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Conserved domains on  [gi|688556839|ref|XP_009300062|]
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caspase recruitment domain-containing protein 9 isoform X2 [Danio rerio]

Protein Classification

kinesin family protein; PEPP family PH domain-containing protein( domain architecture ID 12962322)

kinesin family protein is a microtubule-dependent molecular motor that plays an important role in intracellular transport and in cell division and has an ATPase-containing motor domain; similar to N-type kinesins that are (+) end-directed motors and have an N-terminal motor domain| PEPP (phosphoinositol 3-phosphate-binding protein) family PH (pleckstrin homology) domain-containing protein similar to PH domain region of vertebrate pleckstrin homology domain-containing family A member 4/5/6/7

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 ...
 37-122 2.47e-53

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: 175.88  E-value: 2.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  37 CWARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLELDYPD 116
Cdd:cd08809    1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                 ....*.
gi 688556839 117 VYRKIT 122
Cdd:cd08809   81 LYKKIT 86
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 124-452 3.57e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   124 KEPARVFSVLIDTAGECGLTQFLMSEVSRLQKLAqDERRARLEVSaqvKEQHETI-RQLQLCENELHKQQERVHRIREER 202
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRL-DELSQELSDA---SRKIGEIeKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   203 ERMCEEARTLKDEnyrlmhdLTRLSEEKNcalmcnrDLQLEIEKLKHSLmnaesdskiqrkktvnlkNAMEQRPSPEIIW 282
Cdd:TIGR02169  747 SSLEQEIENVKSE-------LKELEARIE-------ELEEDLHKLEEAL------------------NDLEARLSHSRIP 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   283 KMQRQNDLLKARIQELESAskVQTPEQEKPDSQTLEDFKQQSQAQYQELVNDLynlrrdlhdaEKLRDKYREEKDELELK 362
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----------KEQIKSIEKEIENLNGK 862

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   363 clmlkkdskmygdrmediLKQLEEVIKERDKAICTREEYHLENSKnlqDKDQYRKQIREMGERYDELQVQLFRTQGEVLA 442
Cdd:TIGR02169  863 ------------------KEELEEELEELEAALRDLESRLGDLKK---ERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          330
                   ....*....|
gi 688556839   443 LQATLRKQKS 452
Cdd:TIGR02169  922 LKAKLEALEE 931
 
Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 37-122 2.47e-53

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: 175.88  E-value: 2.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  37 CWARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLELDYPD 116
Cdd:cd08809    1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                 ....*.
gi 688556839 117 VYRKIT 122
Cdd:cd08809   81 LYKKIT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 38-124 3.47e-15

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: 70.67  E-value: 3.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   38 WARLEDYRMLLIKTIE-PSRITPYLRQCKVLSSEDEEQIYNDPSlviRRRKVGVLLDILQRTGLKGYEAFLESLELDYPD 116
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKANPT---RLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 688556839  117 VYRKITGK 124
Cdd:pfam00619  78 LASDLEGL 85
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 124-452 3.57e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   124 KEPARVFSVLIDTAGECGLTQFLMSEVSRLQKLAqDERRARLEVSaqvKEQHETI-RQLQLCENELHKQQERVHRIREER 202
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRL-DELSQELSDA---SRKIGEIeKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   203 ERMCEEARTLKDEnyrlmhdLTRLSEEKNcalmcnrDLQLEIEKLKHSLmnaesdskiqrkktvnlkNAMEQRPSPEIIW 282
Cdd:TIGR02169  747 SSLEQEIENVKSE-------LKELEARIE-------ELEEDLHKLEEAL------------------NDLEARLSHSRIP 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   283 KMQRQNDLLKARIQELESAskVQTPEQEKPDSQTLEDFKQQSQAQYQELVNDLynlrrdlhdaEKLRDKYREEKDELELK 362
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----------KEQIKSIEKEIENLNGK 862

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   363 clmlkkdskmygdrmediLKQLEEVIKERDKAICTREEYHLENSKnlqDKDQYRKQIREMGERYDELQVQLFRTQGEVLA 442
Cdd:TIGR02169  863 ------------------KEELEEELEELEAALRDLESRLGDLKK---ERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          330
                   ....*....|
gi 688556839   443 LQATLRKQKS 452
Cdd:TIGR02169  922 LKAKLEALEE 931
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-459 9.55e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 150 VSRLQKLAQDERRARLEVSAQVKEQHETIRQLQLCENELHKQQERVHRIREERERMCEEARTLKDENYRLMHDLTRLSEE 229
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 230 KncalmcnRDLQLEIEKLKHSLMNAESDSKIQRKKTVNLKNAMEQrpspeiiwKMQRQNDLLKARIQELESASKVQtpEQ 309
Cdd:COG1196  311 R-------RELEERLEELEEELAELEEELEELEEELEELEEELEE--------AEEELEEAEAELAEAEEALLEAE--AE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 310 EKPDSQTLEDFKQQSQAQYQ---ELVNDLYNLRRDLHDAEKLRDKYREEKDELElkclmlkkdskmygdrmedilKQLEE 386
Cdd:COG1196  374 LAEAEEELEELAEELLEALRaaaELAAQLEELEEAEEALLERLERLEEELEELE---------------------EALAE 432

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688556839 387 VIKERDKAICTREEYHLENSKNLQDKDQYRKQIREMGERYDELQVQLFRTQGEVLALQATLRKQKSPIRVNSG 459
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 222-409 6.03e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 39.73  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  222 DLTRLSEEKNcalMCNRDLQLEIEKLKHSLMNAESDSKIQRKKTVNLKNAMEQrpspeiiwKMQRQNDLLKARIQELESA 301
Cdd:pfam07111 482 ELEQLREERN---RLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQ--------ELQRAQESLASVGQQLEVA 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  302 SKVQTPEQEKPDSQTLEDFKQQS---QAQYQELVNDLYNLRRDLHDAEKLRDKYREEKDELELKCLMLKKDSKMYGDRME 378
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEiygQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQ 630

                         170       180       190
                  ....*....|....*....|....*....|.
gi 688556839  379 DILKQLEEVIKERDKAIcTREEYHLENSKNL 409
Cdd:pfam07111 631 ELRRLQDEARKEEGQRL-ARRVQELERDKNL 660
 
Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 37-122 2.47e-53

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: 175.88  E-value: 2.47e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  37 CWARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLELDYPD 116
Cdd:cd08809    1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                 ....*.
gi 688556839 117 VYRKIT 122
Cdd:cd08809   81 LYKKIT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
 37-122 1.24e-29

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: 111.70  E-value: 1.24e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  37 CWARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVirRRKVGVLLDILQRTGLKGYEAFLESLELDYPD 116
Cdd:cd08785    1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78


                 ....*.
gi 688556839 117 VYRKIT 122
Cdd:cd08785   79 LFTKVT 84
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
 38-122 7.33e-23

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: 92.76  E-value: 7.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  38 WARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLELDYPDV 117
Cdd:cd08808    2 WENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPEL 81


                 ....*
gi 688556839 118 YRKIT 122
Cdd:cd08808   82 YKLVT 86
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
 38-122 2.37e-20

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: 85.73  E-value: 2.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  38 WARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLELDYPDV 117
Cdd:cd08807    2 WERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPEH 81


                 ....*
gi 688556839 118 YRKIT 122
Cdd:cd08807   82 FTLLT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
 38-122 4.51e-18

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: 79.15  E-value: 4.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  38 WARLEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLELDYPDV 117
Cdd:cd08806    2 WELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPTL 81


                 ....*
gi 688556839 118 YRKIT 122
Cdd:cd08806   82 YTQVT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 38-124 3.47e-15

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: 70.67  E-value: 3.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   38 WARLEDYRMLLIKTIE-PSRITPYLRQCKVLSSEDEEQIYNDPSlviRRRKVGVLLDILQRTGLKGYEAFLESLELDYPD 116
Cdd:pfam00619   1 RKLLKKNRVALVERLGtLDGLLDYLLEKNVLTEEEEEKIKANPT---RLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 688556839  117 VYRKITGK 124
Cdd:pfam00619  78 LASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 41-121 3.87e-13

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: 64.85  E-value: 3.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  41 LEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIYNDPSlviRRRKVGVLLDILQRTGLKGYEAFLESL-ELDYPDVYR 119
Cdd:cd01671    1 LRKNRVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEKT---RQDKARKLLDILPRRGPKAFEVFCEALrETGQPHLAE 77


                 ..
gi 688556839 120 KI 121
Cdd:cd01671   78 LL 79
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
 41-111 4.95e-09

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: 53.50  E-value: 4.95e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 688556839  41 LEDYRMLLIKTIEPSRITPYLRQCKVLSSEDEEQIyndPSLVIRRRKVGVLLDILQRTGLKGYEAFLESLE 111
Cdd:cd08810    5 LEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEI---QCRTTRKKRVDKLLDILAREGPDGLDALIESIR 72
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 124-452 3.57e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.57e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   124 KEPARVFSVLIDTAGECGLTQFLMSEVSRLQKLAqDERRARLEVSaqvKEQHETI-RQLQLCENELHKQQERVHRIREER 202
Cdd:TIGR02169  671 SEPAELQRLRERLEGLKRELSSLQSELRRIENRL-DELSQELSDA---SRKIGEIeKEIEQLEQEEEKLKERLEELEEDL 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   203 ERMCEEARTLKDEnyrlmhdLTRLSEEKNcalmcnrDLQLEIEKLKHSLmnaesdskiqrkktvnlkNAMEQRPSPEIIW 282
Cdd:TIGR02169  747 SSLEQEIENVKSE-------LKELEARIE-------ELEEDLHKLEEAL------------------NDLEARLSHSRIP 794

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   283 KMQRQNDLLKARIQELESAskVQTPEQEKPDSQTLEDFKQQSQAQYQELVNDLynlrrdlhdaEKLRDKYREEKDELELK 362
Cdd:TIGR02169  795 EIQAELSKLEEEVSRIEAR--LREIEQKLNRLTLEKEYLEKEIQELQEQRIDL----------KEQIKSIEKEIENLNGK 862

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   363 clmlkkdskmygdrmediLKQLEEVIKERDKAICTREEYHLENSKnlqDKDQYRKQIREMGERYDELQVQLFRTQGEVLA 442
Cdd:TIGR02169  863 ------------------KEELEEELEELEAALRDLESRLGDLKK---ERDELEAQLRELERKIEELEAQIEKKRKRLSE 921

                          330
                   ....*....|
gi 688556839   443 LQATLRKQKS 452
Cdd:TIGR02169  922 LKAKLEALEE 931
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 161-448 4.09e-04

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.51  E-value: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   161 RRARLEVSAQVKEQHETIRQLQLCENELHKQQERVHRIREERERMCEEARTLKDEnyrLMHDLTRLSEEKNCALMCNRDL 240
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISA---LRKDLARLEAEVEQLEERIAQL 752

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   241 QLEIEKLKHSLMNAESDSKIQRKKTVNLKNAMEQRPSPeiIWKMQRQNDLLKARIQELESAskvqtpeqekpdsqtledf 320
Cdd:TIGR02168  753 SKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQ--IEQLKEELKALREALDELRAE------------------- 811

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   321 KQQSQAQYQELVNDLYNLRRDLHDAEKLRDKYREEKDELELKCLMLKKDSKMYGDRMEDILKQLEEVIKERDKAICTREE 400
Cdd:TIGR02168  812 LTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALAL 891

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 688556839   401 YHLENSKNLQDKDQYRKQIREMGERYDELQ-------VQLFRTQGEVLALQATLR 448
Cdd:TIGR02168  892 LRSELEELSEELRELESKRSELRRELEELReklaqleLRLEGLEVRIDNLQERLS 946
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 150-459 9.55e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.23  E-value: 9.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 150 VSRLQKLAQDERRARLEVSAQVKEQHETIRQLQLCENELHKQQERVHRIREERERMCEEARTLKDENYRLMHDLTRLSEE 229
Cdd:COG1196  231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEER 310

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 230 KncalmcnRDLQLEIEKLKHSLMNAESDSKIQRKKTVNLKNAMEQrpspeiiwKMQRQNDLLKARIQELESASKVQtpEQ 309
Cdd:COG1196  311 R-------RELEERLEELEEELAELEEELEELEEELEELEEELEE--------AEEELEEAEAELAEAEEALLEAE--AE 373

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 310 EKPDSQTLEDFKQQSQAQYQ---ELVNDLYNLRRDLHDAEKLRDKYREEKDELElkclmlkkdskmygdrmedilKQLEE 386
Cdd:COG1196  374 LAEAEEELEELAEELLEALRaaaELAAQLEELEEAEEALLERLERLEEELEELE---------------------EALAE 432

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 688556839 387 VIKERDKAICTREEYHLENSKNLQDKDQYRKQIREMGERYDELQVQLFRTQGEVLALQATLRKQKSPIRVNSG 459
Cdd:COG1196  433 LEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEG 505
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 239-454 3.18e-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: 3.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   239 DLQLEIEKLKHSL--MNAESDSKIQRKKTVNLKnaMEQRPSPEIIwKMQRQNDLLKARIQELESASKVQTPEQEKPDSQt 316
Cdd:TIGR02169  248 SLEEELEKLTEEIseLEKRLEEIEQLLEELNKK--IKDLGEEEQL-RVKEKIGELEAEIASLERSIAEKERELEDAEER- 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   317 ledfKQQSQAQYQELVNDLYNLRRDLHDAEKLRDKYREEKDELElkclmlkkdskmygDRMEDILKQLEEVIKERDKaic 396
Cdd:TIGR02169  324 ----LAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELK--------------EELEDLRAELEEVDKEFAE--- 382

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 688556839   397 TREEYhlensknlqdkDQYRKQIREMGERYDELQVQLFRTQGEVLALQATLRKQKSPI 454
Cdd:TIGR02169  383 TRDEL-----------KDYREKLEKLKREINELKRELDRLQEELQRLSEELADLNAAI 429
CARD_2 pfam16739
Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain ...
 33-123 3.64e-03

Caspase recruitment domain; In the probable ATP-dependent RNA helicase DDX58 this CARD domain is found near the N-terminus and interacts with the C-terminal domain.


Pssm-ID: 465251  Cd Length: 93  Bit Score: 36.80  E-value: 3.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839   33 EDDECWARLEDYRMLLIKTIEPSRITPYLRQCkvLSSEDEEQIYNDPSLVIRRRKVGVLLDILQRTGLKG-YEAFLESLE 111
Cdd:pfam16739   1 EDDEYRRLLRLFRPRLKDTIKPTEILPHLPEC--LTEDDKERIRAETNNKGNTAAAELLLDRLVRSDREGwFRAFLDALR 78

                          90
                  ....*....|...
gi 688556839  112 LD-YPDVYRKITG 123
Cdd:pfam16739  79 KTgHDGLAEELEG 91
HCR pfam07111
Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha ...
 222-409 6.03e-03

Alpha helical coiled-coil rod protein (HCR); This family consists of several mammalian alpha helical coiled-coil rod HCR proteins. The function of HCR is unknown but it has been implicated in psoriasis in humans and is thought to affect keratinocyte proliferation.


Pssm-ID: 284517 [Multi-domain]  Cd Length: 749  Bit Score: 39.73  E-value: 6.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  222 DLTRLSEEKNcalMCNRDLQLEIEKLKHSLMNAESDSKIQRKKTVNLKNAMEQrpspeiiwKMQRQNDLLKARIQELESA 301
Cdd:pfam07111 482 ELEQLREERN---RLDAELQLSAHLIQQEVGRAREQGEAERQQLSEVAQQLEQ--------ELQRAQESLASVGQQLEVA 550

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839  302 SKVQTPEQEKPDSQTLEDFKQQS---QAQYQELVNDLYNLRRDLHDAEKLRDKYREEKDELELKCLMLKKDSKMYGDRME 378
Cdd:pfam07111 551 RQGQQESTEEAASLRQELTQQQEiygQALQEKVAEVETRLREQLSDTKRRLNEARREQAKAVVSLRQIQHRATQEKERNQ 630

                         170       180       190
                  ....*....|....*....|....*....|.
gi 688556839  379 DILKQLEEVIKERDKAIcTREEYHLENSKNL 409
Cdd:pfam07111 631 ELRRLQDEARKEEGQRL-ARRVQELERDKNL 660
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 238-451 7.77e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 7.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 238 RDLQLEIEKLKHSLM-----NAESDSKIQRKKTVNLKNAMEQRpspeiiwkmQRQNDLLKARIQELESASkvqtpeqekp 312
Cdd:COG1196  216 RELKEELKELEAELLllklrELEAELEELEAELEELEAELEEL---------EAELAELEAELEELRLEL---------- 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 688556839 313 dsQTLEDFKQQSQAQYQELVNDLYNLRRDLHDAEKLRDKYREEKDELELKCLMLKKDSKMYGDRMEDILKQLEEVIKERD 392
Cdd:COG1196  277 --EELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELE 354

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 688556839 393 KAICTREEYHLENSKNLQDKDQYRKQIREMGERYDELQVQLFRTQGEVLALQATLRKQK 451
Cdd:COG1196  355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALL 413
 
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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