NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1728952157|ref|XP_030356062|]
View 

TGF-beta-activated kinase 1 and MAP3K7-binding protein 2 isoform X1 [Strigops habroptila]

Protein Classification

TAB2/TAB3 family protein( domain architecture ID 10198856)

TAB2/TAB3 family protein is a CUE domain-containing zinc finger protein, similar to TGF-beta-activated kinase 1 and MAP3K7-binding proteins, TAB2 and TAB3

Gene Ontology:  GO:0008270|GO:0043130
PubMed:  12665246|12628920

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
CUE_TAB2_TAB3 cd14362
CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins ...
 9-50 3.66e-20

CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins; TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD).


:

Pssm-ID: 270545  Cd Length: 42  Bit Score: 83.89  E-value: 3.66e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1728952157   9 DIQVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:cd14362     1 DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES 42
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 672-695 9.01e-07

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


:

Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 45.39  E-value: 9.01e-07
                           10        20
                   ....*....|....*....|....
gi 1728952157  672 QWSCTACTFLNHPALNRCEQCEMP 695
Cdd:smart00547   2 DWECPACTFLNFASRSKCFACGAP 25
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
532-623 6.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 532 DDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSVSQIPSLE---------------EM 596
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqeeleelqkER 124

                          90       100
                  ....*....|....*....|....*..
gi 1728952157 597 QQLRSCNRQLQIDIDCLTKEIDLFQAR 623
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSEIAEREEE 151
 
Name Accession Description Interval E-value
CUE_TAB2_TAB3 cd14362
CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins ...
 9-50 3.66e-20

CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins; TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD).


Pssm-ID: 270545  Cd Length: 42  Bit Score: 83.89  E-value: 3.66e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1728952157   9 DIQVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:cd14362     1 DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES 42
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
 8-50 7.18e-09

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 51.72  E-value: 7.18e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1728952157    8 IDIQVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:smart00546   1 ENDEALHDLKEMFPNLDEEVIEAVLEANTGNVEATINNLLEGS 43
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
 11-50 1.54e-07

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 47.86  E-value: 1.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728952157  11 QVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:pfam02845   3 QMLETLKEMFPDLDEEVIRAVLEASNGNVEAAINALLEGS 42
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 672-695 9.01e-07

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 45.39  E-value: 9.01e-07
                           10        20
                   ....*....|....*....|....
gi 1728952157  672 QWSCTACTFLNHPALNRCEQCEMP 695
Cdd:smart00547   2 DWECPACTFLNFASRSKCFACGAP 25
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
532-623 6.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 532 DDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSVSQIPSLE---------------EM 596
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqeeleelqkER 124

                          90       100
                  ....*....|....*....|....*..
gi 1728952157 597 QQLRSCNRQLQIDIDCLTKEIDLFQAR 623
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSEIAEREEE 151
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 541-618 1.69e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 541 LVHQKARMERLQRELEIQKK----KLDKLKSEVNEMENNLTRRRLKRSNSVSQiPSLEEMQQ----LRSCNRQLQIDIDC 612
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKekesKISDLEDELNKDDFELKKENLEKEIDEKN-KEIEELKQtqksLKKKQEEKQELIDQ 593


                  ....*.
gi 1728952157 613 LTKEID 618
Cdd:TIGR04523 594 KEKEKK 599
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
672-696 5.15e-04

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 37.72  E-value: 5.15e-04
                          10        20
                  ....*....|....*....|....*
gi 1728952157 672 QWSCTACTFLNHPALNRCEQCEMPR 696
Cdd:pfam00641   4 DWDCSKCLVQNFATSTKCVACQAPK 28
HR1_ROCK2 cd11638
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 538-606 1.38e-03

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 2; ROCK2 is a serine/threonine protein kinase and was the first identified target of activated RhoA. It plays a role in stress fiber and focal adhesion formation, and is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK2 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK2 is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212028 [Multi-domain]  Cd Length: 67  Bit Score: 37.60  E-value: 1.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728952157 538 QALLVHQKARMERlQRELEIQKKKLdkLKSEVNEMENNLtrRRLKRSNSVSQIpSLEEMQQLRscnRQL 606
Cdd:cd11638     1 KALLQHKNTEYQR-KAEHEADRKRN--LENEVNSLKDQL--EDLKKKNQNSQI-SNEKNIQLQ---RQL 60
 
Name Accession Description Interval E-value
CUE_TAB2_TAB3 cd14362
CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins ...
 9-50 3.66e-20

CUE domain found in the N-terminal of TGF-beta-activated kinase 1 and MAP3K7-binding proteins TAB2, TAB3 and similar proteins; TAB2, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 2, TAK1-binding protein 2, or TGF-beta-activated kinase 1-binding protein 2, is an adaptor protein that regulates activation of TAK1, a MAP kinase kinase kinase (MAPKKK), through linking TAK1 to TRAF6 in the Interleukin-1 (IL-1) induced NF-kappaB activation pathway. TAB3, also called mitogen-activated protein kinase kinase kinase 7-interacting protein 3, NF-kappa-B-activating protein 1, TAK1-binding protein 3, or TGF-beta-activated kinase 1-binding protein 3, is a TAB2-like TAK1-binding protein that activates NF-kappaB similar to TAB2. It activates TAK1 and regulates its association with TRAF2 and TRAF6. Moreover, TAB3 interacts with TRAF6 and TRAF2 in an IL-1- and a TNF-dependent manner, respectively. In summary, TAB2 and TAB3 function redundantly as mediators of TAK1 activation in IL-1 and TNF signal transduction. Both of them contain an N-terminal CUE domain, a coiled-coil (CC) region, a TAK1-binding domain and a C-terminal Npl4 zinc finger (NZF) ubiquitin-binding domain (UBD).


Pssm-ID: 270545  Cd Length: 42  Bit Score: 83.89  E-value: 3.66e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1728952157   9 DIQVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:cd14362     1 DMQLFHELKQRFPEVPDAVVSQCMLQNNHNREACCAALQKES 42
CUE smart00546
Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also ...
 8-50 7.18e-09

Domain that may be involved in binding ubiquitin-conjugating enzymes (UBCs); CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2. Ponting (Biochem. J.) "Proteins of the Endoplasmic reticulum" (in press)


Pssm-ID: 214715  Cd Length: 43  Bit Score: 51.72  E-value: 7.18e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1728952157    8 IDIQVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:smart00546   1 ENDEALHDLKEMFPNLDEEVIEAVLEANTGNVEATINNLLEGS 43
CUE pfam02845
CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE ...
 11-50 1.54e-07

CUE domain; CUE domains have been shown to bind ubiquitin. It has been suggested that CUE domains are related to pfam00627 and this has been confirmed by the structure of the domain. CUE domains also occur in two protein of the IL-1 signal transduction pathway, tollip and TAB2.


Pssm-ID: 427018  Cd Length: 42  Bit Score: 47.86  E-value: 1.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1728952157  11 QVLHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVLSQES 50
Cdd:pfam02845   3 QMLETLKEMFPDLDEEVIRAVLEASNGNVEAAINALLEGS 42
ZnF_RBZ smart00547
Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. ...
 672-695 9.01e-07

Zinc finger domain; Zinc finger domain in Ran-binding proteins (RanBPs), and other proteins. In RanBPs, this domain binds RanGDP.


Pssm-ID: 197784 [Multi-domain]  Cd Length: 25  Bit Score: 45.39  E-value: 9.01e-07
                           10        20
                   ....*....|....*....|....
gi 1728952157  672 QWSCTACTFLNHPALNRCEQCEMP 695
Cdd:smart00547   2 DWECPACTFLNFASRSKCFACGAP 25
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
532-623 6.16e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.05  E-value: 6.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 532 DDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSVSQIPSLE---------------EM 596
Cdd:COG4372    45 EELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQeeaeelqeeleelqkER 124

                          90       100
                  ....*....|....*....|....*..
gi 1728952157 597 QQLRSCNRQLQIDIDCLTKEIDLFQAR 623
Cdd:COG4372   125 QDLEQQRKQLEAQIAELQSEIAEREEE 151
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 541-618 1.69e-04

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 45.01  E-value: 1.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 541 LVHQKARMERLQRELEIQKK----KLDKLKSEVNEMENNLTRRRLKRSNSVSQiPSLEEMQQ----LRSCNRQLQIDIDC 612
Cdd:TIGR04523 515 LTKKISSLKEKIEKLESEKKekesKISDLEDELNKDDFELKKENLEKEIDEKN-KEIEELKQtqksLKKKQEEKQELIDQ 593


                  ....*.
gi 1728952157 613 LTKEID 618
Cdd:TIGR04523 594 KEKEKK 599
zf-RanBP pfam00641
Zn-finger in Ran binding protein and others;
672-696 5.15e-04

Zn-finger in Ran binding protein and others;


Pssm-ID: 395516 [Multi-domain]  Cd Length: 30  Bit Score: 37.72  E-value: 5.15e-04
                          10        20
                  ....*....|....*....|....*
gi 1728952157 672 QWSCTACTFLNHPALNRCEQCEMPR 696
Cdd:pfam00641   4 DWDCSKCLVQNFATSTKCVACQAPK 28
CUE cd14279
CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ...
 13-46 5.96e-04

CUE domain found in ubiquitin-binding CUE proteins; This family includes many coupling of ubiquitin conjugation to endoplasmic reticulum degradation (CUE) domain containing proteins that are characterized by an FP and a di-leucine-like sequence and bind to monoubiquitin with varying affinities. Some higher eukaryotic CUE domain proteins do not bind monoubiquitin efficiently, since they carry LP, rather than FP among CUE domains. CUE domains form three-helix bundle structures and are distantly related to the ubiquitin-associated (UBA) domains which are widely occurring ubiquitin-binding motifs found in a broad range of cellular proteins in species ranging from yeast to human. The majority of family members contain one CUE domain, but some family members from fungi harbor two CUE domains.


Pssm-ID: 270465  Cd Length: 38  Bit Score: 37.83  E-value: 5.96e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1728952157  13 LHDLRQKFPEVPEGVVSRCMLQNNNNLDACCAVL 46
Cdd:cd14279     4 LEQLQEMFPDLDEEVLEDVLEANNGDVEAAIDAL 37
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
519-584 8.26e-04

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 8.26e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728952157 519 DRISDARK-LSMGSDDAAyTQAL--LVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRS 584
Cdd:COG1842    69 KWEEKARLaLEKGREDLA-REALerKAELEAQAEALEAQLAQLEEQVEKLKEALRQLESKLEELKAKKD 136
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
546-623 9.05e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 546 ARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSNSVSQIPSL---------------EEMQQLRSCNRQLQIDI 610
Cdd:COG4372    38 FELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELneqlqaaqaelaqaqEELESLQEEAEELQEEL 117

                          90
                  ....*....|...
gi 1728952157 611 DCLTKEIDLFQAR 623
Cdd:COG4372   118 EELQKERQDLEQQ 130
HR1_ROCK2 cd11638
Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated ...
 538-606 1.38e-03

Protein kinase C-related kinase homology region 1 (HR1) Rho-binding domain of Rho-associated coiled-coil containing protein kinase 2; ROCK2 is a serine/threonine protein kinase and was the first identified target of activated RhoA. It plays a role in stress fiber and focal adhesion formation, and is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK2 contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a Rho-binding HR1 domain and a pleckstrin homology (PH) domain. ROCK2 is auto-inhibited by HR1 and PH domains interacting with the catalytic domain. HR1 domains are anti-parallel coiled-coil (ACC) domains that bind small GTPases from the Rho family.


Pssm-ID: 212028 [Multi-domain]  Cd Length: 67  Bit Score: 37.60  E-value: 1.38e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1728952157 538 QALLVHQKARMERlQRELEIQKKKLdkLKSEVNEMENNLtrRRLKRSNSVSQIpSLEEMQQLRscnRQL 606
Cdd:cd11638     1 KALLQHKNTEYQR-KAEHEADRKRN--LENEVNSLKDQL--EDLKKKNQNSQI-SNEKNIQLQ---RQL 60
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 520-625 7.31e-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: 7.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1728952157 520 RISDARKLSMGSDDAAYTQALLVHQKARMERLQRELEIQKKKLDKLKSEVNEMENNLTRRRLKRSnsvsqipslEEMQQL 599
Cdd:COG4942   148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA---------AELAEL 218

                          90       100
                  ....*....|....*....|....*.
gi 1728952157 600 RSCNRQLQIDIDCLTKEIDLFQARGP 625
Cdd:COG4942   219 QQEAEELEALIARLEAEAAAAAERTP 244
 
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