NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|20149572|ref|NP_068815|]
View 

optineurin [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CC2-LZ pfam16516
Leucine zipper of domain CC2 of NEMO, NF-kappa-B essential modulator; CC2-LZ is a ...
 408-507 2.97e-24

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: 96.98  E-value: 2.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   408 EELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHE 487
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90       100
                  ....*....|....*....|
gi 20149572   488 EKEQLALQLAVLLKENDAFE 507
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 9.54e-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: 83.30  E-value: 9.54e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20149572    37 PEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHE 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 ...
 551-576 6.27e-14

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: 65.69  E-value: 6.27e-14
                          10        20
                  ....*....|....*....|....*.
gi 20149572   551 PIHSCPKCGEVLPDIDTLQIHVMDCI 576
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 245-520 5.40e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    245 QKVERLEVALKEAKERVS--DFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKL-- 320
Cdd:TIGR02168  213 ERYKELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELya 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    321 -----SEAELMKKRLQEKCQALERKNSAIPSELNEKQelvytNKKLELQVESMLSEIKMEQAKT--EDEKSKLTVLqmth 393
Cdd:TIGR02168  293 laneiSRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEELKEelESLEAELEEL---- 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    394 NKLLQEHNNALKTIEELTRKESEKVDRAVLKE--LSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEvy 471
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-- 441

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 20149572    472 CSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSR 520
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
 
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 ...
 408-507 2.97e-24

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: 96.98  E-value: 2.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   408 EELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHE 487
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90       100
                  ....*....|....*....|
gi 20149572   488 EKEQLALQLAVLLKENDAFE 507
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQQLK 100
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 421-507 2.71e-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: 91.26  E-value: 2.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 421 AVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLL 500
Cdd:cd09803   1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                ....*..
gi 20149572 501 KENDAFE 507
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 9.54e-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: 83.30  E-value: 9.54e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20149572    37 PEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHE 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 ...
 551-576 6.27e-14

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: 65.69  E-value: 6.27e-14
                          10        20
                  ....*....|....*....|....*.
gi 20149572   551 PIHSCPKCGEVLPDIDTLQIHVMDCI 576
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 245-520 5.40e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    245 QKVERLEVALKEAKERVS--DFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKL-- 320
Cdd:TIGR02168  213 ERYKELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELya 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    321 -----SEAELMKKRLQEKCQALERKNSAIPSELNEKQelvytNKKLELQVESMLSEIKMEQAKT--EDEKSKLTVLqmth 393
Cdd:TIGR02168  293 laneiSRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEELKEelESLEAELEEL---- 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    394 NKLLQEHNNALKTIEELTRKESEKVDRAVLKE--LSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEvy 471
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-- 441

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 20149572    472 CSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSR 520
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 254-551 5.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 254 LKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEK 333
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 334 CQALERKNSAIPSEL----NEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEE 409
Cdd:COG1196 304 IARLEERRRELEERLeeleEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 410 LTRKESEKVDRAVlkELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEvycsdfHAERAAREKIHEEK 489
Cdd:COG1196 384 LAEELLEALRAAA--ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------EALEEAAEEEAELE 455

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20149572 490 EQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIP 551
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
PTZ00121 PTZ00121
MAEBL; Provisional
 78-457 2.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    78 KQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRT-QVVRLQAEKAD 156
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfEEARMAHFARR 1268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   157 LLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKnyfeheeltvsql 236
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK------------- 1335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   237 llclREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETV--GSEVEALNLQVTSLFKELQ 314
Cdd:PTZ00121 1336 ----KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELK 1411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   315 EAHTKLSEAELMKKRLQEKCQALERKNSAipselNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHN 394
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20149572   395 KLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEED 457
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 230-549 6.73e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    230 ELTVSQLLLCLREGNQ----KVERLE-------VALKEAKERVSDFEKKTSNRSEI---------ETQTEGSTEKENDEE 289
Cdd:pfam15921  323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESGNLDDQlqklladlhKREKELSLEKEQNKR 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    290 KGPETVGSEVealnlQVTSLFKELQEAHTKLSEAELMKKRLQEKCQA-LERKNSAIPSElNEKQELVYTnkkLELQVES- 367
Cdd:pfam15921  403 LWDRDTGNSI-----TIDHLRRELDDRNMEVQRLEALLKAMKSECQGqMERQMAAIQGK-NESLEKVSS---LTAQLESt 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    368 --MLSEI--KMEQAKTEDEKSKLTVLQMTHNklLQEHNNALKTIEELTRKESEKVDRAV-----LKELSEKLELAEKALA 438
Cdd:pfam15921  474 keMLRKVveELTAKKMTLESSERTVSDLTAS--LQEKERAIEATNAEITKLRSRVDLKLqelqhLKNEGDHLRNVQTECE 551

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    439 SKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEqlalqlaVLLKENDAFEDGGRQSLMEMQ 518
Cdd:pfam15921  552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR-------LELQEFKILKDKKDAKIRELE 624

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 20149572    519 srhgARTSDSD-QQAYLVQRGAED----RDWRQQRN 549
Cdd:pfam15921  625 ----ARVSDLElEKVKLVNAGSERlravKDIKQERD 656
 
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 ...
 408-507 2.97e-24

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: 96.98  E-value: 2.97e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   408 EELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHE 487
Cdd:pfam16516   1 EELKRKEMEKVYKDEIDCLQAQLQAAEEALAAKQREIDELKQEIAQKEEDLETISVLKAQAEVYRSDFEAERAAREKLHE 80

                          90       100
                  ....*....|....*....|
gi 20149572   488 EKEQLALQLAVLLKENDAFE 507
Cdd:pfam16516  81 EKEQLAAQLEYLQRQNQQLK 100
UBAN cd09803
polyubiquitin binding domain of NEMO and related proteins; NEMO (NF-kappaB essential modulator) ...
 421-507 2.71e-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: 91.26  E-value: 2.71e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 421 AVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLL 500
Cdd:cd09803   1 GEIDELAARLQEAEEALALKQEDIDELKEEIAQQEADLETIPVLKAQAEIYKSDFEAERAAREKLHQEKEQLAEQLEYLQ 80


                ....*..
gi 20149572 501 KENDAFE 507
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 9.54e-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: 83.30  E-value: 9.54e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20149572    37 PEELLQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKEERQFFEIQSKEAKERLMALSHE 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 ...
 551-576 6.27e-14

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: 65.69  E-value: 6.27e-14
                          10        20
                  ....*....|....*....|....*.
gi 20149572   551 PIHSCPKCGEVLPDIDTLQIHVMDCI 576
Cdd:pfam18414   1 PKHCCPKCQEQLPDIDTLQIHVMDCI 26
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 245-520 5.40e-07

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 52.75  E-value: 5.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    245 QKVERLEVALKEAKERVS--DFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKL-- 320
Cdd:TIGR02168  213 ERYKELKAELRELELALLvlRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELya 292

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    321 -----SEAELMKKRLQEKCQALERKNSAIPSELNEKQelvytNKKLELQVESMLSEIKMEQAKT--EDEKSKLTVLqmth 393
Cdd:TIGR02168  293 laneiSRLEQQKQILRERLANLERQLEELEAQLEELE-----SKLDELAEELAELEEKLEELKEelESLEAELEEL---- 363

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    394 NKLLQEHNNALKTIEELTRKESEKVDRAVLKE--LSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEvy 471
Cdd:TIGR02168  364 EAELEELESRLEELEEQLETLRSKVAQLELQIasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAE-- 441

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 20149572    472 CSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSR 520
Cdd:TIGR02168  442 LEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQAR 490
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 254-551 5.54e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 49.55  E-value: 5.54e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 254 LKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEK 333
Cdd:COG1196 224 ELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD 303

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 334 CQALERKNSAIPSEL----NEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEE 409
Cdd:COG1196 304 IARLEERRRELEERLeeleEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 410 LTRKESEKVDRAVlkELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEvycsdfHAERAAREKIHEEK 489
Cdd:COG1196 384 LAEELLEALRAAA--ELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEE------EALEEAAEEEAELE 455

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20149572 490 EQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSDQQAYLVQRGAEDRDWRQQRNIP 551
Cdd:COG1196 456 EEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLA 517
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 240-487 1.44e-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: 48.13  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    240 LREGNQKVERLEVALKEAKERVSDFEK----KTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQE 315
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKeleeLSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    316 AHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQ--------------------------------ELVYTNKKLEL 363
Cdd:TIGR02168  773 AEEELAEAEAEIEELEAQIEQLKEELKALREALDELRaeltllneeaanlrerleslerriaaterrleDLEEQIEELSE 852

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    364 QVESMLSEIKMEQAKTEDEKSKLTVLQmthnKLLQEHNNALKTIEELTRKESEKVD--RAVLKELSEKLELAEKALASKQ 441
Cdd:TIGR02168  853 DIESLAAEIEELEELIEELESELEALL----NERASLEEALALLRSELEELSEELRelESKRSELRRELEELREKLAQLE 928

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 20149572    442 LQMDEMKQTIAKQEEDL--ETMTILRAQMEVYCSDFHAERAAREKIHE 487
Cdd:TIGR02168  929 LRLEGLEVRIDNLQERLseEYSLTLEEAEALENKIEDDEEEARRRLKR 976
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 244-459 6.44e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 46.20  E-value: 6.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    244 NQKVERLEVALKEAKERVSDFEKktsNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEa 323
Cdd:TIGR02168  294 ANEISRLEQQKQILRERLANLER---QLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEE- 369

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    324 elMKKRLQEKCQALERKNSAIPSELNEKQELvytNKKLELQvESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNA 403
Cdd:TIGR02168  370 --LESRLEELEEQLETLRSKVAQLELQIASL---NNEIERL-EARLERLEDRRERLQQEIEELLKKLEEAELKELQAELE 443

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 20149572    404 LKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLE 459
Cdd:TIGR02168  444 ELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 77-416 1.41e-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: 45.06  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572     77 EKQKEERQFFEIQSK--EAKERLMALSHENEKLKEELGKLKGKSERSSEDptddsrlpRAEAEQEKDQLRTQVVRLQAEK 154
Cdd:TIGR02169  696 ELRRIENRLDELSQElsDASRKIGEIEKEIEQLEQEEEKLKERLEELEED--------LSSLEQEIENVKSELKELEARI 767

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    155 ADLLGIVSELQLKLNSsgssedsfVEIRMAEGEAEGSVKEIKhspgptrtvstgtALSKYRSRsADGAKNYFEHEELTVS 234
Cdd:TIGR02169  768 EELEEDLHKLEEALND--------LEARLSHSRIPEIQAELS-------------KLEEEVSR-IEARLREIEQKLNRLT 825

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    235 QLLLCLREgnqKVERLEVALKEAKERVSDFEKKTSN----RSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLF 310
Cdd:TIGR02169  826 LEKEYLEK---EIQELQEQRIDLKEQIKSIEKEIENlngkKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELE 902

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    311 KELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYTN---KKLELQVESMLSEI-KMEQAKT------E 380
Cdd:TIGR02169  903 RKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEElslEDVQAELQRVEEEIrALEPVNMlaiqeyE 982

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 20149572    381 DEKSKLTVLQMTHNKLLQEHNNALKTIEELTRKESE 416
Cdd:TIGR02169  983 EVLKRLDELKEKRAKLEEERKAILERIEEYEKKKRE 1018
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 245-483 1.50e-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: 45.06  E-value: 1.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    245 QKVERLEVALKEAKERVSDFEKKTSnrsEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLSEAE 324
Cdd:TIGR02169  695 SELRRIENRLDELSQELSDASRKIG---EIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELE 771

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    325 LMKKRLQEKCQALERK--NSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQmTHNKLLQEHNN 402
Cdd:TIGR02169  772 EDLHKLEEALNDLEARlsHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQ-EQRIDLKEQIK 850

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    403 ALKTIEELTRKESEKVDrAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAR 482
Cdd:TIGR02169  851 SIEKEIENLNGKKEELE-EELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEAL 929


                   .
gi 20149572    483 E 483
Cdd:TIGR02169  930 E 930
PTZ00121 PTZ00121
MAEBL; Provisional
 78-457 2.09e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 44.36  E-value: 2.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    78 KQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPTDDSRLPRAEAEQEKDQLRT-QVVRLQAEKAD 156
Cdd:PTZ00121 1189 KAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEEAKKAEEERNNEEIRKfEEARMAHFARR 1268

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   157 LLGIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKHSPGPTRTVSTGTALSKYRSRSADGAKnyfeheeltvsql 236
Cdd:PTZ00121 1269 QAAIKAEEARKADELKKAEEKKKADEAKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKKADAAK------------- 1335

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   237 llclREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEKENDEEKGPETV--GSEVEALNLQVTSLFKELQ 314
Cdd:PTZ00121 1336 ----KKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKkkADEAKKKAEEDKKKADELK 1411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   315 EAHTKLSEAELMKKRLQEKCQALERKNSAipselNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTHN 394
Cdd:PTZ00121 1412 KAAAAKKKADEAKKKAEEKKKADEAKKKA-----EEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKAD 1486

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20149572   395 KLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEED 457
Cdd:PTZ00121 1487 EAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKAD 1549
PTZ00121 PTZ00121
MAEBL; Provisional
 50-502 3.12e-04

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 43.98  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    50 ENHQLKEAMKLNNQAMKGrfEELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSE-----RSSED 124
Cdd:PTZ00121 1300 EKKKADEAKKKAEEAKKA--DEAKKKAEEAKKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaaekkKEEAK 1377

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   125 PTDDSRLPRAEAEQEKDQLRTQVVRLQaEKADLLGIVSELQLKLNSSGSSEDsfvEIRMAEgEAEGSVKEIKHSPGPTRT 204
Cdd:PTZ00121 1378 KKADAAKKKAEEKKKADEAKKKAEEDK-KKADELKKAAAAKKKADEAKKKAE---EKKKAD-EAKKKAEEAKKADEAKKK 1452

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   205 VStgtalskyRSRSADGAKNyfEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSEIETQTEGSTEK 284
Cdd:PTZ00121 1453 AE--------EAKKAEEAKK--KAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAK 1522

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   285 ENDEEKGPETVGSEVEALNLQVTSLFKELQEAHtKLSEAElMKKRLQEKCQALERKNSAI----------PSELNEKQEL 354
Cdd:PTZ00121 1523 KADEAKKAEEAKKADEAKKAEEKKKADELKKAE-ELKKAE-EKKKAEEAKKAEEDKNMALrkaeeakkaeEARIEEVMKL 1600

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   355 VYTNKKLELQVESMLSE--IKMEQA-KTEDEKSKLTVLQMTHNKLLQ--------EHNNALKTIEELTRKESEKVDRAVL 423
Cdd:PTZ00121 1601 YEEEKKMKAEEAKKAEEakIKAEELkKAEEEKKKVEQLKKKEAEEKKkaeelkkaEEENKIKAAEEAKKAEEDKKKAEEA 1680

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20149572   424 KELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVycSDFHAERAAREKIHEEKEQLALQLAVLLKE 502
Cdd:PTZ00121 1681 KKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEE--NKIKAEEAKKEAEEDKKKAEEAKKDEEEKK 1757
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 230-549 6.73e-04

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


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 42.80  E-value: 6.73e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    230 ELTVSQLLLCLREGNQ----KVERLE-------VALKEAKERVSDFEKKTSNRSEI---------ETQTEGSTEKENDEE 289
Cdd:pfam15921  323 ESTVSQLRSELREAKRmyedKIEELEkqlvlanSELTEARTERDQFSQESGNLDDQlqklladlhKREKELSLEKEQNKR 402

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    290 KGPETVGSEVealnlQVTSLFKELQEAHTKLSEAELMKKRLQEKCQA-LERKNSAIPSElNEKQELVYTnkkLELQVES- 367
Cdd:pfam15921  403 LWDRDTGNSI-----TIDHLRRELDDRNMEVQRLEALLKAMKSECQGqMERQMAAIQGK-NESLEKVSS---LTAQLESt 473

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    368 --MLSEI--KMEQAKTEDEKSKLTVLQMTHNklLQEHNNALKTIEELTRKESEKVDRAV-----LKELSEKLELAEKALA 438
Cdd:pfam15921  474 keMLRKVveELTAKKMTLESSERTVSDLTAS--LQEKERAIEATNAEITKLRSRVDLKLqelqhLKNEGDHLRNVQTECE 551

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    439 SKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKEqlalqlaVLLKENDAFEDGGRQSLMEMQ 518
Cdd:pfam15921  552 ALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRR-------LELQEFKILKDKKDAKIRELE 624

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 20149572    519 srhgARTSDSD-QQAYLVQRGAED----RDWRQQRN 549
Cdd:pfam15921  625 ----ARVSDLElEKVKLVNAGSERlravKDIKQERD 656
ClyA_Cry6Aa-like cd22656
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ...
 365-469 9.00e-04

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: 41.59  E-value: 9.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 365 VESMLSEIKMEQAKTEDEKSKLTVLQ---MTHNKLLQEHNnalKTIEELTRKESEKVDRAVLKELSEKLELAEKALASKQ 441
Cdd:cd22656 123 LDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLE---KALKDLLTDEGGAIARKEIKDLQKELEKLNEEYAAKL 199

                        90       100
                ....*....|....*....|....*....
gi 20149572 442 L-QMDEMKQTIAKQEEDLETMTILRAQME 469
Cdd:cd22656 200 KaKIDELKALIADDEAKLAAALRLIADLT 228
DUF3584 pfam12128
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ...
 70-531 2.36e-03

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


Pssm-ID: 432349 [Multi-domain]  Cd Length: 1191  Bit Score: 40.98  E-value: 2.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572     70 EELSAWTEKQKEERQFFEIQSKEAKERLMALSHENEKLKEELGKLKGKSERSSEDPT--DDSRLPRAEAEQEK-DQLRTQ 146
Cdd:pfam12128  276 SRQEERQETSAELNQLLRTLDDQWKEKRDELNGELSAADAAVAKDRSELEALEDQHGafLDADIETAAADQEQlPSWQSE 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    147 VVRLQAEKADLLGIVSELQLKLNSSGSSEDSfveirmaegEAEGSVKEIKHSPGPTRtvstgtalsKYRSRSADGAKNYF 226
Cdd:pfam12128  356 LENLEERLKALTGKHQDVTAKYNRRRSKIKE---------QNNRDIAGIKDKLAKIR---------EARDRQLAVAEDDL 417

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    227 EHEELTV-SQLLLCLREGNQKVERLEVALKEAKERVSDfekkTSNRSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQ 305
Cdd:pfam12128  418 QALESELrEQLEAGKLEFNEEEYRLKSRLGELKLRLNQ----ATATPELLLQLENFDERIERAREEQEAANAEVERLQSE 493

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    306 VTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELnekqeLVYTNKKLELQVESMLSEIKMEQAKTED---- 381
Cdd:pfam12128  494 LRQARKRRDQASEALRQASRRLEERQSALDELELQLFPQAGTL-----LHFLRKEAPDWEQSIGKVISPELLHRTDldpe 568

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    382 -----EKSKLTVLQMTHNKLLQEHNNALKTIEELTRK-----ESEKVDRAVLKELSEKLELAEKALASKQLQMDEMKQTI 451
Cdd:pfam12128  569 vwdgsVGGELNLYGVKLDLKRIDVPEWAASEEELRERldkaeEALQSAREKQAAAEEQLVQANGELEKASREETFARTAL 648

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    452 AKQEEDLETMTILRAQMEVYCSDFHAER--AAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSLMEMQSRHGARTSDSD 529
Cdd:pfam12128  649 KNARLDLRRLFDEKQSEKDKKNKALAERkdSANERLNSLEAQLKQLDKKHQAWLEEQKEQKREARTEKQAYWQVVEGALD 728


                   ..
gi 20149572    530 QQ 531
Cdd:pfam12128  729 AQ 730
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
 245-471 3.39e-03

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 40.30  E-value: 3.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  245 QKVERLEVALKEAKERVSDFEKKtsNRSEIETQTEGSTEKENDEEKGPETVGSEVEalnlqvtslfKELQEAHTKLSEAE 324
Cdd:PRK05771  46 RKLRSLLTKLSEALDKLRSYLPK--LNPLREEKKKVSVKSLEELIKDVEEELEKIE----------KEIKELEEEISELE 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  325 LMKKRLQEKCQALErKNSAIPSELNEKQEL----VYTNKKLELQVESMLSEIKMEQAKT-EDEKSKLTVLQMTHNKLLQE 399
Cdd:PRK05771 114 NEIKELEQEIERLE-PWGNFDLDLSLLLGFkyvsVFVGTVPEDKLEELKLESDVENVEYiSTDKGYVYVVVVVLKELSDE 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20149572  400 HNNALKTI--EELTRKESEKVDRaVLKELSEKLELAEKALASKQlqmDEMKQtIAKQEEDL-----ETMTILRAQMEVY 471
Cdd:PRK05771 193 VEEELKKLgfERLELEEEGTPSE-LIREIKEELEEIEKERESLL---EELKE-LAKKYLEEllalyEYLEIELERAEAL 266
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 240-450 3.69e-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: 40.44  E-value: 3.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    240 LREGNQKVERLEVALKEAKERVSDFEKKTSN----RSEIETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQE 315
Cdd:TIGR02169  296 IGELEAEIASLERSIAEKERELEDAEERLAKleaeIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEE 375

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572    316 AHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVYtnkklelQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNK 395
Cdd:TIGR02169  376 VDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEELQ-------RLSEELADLNAAIAGIEAKINELEEEKEDKAL 448

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 20149572    396 LLQEHNNALKTIEELTRKESEKvdravLKELSEKLELAEKALASKQLQMDEMKQT 450
Cdd:TIGR02169  449 EIKKQEWKLEQLAADLSKYEQE-----LYDLKEEYDRVEKELSKLQRELAEAEAQ 498
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
71-490 3.71e-03

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 40.41  E-value: 3.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   71 ELSAWTEKQKEERQFFEIQSKEAKERLmalsHENEKLKEELGKLkgkserssEDPTDDSRLPRAEAEQEKDQLRTQVVRL 150
Cdd:PRK02224 217 ELDEEIERYEEQREQARETRDEADEVL----EEHEERREELETL--------EAEIEDLRETIAETEREREELAEEVRDL 284

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  151 QAEKADLL----GIVSELQLklnssGSSEDSFVEIRMAEGEAEGSvkEIKHSPGPTRtvstgTALSKYRSRSADGAKNYF 226
Cdd:PRK02224 285 RERLEELEeerdDLLAEAGL-----DDADAEAVEARREELEDRDE--ELRDRLEECR-----VAAQAHNEEAESLREDAD 352

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  227 EHEELTvsqlllclREGNQKVERLEVALKEAKERVSDFEKKTSN-RSEIET---QTEGSTEKENDEEKGPETVGSEVEAL 302
Cdd:PRK02224 353 DLEERA--------EELREEAAELESELEEAREAVEDRREEIEElEEEIEElreRFGDAPVDLGNAEDFLEELREERDEL 424

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  303 NLQVTSLFKELQEAHTKLSEAElmkkRLQE--KCQALER--KNSAIPSELNEKQELVYT----NKKLELQVESMLSEIKM 374
Cdd:PRK02224 425 REREAELEATLRTARERVEEAE----ALLEagKCPECGQpvEGSPHVETIEEDRERVEEleaeLEDLEEEVEEVEERLER 500

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  375 --EQAKTEDEKSKLTVLQMTHNKLLQEHNNalkTIEELTRKESEKVDRAvlKELSEKLELAEKALASKQLQMDEMKQTIA 452
Cdd:PRK02224 501 aeDLVEAEDRIERLEERREDLEELIAERRE---TIEEKRERAEELRERA--AELEAEAEEKREAAAEAEEEAEEAREEVA 575

                        410       420       430
                 ....*....|....*....|....*....|....*...
gi 20149572  453 KQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEKE 490
Cdd:PRK02224 576 ELNSKLAELKERIESLERIRTLLAAIADAEDEIERLRE 613
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 312-460 4.53e-03

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: 39.14  E-value: 4.53e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 312 ELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELNEKQELVytnKKLELQVESMLSEIKMEQAKTEDEKSKLTvlQM 391
Cdd:COG1579  11 DLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTEL---EDLEKEIKRLELEIEEVEARIKKYEEQLG--NV 85

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20149572 392 THNKllqEHNNALKTIEELTRKESEKVDRavLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLET 460
Cdd:COG1579  86 RNNK---EYEALQKEIESLKRRISDLEDE--ILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
41-489 5.06e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.05  E-value: 5.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   41 LQQMKELLTENHQLKEAMKLNNQAMKGRFEELSAWTEKQKE-ERQFFEIQSKEakERLMALSHENEKLKEELGKLKgkse 119
Cdd:PRK03918 285 LKELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGiEERIKELEEKE--ERLEELKKKLKELEKRLEELE---- 358

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  120 rssedptddsrlPRAEAEQEKDQLRTQVVRLQAEKADLL--GIVSELQLKLNSSGSSEDSFVEIRMAEGEAEGSVKEIKh 197
Cdd:PRK03918 359 ------------ERHELYEEAKAKKEELERLKKRLTGLTpeKLEKELEELEKAKEEIEEEISKITARIGELKKEIKELK- 425

