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Conserved domains on  [gi|2217271093|ref|XP_047286919|]
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TRAF3-interacting JNK-activating modulator isoform X2 [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; ...
189-233 8.26e-16

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: 71.22  E-value: 8.26e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217271093 189 VLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 233
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-412 5.85e-06

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 241 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRS 320
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 321 QYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLK 400
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                         170
                  ....*....|..
gi 2217271093 401 RSEAEKLTLVTR 412
Cdd:COG1196   362 EAEEALLEAEAE 373
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
189-233 8.26e-16

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: 71.22  E-value: 8.26e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217271093 189 VLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 233
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-412 5.85e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 241 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRS 320
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 321 QYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLK 400
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                         170
                  ....*....|..
gi 2217271093 401 RSEAEKLTLVTR 412
Cdd:COG1196   362 EAEEALLEAEAE 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
268-406 7.27e-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: 45.43  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  268 VLLEMEDQKNSYEQKAK--ESLQKVLEEKMNAE-----QQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELE 340
Cdd:TIGR02168  194 ILNELERQLKSLERQAEkaERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217271093  341 SQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKRSEAEK 406
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
274-407 7.11e-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: 41.97  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 274 DQKNSYEQKAKESLQKVLEEKMNAE-------QQLQSTQRSLALAEQKCEEWRSQYEALK--------------EDWRTL 332
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKENLEvelasctENLESTKSQLQESEQLIAELRSELASLKesnslaetqlkcmaESYEDL 756
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217271093 333 GTQHRELESQLHVLQSKLQGadsrdlqmnqalrfLENEhqqLQAKIECLQGDRDLCsldtQDLQDQLKRSEAEKL 407
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEA--------------LEVE---LEEEKNCHEELEAKC----LELQEQLERNEKKES 810
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
241-379 7.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 241 KLKGKLRSLENQLYTCTQKYSPWGMKKV------LLEMEDQKNSYEQ--KAKESLQKVLEEKMNAEQQLQSTQRSLALAE 312
Cdd:PRK03918  560 ELEKKLDELEEELAELLKELEELGFESVeeleerLKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETE 639
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217271093 313 QKCEEWRSQYEALK-----EDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIE 379
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; ...
189-233 8.26e-16

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: 71.22  E-value: 8.26e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217271093 189 VLDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 233
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
193-253 1.85e-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: 61.93  E-value: 1.85e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217271093 193 EIIQLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSWKGQLNEDKLKGKLRSLENQL 253
Cdd:cd21911     2 ELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQL 62
CC1_SLMAP-like cd21868
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ...
196-233 2.45e-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: 55.18  E-value: 2.45e-10
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2217271093 196 QLSDYLKEALQRELVLKQKMVILQDLLSTLIQASDSSW 233
Cdd:cd21868     1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
241-412 5.85e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 48.78  E-value: 5.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 241 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRS 320
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 321 QYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLK 400
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
                         170
                  ....*....|..
gi 2217271093 401 RSEAEKLTLVTR 412
Cdd:COG1196   362 EAEEALLEAEAE 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
268-406 7.27e-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: 45.43  E-value: 7.27e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  268 VLLEMEDQKNSYEQKAK--ESLQKVLEEKMNAE-----QQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELE 340
Cdd:TIGR02168  194 ILNELERQLKSLERQAEkaERYKELKAELRELElallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217271093  341 SQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKRSEAEK 406
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEEL 339
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
296-413 3.86e-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: 43.12  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  296 NAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQ 375
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 2217271093  376 AKIECLQGD-------RDLCSLDTQDLQDQLKRSEAEKLTLVTRV 413
Cdd:TIGR02168  747 ERIAQLSKElteleaeIEELEERLEEAEEELAEAEAEIEELEAQI 791
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
235-413 4.09e-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: 4.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  235 GQLNEDKLKGK---LRSLENQLYTCTQKYSpwGMKKVLLEMEDQKNSYEQKAK--------ESLQKVLEEKMNAEQQLQS 303
Cdd:COG4913    605 GFDNRAKLAALeaeLAELEEELAEAEERLE--ALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDA 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  304 TQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRflENEHQQLQAKIECLQG 383
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAALG 760
                          170       180       190
                   ....*....|....*....|....*....|
gi 2217271093  384 DRDLCSLdTQDLQDQLKRSEAEKLTLVTRV 413
Cdd:COG4913    761 DAVEREL-RENLEERIDALRARLNRAEEEL 789
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
260-409 6.13e-04

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 6.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 260 YSPWGMKKVLLEMEDQKNSYEQKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQhREL 339
Cdd:COG4717    59 FKPQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQEL-EAL 137
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217271093 340 ESQLHVLQSKLQGADSRDLQMNQA---LRFLENEHQQLQAKIECLQGDRDLCSLDT-QDLQDQLKRSEAEKLTL 409
Cdd:COG4717   138 EAELAELPERLEELEERLEELRELeeeLEELEAELAELQEELEELLEQLSLATEEElQDLAEELEELQQRLAEL 211
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
274-407 7.11e-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: 41.97  E-value: 7.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 274 DQKNSYEQKAKESLQKVLEEKMNAE-------QQLQSTQRSLALAEQKCEEWRSQYEALK--------------EDWRTL 332
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKENLEvelasctENLESTKSQLQESEQLIAELRSELASLKesnslaetqlkcmaESYEDL 756
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217271093 333 GTQHRELESQLHVLQSKLQGadsrdlqmnqalrfLENEhqqLQAKIECLQGDRDLCsldtQDLQDQLKRSEAEKL 407
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEA--------------LEVE---LEEEKNCHEELEAKC----LELQEQLERNEKKES 810
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
190-386 2.34e-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: 40.43  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  190 LDKEIIQLSDYLKEALQRELVLKQKMVILQDLLSTLiQASDSSWKGQLNEdkLKGKLRSLENQLYTCTQkyspwgmkkvl 269
Cdd:TIGR02168  314 LERQLEELEAQLEELESKLDELAEELAELEEKLEEL-KEELESLEAELEE--LEAELEELESRLEELEE----------- 379
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  270 lEMEDQKNSYEQkAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYE--ALKEDWRTLGTQHRELE---SQLH 344
Cdd:TIGR02168  380 -QLETLRSKVAQ-LELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeaELKELQAELEELEEELEelqEELE 457
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2217271093  345 VLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRD 386
Cdd:TIGR02168  458 RLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQE 499
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
190-379 3.67e-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: 40.00  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 190 LDKEIIQLSDYLKEaLQRELVLKQKmvILQDLLSTLIQASDSS--WKGQLNE-----DKLKGKLRSLENQLYTC------ 256
Cdd:TIGR04523 223 LKKQNNQLKDNIEK-KQQEINEKTT--EISNTQTQLNQLKDEQnkIKKQLSEkqkelEQNNKKIKELEKQLNQLkseisd 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 257 --TQKYSPWgMKKVLLEMEDQKNSYEQ-------------KAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQ 321
Cdd:TIGR04523 300 lnNQKEQDW-NKELKSELKNQEKKLEEiqnqisqnnkiisQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKE 378
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217271093 322 YEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIE 379
Cdd:TIGR04523 379 NQSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETII 436
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
211-377 4.07e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 4.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 211 LKQKMVILQDLLSTLIQASDSSWKGQLNEDKLKGKLRSLENQLYTCTQKYSPWGMKKVLLEMEDQKNSYEQKAKESLQKV 290
Cdd:COG4717    76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERL 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 291 LEEKmNAEQQLQSTQRSLALAEQKCEEWRSQY-EALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLEN 369
Cdd:COG4717   156 EELR-ELEEELEELEAELAELQEELEELLEQLsLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLEN 234

                  ....*...
gi 2217271093 370 EHQQLQAK 377
Cdd:COG4717   235 ELEAAALE 242
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
241-379 7.61e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 7.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 241 KLKGKLRSLENQLYTCTQKYSPWGMKKV------LLEMEDQKNSYEQ--KAKESLQKVLEEKMNAEQQLQSTQRSLALAE 312
Cdd:PRK03918  560 ELEKKLDELEEELAELLKELEELGFESVeeleerLKELEPFYNEYLElkDAEKELEREEKELKKLEEELDKAFEELAETE 639
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217271093 313 QKCEEWRSQYEALK-----EDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQAKIE 379
Cdd:PRK03918  640 KRLEELRKELEELEkkyseEEYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKK 711
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
201-401 7.81e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 38.74  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  201 LKEALQRELVLKQKMVILQDLLSTLiqasdSSWKGQLNEDKLKGKLRSLENQLytctqkyspwgmkKVLLEMEDQKNSYE 280
Cdd:COG4913    257 IRELAERYAAARERLAELEYLRAAL-----RLWFAQRRLELLEAELEELRAEL-------------ARLEAELERLEARL 318
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  281 QKAKESLQKVLEEKMNAE-QQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLG-----------TQHRELESQLHVLQS 348
Cdd:COG4913    319 DALREELDELEAQIRGNGgDRLEQLEREIERLERELEERERRRARLEALLAALGlplpasaeefaALRAEAAALLEALEE 398
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 2217271093  349 KLQGADSRDLQMNQALRFLENEHQQLQAKIECLQGDRDLCSLDTQDLQDQLKR 401
Cdd:COG4913    399 ELEALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIPARLLALRDALAE 451
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
238-409 7.91e-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: 7.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 238 NEDKLKGKLRSLENQLYTCTQKYSpwGMKKVLLEMEDQKNSYEqKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEE 317
Cdd:TIGR04523 139 NIDKFLTEIKKKEKELEKLNNKYN--DLKKQKEELENELNLLE-KEKLNIQKNIDKIKNKLLKLELLLSNLKKKIQKNKS 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 318 WRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSrdlQMNQALRFLENEHQQLQAKIECLQGDRDLCSldtqDLQD 397
Cdd:TIGR04523 216 LESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQT---QLNQLKDEQNKIKKQLSEKQKELEQNNKKIK----ELEK 288
                         170
                  ....*....|..
gi 2217271093 398 QLKRSEAEKLTL 409
Cdd:TIGR04523 289 QLNQLKSEISDL 300
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
271-379 8.26e-03

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


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 37.50  E-value: 8.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 271 EMEDQKNSYEQKAKESLQK--------VLEEKMNAEQQLQSTQRSLALAEQkceewrsQYEALKEDWRTLGTQHRELESQ 342
Cdd:COG1842    62 ELEAEAEKWEEKARLALEKgredlareALERKAELEAQAEALEAQLAQLEE-------QVEKLKEALRQLESKLEELKAK 134
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2217271093 343 LHVLQSKLQGADSRdLQMNQALRFLENE-----HQQLQAKIE 379
Cdd:COG1842   135 KDTLKARAKAAKAQ-EKVNEALSGIDSDdatsaLERMEEKIE 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
201-409 9.02e-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: 38.50  E-value: 9.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  201 LKEALQRELVLKQKMVILQDLLSTLIQASDSSWkgqlneDKLKGKLRSLENQLYTCTQKYspWGMKKVLLEMEDQKnsye 280
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKL------EELRLEVSELEEEIEELQKEL--YALANEISRLEQQK---- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093  281 QKAKESLQKVLEEKMNAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQM 360
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2217271093  361 NQALRFLENEHQQLQAKIECLqgDRDLcsldtQDLQDQLKRSEAEKLTL 409
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERL--EARL-----ERLEDRRERLQQEIEEL 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
310-442 9.23e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 38.76  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 310 LAEQKCEEWRSQYEALKEDWRTLGTQHRELESQLHVLQSKLQGADSRDLQMNQALRFLENEHQQLQA-------KIECLQ 382
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAeeyellaELARLE 301
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217271093 383 GDRDLCSLDTQDLQDQLKRSEAEKLTLVTRVQQLQGLLQNQSLQLQEQEKLLTKKEAMWA 442
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361
 
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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