEQGAPETLQRCLEENQELRDAIRQSNQILRERCEELLHFQASQREEKEflmckfqearklverlgleklDLKRQKEQ 120
Cdd:TIGR02169  345 IEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREKLE---------------------KLKREINE 403

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   121 ALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQVD 200
Cdd:TIGR02169  404 LKRELDRLQEELQRLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQELYDLKEEYDRVEK 483

                          170       180
                   ....*....|....*....|....*
gi 153792133   201 QLRmQGQSVEAALRMERQAASEEKR 225
Cdd:TIGR02169  484 ELS-KLQRELAEAEAQARASEERVR 507
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 27-291 8.97e-03

Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. Proteins in this family are typically between 943 to 1234 amino acids in length. This family contains a P-loop motif suggesting it is a nucleotide binding protein. It may be involved in replication.


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 38.67  E-value: 8.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133    27 LGEESPLGKPAMLHLPSEQGAPETLQRCLEENQELRDAIRQS-NQILRERCEELLHFQASQREEKEFLMCKFQEARKLVE 105
Cdd:pfam12128  246 LQQEFNTLESAELRLSHLHFGYKSDETLIASRQEERQETSAElNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELE 325

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   106 RLGLEKLD-LKRQKEQALREVEHLKRCQQQMAEDKASVKAQVTSLLGELQESQSRLEAATKECQAL-----EGRARAASE 179
Cdd:pfam12128  326 ALEDQHGAfLDADIETAAADQEQLPSWQSELENLEERLKALTGKHQDVTAKYNRRRSKIKEQNNRDiagikDKLAKIREA 405

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   180 QARQLESEREALQQQHSVQVDQLRMQGQSVEAALRMERQAASEEKRKLAQLQVAYHQLFQeydnhIKSSVVGSERKRGMQ 259
Cdd:pfam12128  406 RDRQLAVAEDDLQALESELREQLEAGKLEFNEEEYRLKSRLGELKLRLNQATATPELLLQ-----LENFDERIERAREEQ 480

                          250       260       270
                   ....*....|....*....|....*....|..
gi 153792133   260 LEDLKQQLQQAEEALVAkqeviDKLKEEAEQH 291
Cdd:pfam12128  481 EAANAEVERLQSELRQA-----RKRRDQASEA 507
PTZ00121 PTZ00121
MAEBL; Provisional
 47-366 1.00e-02

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.58  E-value: 1.00e-02
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133   47 APETLQRCLEENQELRDAIRQSNQILR----ERCEELLHFQASQREE---KEFLMCKFQEARKLVERlglEKLDLKRQKE 119
Cdd:PTZ00121 1103 AKKTETGKAEEARKAEEAKKKAEDARKaeeaRKAEDARKAEEARKAEdakRVEIARKAEDARKAEEA---RKAEDAKKAE 1179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  120 QALREVEHLKRCQQQMAEDKASVKAqvtsllGELQESQSRLEAATKECQALEGRARAASEQARQLESEREALQQQHSVQV 199
Cdd:PTZ00121 1180 AARKAEEVRKAEELRKAEDARKAEA------ARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEE 1253

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  200 DQLRMQGQSVEAALRMERQAAsEEKRKLAQLQVAYHQlfQEYDNHIKSSvvgsERKRGMQLEDLKQQLQQAEEALVAKQE 279
Cdd:PTZ00121 1254 IRKFEEARMAHFARRQAAIKA-EEARKADELKKAEEK--KKADEAKKAE----EKKKADEAKKKAEEAKKADEAKKKAEE 1326

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 153792133  280 V---IDKLKEEAEQHKIVMEtvpVLKAQADIYKADFQAERQAREKLAEKKELLQEQLEQLQREYSKLKASCQESARIEDM 356
Cdd:PTZ00121 1327 AkkkADAAKKKAEEAKKAAE---AAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEED 1403

                         330
                  ....*....|
gi 153792133  357 RKRHVEVSQA 366
Cdd:PTZ00121 1404 KKKADELKKA 1413
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH