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Conserved domains on  [gi|16554562|ref|NP_434701|]
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caspase recruitment domain-containing protein 9 isoform 2 [Homo sapiens]

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 1.10e-56

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: 183.20  E-value: 1.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  10 CWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQ 89
Cdd:cd08809   1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                ....*.
gi 16554562  90 LYKKVT 95
Cdd:cd08809  81 LYKKIT 86
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-423 2.91e-09

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: 59.69  E-value: 2.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    172 SRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQRPSQ-----EL 246
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlsKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    247 LWELQQEKALLQARVQELEASVQEGKLDrsspyIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFE 326
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    327 LQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQL 406
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250
                   ....*....|....*....
gi 16554562    407 LAVEGRLR--RQQLETLVL 423
Cdd:TIGR02168  911 SELRRELEelREKLAQLEL 929
 
Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 10-95 1.10e-56

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: 183.20  E-value: 1.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  10 CWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQ 89
Cdd:cd08809   1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                ....*.
gi 16554562  90 LYKKVT 95
Cdd:cd08809  81 LYKKIT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 11-97 4.64e-12

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: 61.81  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    11 WSVLEGFRVTL-TSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNlviRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQ 89
Cdd:pfam00619   1 RKLLKKNRVALvERLGTLDGLLDYLLEKNVLTEEEEEKIKANPT---RLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 16554562    90 LYKKVTGK 97
Cdd:pfam00619  78 LASDLEGL 85
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-423 2.91e-09

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: 59.69  E-value: 2.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    172 SRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQRPSQ-----EL 246
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlsKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    247 LWELQQEKALLQARVQELEASVQEGKLDrsspyIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFE 326
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    327 LQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQL 406
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250
                   ....*....|....*....
gi 16554562    407 LAVEGRLR--RQQLETLVL 423
Cdd:TIGR02168  911 SELRRELEelREKLAQLEL 929
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-429 1.57e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 249 ELQQEKAL----LQARVQELEASVQEGKLDRsspyiqvLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEM 324
Cdd:COG1196 206 ERQAEKAEryreLKEELKELEAELLLLKLRE-------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 325 FELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEA 404
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                       170       180
                ....*....|....*....|....*
gi 16554562 405 QLLAVEGRLRRQQLETLVLSSDLED 429
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE 383
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 144-419 4.40e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562   144 IKELRVKDSLLRKHQERVQRLKEEceaGSRELKRCKeenydlamRLAHQSEEKGAALMRNRDLQLEidqlkHSLMKAEDD 223
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEE---KAREVERRR--------KLEEAEKARQAEMDRQAAIYAE-----QERMAMERE 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562   224 CKVERKHTLKLRHAMEQRPSQELLWE---------LQQEKALLQARV-QELEASVQegkldrsspyIQVLEEDWRQALRD 293
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEEIAMEisrmrelerLQMERQQKNERVrQELEAARK----------VKILEEERQRKIQQ 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562   294 HQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQaiATREELHAQHAR 373
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK--RDRKRAEEQRRK 495

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16554562   374 GLQEKDALRKQV-------RELGEKA-DELQLQVFQCEAQLLAVEGRLRRQQLE 419
Cdd:pfam17380 496 ILEKELEERKQAmieeerkRKLLEKEmEERQKAIYEEERRREAEEERRKQQEME 549
 
Name Accession Description Interval E-value
CARD_CARD9 cd08809
Caspase activation and recruitment domain of CARD9-like proteins; Caspase activation and ...
 10-95 1.10e-56

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: 183.20  E-value: 1.10e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  10 CWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQ 89
Cdd:cd08809   1 CWNRLEDYRVKLISVIDPSRITPYLRQCKVLNSDDEEQVLNDPSLVIRKRKVGVLLDILQRTGLKGYEAFLESLELYYPQ 80


                ....*.
gi 16554562  90 LYKKVT 95
Cdd:cd08809  81 LYKKIT 86
CARD_CARD9-like cd08785
Caspase activation and recruitment domain of CARD9 and related proteins; Caspase activation ...
 10-95 7.57e-37

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: 130.57  E-value: 7.57e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  10 CWSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVirKRKVGVLLDILQRTGHKGYVAFLESLELYYPQ 89
Cdd:cd08785   1 LWEALERHRHRLSRYINPSRLTPYLRQKKVLSEDDEEEILSKPSLP--RNRAGYLLDILKTRGKNGYDAFLESLEFYYPE 78


                ....*.
gi 16554562  90 LYKKVT 95
Cdd:cd08785  79 LFTKVT 84
CARD_CARD11_CARMA1 cd08808
Caspase activation and recruitment domain of CARD11-like proteins; Caspase activation and ...
 11-95 3.40e-26

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: 101.62  E-value: 3.40e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  11 WSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQL 90
Cdd:cd08808   2 WENVECNRHMLSRYINPAKLTPYLRQCKVIDEQDEDEVLNAPMLPSKINRAGRLLDILHTKGQRGYVVFLESLEFYYPEL 81


                ....*
gi 16554562  91 YKKVT 95
Cdd:cd08808  82 YKLVT 86
CARD_CARD10_CARMA3 cd08807
Caspase activation and recruitment domain of CARD10-like proteins; Caspase activation and ...
 11-95 2.85e-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: 90.74  E-value: 2.85e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  11 WSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQL 90
Cdd:cd08807   2 WERIEGVRHRLTRALNPAKLTPYLRQCRVIDEQDEEEVLNSYRFPCRINRTGRLMDILRCRGKRGYEAFLESLEFYYPEH 81


                ....*
gi 16554562  91 YKKVT 95
Cdd:cd08807  82 FTLLT 86
CARD_CARD14_CARMA2 cd08806
Caspase activation and recruitment domain of CARD14-like proteins; Caspase activation and ...
 11-95 2.85e-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: 79.53  E-value: 2.85e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  11 WSVLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNLVIRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQL 90
Cdd:cd08806   2 WELINDNRHRIVLGIRPCRLIPYLRQARVLTQLDEDEILHCPRLTNRSMRTSHMLDLLRTQGRNGAIALLESLMIHYPTL 81


                ....*
gi 16554562  91 YKKVT 95
Cdd:cd08806  82 YTQVT 86
CARD pfam00619
Caspase recruitment domain; Motif contained in proteins involved in apoptotic signaling. ...
 11-97 4.64e-12

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: 61.81  E-value: 4.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    11 WSVLEGFRVTL-TSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNlviRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQ 89
Cdd:pfam00619   1 RKLLKKNRVALvERLGTLDGLLDYLLEKNVLTEEEEEKIKANPT---RLDKARELLDLVLKKGPKACQIFLEALKEGDPD 77


                  ....*...
gi 16554562    90 LYKKVTGK 97
Cdd:pfam00619  78 LASDLEGL 85
CARD cd01671
Caspase activation and recruitment domain: a protein-protein interaction domain; Caspase ...
 18-93 4.92e-11

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: 58.68  E-value: 4.92e-11
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 16554562  18 RVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPnlvIRKRKVGVLLDILQRTGHKGYVAFLESL-ELYYPQLYKK 93
Cdd:cd01671   5 RVELVEDLDVEDILDHLIQKGVLTEEDKEEILSEK---TRQDKARKLLDILPRRGPKAFEVFCEALrETGQPHLAEL 78
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 172-423 2.91e-09

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: 59.69  E-value: 2.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    172 SRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQRPSQ-----EL 246
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERiaqlsKE 755

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    247 LWELQQEKALLQARVQELEASVQEGKLDrsspyIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFE 326
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLE 830

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    327 LQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQL 406
Cdd:TIGR02168  831 RRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKR 910

                          250
                   ....*....|....*....
gi 16554562    407 LAVEGRLR--RQQLETLVL 423
Cdd:TIGR02168  911 SELRRELEelREKLAQLEL 929
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 144-417 4.37e-09

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: 59.30  E-value: 4.37e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    144 IKELRVKDSLLRKHQERVQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDd 223
Cdd:TIGR02168  231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE- 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    224 cKVERKHTLKLRHAMEQRPSQELLWELQQEKALLQARVQELEASVQ--EGKLDRSSPYIQVLEEDWRQALRDHQEQANTI 301
Cdd:TIGR02168  310 -RLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELEslEAELEELEAELEELESRLEELEEQLETLRSKV 388

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    302 FSLRKDLRQGEARRLRCMEEKEMFELQclALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDAL 381
Cdd:TIGR02168  389 AQLELQIASLNNEIERLEARLERLEDR--RERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEEL 466

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 16554562    382 RKQVRELGEKADELQLQVFQCEAQLLAVEGRLRRQQ 417
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 154-417 5.81e-09

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: 58.91  E-value: 5.81e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    154 LRKHQERVQRLKEECEAGSRELKRCKEENYDLAMRLahqseekgaalmrnRDLQLEIDQLKHSLMKAEDDCKVERKHTLK 233
Cdd:TIGR02168  679 IEELEEKIEELEEKIAELEKALAELRKELEELEEEL--------------EQLRKELEELSRQISALRKDLARLEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    234 LRHAMEQRpsQELLWELQQEKALLQARVQELEASVQEGKLDrsspyIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEA 313
Cdd:TIGR02168  745 LEERIAQL--SKELTELEAEIEELEERLEEAEEELAEAEAE-----IEELEAQIEQLKEELKALREALDELRAELTLLNE 817

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    314 RRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDA------------- 380
Cdd:TIGR02168  818 EAANLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASleealallrsele 897

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 16554562    381 --------LRKQVRELGEKADELQLQVFQCEAQLLAVEGRLRRQQ 417
Cdd:TIGR02168  898 elseelreLESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQ 942
CARD_BCL10 cd08810
Caspase activation and recruitment domain of B-cell lymphoma 10; Caspase activation and ...
 13-91 6.40e-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: 52.73  E-value: 6.40e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 16554562  13 VLEGFRVTLTSVIDPSRITPYLRQCKVLNPDDEEQVLSDPNlviRKRKVGVLLDILQRTGHKGYVAFLESLELYYPQLY 91
Cdd:cd08810   4 VLEEQRHYLCDKLIADRHFDYLRSKRILTRDDCEEIQCRTT---RKKRVDKLLDILAREGPDGLDALIESIRRNGTQNF 79
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 202-435 1.24e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.13  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    202 RNRDLQLEIDQLKHSLMKAEDDCKVERKHTLklrhameqrpsQELLWELQQEKALLQARVQELEASVQEGKLdrsspYIQ 281
Cdd:TIGR02168  214 RYKELKAELRELELALLVLRLEELREELEEL-----------QEELKEAEEELEELTAELQELEEKLEELRL-----EVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    282 VLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAI 361
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLE 357

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 16554562    362 ATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQLLAVEGRLRRQQLETLVLSSDLEDGSPRRS 435
Cdd:TIGR02168  358 AELEELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLE 431
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 155-419 1.36e-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: 47.76  E-value: 1.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    155 RKHQERVQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAeddckVERKHTLKl 234
Cdd:TIGR02169  670 RSEPAELQRLRERLEGLKRELSSLQSELRRIENRLDELSQELSDASRKIGEIEKEIEQLEQEEEKL-----KERLEELE- 743

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    235 rhaMEQRPSQELLWELQQEKALLQARVQELEASVQEGKLDRSSPYIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEAR 314
Cdd:TIGR02169  744 ---EDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQK 820

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    315 RLRCMEEKEMFElqclalrkdskmykDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADE 394
Cdd:TIGR02169  821 LNRLTLEKEYLE--------------KEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD 886

                          250       260
                   ....*....|....*....|....*
gi 16554562    395 LQLQVFQCEAQLLAVEGRLRRQQLE 419
Cdd:TIGR02169  887 LKKERDELEAQLRELERKIEELEAQ 911
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 121-395 1.43e-05

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 47.74  E-value: 1.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    121 TEVMKLQKKVQDLTALLSSKDDFIKELRVKDSLLRK----HQERVQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEK 196
Cdd:TIGR02168  698 KALAELRKELEELEEELEQLRKELEELSRQISALRKdlarLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    197 GAALMRNRDLQLEIDQLKHSLMKAEDDCKVERK---------HTLKLRHAMEQRPS---QELLWELQQEKALLQARVQEL 264
Cdd:TIGR02168  778 AEAEAEIEELEAQIEQLKEELKALREALDELRAeltllneeaANLRERLESLERRIaatERRLEDLEEQIEELSEDIESL 857

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    265 EASV---------QEGKLDRSSPYIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQClalrkd 335
Cdd:TIGR02168  858 AAEIeeleelieeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRL------ 931

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    336 skmykDRIEAILLQMEEVAieRDQAIATREELHAQHARGLQEKDALRKQVRELGEKADEL 395
Cdd:TIGR02168  932 -----EGLEVRIDNLQERL--SEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKEL 984
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-429 1.57e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.62  E-value: 1.57e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 249 ELQQEKAL----LQARVQELEASVQEGKLDRsspyiqvLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEM 324
Cdd:COG1196 206 ERQAEKAEryreLKEELKELEAELLLLKLRE-------LEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 325 FELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEA 404
Cdd:COG1196 279 LELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                       170       180
                ....*....|....*....|....*
gi 16554562 405 QLLAVEGRLRRQQLETLVLSSDLED 429
Cdd:COG1196 359 ELAEAEEALLEAEAELAEAEEELEE 383
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 249-429 1.91e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 47.24  E-value: 1.91e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 249 ELQQEKALLQARVQELEASVQEGKLDrsspyIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEmfelq 328
Cdd:COG1196 236 ELEAELEELEAELEELEAELEELEAE-----LAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA----- 305

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 329 clALRKDSKMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQLLA 408
Cdd:COG1196 306 --RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEE 383

                       170       180
                ....*....|....*....|.
gi 16554562 409 VEGRLRRQQLETLVLSSDLED 429
Cdd:COG1196 384 LAEELLEALRAAAELAAQLEE 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 125-418 2.11e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 2.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 125 KLQKKVQDLTALLSSKDDFIKELRVKDSLLRKHQERVQRLKEECEAGSRELKRCKEEnydlamrLAHQSEEKGAALMRNR 204
Cdd:COG1196 282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE-------LEELEEELEEAEEELE 354

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 205 DLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEqrpsqellwELQQEKALLQARVQELEASVQEGKLDRSSpyiqvLE 284
Cdd:COG1196 355 EAEAELAEAEEALLEAEAELAEAEEELEELAEELL---------EALRAAAELAAQLEELEEAEEALLERLER-----LE 420

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 285 EDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEvAIERDQAIATR 364
Cdd:COG1196 421 EELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAE-AAARLLLLLEA 499

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 16554562 365 EELHAQHARGLQEKDALRKQVRELGEKADELQLqVFQCEAQLLAVEGRLRRQQL 418
Cdd:COG1196 500 EADYEGFLEGVKAALLLAGLRGLAGAVAVLIGV-EAAYEAALEAALAAALQNIV 552
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
228-418 2.42e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.75  E-value: 2.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  228 RKHTLKLRHAMEQRP-----SQELLWELQQEKALLQARVQELEASVQEgkldrsspyIQVLEEDWRQALRDHQEQANTIF 302
Cdd:COG4913  588 TRHEKDDRRRIRSRYvlgfdNRAKLAALEAELAELEEELAEAEERLEA---------LEAELDALQERREALQRLAEYSW 658

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  303 SlRKDLRQGEARRLRCMEEKEmfelqclALRKDS---KMYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKD 379
Cdd:COG4913  659 D-EIDVASAEREIAELEAELE-------RLDASSddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELD 730

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 16554562  380 ALRKQVRELGEKADelQLQVFQCEAQLLAVEGRLRRQQL 418
Cdd:COG4913  731 ELQDRLEAAEDLAR--LELRALLEERFAAALGDAVEREL 767
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
247-416 4.01e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 4.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  247 LWELQQEKALLQARVQELEASVQ--EGKLDRSSPYIQVLEEDWRQALRDHQEQ-ANTIFSLRKDLRQGEARRLRCMEEKE 323
Cdd:COG4913  283 LWFAQRRLELLEAELEELRAELArlEAELERLEARLDALREELDELEAQIRGNgGDRLEQLEREIERLERELEERERRRA 362

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562  324 MFELQCLALRKDskmYKDRIEAILLQMEEVAIERDQAIATREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCE 403
Cdd:COG4913  363 RLEALLAALGLP---LPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439

                        170
                 ....*....|...
gi 16554562  404 AQLLAVEGRLRRQ 416
Cdd:COG4913  440 ARLLALRDALAEA 452
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 144-419 4.40e-04

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 42.80  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562   144 IKELRVKDSLLRKHQERVQRLKEEceaGSRELKRCKeenydlamRLAHQSEEKGAALMRNRDLQLEidqlkHSLMKAEDD 223
Cdd:pfam17380 284 VSERQQQEKFEKMEQERLRQEKEE---KAREVERRR--------KLEEAEKARQAEMDRQAAIYAE-----QERMAMERE 347

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562   224 CKVERKHTLKLRHAMEQRPSQELLWE---------LQQEKALLQARV-QELEASVQegkldrsspyIQVLEEDWRQALRD 293
Cdd:pfam17380 348 RELERIRQEERKRELERIRQEEIAMEisrmrelerLQMERQQKNERVrQELEAARK----------VKILEEERQRKIQQ 417

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562   294 HQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQaiATREELHAQHAR 373
Cdd:pfam17380 418 QKVEMEQIRAEQEEARQREVRRLEEERAREMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEK--RDRKRAEEQRRK 495

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 16554562   374 GLQEKDALRKQV-------RELGEKA-DELQLQVFQCEAQLLAVEGRLRRQQLE 419
Cdd:pfam17380 496 ILEKELEERKQAmieeerkRKLLEKEmEERQKAIYEEERRREAEEERRKQQEME 549
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 283-447 1.74e-03

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: 41.20  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    283 LEEDWRQALRDHQEQANTIFSLRKDLRQGEARRLRCMEEKEMFELQCLALRKDSKMYKDRIEAILLQMEEVAIERDQAIA 362
Cdd:TIGR02168  682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEA 761

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    363 TREELHAQHARGLQEKDALRKQVRELGEKADELQLQVFQCEAQLLAVEGRLRRQQLETLVLSSDLEDGSPRRSQELSLPQ 442
Cdd:TIGR02168  762 EIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLE 841


                   ....*
gi 16554562    443 DLEDT 447
Cdd:TIGR02168  842 DLEEQ 846
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
161-353 3.86e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 3.86e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 161 VQRLKEECEAGSRELKRCKEENYDLAMRLAHQSEEKGAALMRNRDLQLEIDQLKHSLMKAEDDCKVERKHTLKLRHAMEQ 240
Cdd:COG4717  48 LERLEKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562 241 RPSQELLWELQQEKALLQARVQELEASVQEgkldrsspyIQVLEEDWRQALRDHQEQANTIFSLRKDLRQGEARRL-RCM 319
Cdd:COG4717 128 LPLYQELEALEAELAELPERLEELEERLEE---------LRELEEELEELEAELAELQEELEELLEQLSLATEEELqDLA 198

                       170       180       190
                ....*....|....*....|....*....|....
gi 16554562 320 EEKEMFELQCLALRKDSKMYKDRIEAILLQMEEV 353
Cdd:COG4717 199 EELEELQQRLAELEEELEEAQEELEELEEELEQL 232
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 125-398 4.02e-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: 40.10  E-value: 4.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    125 KLQKKVQDLTALLSSKDDFIKELRVKDSLLRK----HQERVQRLKE---ECEAGSRelKRCKEENydlAMRLAHQSEEKG 197
Cdd:pfam15921  146 QLQNTVHELEAAKCLKEDMLEDSNTQIEQLRKmmlsHEGVLQEIRSilvDFEEASG--KKIYEHD---SMSTMHFRSLGS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    198 AALMRNRDLQLEIDQLKHSLMKAEDDCKverkhTLKlrhaMEQRPSQELLweLQQEKALLQARVQELEASVQeGKLDRSS 277
Cdd:pfam15921  221 AISKILRELDTEISYLKGRIFPVEDQLE-----ALK----SESQNKIELL--LQQHQDRIEQLISEHEVEIT-GLTEKAS 288

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 16554562    278 pyiqvleedwrqalrDHQEQANTIFSlRKDLRQGEARRLRCMEEKEMFELQCLA------LRKDSKMYKDRIEAILLQME 351
Cdd:pfam15921  289 ---------------SARSQANSIQS-QLEIIQEQARNQNSMYMRQLSDLESTVsqlrseLREAKRMYEDKIEELEKQLV 352

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 16554562    352 EVAIERDQAIATREELhAQHARGLQekDALRKQVRELGEKADELQLQ 398
Cdd:pfam15921  353 LANSELTEARTERDQF-SQESGNLD--DQLQKLLADLHKREKELSLE 396
 
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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