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Conserved domains on  [gi|528972591|ref|XP_005214269|]
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optineurin isoform X2 [Bos taurus]

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 ...
 402-501 2.05e-25

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: 100.44  E-value: 2.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  402 EELKRRESEKVDKVVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIHE 481
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90       100
                  ....*....|....*....|
gi 528972591  482 EKEQLALQLAVLLKENNAFE 501
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQQLK 100
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
 37-103 2.74e-20

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


:

Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 84.84  E-value: 2.74e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528972591   37 PHELLQQMRELLIENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLYFETQSKEAKERLTALSLE 103
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
zf_C2H2_10 super family cl39752
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 546-571 1.71e-11

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


The actual alignment was detected with superfamily member pfam18414:

Pssm-ID: 436483  Cd Length: 26  Bit Score: 58.76  E-value: 1.71e-11
                          10        20
                  ....*....|....*....|....*.
gi 528972591  546 PIHSCPKCGEVLPDIDTLLIHVTDCI 571
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 198-452 6.77e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 6.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   198 SPGPTRTDSVDTSKSAEGTRNYVEFEELTVSqllhcLREGNQKVERLEVALKEAKERISDFEK----KAKDHSETETQTE 273
Cdd:TIGR02168  662 TGGSAKTNSSILERRREIEELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   274 EHTEQEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQElVYKNK 353
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   354 KLELQveSMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNNALKTIEELKRRESEKVDKvvLQELSGKLELAEKALAS 433
Cdd:TIGR02168  816 NEEAA--NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALAL 891

                          250
                   ....*....|....*....
gi 528972591   434 KQLQMDGMKQTIAKQEKDL 452
Cdd:TIGR02168  892 LRSELEELSEELRELESKR 910
 
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 ...
 402-501 2.05e-25

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: 100.44  E-value: 2.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  402 EELKRRESEKVDKVVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIHE 481
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90       100
                  ....*....|....*....|
gi 528972591  482 EKEQLALQLAVLLKENNAFE 501
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQQLK 100
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 415-501 1.83e-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: 91.64  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 415 VVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLL 494
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 528972591 495 KENNAFE 501
Cdd:cd09803   81 RENQELK 87
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
 37-103 2.74e-20

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


Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 84.84  E-value: 2.74e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528972591   37 PHELLQQMRELLIENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLYFETQSKEAKERLTALSLE 103
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 546-571 1.71e-11

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


Pssm-ID: 436483  Cd Length: 26  Bit Score: 58.76  E-value: 1.71e-11
                          10        20
                  ....*....|....*....|....*.
gi 528972591  546 PIHSCPKCGEVLPDIDTLLIHVTDCI 571
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 198-452 6.77e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 6.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   198 SPGPTRTDSVDTSKSAEGTRNYVEFEELTVSqllhcLREGNQKVERLEVALKEAKERISDFEK----KAKDHSETETQTE 273
Cdd:TIGR02168  662 TGGSAKTNSSILERRREIEELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   274 EHTEQEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQElVYKNK 353
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   354 KLELQveSMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNNALKTIEELKRRESEKVDKvvLQELSGKLELAEKALAS 433
Cdd:TIGR02168  816 NEEAA--NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALAL 891

                          250
                   ....*....|....*....
gi 528972591   434 KQLQMDGMKQTIAKQEKDL 452
Cdd:TIGR02168  892 LRSELEELSEELRELESKR 910
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-538 4.78e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 223 EELTVSQLLHCLREGNQKVERLEVALKEAKERISDFEKKAKDHSETETQTEEHTEQEKEEEKDTKTIGSEVETLNLQVTT 302
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 303 LFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQELVyknKKLELQVESMRSEIKMEQAKTEDEKSRLGT 382
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL---EEAEEELEEAEAELAEAEEALLEAEAELAE 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 383 LQLTHNRLLQEYNNALKTIEELKRRESEKvdKVVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQM 462
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528972591 463 EVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENNAFEDGGRQTLMEMQSRHGA--RASDADQQAYLVQRGAEDRNW 538
Cdd:COG1196  455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGV 532
PTZ00121 PTZ00121
MAEBL; Provisional
 78-435 8.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   78 KQKEERLYFETQSKEAKERLTALSLENEKLKQELGTLTGKTERAFEDIIGDPKVPKAEVEQEVEQLKTQVARlqaeKADL 157
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----KADE 1282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  158 LGIVSELQLKLNSSGSSEDSFVEIRMAEGEAAVAAKEIKPSPGPTRTDSVDTSKSAEGTRNYVEFEELTVSQLLHCLREG 237
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  238 NQKVERLEVALKEAKERISDFEKKAKDHSETETQTEEHTEQEKEEekdtktigsevetlnlqvttlfKELQEAHTKLSEA 317
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----------------------DELKKAAAAKKKA 1420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  318 ELMKKRLQEKCQALERKNSASpselnEKQELVYKNKKLELQVESMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNNA 397
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAE-----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 528972591  398 LKTIEELKRRESE--KVDKVVLQELSGKLELAEKALASKQ 435
Cdd:PTZ00121 1496 KKKADEAKKAAEAkkKADEAKKAEEAKKADEAKKAEEAKK 1535
 
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 ...
 402-501 2.05e-25

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: 100.44  E-value: 2.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  402 EELKRRESEKVDKVVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIHE 481
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90       100
                  ....*....|....*....|
gi 528972591  482 EKEQLALQLAVLLKENNAFE 501
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQQLK 100
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 415-501 1.83e-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: 91.64  E-value: 1.83e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 415 VVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLL 494
Cdd:cd09803    1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                 ....*..
gi 528972591 495 KENNAFE 501
Cdd:cd09803   81 RENQELK 87
NEMO pfam11577
NF-kappa-B essential modulator NEMO; NEMO is a regulatory protein which is part of the IKK ...
 37-103 2.74e-20

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


Pssm-ID: 431942 [Multi-domain]  Cd Length: 67  Bit Score: 84.84  E-value: 2.74e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528972591   37 PHELLQQMRELLIENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLYFETQSKEAKERLTALSLE 103
Cdd:pfam11577   1 DEETLEQMKELLTENHQLKEAMKQSNQAMKERCEELSAWQEKQKEEREFLECRFREARELLRRLSLE 67
zf_C2H2_10 pfam18414
C2H2 type zinc-finger; This is a zinc finger domain C2H2 which can be found in optineurin ...
 546-571 1.71e-11

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


Pssm-ID: 436483  Cd Length: 26  Bit Score: 58.76  E-value: 1.71e-11
                          10        20
                  ....*....|....*....|....*.
gi 528972591  546 PIHSCPKCGEVLPDIDTLLIHVTDCI 571
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 198-452 6.77e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 49.28  E-value: 6.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   198 SPGPTRTDSVDTSKSAEGTRNYVEFEELTVSqllhcLREGNQKVERLEVALKEAKERISDFEK----KAKDHSETETQTE 273
Cdd:TIGR02168  662 TGGSAKTNSSILERRREIEELEEKIEELEEK-----IAELEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLA 736

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   274 EHTEQEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQElVYKNK 353
Cdd:TIGR02168  737 RLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRA-ELTLL 815

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   354 KLELQveSMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNNALKTIEELKRRESEKVDKvvLQELSGKLELAEKALAS 433
Cdd:TIGR02168  816 NEEAA--NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESE--LEALLNERASLEEALAL 891

                          250
                   ....*....|....*....
gi 528972591   434 KQLQMDGMKQTIAKQEKDL 452
Cdd:TIGR02168  892 LRSELEELSEELRELESKR 910
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 221-514 4.60e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   221 EFEELTVSQLLHCLREGNQKVERLEVALKEAKERISDFEKKakdhsetetqteehteqEKEEEKDTKTIGSEVETLNLQV 300
Cdd:TIGR02168  221 ELRELELALLVLRLEELREELEELQEELKEAEEELEELTAE-----------------LQELEEKLEELRLEVSELEEEI 283

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   301 TTLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQElvyKNKKLELQVESMRSEIKMEQAKTEDEKSRL 380
Cdd:TIGR02168  284 EELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAEL 360

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   381 GTLqlthNRLLQEYNNALKTIEELKRRESEKVDKVVLQE--LSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVL 458
Cdd:TIGR02168  361 EEL----EAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELK 436

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 528972591   459 RAQMEvyCSDFHAERAAREKIHEEKEQLALQLAVLLKENNAFEDGGRQTLMEMQSR 514
Cdd:TIGR02168  437 ELQAE--LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 223-538 4.78e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 4.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 223 EELTVSQLLHCLREGNQKVERLEVALKEAKERISDFEKKAKDHSETETQTEEHTEQEKEEEKDTKTIGSEVETLNLQVTT 302
Cdd:COG1196  220 EELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELAR 299

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 303 LFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQELVyknKKLELQVESMRSEIKMEQAKTEDEKSRLGT 382
Cdd:COG1196  300 LEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEEL---EEAEEELEEAEAELAEAEEALLEAEAELAE 376

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 383 LQLTHNRLLQEYNNALKTIEELKRRESEKvdKVVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQM 462
Cdd:COG1196  377 AEEELEELAEELLEALRAAAELAAQLEEL--EEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAEL 454

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 528972591 463 EVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENNAFEDGGRQTLMEMQSRHGA--RASDADQQAYLVQRGAEDRNW 538
Cdd:COG1196  455 EEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGV 532
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 239-546 4.96e-05

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.59  E-value: 4.96e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   239 QKVERLEVALKEAKERIS--DFEKKAKDHSETETQTEEHTEQEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTKL-- 314
Cdd:TIGR02168  213 ERYKELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELya 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   315 -----SEAELMKKRLQEKCQALERKNSASPSELNEKQElvyKNKKLELQVESMRSEIKMEQAKTEDEKSRLGTLqlthNR 389
Cdd:TIGR02168  293 laneiSRLEQQKQILRERLANLERQLEELEAQLEELES---KLDELAEELAELEEKLEELKEELESLEAELEEL----EA 365

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   390 LLQEYNNALKTIEELKRRESEKVDKVVLQE--LSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEvyCS 467
Cdd:TIGR02168  366 ELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE--LE 443

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528972591   468 DFHAERAAREKIHEEKEQLALQLAVLLKENNAFEDGGRQTLMEMQSRhgaRASDADQQAYLVQRGAEDRNWLQQQQNIP 546
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR---LDSLERLQENLEGFSEGVKALLKNQSGLS 519
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 306-463 9.24e-05

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: 44.15  E-value: 9.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 306 ELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQELVyknKKLELQVESMRSEIKMEQAKTEDEKSRLGTLql 385
Cdd:COG1579   11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---EDLEKEIKRLELEIEEVEARIKKYEEQLGNV-- 85

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528972591 386 thnRLLQEYNNALKTIEELKRRESEKVDKvvLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLET-MAVLRAQME 463
Cdd:COG1579   86 ---RNNKEYEALQKEIESLKRRISDLEDE--ILELMERIEELEEELAELEAELAELEAELEEKKAELDEeLAELEAELE 159
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
317-431 1.64e-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: 1.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 317 AELMKKRLQEKCQALERKNSASPSELNEKQElvyKNKKLELQVESMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNN 396
Cdd:COG2433  383 EELIEKELPEEEPEAEREKEHEERELTEEEE---EIRRLEEQVERLEAEVEELEAELEEKDERIERLERELSEARSEERR 459

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 528972591 397 ALKTIEELKRRESE------KVDKV--VLQELSGKLELAEKAL 431
Cdd:COG2433  460 EIRKDREISRLDREierlerELEEEreRIEELKRKLERLKELW 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 234-463 1.88e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 44.66  E-value: 1.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   234 LREGNQKVERLEVALKEAKERISDFEKKAKdhsetetqteehteqekeEEKDTKTIGSEVETLNLQVTTLfkELQEAHTK 313
Cdd:TIGR02168  181 LERTRENLDRLEDILNELERQLKSLERQAE------------------KAERYKELKAELRELELALLVL--RLEELREE 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   314 LSEAELMKKRLQEKCQALERKNSASPSELNEKQELVYKNKKLELQVESMRSEIKMEQAKTEDEK----SRLGTLQLTHNR 389
Cdd:TIGR02168  241 LEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKqilrERLANLERQLEE 320

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 528972591   390 LLQEYNNALKTIEELKRRESEKVDKvvLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMAVLRAQME 463
Cdd:TIGR02168  321 LEAQLEELESKLDELAEELAELEEK--LEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLE 392
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 77-405 2.21e-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: 44.29  E-value: 2.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591    77 EKQKEERLYFETQSK--EAKERLTALSLENEKLKQELGTLTGKTERAFEDIigdpkvpkAEVEQEVEQLKTQVARLQAEK 154
Cdd:TIGR02169  696 ELRRIENRLDELSQElsDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDL--------SSLEQEIENVKSELKELEARI 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   155 ADLLGIVSELQLKLNSSGSSED-----------SFVEIRMAEGEAAVAAKEIKPSPGPTRTDSVDtsKSAEGTRNYVEFE 223
Cdd:TIGR02169  768 EELEEDLHKLEEALNDLEARLShsripeiqaelSKLEEEVSRIEARLREIEQKLNRLTLEKEYLE--KEIQELQEQRIDL 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   224 ELTVSQLLHCLREGNQKVERLEVALKEAKERISDFEKKAKDhsetetqteehteqekeeekdtktIGSEVETLNLQVTTL 303
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD------------------------LKKERDELEAQLREL 901

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   304 FKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQELVYKNKKLElqvesmrsEIKMEQAKTEDEKSRLGTL 383
Cdd:TIGR02169  902 ERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLE--------DVQAELQRVEEEIRALEPV 973

                          330       340
                   ....*....|....*....|..
gi 528972591   384 qltHNRLLQEYNNALKTIEELK 405
Cdd:TIGR02169  974 ---NMLAIQEYEEVLKRLDELK 992
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 70-407 4.99e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.12  E-value: 4.99e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591    70 EELSAWTEKQKEERLYFETQSKEAKERLTALSLENEKLKQELGTLTGKTERAFEDIigdpkvpkAEVEQEVEQLKTQVAR 149
Cdd:TIGR02168  680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDL--------ARLEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   150 LQAEKADLLGIVSELQLKLNSSgSSEDSFVEIRMAEGEAAVAAKEIKPSPGPTRTDSV-----DTSKSAEGTRNYVEFEE 224
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALREALDELraeltLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   225 LTVSQLLHCLREGNQKVERLEVALKEAKERISDFEKKAKDHSETETQTEEHTEQEKEEEKDTKtigSEVETLNLQVTTLF 304
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLR---SELEELSEELRELE 907

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   305 KELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSELNEKQELVYKN-KKLELQVESMRSEIKMEQAKTEDEKSRLGTL 383
Cdd:TIGR02168  908 SKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEaEALENKIEDDEEEARRRLKRLENKIKELGPV 987

                          330       340
                   ....*....|....*....|....
gi 528972591   384 QLThnrllqeynnALKTIEELKRR 407
Cdd:TIGR02168  988 NLA----------AIEEYEELKER 1001
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 40-409 6.55e-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: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591    40 LLQQMRELLIENHQLKEAMklnnQAMKGRFEELSAWTEKQKEERLYFETQSKEAKERLTALSLENEKLKQELGTLTGKTE 119
Cdd:TIGR02169  693 LQSELRRIENRLDELSQEL----SDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIE 768

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   120 RAFEDI------IGDPKvpKAEVEQEVEQLKTQVARLQAEKADLLGIVSELQLKLNSSgSSEDSFVEIRMAEGEAAVAAK 193
Cdd:TIGR02169  769 ELEEDLhkleeaLNDLE--ARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRL-TLEKEYLEKEIQELQEQRIDL 845

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   194 EIKPSPGPTRTDSVDTSKsaegtrnyvefeeltvsqllhclREGNQKVERLEVALKEAKERISDFEKKAKDHsetetqte 273
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKK-----------------------EELEEELEELEAALRDLESRLGDLKKERDEL-------- 894

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   274 ehTEQEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTKLSEAELMKKRLQEkcqalerknsaSPSELNEKQELVYKNK 353
Cdd:TIGR02169  895 --EAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEE-----------IPEEELSLEDVQAELQ 961

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 528972591   354 KLELQVESMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNNALKTIEEL--KRRES 409
Cdd:TIGR02169  962 RVEEEIRALEPVNMLAIQEYEEVLKRLDELKEKRAKLEEERKAILERIEEYekKKREV 1019
PTZ00121 PTZ00121
MAEBL; Provisional
 78-435 8.49e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 42.44  E-value: 8.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591   78 KQKEERLYFETQSKEAKERLTALSLENEKLKQELGTLTGKTERAFEDIIGDPKVPKAEVEQEVEQLKTQVARlqaeKADL 157
Cdd:PTZ00121 1207 KAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKFEEARMAHFARRQAAIKAEEAR----KADE 1282

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  158 LGIVSELQLKLNSSGSSEDSFVEIRMAEGEAAVAAKEIKPSPGPTRTDSVDTSKSAEGTRNYVEFEELTVSQLLHCLREG 237
Cdd:PTZ00121 1283 LKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAA 1362

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  238 NQKVERLEVALKEAKERISDFEKKAKDHSETETQTEEHTEQEKEEekdtktigsevetlnlqvttlfKELQEAHTKLSEA 317
Cdd:PTZ00121 1363 EEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKKKA----------------------DELKKAAAAKKKA 1420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  318 ELMKKRLQEKCQALERKNSASpselnEKQELVYKNKKLELQVESMRSEIKMEQAKTEDEKSRLGTLQLTHNRLLQEYNNA 397
Cdd:PTZ00121 1421 DEAKKKAEEKKKADEAKKKAE-----EAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEA 1495

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 528972591  398 LKTIEELKRRESE--KVDKVVLQELSGKLELAEKALASKQ 435
Cdd:PTZ00121 1496 KKKADEAKKAAEAkkKADEAKKAEEAKKADEAKKAEEAKK 1535
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 40-543 3.14e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 3.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  40 LLQQMRELLIENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERLYFETQSKEAKERLTALSLENEKLKQELGTLTGKTE 119
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 120 R--AFEDIIGDPKVPKAEVEQEVEQLKTQVARLQAEKADLLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAAVAAKEikp 197
Cdd:COG1196  310 RrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE--- 386

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 198 spgptrtDSVDTSKSAEGTRNYVEFEELTVSQLLhclregnQKVERLEVALKEAKERISDFEKKAKDHSETETQTEEHTE 277
Cdd:COG1196  387 -------ELLEALRAAAELAAQLEELEEAEEALL-------ERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEA 452

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 278 QEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTKLSEAELMKKRLQEkcQALERKNSASPSELNEKQELVYKNKKLEL 357
Cdd:COG1196  453 ELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEA--DYEGFLEGVKAALLLAGLRGLAGAVAVLI 530

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 358 QVEsmrseikmEQAKTEDEKSRLGTLQLTHNRLLQEynnALKTIEELKRRESEKVDKVVLQELSGKLELAEK-------- 429
Cdd:COG1196  531 GVE--------AAYEAALEAALAAALQNIVVEDDEV---AAAAIEYLKAAKAGRATFLPLDKIRARAALAAAlargaiga 599

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 430 --ALASKQLQMDGMKQTIAKQEKDLETMAVLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENNAFEDGGRQT 507
Cdd:COG1196  600 avDLVASDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEA 679

                        490       500       510
                 ....*....|....*....|....*....|....*.
gi 528972591 508 LMEMQSRHGARASDADQQAYLVQRGAEDRNWLQQQQ 543
Cdd:COG1196  680 ELEELAERLAEEELELEEALLAEEEEERELAEAEEE 715
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 238-456 5.21e-03

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


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 39.36  E-value: 5.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 238 NQKVERLEVALKEAKERISDFEKK----AKDHSETETQTEEHTEQEKEEEKDTKTIGSEVETLNLQVTTLFKELQEAHTK 313
Cdd:COG4942   19 ADAAAEAEAELEQLQQEIAELEKElaalKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 314 LSEaelMKKRLQEKCQALERKNSASPSEL----NEKQELVYKNKKLELQVESMRSEIKMEQAKTEDEKSRLGTLQLTHNR 389
Cdd:COG4942   99 LEA---QKEELAELLRALYRLGRQPPLALllspEDFLDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAE 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528972591 390 LLQEYNNALKTIEELKRRESEKvdKVVLQELSGKLELAEKALASKQLQMDGMKQTIAKQEKDLETMA 456
Cdd:COG4942  176 LEALLAELEEERAALEALKAER--QKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
56-484 8.00e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 39.25  E-value: 8.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591  56 EAMKLNNQAMKGRFEELSAWTEKQKEERLYFETQSKEAKERLTALSLENEKLKQELGTLTGKTERAFEDIiGDPKVPKAE 135
Cdd:PRK02224 310 EAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAV-EDRREEIEE 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 136 VEQEVEQLKTQVA--------------RLQAEKADLLGIVSELQLKLNSsgssedsfVEIRMAEGEAAVAAKEIkpspgP 201
Cdd:PRK02224 389 LEEEIEELRERFGdapvdlgnaedfleELREERDELREREAELEATLRT--------ARERVEEAEALLEAGKC-----P 455

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 202 TRTDSVDTSKSAEGT---RNYVEFEELTVSQLLHCLREGNQKVERLEvALKEAKERISDFEKKAKDHSETETQTEEHTEQ 278
Cdd:PRK02224 456 ECGQPVEGSPHVETIeedRERVEELEAELEDLEEEVEEVEERLERAE-DLVEAEDRIERLEERREDLEELIAERRETIEE 534

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 279 EKEEekdtktigseVETLNLQVTTLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSASPSE---LNEKQELVYKNKKL 355
Cdd:PRK02224 535 KRER----------AEELRERAAELEAEAEEKREAAAEAEEEAEEAREEVAELNSKLAELKERiesLERIRTLLAAIADA 604

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528972591 356 ELQVESMRSEIKMEQAKTEDEKSRLGTLQlthnrllqeynnalktieELKRRESEKVDKVVLQELSGKLELAEKALA--- 432
Cdd:PRK02224 605 EDEIERLREKREALAELNDERRERLAEKR------------------ERKRELEAEFDEARIEEAREDKERAEEYLEqve 666

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 528972591 433 ----SKQLQMDGMKQTIAKQEKDLETMAVLRAQMEvycsDFHAERAAREKIHEEKE 484
Cdd:PRK02224 667 ekldELREERDDLQAEIGAVENELEELEELRERRE----ALENRVEALEALYDEAE 718
 
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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