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  198 spgptrtvstgTALSKYRSRSAD----GAKNYFEHEELTVSQLLLCLREGNQKVERLEVALKEAKERVSDFEKKTSNRSE 273
Cdd:PRK03918 426 -----------KAIEELKKAKGKcpvcGRELTEEHRKELLEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKKESE 494

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  274 IETQTEGSTEKENDEEKGPETVGSEVEA-------LNLQVTSLFKELQEAHTKLSEAELMKKR---LQEKCQALERKNSA 343
Cdd:PRK03918 495 LIKLKELAEQLKELEEKLKKYNLEELEKkaeeyekLKEKLIKLKGEIKSLKKELEKLEELKKKlaeLEKKLDELEEELAE 574

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  344 IPSELNEK-----QELVYTNKKLE------LQVESMLSEIKMEQAKTEDEKSKLTVLQMTHNKLLQEHNNALKTIEELTR 412
Cdd:PRK03918 575 LLKELEELgfesvEELEERLKELEpfyneyLELKDAEKELEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  413 KESEKVDRAV---LKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETMTILRAQMEVYCSDFHAERAAREKIHEEK 489
Cdd:PRK03918 655 KYSEEEYEELreeYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKELEKLEKALERVEELREKVKKYK 734
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 240-469 5.77e-03

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: 39.62  E-value: 5.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   240 LREGNQKVERLEVALKEAKERVSDFEKKTSN------RSEIETQTEGSTEKENDEEKGPETVGSeveaLNLQVTSLFKEL 313
Cdd:TIGR04523 276 LEQNNKKIKELEKQLNQLKSEISDLNNQKEQdwnkelKSELKNQEKKLEEIQNQISQNNKIISQ----LNEQISQLKKEL 351

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   314 QEahtklSEAELMKKRLQekcqaLERKNSAIPSELNEKQELVYTNKKLELQVESMLSEIKMEQAKTEDEKSKLTVLQMTH 393
Cdd:TIGR04523 352 TN-----SESENSEKQRE-----LEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEK 421

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572   394 NKLLQEHNNAL-------KTIEELTRKESEKVD-----RAVLKELSEKLELAEKALASKQLQMDEMKQTIAKQEEDLETM 461
Cdd:TIGR04523 422 ELLEKEIERLKetiiknnSEIKDLTNQDSVKELiiknlDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKL 501


                  ....*...
gi 20149572   462 TILRAQME 469
Cdd:TIGR04523 502 NEEKKELE 509
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 275-519 7.62e-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: 7.62e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 275 ETQTEGSTEKENDEEKGPETVGSEVEALNLQVTSLFKELQEAHTKLseaelmkKRLQEKCQALERKNSAIPSELNEKQEl 354
Cdd:COG3883  15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAEL-------EALQAEIDKLQAEIAEAEAEIEERRE- 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 355 vytnkKLELQVESMlseikmeqAKTEDEKSKLTVLQMTHNklLQEHNNALKTIEELTRKESEKVDRavLKELSEKLELAE 434
Cdd:COG3883  87 -----ELGERARAL--------YRSGGSVSYLDVLLGSES--FSDFLDRLSALSKIADADADLLEE--LKADKAELEAKK 149

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572 435 KALASKQLQMDEMKQTIAKQEEDLETmtiLRAQMEVYCSDFHAERAAREKIHEEKEQLALQLAVLLKENDAFEDGGRQSL 514
Cdd:COG3883 150 AELEAKLAELEALKAELEAAKAELEA---QQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAA 226


                ....*
gi 20149572 515 MEMQS 519
Cdd:COG3883 227 AAAAA 231
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
299-480 8.84e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 8.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  299 VEALNLQVTSLFKELQEAHTKLSEAELMKKRLQEKCQALERKNSAIPSELN-------------EKQELVYTNKKLElQV 365
Cdd:COG4913  612 LAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIDvasaereiaeleaELERLDASSDDLA-AL 690

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20149572  366 ESMLSEIKMEQAKTEDEKSKLtvlqmthNKLLQEHNNALKTIEELTRKESEKVDRAVLKELSEKLELAEKAL--ASKQLQ 443
Cdd:COG4913  691 EEQLEELEAELEELEEELDEL-------KGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLEERFaaALGDAV 763

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 20149572  444 MDEMKQTIAKQEEDLETM-----TILRAQMEVYCSDFHAERA 480
Cdd:COG4913  764 ERELRENLEERIDALRARlnraeEELERAMRAFNREWPAETA 805
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH