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Conserved domains on  [gi|755496880|ref|XP_011237290|]
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optineurin isoform X3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 210-306 1.54e-22

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: 90.81  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  210 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 289
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90
                  ....*....|....*..
gi 755496880  290 EKEQLALQLAILLKENN 306
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQ 97
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 357-382 3.13e-13

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: 62.99  E-value: 3.13e-13
                          10        20
                  ....*....|....*....|....*.
gi 755496880  357 PIHSCPKCGEVLPDIDTLQIHVMDCI 382
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-271 5.27e-09

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: 58.02  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  23 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 102
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 103 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 182
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 183 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 260
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250
                 ....*....|.
gi 755496880 261 ETMAVLRAQME 271
Cdd:COG1196  477 AALAELLEELA 487
 
Name Accession Description Interval E-value
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 210-306 1.54e-22

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: 90.81  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  210 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 289
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90
                  ....*....|....*..
gi 755496880  290 EKEQLALQLAILLKENN 306
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQ 97
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 225-309 6.49e-22

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: 88.95  E-value: 6.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 225 LQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKE 304
Cdd:cd09803    3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82


                 ....*
gi 755496880 305 NNDIE 309
Cdd:cd09803   83 NQELK 87
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 357-382 3.13e-13

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: 62.99  E-value: 3.13e-13
                          10        20
                  ....*....|....*....|....*.
gi 755496880  357 PIHSCPKCGEVLPDIDTLQIHVMDCI 382
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-271 5.27e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  23 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 102
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 103 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 182
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 183 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 260
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250
                 ....*....|.
gi 755496880 261 ETMAVLRAQME 271
Cdd:COG1196  477 AALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-321 3.37e-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: 55.45  E-value: 3.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    43 LREGNQKVERLEVALREAKERISDFEKKanghsstekqtARRADREKEDKGQESvgsevetlSIQVTSLFKELQEAHTKL 122
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQ-----------AEKAERYKELKAELR--------ELELALLVLRLEELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   123 SEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK----SRLATLQATHNKL 198
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEEL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   199 LQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEvycsdfH 278
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------L 393

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 755496880   279 AERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 321
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-321 1.48e-04

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: 43.95  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    33 ELTVSQLLLCLREGNQ----KVERLE-------VALREAKERISDFEKKA-NGHSSTEKQTARRADREKE---DKGQESV 97
Cdd:pfam15921  323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKElslEKEQNKR 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    98 GSEVET-LSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSnkkLELQVESMRSEIKM 176
Cdd:pfam15921  403 LWDRDTgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS---LTAQLESTKEMLRK 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   177 EQAKTEEEKSRLATLQATHNKL---LQEHNKALK-TIEELTKQQAeKVDkMLLQELS------EKLELAEQALASKQLQM 246
Cdd:pfam15921  480 VVEELTAKKMTLESSERTVSDLtasLQEKERAIEaTNAEITKLRS-RVD-LKLQELQhlknegDHLRNVQTECEALKLQM 557

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755496880   247 DEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK-IHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 321
Cdd:pfam15921  558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
PTZ00121 PTZ00121
MAEBL; Provisional
 23-259 2.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   23 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVE 102
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  103 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAtpselNEKQELVYSNKKLELQVESMRSEIKMEQAKTE 182
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755496880  183 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEED 259
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
 
Name Accession Description Interval E-value
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 210-306 1.54e-22

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: 90.81  E-value: 1.54e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  210 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 289
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90
                  ....*....|....*..
gi 755496880  290 EKEQLALQLAILLKENN 306
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQ 97
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 225-309 6.49e-22

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: 88.95  E-value: 6.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 225 LQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKE 304
Cdd:cd09803    3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82


                 ....*
gi 755496880 305 NNDIE 309
Cdd:cd09803   83 NQELK 87
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 357-382 3.13e-13

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: 62.99  E-value: 3.13e-13
                          10        20
                  ....*....|....*....|....*.
gi 755496880  357 PIHSCPKCGEVLPDIDTLQIHVMDCI 382
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 23-271 5.27e-09

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 58.02  E-value: 5.27e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  23 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 102
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 103 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 182
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 183 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 260
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250
                 ....*....|.
gi 755496880 261 ETMAVLRAQME 271
Cdd:COG1196  477 AALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-321 3.37e-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: 55.45  E-value: 3.37e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    43 LREGNQKVERLEVALREAKERISDFEKKanghsstekqtARRADREKEDKGQESvgsevetlSIQVTSLFKELQEAHTKL 122
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQ-----------AEKAERYKELKAELR--------ELELALLVLRLEELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   123 SEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK----SRLATLQATHNKL 198
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEEL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   199 LQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEvycsdfH 278
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------L 393

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 755496880   279 AERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 321
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 18-265 6.06e-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: 54.68  E-value: 6.06e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    18 LSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSStEKQTARRADREKEDKgQESV 97
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAEAEAE-IEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    98 GSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELnekQELVYSNKKLELQVESMRSEIKME 177
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL---EDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   178 QAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM-----LLQELSEKLELAEQALASKQLQMDEMKQT 252
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRselrrELEELREKLAQLELRLEGLEVRIDNLQER 944

                          250
                   ....*....|...
gi 755496880   253 LAKQEEDLETMAV 265
Cdd:TIGR02168  945 LSEEYSLTLEEAE 957
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-260 1.08e-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: 53.91  E-value: 1.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    43 LREGNQKVERLEVALREAKERISDFEKKAN----GHSSTEKQTAR-RADREKEDKGQESVGSEVETLSIQVTSLFKELQE 117
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEelsrQISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   118 AHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQElVYSNKKLELQveSMRSEIKMEQAKTEEEKSRLATLQATHNK 197
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQIEE 849

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755496880   198 LLQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 260
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELRELESKR 910
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 29-310 1.22e-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: 53.91  E-value: 1.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    29 AEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGhSSTEKQTARRADREKEDKGQEsvgsevetlsiqv 108
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEE------------- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   109 tsLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQelvysNKKLELQVESMRSEIKMEQAKteEEKSRL 188
Cdd:TIGR02168  286 --LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEELK--EELESL 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   189 ATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKlelAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRA 268
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 755496880   269 QMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 310
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 78-310 8.21e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.01  E-value: 8.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  78 EKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSEL----NEK 153
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLeeleEEL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 154 QELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKML-LQELSEKL 232
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEEL 405

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755496880 233 ELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQmevycsDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 310
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 43-308 1.35e-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: 47.36  E-value: 1.35e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    43 LREGNQKVERLEVALREAKERISDFEKKANGHssteKQTARRADREKE--DKGQESVGSEVETLSIQVTSLFKELQEAHT 120
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYAL----ANEISRLEQQKQilRERLANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   121 KLSEaelMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQ 200
Cdd:TIGR02168  338 ELAE---LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   201 EHNKALKTIEELTKQQAEKVdkmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAE 280
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAE----LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490

                          250       260
                   ....*....|....*....|....*...
gi 755496880   281 RAAREKIHEEKEQLALQLAILLKENNDI 308
Cdd:TIGR02168  491 LDSLERLQENLEGFSEGVKALLKNQSGL 518
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 43-264 3.74e-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: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  43 LREGNQKVERLEVALREAKERISDFEKKANGHSST-EKQTARRADREKEDKGQESvgsEVETLSIQVTSLFKELQEAHTK 121
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 122 LSEaelMKKRLQEKCQALERKNSATPSEL----NEKQELVYSNKKLELQVESMRS---EIKMEQAKTEEEKSRLATLQAT 194
Cdd:COG4942   99 LEA---QKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRAELEAERAE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 195 HNKLLQEHNKALKTIEELTKQQAEkvdkmLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMA 264
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
125-257 1.03e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.46  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 125 AELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNK 204
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHEERELTEEEEEI---RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 755496880 205 ALKTIEELTKQQAEKvdKMLLQELSEKLELAEQaLASKQLQMDEMKQTLAKQE 257
Cdd:COG2433  460 EIRKDREISRLDREI--ERLERELEEERERIEE-LKRKLERLKELWKLEHSGE 509
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
47-271 1.39e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.85  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  47 NQKVERLEVALREAKERISDFekkanghsstekqtarradreKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAE 126
Cdd:COG3206  181 EEQLPELRKELEEAEAALEEF---------------------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 127 LMKKRLQekcQALERKNSATPSELNEKQelvysnkklelqVESMRSEIKMEQAKTEEEKSRLatlQATHNKLLQehnkal 206
Cdd:COG3206  240 ARLAALR---AQLGSGPDALPELLQSPV------------IQQLRAQLAELEAELAELSARY---TPNHPDVIA------ 295

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755496880 207 ktieelTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQME 271
Cdd:COG3206  296 ------LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 33-321 1.48e-04

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: 43.95  E-value: 1.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    33 ELTVSQLLLCLREGNQ----KVERLE-------VALREAKERISDFEKKA-NGHSSTEKQTARRADREKE---DKGQESV 97
Cdd:pfam15921  323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKElslEKEQNKR 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    98 GSEVET-LSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSnkkLELQVESMRSEIKM 176
Cdd:pfam15921  403 LWDRDTgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS---LTAQLESTKEMLRK 479

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   177 EQAKTEEEKSRLATLQATHNKL---LQEHNKALK-TIEELTKQQAeKVDkMLLQELS------EKLELAEQALASKQLQM 246
Cdd:pfam15921  480 VVEELTAKKMTLESSERTVSDLtasLQEKERAIEaTNAEITKLRS-RVD-LKLQELQhlknegDHLRNVQTECEALKLQM 557

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755496880   247 DEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK-IHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 321
Cdd:pfam15921  558 AEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
PTZ00121 PTZ00121
MAEBL; Provisional
 23-259 2.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.21  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   23 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVE 102
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  103 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAtpselNEKQELVYSNKKLELQVESMRSEIKMEQAKTE 182
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755496880  183 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEED 259
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 43-262 3.15e-04

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 42.70  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   43 LREGNQKVERLEVALREAKERISDFEKkanghsstEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKL 122
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNN--------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  123 sEAELMKKRL--QEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQ 200
Cdd:TIGR04523 348 -KKELTNSESenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755496880  201 EH-------NKALKTIEELTKQQAEKvdKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET 262
Cdd:TIGR04523 427 EIerlketiIKNNSEIKDLTNQDSVK--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 43-261 3.38e-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: 42.75  E-value: 3.38e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    43 LREGNQKVERLEVALREAKERISDFEKkanghsstEKQTARRAD---REKEDKGQESVGSEVETLSIQVTSLFKELQEAH 119
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRR--------EREKAERYQallKEKREYEGYELLKEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   120 tklSEAELMKKRLQEKCQALERKNsATPSELNEKQELVYSNKKLELQ--VESMRSEIKMEQAKTEEEKSRLATLQATHNK 197
Cdd:TIGR02169  251 ---EELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755496880   198 LLQEHNKALKTIEELTKQQAE-KVDKMLLQE----LSEKLELAEQALASKQLQMDEMKQTLAKQEEDLE 261
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEeRKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
23-310 3.68e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 42.72  E-value: 3.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  23 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKE-----DKGQESV 97
Cdd:PRK02224 296 DDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREeaaelESELEEA 375

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  98 GSEVETLSIQVTSLFKELQE-------AHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKL------- 163
Cdd:PRK02224 376 REAVEDRREEIEELEEEIEElrerfgdAPVDLGNAEDFLEELREERDELREREAELEATLRTARERVEEAEALleagkcp 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 164 ----ELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKAlktiEELTKQQAEkvdkmlLQELSEKLELAEQAL 239
Cdd:PRK02224 456 ecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA----EDLVEAEDR------IERLEERREDLEELI 525

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755496880 240 ASKQlqmdemkqtlAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 310
Cdd:PRK02224 526 AERR----------ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKE 586
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 71-286 4.48e-04

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 42.06  E-value: 4.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  71 ANGHSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSEL 150
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 151 N------EKQELVYSNKKLELQVESMRSEIKM-----EQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEK 219
Cdd:COG4942   93 AelraelEAQKEELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755496880 220 VDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK 286
Cdd:COG4942  173 RAELeaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 114-262 6.25e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 41.06  E-value: 6.25e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 114 ELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSRLATLQA 193
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---EDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755496880 194 THnkllqEHNKALKTIEELTKQQAEKVDKMLlqELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET 262
Cdd:COG1579   88 NK-----EYEALQKEIESLKRRISDLEDEIL--ELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
PRK12704 PRK12704
phosphodiesterase; Provisional
 113-282 1.14e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 113 KELQEAHTKLSEAElmkKRLQEKCQALERKnsatpSELNEKQElvysnkklelqvesmrSEIKMEQAKTEEEKSRLATLQ 192
Cdd:PRK12704  75 KELRERRNELQKLE---KRLLQKEENLDRK-----LELLEKRE----------------EELEKKEKELEQKQQELEKKE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 193 ATHNKLLQEHNKALKTIEELTKQQAEkvdKMLLQELSEKLElAEQALASKQLQMDemkqtlAKQEEDLETMAVLRAQMEV 272
Cdd:PRK12704 131 EELEELIEEQLQELERISGLTAEEAK---EILLEKVEEEAR-HEAAVLIKEIEEE------AKEEADKKAKEILAQAIQR 200

                        170
                 ....*....|
gi 755496880 273 YCSDFHAERA 282
Cdd:PRK12704 201 CAADHVAETT 210
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
101-282 1.78e-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: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  101 VETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELN-------------EKQELVYSNKKLElQV 167
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaeleaELERLDASSDDLA-AL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  168 ESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKL--ELAEQALASKQLQ 245
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFaaALGDAVERELREN 770

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 755496880  246 MDEMKQTLAKQEEDLETMavLRAQMEVYCSDFHAERA 282
Cdd:COG4913   771 LEERIDALRARLNRAEEE--LERAMRAFNREWPAETA 805
PTZ00121 PTZ00121
MAEBL; Provisional
 43-317 2.23e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 40.51  E-value: 2.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   43 LREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEV-----ETLSIQVTSLF----- 112
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeEARIEEVMKLYeeekk 1606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  113 ---KELQEAHTKLSEAELMKKRLQEKCQALERKNSAT----PSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK 185
Cdd:PTZ00121 1607 mkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  186 SRLATLQathnklLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMK-QTLAKQEEDLETMA 264
Cdd:PTZ00121 1687 EKKAAEA------LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDEEEKKKIA 1760

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 755496880  265 VLRAQMEVYCSDFHAERAA--REKIHEEKEQLALQLAILLKENND----IEEGGSRQSL 317
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDnfanIIEGGKEGNL 1819
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 78-256 3.22e-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: 39.57  E-value: 3.22e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    78 EKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATP--------SE 149
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQ 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   150 LNEKQELVY----SNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLL 225
Cdd:TIGR00618  305 IEQQAQRIHtelqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384

                          170       180       190
                   ....*....|....*....|....*....|.
gi 755496880   226 QELSEKLELAEQALASKQLQMDEMKQTLAKQ 256
Cdd:TIGR00618  385 QQQKTTLTQKLQSLCKELDILQREQATIDTR 415
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 161-271 3.69e-03

Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes pesticidal Cry6Aa toxin from Bacillus thuringiensis, one of the many parasporal crystal (Cry) toxins produced during the sporulation phase of growth. Many of these proteins are toxic to numerous insect species and have been effectively used as proteinaceous insecticides to directly kill insect pests; some have been used to control insect growth on transgenic agricultural plants. Cry6Aa exists as a protoxin, which is activated by cleavage using trypsin. Structure studies for Cry6Aa support a mechanism of action by pore formation, similar to cytolysin A (ClyA)-type alpha pore-forming toxins (alpha-PFTs) such as HblB, and bioassay and mutation studies show that Cry6Aa is an active pore-forming toxin. Cry6Aa shows atypical features compared to other members of alpha-PFTs, including internal repeat sequences and small loop regions within major alpha helices.


Pssm-ID: 439154 [Multi-domain]  Cd Length: 309  Bit Score: 38.89  E-value: 3.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 161 KKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKAL--KTIEELTKQQAEKVDkmllqelseklELAEQA 238
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIarKEIKDLQKELEKLNE-----------EYAAKL 199

                         90       100       110
                 ....*....|....*....|....*....|...
gi 755496880 239 LAskqlQMDEMKQTLAKQEEDLETMAVLRAQME 271
Cdd:cd22656  200 KA----KIDELKALIADDEAKLAAALRLIADLT 228
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 85-271 4.31e-03

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.04  E-value: 4.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880  85 ADREKEDKGQE--SVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysNKK 162
Cdd:COG3883   14 ADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880 163 LELQVESMRSEIKMEQ---AKTEEE----KSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLE 233
Cdd:COG3883   92 ARALYRSGGSVSYLDVllgSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELeaLKAELEAAKA 171

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 755496880 234 LAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQME 271
Cdd:COG3883  172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 48-218 6.41e-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: 6.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880    48 QKVERLEVALREAKERISDFEK--------KANGHSSTEKQTARRADREKEDKGQESvgsEVETLSIQVTSLFKELQEAH 119
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKeienlngkKEELEEELEELEAALRDLESRLGDLKK---ERDELEAQLRELERKIEELE 909

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755496880   120 TKLSEAELMKKRLQEKCQALERKNSA---TPSELNEKQELVYSNKKLELQVESMRSEI-KMEQAKT------EEEKSRLA 189
Cdd:TIGR02169  910 AQIEKKRKRLSELKAKLEALEEELSEiedPKGEDEEIPEEELSLEDVQAELQRVEEEIrALEPVNMlaiqeyEEVLKRLD 989

                          170       180
                   ....*....|....*....|....*....
gi 755496880   190 TLQATHNKLLQEHNKALKTIEELTKQQAE 218
Cdd:TIGR02169  990 ELKEKRAKLEEERKAILERIEEYEKKKRE 1018
 
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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