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Conserved domains on  [gi|568912557|ref|XP_006497611|]
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optineurin isoform X2 [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 ...
 254-350 4.53e-23

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: 92.74  E-value: 4.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  254 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 333
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90
                  ....*....|....*..
gi 568912557  334 EKEQLALQLAILLKENN 350
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 ...
 401-426 1.10e-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: 64.53  E-value: 1.10e-13
                          10        20
                  ....*....|....*....|....*.
gi 568912557  401 PIHSCPKCGEVLPDIDTLQIHVMDCI 426
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-315 7.57e-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: 7.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  67 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 146
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 147 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 226
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 227 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 304
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250
                 ....*....|.
gi 568912557 305 ETMAVLRAQME 315
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 ...
 254-350 4.53e-23

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: 92.74  E-value: 4.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  254 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 333
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90
                  ....*....|....*..
gi 568912557  334 EKEQLALQLAILLKENN 350
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQ 97
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 269-353 1.98e-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: 90.87  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 269 LQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKE 348
Cdd:cd09803    3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82


                 ....*
gi 568912557 349 NNDIE 353
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 ...
 401-426 1.10e-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: 64.53  E-value: 1.10e-13
                          10        20
                  ....*....|....*....|....*.
gi 568912557  401 PIHSCPKCGEVLPDIDTLQIHVMDCI 426
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-315 7.57e-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: 7.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  67 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 146
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 147 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 226
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 227 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 304
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250
                 ....*....|.
gi 568912557 305 ETMAVLRAQME 315
Cdd:COG1196  477 AALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-365 3.61e-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: 55.83  E-value: 3.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    87 LREGNQKVERLEVALREAKERISDFEKKanghsstekqtARRADREKEDKGQESvgsevetlSIQVTSLFKELQEAHTKL 166
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQ-----------AEKAERYKELKAELR--------ELELALLVLRLEELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   167 SEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK----SRLATLQATHNKL 242
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEEL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   243 LQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEvycsdfH 322
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------L 393

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 568912557   323 AERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 365
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 77-365 5.63e-05

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: 45.49  E-value: 5.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    77 ELTVSQLLLCLREGNQ----KVERLE-------VALREAKERISDFEKKA-NGHSSTEKQTARRADREKE---DKGQESV 141
Cdd:pfam15921  323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKElslEKEQNKR 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   142 GSEVET-LSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSnkkLELQVESMRseiKM 220
Cdd:pfam15921  403 LWDRDTgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS---LTAQLESTK---EM 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   221 EQAKTEEEKSRLATLQATHNKL------LQEHNKALK-TIEELTKQQAeKVDkMLLQELS------EKLELAEQALASKQ 287
Cdd:pfam15921  477 LRKVVEELTAKKMTLESSERTVsdltasLQEKERAIEaTNAEITKLRS-RVD-LKLQELQhlknegDHLRNVQTECEALK 554

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557   288 LQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK-IHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 365
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
PTZ00121 PTZ00121
MAEBL; Provisional
 67-303 1.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   67 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVE 146
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  147 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAtpselNEKQELVYSNKKLELQVESMRSEIKMEQAKTE 226
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912557  227 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEED 303
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 ...
 254-350 4.53e-23

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: 92.74  E-value: 4.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  254 EELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHE 333
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90
                  ....*....|....*..
gi 568912557  334 EKEQLALQLAILLKENN 350
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQ 97
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 269-353 1.98e-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: 90.87  E-value: 1.98e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 269 LQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKE 348
Cdd:cd09803    3 IDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQRE 82


                 ....*
gi 568912557 349 NNDIE 353
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 ...
 401-426 1.10e-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: 64.53  E-value: 1.10e-13
                          10        20
                  ....*....|....*....|....*.
gi 568912557  401 PIHSCPKCGEVLPDIDTLQIHVMDCI 426
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 67-315 7.57e-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: 7.57e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  67 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVgsEVE 146
Cdd:COG1196  242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEE--RLE 319

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 147 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTE 226
Cdd:COG1196  320 ELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL---AEAEEELEELAEELLEALRAAA 396

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 227 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 304
Cdd:COG1196  397 ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEeeEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLE 476

                        250
                 ....*....|.
gi 568912557 305 ETMAVLRAQME 315
Cdd:COG1196  477 AALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-365 3.61e-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: 55.83  E-value: 3.61e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    87 LREGNQKVERLEVALREAKERISDFEKKanghsstekqtARRADREKEDKGQESvgsevetlSIQVTSLFKELQEAHTKL 166
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQ-----------AEKAERYKELKAELR--------ELELALLVLRLEELREEL 241

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   167 SEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK----SRLATLQATHNKL 242
Cdd:TIGR02168  242 EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEEL 321

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   243 LQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEvycsdfH 322
Cdd:TIGR02168  322 EAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE------L 393

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 568912557   323 AERAAREKIHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 365
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 62-309 6.30e-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: 55.06  E-value: 6.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    62 LSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSStEKQTARRADREKEDKgQESV 141
Cdd:TIGR02168  710 LEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEE-RLEEAEEELAEAEAE-IEEL 787

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   142 GSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELnekQELVYSNKKLELQVESMRSEIKME 221
Cdd:TIGR02168  788 EAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRL---EDLEEQIEELSEDIESLAAEIEEL 864

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   222 QAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM-----LLQELSEKLELAEQALASKQLQMDEMKQT 296
Cdd:TIGR02168  865 EELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRselrrELEELREKLAQLELRLEGLEVRIDNLQER 944

                          250
                   ....*....|...
gi 568912557   297 LAKQEEDLETMAV 309
Cdd:TIGR02168  945 LSEEYSLTLEEAE 957
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-304 1.20e-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: 54.29  E-value: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    87 LREGNQKVERLEVALREAKERISDFEKKANG----HSSTEKQTAR-RADREKEDKGQESVGSEVETLSIQVTSLFKELQE 161
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEElsrqISALRKDLARlEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   162 AHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQElVYSNKKLELQveSMRSEIKMEQAKTEEEKSRLATLQATHNK 241
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLLNEEAA--NLRERLESLERRIAATERRLEDLEEQIEE 849

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568912557   242 LLQEHNKALKTIEELTKQQAEKVDKmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDL 304
Cdd:TIGR02168  850 LSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALALLRSELEELSEELRELESKR 910
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 73-354 1.41e-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: 1.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    73 AEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGhSSTEKQTARRADREKEDKGQEsvgsevetlsiqv 152
Cdd:TIGR02168  220 AELRELELALLVLRLEELREELEELQEELKEAEEELEELTAELQE-LEEKLEELRLEVSELEEEIEE------------- 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   153 tsLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQelvysNKKLELQVESMRSEIKMEQAKteEEKSRL 232
Cdd:TIGR02168  286 --LQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEELK--EELESL 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   233 ATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKlelAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRA 312
Cdd:TIGR02168  357 EAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLN---NEIERLEARLERLEDRRERLQQEIEELLKKLEEA 433

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 568912557   313 QMEVYCSDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 354
Cdd:TIGR02168  434 ELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 122-354 1.03e-05

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: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 122 EKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSEL----NEK 197
Cdd:COG1196  246 AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLeeleEEL 325

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 198 QELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKML-LQELSEKL 276
Cdd:COG1196  326 AELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAeLAAQLEEL 405

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568912557 277 ELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQmevycsDFHAERAAREKIHEEKEQLALQLAILLKENNDIEE 354
Cdd:COG1196  406 EEAEEALLERLERLEEELEELEEALAELEEEEEEEEE------ALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 87-352 1.48e-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: 1.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    87 LREGNQKVERLEVALREAKERISDFEKKANGHssteKQTARRADREKE--DKGQESVGSEVETLSIQVTSLFKELQEAHT 164
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYAL----ANEISRLEQQKQilRERLANLERQLEELEAQLEELESKLDELAE 337

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   165 KLSEaelMKKRLQEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQ 244
Cdd:TIGR02168  338 ELAE---LEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLED 414

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   245 EHNKALKTIEELTKQQAEKVdkmlLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAE 324
Cdd:TIGR02168  415 RRERLQQEIEELLKKLEEAE----LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490

                          250       260
                   ....*....|....*....|....*...
gi 568912557   325 RAAREKIHEEKEQLALQLAILLKENNDI 352
Cdd:TIGR02168  491 LDSLERLQENLEGFSEGVKALLKNQSGL 518
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 87-308 3.53e-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: 3.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  87 LREGNQKVERLEVALREAKERISDFEKKANGHSST-EKQTARRADREKEDKGQESvgsEVETLSIQVTSLFKELQEAHTK 165
Cdd:COG4942   22 AAEAEAELEQLQQEIAELEKELAALKKEEKALLKQlAALERRIAALARRIRALEQ---ELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 166 LSEaelMKKRLQEKCQALERKNSATPSEL----NEKQELVYSNKKLELQVESMRS---EIKMEQAKTEEEKSRLATLQAT 238
Cdd:COG4942   99 LEA---QKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREqaeELRADLAELAALRAELEAERAE 175

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 239 HNKLLQEHNKALKTIEELTKQQAEkvdkmLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMA 308
Cdd:COG4942  176 LEALLAELEEERAALEALKAERQK-----LLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 77-365 5.63e-05

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: 45.49  E-value: 5.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    77 ELTVSQLLLCLREGNQ----KVERLE-------VALREAKERISDFEKKA-NGHSSTEKQTARRADREKE---DKGQESV 141
Cdd:pfam15921  323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESgNLDDQLQKLLADLHKREKElslEKEQNKR 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   142 GSEVET-LSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVYSnkkLELQVESMRseiKM 220
Cdd:pfam15921  403 LWDRDTgNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSS---LTAQLESTK---EM 476

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   221 EQAKTEEEKSRLATLQATHNKL------LQEHNKALK-TIEELTKQQAeKVDkMLLQELS------EKLELAEQALASKQ 287
Cdd:pfam15921  477 LRKVVEELTAKKMTLESSERTVsdltasLQEKERAIEaTNAEITKLRS-RVD-LKLQELQhlknegDHLRNVQTECEALK 554

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557   288 LQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK-IHEEKEQLALQLAILLKENNDIEEGGSRQSLMEMQ 365
Cdd:pfam15921  555 LQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKeINDRRLELQEFKILKDKKDAKIRELEARVSDLELE 633
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 87-306 1.02e-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: 44.63  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   87 LREGNQKVERLEVALREAKERISDFEKkanghsstEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKL 166
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNN--------QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQL 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  167 sEAELMKKRL--QEKCQALERKNSATPSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQ 244
Cdd:TIGR04523 348 -KKELTNSESenSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557  245 EH-------NKALKTIEELTKQQAEKvdKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET 306
Cdd:TIGR04523 427 EIerlketiIKNNSEIKDLTNQDSVK--ELIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKS 493
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
169-301 1.39e-04

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


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 44.08  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 169 AELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNK 248
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHEERELTEEEEEI---RRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 568912557 249 ALKTIEELTKQQAEKvdKMLLQELSEKLELAEQaLASKQLQMDEMKQTLAKQE 301
Cdd:COG2433  460 EIRKDREISRLDREI--ERLERELEEERERIEE-LKRKLERLKELWKLEHSGE 509
PTZ00121 PTZ00121
MAEBL; Provisional
 67-303 1.46e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   67 EDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEVE 146
Cdd:PTZ00121 1318 DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAK 1397

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  147 TLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAtpselNEKQELVYSNKKLELQVESMRSEIKMEQAKTE 226
Cdd:PTZ00121 1398 KKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKA 1472

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568912557  227 EEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEED 303
Cdd:PTZ00121 1473 DEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
91-315 2.53e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 43.47  E-value: 2.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  91 NQKVERLEVALREAKERISDFekkanghsstekqtarradreKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAE 170
Cdd:COG3206  181 EEQLPELRKELEEAEAALEEF---------------------RQKNGLVDLSEEAKLLLQQLSELESQLAEARAELAEAE 239

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 171 LMKKRLQekcQALERKNSATPSELNEKQelvysnkklelqVESMRSEIKMEQAKTEEEKSRLatlQATHNKLLQehnkal 250
Cdd:COG3206  240 ARLAALR---AQLGSGPDALPELLQSPV------------IQQLRAQLAELEAELAELSARY---TPNHPDVIA------ 295

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568912557 251 ktieelTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQME 315
Cdd:COG3206  296 ------LRAQIAALRAQLQQEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPELEAELR 354
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
33-354 3.03e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 43.11  E-value: 3.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  33 EIRMTEGETEGAMKEMKNCPTPTRTDPISLSNCTEDARSCAEFEELTVSQLLLCLREGNQKVERLEVALREAKERISDFE 112
Cdd:PRK02224 262 DLRETIAETEREREELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAVEARREELEDRDEELRDRLEECRVAAQAHN 341

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 113 KKANGHSSTEKQTARRADREKE-----DKGQESVGSEVETLSIQVTSLFKELQE-------AHTKLSEAELMKKRLQEKC 180
Cdd:PRK02224 342 EEAESLREDADDLEERAEELREeaaelESELEEAREAVEDRREEIEELEEEIEElrerfgdAPVDLGNAEDFLEELREER 421

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 181 QALERKNSATPSELNEKQELVYSNKKL-----------ELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKA 249
Cdd:PRK02224 422 DELREREAELEATLRTARERVEEAEALleagkcpecgqPVEGSPHVETIEEDRERVEELEAELEDLEEEVEEVEERLERA 501

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 250 lktiEELTKQQAEkvdkmlLQELSEKLELAEQALASKQlqmdemkqtlAKQEEDLETMAVLRAQMEVYCSDFHAERAARE 329
Cdd:PRK02224 502 ----EDLVEAEDR------IERLEERREDLEELIAERR----------ETIEEKRERAEELRERAAELEAEAEEKREAAA 561

                        330       340
                 ....*....|....*....|....*
gi 568912557 330 KIHEEKEQLALQLAILLKENNDIEE 354
Cdd:PRK02224 562 EAEEEAEEAREEVAELNSKLAELKE 586
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 87-305 3.53e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.13  E-value: 3.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    87 LREGNQKVERLEVALREAKERISDFEKkanghsstEKQTARRAD---REKEDKGQESVGSEVETLSIQVTSLFKELQEAH 163
Cdd:TIGR02169  179 LEEVEENIERLDLIIDEKRQQLERLRR--------EREKAERYQallKEKREYEGYELLKEKEALERQKEAIERQLASLE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   164 tklSEAELMKKRLQEKCQALERKNsATPSELNEKQELVYSNKKLELQ--VESMRSEIKMEQAKTEEEKSRLATLQATHNK 241
Cdd:TIGR02169  251 ---EELEKLTEEISELEKRLEEIE-QLLEELNKKIKDLGEEEQLRVKekIGELEAEIASLERSIAEKERELEDAEERLAK 326

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557   242 LLQEHNKALKTIEELTKQQAE-KVDKMLLQE----LSEKLELAEQALASKQLQMDEMKQTLAKQEEDLE 305
Cdd:TIGR02169  327 LEAEIDKLLAEIEELEREIEEeRKRRDKLTEeyaeLKEELEDLRAELEEVDKEFAETRDELKDYREKLE 395
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 115-330 4.57e-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: 4.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 115 ANGHSSTEKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSEL 194
Cdd:COG4942   13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEI 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 195 N------EKQELVYSNKKLELQVESMRSEIKM-----EQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEK 263
Cdd:COG4942   93 AelraelEAQKEELAELLRALYRLGRQPPLALllspeDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAE 172

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557 264 VDKM--LLQELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQMEVYCSDFHAERAAREK 330
Cdd:COG4942  173 RAELeaLLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAAE 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 158-306 4.63e-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: 41.45  E-value: 4.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 158 ELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysnKKLELQVESMRSEIKMEQAKTEEEKSRLATLQA 237
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---EDLEKEIKRLELEIEEVEARIKKYEEQLGNVRN 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557 238 THnkllqEHNKALKTIEELTKQQAEKVDKMLlqELSEKLELAEQALASKQLQMDEMKQTLAKQEEDLET 306
Cdd:COG1579   88 NK-----EYEALQKEIESLKRRISDLEDEIL--ELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
PTZ00121 PTZ00121
MAEBL; Provisional
 87-361 9.70e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 9.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   87 LREGNQKVERLEVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQESVGSEV-----ETLSIQVTSLF----- 156
Cdd:PTZ00121 1527 AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDKNMALRKAEEakkaeEARIEEVMKLYeeekk 1606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  157 ---KELQEAHTKLSEAELMKKRLQEKCQALERKNSAT----PSELNEKQELVYSNKKLELQVESMRSEIKMEQAKTEEEK 229
Cdd:PTZ00121 1607 mkaEEAKKAEEAKIKAEELKKAEEEKKKVEQLKKKEAeekkKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEED 1686

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  230 SRLATLQathnklLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKLELAEQALASKQLQMDEMK-QTLAKQEEDLETMA 308
Cdd:PTZ00121 1687 EKKAAEA------LKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKaEEAKKDEEEKKKIA 1760

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 568912557  309 VLRAQMEVYCSDFHAERAA--REKIHEEKEQLALQLAILLKENND----IEEGGSRQSL 361
Cdd:PTZ00121 1761 HLKKEEEKKAEEIRKEKEAviEEELDEEDEKRRMEVDKKIKDIFDnfanIIEGGKEGNL 1819
PRK12704 PRK12704
phosphodiesterase; Provisional
 157-326 1.31e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 157 KELQEAHTKLSEAElmkKRLQEKCQALERKnsatpSELNEKQElvysnkklelqvesmrSEIKMEQAKTEEEKSRLATLQ 236
Cdd:PRK12704  75 KELRERRNELQKLE---KRLLQKEENLDRK-----LELLEKRE----------------EELEKKEKELEQKQQELEKKE 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 237 ATHNKLLQEHNKALKTIEELTKQQAEkvdKMLLQELSEKLElAEQALASKQLQMDemkqtlAKQEEDLETMAVLRAQMEV 316
Cdd:PRK12704 131 EELEELIEEQLQELERISGLTAEEAK---EILLEKVEEEAR-HEAAVLIKEIEEE------AKEEADKKAKEILAQAIQR 200

                        170
                 ....*....|
gi 568912557 317 YCSDFHAERA 326
Cdd:PRK12704 201 CAADHVAETT 210
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 122-300 1.86e-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: 40.72  E-value: 1.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   122 EKQTARRADREKEDKGQESVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATP--------SE 193
Cdd:TIGR00618  225 EKELKHLREALQQTQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPlaahikavTQ 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   194 LNEKQELVY----SNKKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLL 269
Cdd:TIGR00618  305 IEQQAQRIHtelqSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTL 384

                          170       180       190
                   ....*....|....*....|....*....|.
gi 568912557   270 QELSEKLELAEQALASKQLQMDEMKQTLAKQ 300
Cdd:TIGR00618  385 QQQKTTLTQKLQSLCKELDILQREQATIDTR 415
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
145-326 1.92e-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: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  145 VETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELN-------------EKQELVYSNKKLElQV 211
Cdd:COG4913   612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaeleaELERLDASSDDLA-AL 690

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  212 ESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKMLLQELSEKL--ELAEQALASKQLQ 289
Cdd:COG4913   691 EEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFaaALGDAVERELREN 770

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 568912557  290 MDEMKQTLAKQEEDLETMavLRAQMEVYCSDFHAERA 326
Cdd:COG4913   771 LEERIDALRARLNRAEEE--LERAMRAFNREWPAETA 805
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 205-315 3.01e-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: 39.28  E-value: 3.01e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 205 KKLELQVESMRSEIKMEQAKTEEEKSRLATLQATHNKLLQEHNKAL--KTIEELTKQQAEKVDkmllqelseklELAEQA 282
Cdd:cd22656  131 KKYQDKAAKVVDKLTDFENQTEKDQTALETLEKALKDLLTDEGGAIarKEIKDLQKELEKLNE-----------EYAAKL 199

                         90       100       110
                 ....*....|....*....|....*....|...
gi 568912557 283 LAskqlQMDEMKQTLAKQEEDLETMAVLRAQME 315
Cdd:cd22656  200 KA----KIDELKALIADDEAKLAAALRLIADLT 228
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 129-315 4.88e-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: 4.88e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 129 ADREKEDKGQE--SVGSEVETLSIQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSATPSELNEKQELVysNKK 206
Cdd:COG3883   14 ADPQIQAKQKElsELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREEL--GER 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557 207 LELQVESMRSEIKMEQ---AKTEEE----KSRLATLQATHNKLLQEHNKALKTIEELTKQQAEKVDKM--LLQELSEKLE 277
Cdd:COG3883   92 ARALYRSGGSVSYLDVllgSESFSDfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELeaLKAELEAAKA 171

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 568912557 278 LAEQALASKQLQMDEMKQTLAKQEEDLETMAVLRAQME 315
Cdd:COG3883  172 ELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAE 209
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 92-262 6.38e-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: 6.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557    92 QKVERLEVALREAKERISDFEK--------KANGHSSTEKQTARRADREKEDKGQESvgsEVETLSIQVTSLFKELQEAH 163
Cdd:TIGR02169  833 KEIQELQEQRIDLKEQIKSIEKeienlngkKEELEEELEELEAALRDLESRLGDLKK---ERDELEAQLRELERKIEELE 909

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   164 TKLSEAELMKKRLQEKCQALERKNSA---TPSELNEKQELVYSNKKLELQVESMRSEI-KMEQAKT------EEEKSRLA 233
Cdd:TIGR02169  910 AQIEKKRKRLSELKAKLEALEEELSEiedPKGEDEEIPEEELSLEDVQAELQRVEEEIrALEPVNMlaiqeyEEVLKRLD 989

                          170       180
                   ....*....|....*....|....*....
gi 568912557   234 TLQATHNKLLQEHNKALKTIEELTKQQAE 262
Cdd:TIGR02169  990 ELKEKRAKLEEERKAILERIEEYEKKKRE 1018
mukB PRK04863
chromosome partition protein MukB;
98-307 9.66e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 38.40  E-value: 9.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557   98 EVALREAKERISDFEKKANGHSSTEKQTARRADREKEDKGQ-------------ESVGSEVETLSIQVT----------- 153
Cdd:PRK04863  836 EAELRQLNRRRVELERALADHESQEQQQRSQLEQAKEGLSAlnrllprlnlladETLADRVEEIREQLDeaeeakrfvqq 915

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  154 ------------SLFKELQEAHTKLS----EAELMKKRLQEKCQAL----ERKN----SATPSELNEKQELVYSNKKLEL 209
Cdd:PRK04863  916 hgnalaqlepivSVLQSDPEQFEQLKqdyqQAQQTQRDAKQQAFALtevvQRRAhfsyEDAAEMLAKNSDLNEKLRQRLE 995

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568912557  210 QVESMRSEIKME----QAKTEEEKSRLATLQATHNKLLQEHNKALKTIEELTKQ---QAEKVDKMLLQELSEKL------ 276
Cdd:PRK04863  996 QAEQERTRAREQlrqaQAQLAQYNQVLASLKSSYDAKRQMLQELKQELQDLGVPadsGAEERARARRDELHARLsanrsr 1075

                         250       260       270
                  ....*....|....*....|....*....|..
gi 568912557  277 -ELAEQALASKQLQMDEMKQTLAKQEEDLETM 307
Cdd:PRK04863 1076 rNQLEKQLTFCEAEMDNLTKKLRKLERDYHEM 1107
 
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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