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Conserved domains on  [gi|2043833306|ref|XP_030142741|]
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caspase recruitment domain-containing protein 9 isoform X3 [Taeniopygia guttata]

Protein Classification

CARD_CARD9 and SMC_prok_B domain-containing protein( domain architecture ID 12962325)

CARD_CARD9 and SMC_prok_B domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 10-95 1.49e-54

Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260071  Cd Length: 86  Bit Score: 178.57  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  10 CWNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQ 89
Cdd:cd08809     1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                  ....*.
gi 2043833306  90 LYKKIT 95
Cdd:cd08809    81 LYKKIT 86
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-430 4.17e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 4.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  174 ERDSLSKELRKCKDEnysLALSYAKQSEEKSAALMKNRDLLLEIDQLKHSLMKAEDDCKLERKHTMKLKHAIEQRPshEV 253
Cdd:TIGR02168  674 ERRREIEELEEKIEE---LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  254 VWEIQQEKELLLAKNQELENTLQVAREQNLEKSLSKETLENDCSQTMEERRELVNTIYSLRKELRRAKVLQDKQfAEEKE 333
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-RERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  334 MLELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQALLTREQFHMQYCKNLLERDAYRKQIRELGERCDEMQLQLFQKE 413
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          250
                   ....*....|....*..
gi 2043833306  414 SQLLATEAKLKRLQLEL 430
Cdd:TIGR02168  908 SKRSELRRELEELREKL 924
 
Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 10-95 1.49e-54

Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260071  Cd Length: 86  Bit Score: 178.57  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  10 CWNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQ 89
Cdd:cd08809     1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                  ....*.
gi 2043833306  90 LYKKIT 95
Cdd:cd08809    81 LYKKIT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 11-97 8.57e-13

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 64.12  E-value: 8.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  11 WNNLENFRVKLI-SVIDPSRITPYLRQCKVLSPDDEEQVLNDPSlvmRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQ 89
Cdd:pfam00619   1 RKLLKKNRVALVeRLGTLDGLLDYLLEKNVLTEEEEEKIKANPT---RLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 2043833306  90 LYKKITGK 97
Cdd:pfam00619  78 LASDLEGL 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-430 4.17e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 4.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  174 ERDSLSKELRKCKDEnysLALSYAKQSEEKSAALMKNRDLLLEIDQLKHSLMKAEDDCKLERKHTMKLKHAIEQRPshEV 253
Cdd:TIGR02168  674 ERRREIEELEEKIEE---LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  254 VWEIQQEKELLLAKNQELENTLQVAREQNLEKSLSKETLENDCSQTMEERRELVNTIYSLRKELRRAKVLQDKQfAEEKE 333
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-RERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  334 MLELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQALLTREQFHMQYCKNLLERDAYRKQIRELGERCDEMQLQLFQKE 413
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          250
                   ....*....|....*..
gi 2043833306  414 SQLLATEAKLKRLQLEL 430
Cdd:TIGR02168  908 SKRSELRRELEELREKL 924
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 256-480 1.10e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306 256 EIQQEKELLLAKNQELENTLQVAREQNLEKSLSKETLENDCSQTMEERRELVNTIYSLRKELRRAKvLQDKQFAEEKEML 335
Cdd:COG1196   264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-EELEELEEELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306 336 ELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQALLTREQFHMQYCKNLLERDAYRKQIRELGERCDEMQLQLFQKESQ 415
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2043833306 416 LLATEAKLKRLQLELPTLTSDLDDSSSRDSQELVLHVHLDEDTQAAKKDCLEVQKQELSPRESRL 480
Cdd:COG1196   423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 122-338 1.73e-03

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: 41.26  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  122 EIMKLQSAVQEERRKAQELTVWLHSKEDTLREMWVRDS--------LLRKHQER---AQRMKEERDSLSKELRKCKDENY 190
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelekvkLVNAGSERlraVKDIKQERDQLLNEVKTSRNELN 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  191 SLALSYAKQseeKSAALMKNRDLLLEIDQLKHSLMKAEDDCKlERKHTMKlkhAIEQRPSHEVVWEIQQEKELLLAKNQ- 269
Cdd:pfam15921  671 SLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELE-QTRNTLK---SMEGSDGHAMKVAMGMQKQITAKRGQi 743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  270 -ELENTLQVARE----QNLEKSLSKE---TLENDCSQTMEERRELVNTIYSLRKELRRAK-------VLQDK---QFAEE 331
Cdd:pfam15921  744 dALQSKIQFLEEamtnANKEKHFLKEeknKLSQELSTVATEKNKMAGELEVLRSQERRLKekvanmeVALDKaslQFAEC 823


                   ....*..
gi 2043833306  332 KEMLELQ 338
Cdd:pfam15921  824 QDIIQRQ 830
 
Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 10-95 1.49e-54

Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD9. CARD9 is a central regulator of innate immunity and is highly expressed in dendritic cells and macrophages. Together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), it forms the M-CBM signalosome (the CBM complex in myeloid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARD9 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260071  Cd Length: 86  Bit Score: 178.57  E-value: 1.49e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  10 CWNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQ 89
Cdd:cd08809     1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                  ....*.
gi 2043833306  90 LYKKIT 95
Cdd:cd08809    81 LYKKIT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
 10-95 1.91e-33

Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation and recruitment domain (CARD) found in CARD9, CARD14 (CARMA2), CARD10 (CARMA3), CARD11 (CARMA1) and BCL10. BCL10 (B-cell lymphoma 10), together with Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), are integral components of the CBM signalosome. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells), and with CARD11 to form L-CBM (CBM complex in lymphoid immune cells), which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. BCL10/Malt1 also associates with CARD10, which is more widely expressed and is not restricted to hematopoietic cells, to play a role in GPCR-induced NF-kB activation. CARD14 has also been shown to associate with BCL10. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260055  Cd Length: 84  Bit Score: 122.10  E-value: 1.91e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  10 CWNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVmrKRKAGVLLDILQRTGHKGFEAFMESLELYYPQ 89
Cdd:cd08785     1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78


                  ....*.
gi 2043833306  90 LYKKIT 95
Cdd:cd08785    79 LFTKVT 84
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
 11-95 5.30e-25

Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD11, also known as caspase recruitment domain-containing membrane-associated guanylate kinase protein 1 (CARMA1). CARMA1, together with BCL10 (B-cell lymphoma 10) and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1), form the L-CBM signalosome (CBM complex in lymphoid immune cells) which mediates activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. CARMA1 associates with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260070  Cd Length: 86  Bit Score: 98.54  E-value: 5.30e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  11 WNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQL 90
Cdd:cd08808     2 WENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPEL 81


                  ....*
gi 2043833306  91 YKKIT 95
Cdd:cd08808    82 YKLVT 86
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
 11-95 2.46e-22

Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD10, also known as CARMA3 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 3) or BIMP1. The CARMA3-BCL10-MALT1 signalosome plays a role in the GPCR-induced NF-kB activation. CARMA3 is more widely expressed than CARMA1, which is found only in hematopoietic cells. In endothelial and smooth muscle cells, CARMA3-mediated NF-kB activation induces pro-inflammatory signals within the vasculature and is a key factor in atherogenesis. In bronchial epithelial cells, CARMA3-mediated NF-kB signaling is important for the development of allergic airway inflammation. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260069  Cd Length: 86  Bit Score: 91.13  E-value: 2.46e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  11 WNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQL 90
Cdd:cd08807     2 WERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPEH 81


                  ....*
gi 2043833306  91 YKKIT 95
Cdd:cd08807    82 FTLLT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
 11-95 3.22e-17

Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and recruitment domain (CARD) similar to that found in CARD14, also known as BIMP2 or CARMA2 (caspase recruitment domain-containing membrane-associated guanylate kinase protein 2). CARD14 has been identified as a novel member of the MAGUK (membrane-associated guanylate kinase) family that functions as upstream activators of BCL10 (B-cell lymphoma 10) and NF-kB signaling. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260068  Cd Length: 86  Bit Score: 76.45  E-value: 3.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  11 WNNLENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQL 90
Cdd:cd08806     2 WELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPTL 81


                  ....*
gi 2043833306  91 YKKIT 95
Cdd:cd08806    82 YTQVT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 11-97 8.57e-13

Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. Predicted to possess a DEATH (pfam00531) domain-like fold.


Pssm-ID: 459874 [Multi-domain]  Cd Length: 85  Bit Score: 64.12  E-value: 8.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  11 WNNLENFRVKLI-SVIDPSRITPYLRQCKVLSPDDEEQVLNDPSlvmRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQ 89
Cdd:pfam00619   1 RKLLKKNRVALVeRLGTLDGLLDYLLEKNVLTEEEEEKIKANPT---RLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 2043833306  90 LYKKITGK 97
Cdd:pfam00619  78 LASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 18-94 1.27e-12

Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase activation and recruitment domains (CARDs) are death domains (DDs) found associated with caspases. Caspases are aspartate-specific cysteine proteases with functions in apoptosis, immune signaling, inflammation, and host-defense mechanisms. In addition to caspases, proteins containing CARDs include adaptor proteins such as RAIDD, CARD9, and RIG-I-like helicases, which can form multiprotein complexes and play important roles in mediating the signals to induce immune and inflammatory responses. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260018 [Multi-domain]  Cd Length: 79  Bit Score: 63.30  E-value: 1.27e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043833306  18 RVKLISVIDPSRITPYLRQCKVLSPDDEEQVLNDPSlvmRKRKAGVLLDILQRTGHKGFEAFMESL-ELYYPQLYKKI 94
Cdd:cd01671     5 RVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKT---RQDKARKLLDILPRRGPKAFEVFCEALrETGQPHLAELL 79
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
 14-91 1.28e-08

Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and recruitment domain (CARD) similar to that found in BCL10 (B-cell lymphoma 10). BCL10 and Malt1 (mucosa-associated lymphoid tissue-lymphoma-translocation gene 1) are the integral components of CBM signalosomes. They associate with CARD9 to form M-CBM (CBM complex in myeloid immune cells) and with CARMA1 to form L-CBM (CBM complex in lymphoid immune cells), to mediate activation of NF-kB and MAPK by ITAM-coupled receptors expressed on immune cells. Both CARMA1 and CARD9 associate with BCL10 via a CARD-CARD interaction. In general, CARDs are death domains (DDs) found associated with caspases. They are known to be important in the signaling pathways for apoptosis, inflammation, and host-defense mechanisms. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including PYRIN and DED (Death Effector Domain). They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260072 [Multi-domain]  Cd Length: 85  Bit Score: 51.96  E-value: 1.28e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2043833306  14 LENFRVKLISVIDPSRITPYLRQCKVLSPDDEEQVLndpSLVMRKRKAGVLLDILQRTGHKGFEAFMESLELYYPQLY 91
Cdd:cd08810     5 LEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQ---CRTTRKKRVDKLLDILAREGPDGLDALIESIRRNGTQNF 79
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-430 4.17e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 56.22  E-value: 4.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  174 ERDSLSKELRKCKDEnysLALSYAKQSEEKSAALMKNRDLLLEIDQLKHSLMKAEDDCKLERKHTMKLKHAIEQRPshEV 253
Cdd:TIGR02168  674 ERRREIEELEEKIEE---LEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE--ER 748

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  254 VWEIQQEKELLLAKNQELENTLQVAREQNLEKSLSKETLENDCSQTMEERRELVNTIYSLRKELRRAKVLQDKQfAEEKE 333
Cdd:TIGR02168  749 IAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANL-RERLE 827

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  334 MLELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQALLTREQFHMQYCKNLLERDAYRKQIRELGERCDEMQLQLFQKE 413
Cdd:TIGR02168  828 SLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELE 907

                          250
                   ....*....|....*..
gi 2043833306  414 SQLLATEAKLKRLQLEL 430
Cdd:TIGR02168  908 SKRSELRRELEELREKL 924
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 256-480 1.10e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.94  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306 256 EIQQEKELLLAKNQELENTLQVAREQNLEKSLSKETLENDCSQTMEERRELVNTIYSLRKELRRAKvLQDKQFAEEKEML 335
Cdd:COG1196   264 ELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELE-EELEELEEELEEL 342

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306 336 ELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQALLTREQFHMQYCKNLLERDAYRKQIRELGERCDEMQLQLFQKESQ 415
Cdd:COG1196   343 EEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2043833306 416 LLATEAKLKRLQLELPTLTSDLDDSSSRDSQELVLHVHLDEDTQAAKKDCLEVQKQELSPRESRL 480
Cdd:COG1196   423 LEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-467 2.82e-05

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: 46.98  E-value: 2.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  157 RDSLLRKHQERAQRMKEERDSLSKELRKCkdENYSLALSYAKQSEEKSAALMKnrDLLLEIDQLKHSL-----MKAEDDC 231
Cdd:TIGR02169  690 LSSLQSELRRIENRLDELSQELSDASRKI--GEIEKEIEQLEQEEEKLKERLE--ELEEDLSSLEQEIenvksELKELEA 765

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  232 KLERK----HTMKLK-HAIEQRPSHEVVWEIQQEKELLLAKNQELEntlqvAREQNLEKSLSKETLENDCSQtmEERREL 306
Cdd:TIGR02169  766 RIEELeedlHKLEEAlNDLEARLSHSRIPEIQAELSKLEEEVSRIE-----ARLREIEQKLNRLTLEKEYLE--KEIQEL 838

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  307 VntiyslrkelrrakvlqdkqfaEEKEMLELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQalLTREQFHMQYcknll 386
Cdd:TIGR02169  839 Q----------------------EQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRD--LESRLGDLKK----- 889

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  387 ERDAYRKQIRELGERCDEMQLQLFQKESQLLATEAKLKRLQLELPTLTSDLDDSSSRDSQELVLhvhldEDTQAAKKDCL 466
Cdd:TIGR02169  890 ERDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSL-----EDVQAELQRVE 964


                   .
gi 2043833306  467 E 467
Cdd:TIGR02169  965 E 965
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 148-446 7.17e-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: 42.74  E-value: 7.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  148 EDTLREMWVRDSLLRKHQERAQRMKEerdsLSKELRkckdenyslalsyakqSEEKSAALMKNRDLLLEIDQLKHSLMKA 227
Cdd:TIGR02168  192 EDILNELERQLKSLERQAEKAERYKE----LKAELR----------------ELELALLVLRLEELREELEELQEELKEA 251

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  228 EDDCKlerKHTMKLKhaieqrpshevvwEIQQEKELLLAKNQELENTLQVAREQNLEKSLSKETLENDCSQTMEERRELV 307
Cdd:TIGR02168  252 EEELE---ELTAELQ-------------ELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLE 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  308 NTIYSL----------RKELRRAKVLQDKQFAE---EKEMLELQCTSLRKDSQMYKKRIEAVLQQMEEVALERDQAL--- 371
Cdd:TIGR02168  316 RQLEELeaqleeleskLDELAEELAELEEKLEElkeELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLElqi 395

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  372 ----------------LTREQFHMQYCKNLLERDAYRKQIRELGERCDEMQLQLFQKESQLLATEAKLKRLQLELPTLTS 435
Cdd:TIGR02168  396 aslnneierlearlerLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQ 475

                          330
                   ....*....|.
gi 2043833306  436 DLDDSSSRDSQ 446
Cdd:TIGR02168  476 ALDAAERELAQ 486
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 122-338 1.73e-03

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: 41.26  E-value: 1.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  122 EIMKLQSAVQEERRKAQELTVWLHSKEDTLREMWVRDS--------LLRKHQER---AQRMKEERDSLSKELRKCKDENY 190
Cdd:pfam15921  591 EKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVSdlelekvkLVNAGSERlraVKDIKQERDQLLNEVKTSRNELN 670

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  191 SLALSYAKQseeKSAALMKNRDLLLEIDQLKHSLMKAEDDCKlERKHTMKlkhAIEQRPSHEVVWEIQQEKELLLAKNQ- 269
Cdd:pfam15921  671 SLSEDYEVL---KRNFRNKSEEMETTTNKLKMQLKSAQSELE-QTRNTLK---SMEGSDGHAMKVAMGMQKQITAKRGQi 743

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2043833306  270 -ELENTLQVARE----QNLEKSLSKE---TLENDCSQTMEERRELVNTIYSLRKELRRAK-------VLQDK---QFAEE 331
Cdd:pfam15921  744 dALQSKIQFLEEamtnANKEKHFLKEeknKLSQELSTVATEKNKMAGELEVLRSQERRLKekvanmeVALDKaslQFAEC 823


                   ....*..
gi 2043833306  332 KEMLELQ 338
Cdd:pfam15921  824 QDIIQRQ 830
 
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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