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Conserved domains on  [gi|2462513890|ref|XP_054194853|]
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TRAF3-interacting JNK-activating modulator isoform X8 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
 169-213 3.06e-15

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


:

Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 69.30  E-value: 3.06e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462513890 169 VLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 213
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-399 6.60e-08

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


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 6.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  222 LKGKLRSLENQLyTCTQKYspwgmkkvllemEDQKNSYEQKAKESLQKVLEEkmnAEQQLQSTQRSLALAEQKCEEWRSQ 301
Cdd:TIGR02168  198 LERQLKSLERQA-EKAERY------------KELKAELRELELALLVLRLEE---LREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  302 YEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKR 381
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170
                   ....*....|....*...
gi 2462513890  382 SEAEKLTLVTRVQQLQEA 399
Cdd:TIGR02168  342 LEEKLEELKEELESLEAE 359
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
 169-213 3.06e-15

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 69.30  E-value: 3.06e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462513890 169 VLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 213
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-399 6.60e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 6.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  222 LKGKLRSLENQLyTCTQKYspwgmkkvllemEDQKNSYEQKAKESLQKVLEEkmnAEQQLQSTQRSLALAEQKCEEWRSQ 301
Cdd:TIGR02168  198 LERQLKSLERQA-EKAERY------------KELKAELRELELALLVLRLEE---LREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  302 YEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKR 381
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170
                   ....*....|....*...
gi 2462513890  382 SEAEKLTLVTRVQQLQEA 399
Cdd:TIGR02168  342 LEEKLEELKEELESLEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-400 3.67e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 221 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRS 300
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 301 QYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLK 380
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180
                  ....*....|....*....|
gi 2462513890 381 RSEAEKLTLVTRVQQLQEAA 400
Cdd:COG1196   362 EAEEALLEAEAELAEAEEEL 381
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 254-387 7.62e-04

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 41.58  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 254 DQKNSYEQKAKESLQKVLEEKMNAE-------QQLQSTQRSLALAEQKCEEWRSQYEALK--------------EDWRTL 312
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKENLEvelasctENLESTKSQLQESEQLIAELRSELASLKesnslaetqlkcmaESYEDL 756

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462513890 313 GTQHRELESQLHVLQSKLQGadsrdlqmnqalrfLENEhqqLQAKIECLQGDRDLCsldtQDLQDQLKRSEAEKL 387
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEA--------------LEVE---LEEEKNCHEELEAKC----LELQEQLERNEKKES 810
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-359 9.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 221 KLKGKLRSLENQLYTCTQKYSPWGMKKV------LLEMEDQKNSYEQ--KAKESLQKVLEEKMNAEQQLQSTQRSLALAE 292
Cdd:PRK03918  560 ELEKKLDELEEELAELLKELEELGFESVeeleerLKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETE 639

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462513890 293 QKCEEWRSQYEALK-----EDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIE 359
Cdd:PRK03918  640 KRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
 169-213 3.06e-15

first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; TRAF3-interacting JNK-activating modulator (T3JAM), also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. The model corresponds to a conserved region that shows high sequence similarity with the first CC (CC1) domain of Sarcolemmal membrane-associated protein (SLMAP), which is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409288 [Multi-domain]  Cd Length: 45  Bit Score: 69.30  E-value: 3.06e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2462513890 169 VLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 213
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
 173-233 9.87e-12

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal membrane-associated protein (SLMAP), also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. SLMAP contains an N-terminal FHA domain followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409287 [Multi-domain]  Cd Length: 63  Bit Score: 60.01  E-value: 9.87e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2462513890 173 EIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSWKGQLNEDKLKGKLRSLENQL 233
Cdd:cd21911     2 ELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQL 62
CC1_SLMAP-like cd21868
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ...
 176-213 7.01e-10

first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar proteins; The family includes Sarcolemmal membrane-associated protein (SLMAP), its paralog TRAF3-interacting JNK-activating modulator (T3JAM), and similar proteins. SLMAP, also called Sarcolemmal membrane-associated protein, is a cardiac tail-anchored membrane protein that may play a role during myoblast fusion. T3JAM, also called TRAF3-interacting protein 3 (TRAF3IP3), is a novel protein that specifically interacts with TRAF3 and promotes the activation of JNK. It may function as an adapter molecule that regulates TRAF3-mediated JNK activation. SLMAP contains an N-terminal FHA domain, followed by four coiled-coil (CC) domains and a transmembrane domain. The model corresponds to the first CC (CC1) domain that is responsible for the binding of suppressor of IKBKE 1 (SIKE1).


Pssm-ID: 409286 [Multi-domain]  Cd Length: 38  Bit Score: 54.03  E-value: 7.01e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2462513890 176 QLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 213
Cdd:cd21868     1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 222-399 6.60e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 6.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  222 LKGKLRSLENQLyTCTQKYspwgmkkvllemEDQKNSYEQKAKESLQKVLEEkmnAEQQLQSTQRSLALAEQKCEEWRSQ 301
Cdd:TIGR02168  198 LERQLKSLERQA-EKAERY------------KELKAELRELELALLVLRLEE---LREELEELQEELKEAEEELEELTAE 261

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  302 YEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKR 381
Cdd:TIGR02168  262 LQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAE 341

                          170
                   ....*....|....*...
gi 2462513890  382 SEAEKLTLVTRVQQLQEA 399
Cdd:TIGR02168  342 LEEKLEELKEELESLEAE 359
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-400 3.67e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.25  E-value: 3.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 221 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRS 300
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 301 QYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLK 380
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                         170       180
                  ....*....|....*....|
gi 2462513890 381 RSEAEKLTLVTRVQQLQEAA 400
Cdd:COG1196   362 EAEEALLEAEAELAEAEEEL 381
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 276-400 7.03e-06

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: 48.51  E-value: 7.03e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  276 NAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQ 355
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 2462513890  356 AKIECLQGD-------RDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQEAA 400
Cdd:TIGR02168  747 ERIAQLSKElteleaeIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEEL 798
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
240-398 1.02e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 44.37  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 240 YSPWGMKKVLLEMEDQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQhREL 319
Cdd:COG4717    59 FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL-EAL 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 320 ESQLHVLQSKLQGADSRDLQMNQA---LRFLENEHQQLQAKIECLQGDRDLCSLDT-QDLQDQLKRSEAEKLTLVTRVQQ 395
Cdd:COG4717   138 EAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAELEEELEE 217


                  ...
gi 2462513890 396 LQE 398
Cdd:COG4717   218 AQE 220
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
215-399 3.52e-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: 3.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  215 GQLNEDKLKGK---LRSLENQLYTCTQKYSpwGMKKVLLEMEDQKNSYEQKAK--------ESLQKVLEEKMNAEQQLQS 283
Cdd:COG4913    605 GFDNRAKLAALeaeLAELEEELAEAEERLE--ALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDA 682

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  284 TQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRflENEHQQLQAKIECLQG 363
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAALG 760

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2462513890  364 DRDLCSLdTQDLQDQLKRSEAEKLTLVTRVQQLQEA 399
Cdd:COG4913    761 DAVEREL-RENLEERIDALRARLNRAEEELERAMRA 795
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
291-401 3.77e-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: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  291 AEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLqgadsRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSL 370
Cdd:COG4913    608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERR-----EALQRLAEYSWDEIDVASAEREIAELEAELERLDA 682

                           90       100       110
                   ....*....|....*....|....*....|....
gi 2462513890  371 DTQD---LQDQLKRSEAEKLTLVTRVQQLQEAAG 401
Cdd:COG4913    683 SSDDlaaLEEQLEELEAELEELEEELDELKGEIG 716
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
 254-387 7.62e-04

Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant proteins that are filament-like. It interacts with the nuclear envelope-associated protein, MAF1, the WPP family pfam13943.


Pssm-ID: 461778 [Multi-domain]  Cd Length: 859  Bit Score: 41.58  E-value: 7.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 254 DQKNSYEQKAKESLQKVLEEKMNAE-------QQLQSTQRSLALAEQKCEEWRSQYEALK--------------EDWRTL 312
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKENLEvelasctENLESTKSQLQESEQLIAELRSELASLKesnslaetqlkcmaESYEDL 756

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462513890 313 GTQHRELESQLHVLQSKLQGadsrdlqmnqalrfLENEhqqLQAKIECLQGDRDLCsldtQDLQDQLKRSEAEKL 387
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEA--------------LEVE---LEEEKNCHEELEAKC----LELQEQLERNEKKES 810
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 184-400 1.59e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 1.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 184 ALQRELVLKQKMVILQDLLSTLIQASDSswkgQLNEDKLKGKLRSLENQLYTCTQKYSpwGMKKVLLEMEDQKNSY---E 260
Cdd:COG1196   217 ELKEELKELEAELLLLKLRELEAELEEL----EAELEELEAELEELEAELAELEAELE--ELRLELEELELELEEAqaeE 290

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 261 QKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQM 340
Cdd:COG1196   291 YELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEA 370

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 341 NQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQEAA 400
Cdd:COG1196   371 EAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEAL 430
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 168-358 1.82e-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: 40.81  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  168 AVLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSwKGQLNEdkLKGKLRSLENQLYTCTQKYSPWGMKK 247
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDEL-RAELTL--LNEEAANLRERLESLERRIAATERRL 840

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  248 VLLEMEDQKNSYEQKAKESLQKVLEEKMN-AEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVL 326
Cdd:TIGR02168  841 EDLEEQIEELSEDIESLAAEIEELEELIEeLESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEEL 920

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2462513890  327 QSKLQgadsrdlQMNQALRFLENEHQQLQAKI 358
Cdd:TIGR02168  921 REKLA-------QLELRLEGLEVRIDNLQERL 945
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 252-398 4.16e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 39.39  E-value: 4.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  252 MEDQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGT-------QHRELESQLH 324
Cdd:pfam01576  336 LEEETRSHEAQLQEMRQKHTQALEELTEQLEQAKRNKANLEKAKQALESENAELQAELRTLQQakqdsehKRKKLEGQLQ 415

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  325 VLQSKLQGADSRDLQMNQALRFLENEHQQL-----QAKIECLQGDRDLCSLDT--QDLQDQLKRSEAEKLTLVTRVQQLQ 397
Cdd:pfam01576  416 ELQARLSESERQRAELAEKLSKLQSELESVssllnEAEGKNIKLSKDVSSLESqlQDTQELLQEETRQKLNLSTRLRQLE 495


                   .
gi 2462513890  398 E 398
Cdd:pfam01576  496 D 496
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 154-398 5.42e-03

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


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 38.85  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 154 TIKNDASQQTNYGVAVLDKEIIQLSDYLKEALQRELVLKQKMVILQDL---LSTLIQASDSSWKGQLNED--KLKGKLRS 228
Cdd:TIGR04523 246 TEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLkseISDLNNQKEQDWNKELKSElkNQEKKLEE 325

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 229 LENQLYTCTQKYSPWGMKKVLLEME---------------DQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQ 293
Cdd:TIGR04523 326 IQNQISQNNKIISQLNEQISQLKKEltnsesensekqrelEEKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQNQEK 405

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 294 KCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQ 373
Cdd:TIGR04523 406 LNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQLKVLSRSINKIKQNLE 485

                         250       260
                  ....*....|....*....|....*
gi 2462513890 374 DLQDQLKRSEAEKLTLVTRVQQLQE 398
Cdd:TIGR04523 486 QKQKELKSKEKELKKLNEEKKELEE 510
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 181-400 5.72e-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: 38.88  E-value: 5.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  181 LKEALQRELVLKQKMVILQDLLSTLIQASDSSWkgqlneDKLKGKLRSLENQLYTCTQKYspWGMKKVLLEMEDQKnsye 260
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKL------EELRLEVSELEEEIEELQKEL--YALANEISRLEQQK---- 304

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  261 QKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQM 340
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462513890  341 NQALRFLENEHQQLQAKIECL-------------------QGDRDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQEAA 400
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERLearlerledrrerlqqeieELLKKLEEAELKELQAELEELEEELEELQEELERLEEAL 463
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 170-366 6.57e-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: 38.88  E-value: 6.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  170 LDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLiQASDSSWKGQLNEdkLKGKLRSLENQLYTCTQkyspwgmkkvl 249
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEEL-KEELESLEAELEE--LEAELEELESRLEELEE----------- 379

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890  250 lEMEDQKNSYEQkAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYE--ALKEDWRTLGTQHRELE---SQLH 324
Cdd:TIGR02168  380 -QLETLRSKVAQ-LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEelqEELE 457

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2462513890  325 VLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRD 366
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-359 9.46e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.12  E-value: 9.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462513890 221 KLKGKLRSLENQLYTCTQKYSPWGMKKV------LLEMEDQKNSYEQ--KAKESLQKVLEEKMNAEQQLQSTQRSLALAE 292
Cdd:PRK03918  560 ELEKKLDELEEELAELLKELEELGFESVeeleerLKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETE 639

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2462513890 293 QKCEEWRSQYEALK-----EDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIE 359
Cdd:PRK03918  640 KRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
 
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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