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Conserved domains on  [gi|1953400674|ref|XP_038526813|]
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TRAF3-interacting JNK-activating modulator isoform X1 [Canis lupus familiaris]

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; ...
190-234 7.47e-14

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: 65.83  E-value: 7.47e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1953400674 190 VLDKEIIQLSEYLKEALQRELVLKQKMVILQDLLSTLIRASDSSW 234
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
242-405 5.44e-07

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: 52.63  E-value: 5.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 242 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMSAEQQLQSTQRSLALAEQKCEEWRS 321
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 322 QYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKIELLQGDRDSSDTQHLQDQLKRS 401
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                  ....
gi 1953400674 402 EEEK 405
Cdd:COG1196   362 EAEE 365
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
297-516 8.60e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 48.90  E-value: 8.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  297 SAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQ 376
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  377 AKIELLQGDRDSSDTQ---------HLQDQLKRSEEEKLTLMAKVQQLQGLLQNQSLQLQEQEKLLTK-----KDQALPL 442
Cdd:TIGR02168  747 ERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERL 826
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953400674  443 WSPKPSHNEVEPEGTGKEKEW-DFRDQLQKKTLQLQAKEKECRELHSELDNLSDEYLSCLRKLQHCREELNQSQQ 516
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIeELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
190-234 7.47e-14

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: 65.83  E-value: 7.47e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1953400674 190 VLDKEIIQLSEYLKEALQRELVLKQKMVILQDLLSTLIRASDSSW 234
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
242-405 5.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 242 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMSAEQQLQSTQRSLALAEQKCEEWRS 321
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 322 QYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKIELLQGDRDSSDTQHLQDQLKRS 401
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                  ....
gi 1953400674 402 EEEK 405
Cdd:COG1196   362 EAEE 365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
269-505 6.04e-07

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: 52.37  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  269 VLLEMEDQKNSYEQKAK------------ESLQKVL--EEKMSAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLG 334
Cdd:TIGR02168  194 ILNELERQLKSLERQAEkaerykelkaelRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  335 TQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKIELLQG--DRDSSDTQHLQDQLKRSEEEKLTLMAKV 412
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDELAEELAELEEKLEELKEEL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  413 QQLQGLLQNQSLQLQEQEKLLTKKDQALplwspkpshnevepeGTGKEKEWDFRDQLQKKTLQLQAKEKECRELHSELDN 492
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQL---------------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
                          250
                   ....*....|...
gi 1953400674  493 LSDEYLSCLRKLQ 505
Cdd:TIGR02168  419 LQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
297-516 8.60e-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: 48.90  E-value: 8.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  297 SAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQ 376
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  377 AKIELLQGDRDSSDTQ---------HLQDQLKRSEEEKLTLMAKVQQLQGLLQNQSLQLQEQEKLLTK-----KDQALPL 442
Cdd:TIGR02168  747 ERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERL 826
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953400674  443 WSPKPSHNEVEPEGTGKEKEW-DFRDQLQKKTLQLQAKEKECRELHSELDNLSDEYLSCLRKLQHCREELNQSQQ 516
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIeELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
275-406 3.33e-03

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: 40.43  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 275 DQKNSYEQKAKESLQKVLEEK-------MSAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQ-------HREL 340
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKenlevelASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQlkcmaesYEDL 756
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953400674 341 ESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKiellqgdrdssdTQHLQDQLKRSEEEKL 406
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAK------------CLELQEQLERNEKKES 810
 
Name Accession Description Interval E-value
CC1_T3JAM cd21912
first coiled-coil (CC1) domain found in TRAF3-interacting JNK-activating modulator; ...
190-234 7.47e-14

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: 65.83  E-value: 7.47e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1953400674 190 VLDKEIIQLSEYLKEALQRELVLKQKMVILQDLLSTLIRASDSSW 234
Cdd:cd21912     1 VLEKEILQLSDYLQEALHRERALKKKLAALQELLSTLLQASEKSW 45
CC1_SLMAP cd21911
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein; Sarcolemmal ...
194-254 1.67e-11

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: 59.62  E-value: 1.67e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953400674 194 EIIQLSEYLKEALQRELVLKQKMVILQDLLSTLIRASDSSWKGQLNEDKLKGKLRSLENQL 254
Cdd:cd21911     2 ELFQLQQYLQEALHREQILEQKLETLQRLLSSTQEASESSWQALIDEDRLLSRLELLENQL 62
CC1_SLMAP-like cd21868
first coiled-coil (CC1) domain found in Sarcolemmal membrane-associated protein and similar ...
197-234 1.33e-09

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: 53.64  E-value: 1.33e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1953400674 197 QLSEYLKEALQRELVLKQKMVILQDLLSTLIRASDSSW 234
Cdd:cd21868     1 QLNQYIQEALQREQSLENKLANLQEILEATKKAAEESW 38
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
242-405 5.44e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 5.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 242 KLKGKLRSLENQLYtctqkyspwgmkkvLLEMEDQKNSYEQKAKEsLQKVLEEKMSAEQQLQSTQRSLALAEQKCEEWRS 321
Cdd:COG1196   217 ELKEELKELEAELL--------------LLKLRELEAELEELEAE-LEELEAELEELEAELAELEAELEELRLELEELEL 281
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 322 QYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKIELLQGDRDSSDTQHLQDQLKRS 401
Cdd:COG1196   282 ELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELA 361

                  ....
gi 1953400674 402 EEEK 405
Cdd:COG1196   362 EAEE 365
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
269-505 6.04e-07

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: 52.37  E-value: 6.04e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  269 VLLEMEDQKNSYEQKAK------------ESLQKVL--EEKMSAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLG 334
Cdd:TIGR02168  194 ILNELERQLKSLERQAEkaerykelkaelRELELALlvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELR 273
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  335 TQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKIELLQG--DRDSSDTQHLQDQLKRSEEEKLTLMAKV 412
Cdd:TIGR02168  274 LEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAqlEELESKLDELAEELAELEEKLEELKEEL 353
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  413 QQLQGLLQNQSLQLQEQEKLLTKKDQALplwspkpshnevepeGTGKEKEWDFRDQLQKKTLQLQAKEKECRELHSELDN 492
Cdd:TIGR02168  354 ESLEAELEELEAELEELESRLEELEEQL---------------ETLRSKVAQLELQIASLNNEIERLEARLERLEDRRER 418
                          250
                   ....*....|...
gi 1953400674  493 LSDEYLSCLRKLQ 505
Cdd:TIGR02168  419 LQQEIEELLKKLE 431
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
297-516 8.60e-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: 48.90  E-value: 8.60e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  297 SAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQ 376
Cdd:TIGR02168  667 KTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLE 746
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  377 AKIELLQGDRDSSDTQ---------HLQDQLKRSEEEKLTLMAKVQQLQGLLQNQSLQLQEQEKLLTK-----KDQALPL 442
Cdd:TIGR02168  747 ERIAQLSKELTELEAEieeleerleEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLlneeaANLRERL 826
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953400674  443 WSPKPSHNEVEPEGTGKEKEW-DFRDQLQKKTLQLQAKEKECRELHSELDNLSDEYLSCLRKLQHCREELNQSQQ 516
Cdd:TIGR02168  827 ESLERRIAATERRLEDLEEQIeELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSE 901
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
270-440 5.45e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 5.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 270 LLEMEDQKNSYEQKAKESLQKVLEekmsAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQS 349
Cdd:COG1196   297 LARLEQDIARLEERRRELEERLEE----LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 350 KLQGADSRDLQMNQALQLLENEHQELQAKIELLQGDRdssdtQHLQDQLKRSEEEKLTLMAKVQQLQGLLQNQSLQLQEQ 429
Cdd:COG1196   373 ELAEAEEELEELAEELLEALRAAAELAAQLEELEEAE-----EALLERLERLEEELEELEEALAELEEEEEEEEEALEEA 447
                         170
                  ....*....|.
gi 1953400674 430 EKLLTKKDQAL 440
Cdd:COG1196   448 AEEEAELEEEE 458
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
202-495 2.15e-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: 44.28  E-value: 2.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  202 LKEALQRELVLKQKMVILQDLLSTLIRASDSSWkgqlneDKLKGKLRSLENQLYTCTQKYspWGMKKVLLEMEDQKnsye 281
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKL------EELRLEVSELEEEIEELQKEL--YALANEISRLEQQK---- 304
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  282 QKAKESLQKVLEEKMSAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQM 361
Cdd:TIGR02168  305 QILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETL 384
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  362 NQALQLLENEHQELQAKIELLqgdrdSSDTQHLQDQLKRSEEEKLTLMAKVQQLQGLLQNQSlqlqeqeklLTKKDQALp 441
Cdd:TIGR02168  385 RSKVAQLELQIASLNNEIERL-----EARLERLEDRRERLQQEIEELLKKLEEAELKELQAE---------LEELEEEL- 449
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1953400674  442 lwspkpsHNEVEPEGTGKEKEWDFRDQLQKKTLQLQAKEKECRELHSELDNLSD 495
Cdd:TIGR02168  450 -------EELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLER 496
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
236-405 4.64e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 43.37  E-value: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  236 GQLNEDKLKGK---LRSLENQLYTCTQKYSpwGMKKVLLEMEDQKNSYEQKAK--------ESLQKVLEEKMSAEQQLQS 304
Cdd:COG4913    605 GFDNRAKLAALeaeLAELEEELAEAEERLE--ALEAELDALQERREALQRLAEyswdeidvASAEREIAELEAELERLDA 682
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  305 TQRSLALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQllENEHQELQAKIELLQG 384
Cdd:COG4913    683 SSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLAR--LELRALLEERFAAALG 760
                          170       180
                   ....*....|....*....|..
gi 1953400674  385 DRDSSD-TQHLQDQLKRSEEEK 405
Cdd:COG4913    761 DAVERElRENLEERIDALRARL 782
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
189-388 1.78e-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: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  189 AVLDKEIIQLSEYLKEALQRELVLKQKMVILQDLLSTLIRASDS--SWKGQLNED--KLKGKLRSLENQLYTCTQ----- 259
Cdd:TIGR02168  764 EELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDElrAELTLLNEEaaNLRERLESLERRIAATERrledl 843
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  260 KYSPWGMKKVLLEMEDQKNSYEQ---KAKESLQKVLEEKMSAEQQLQSTQRSLALAEQKCEEWRS-------QYEALKED 329
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEElieELESELEALLNERASLEEALALLRSELEELSEELRELESkrselrrELEELREK 923
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674  330 WRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQL-LENEHQELQAKIELLQGDRDS 388
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENkIEDDEEEARRRLKRLENKIKE 983
FPP pfam05911
Filament-like plant protein, long coiled-coil; FPP is a family of long coiled-coil plant ...
275-406 3.33e-03

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: 40.43  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 275 DQKNSYEQKAKESLQKVLEEK-------MSAEQQLQSTQRSLALAEQKCEEWRSQYEALKEDWRKLGTQ-------HREL 340
Cdd:pfam05911 677 DLKTEENKRLKEEFEQLKSEKenlevelASCTENLESTKSQLQESEQLIAELRSELASLKESNSLAETQlkcmaesYEDL 756
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953400674 341 ESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKiellqgdrdssdTQHLQDQLKRSEEEKL 406
Cdd:pfam05911 757 ETRLTELEAELNELRQKFEALEVELEEEKNCHEELEAK------------CLELQEQLERNEKKES 810
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
229-496 5.74e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 5.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 229 ASDSSWKGQLNEDKLKGKLRSLENQLytctqkyspwgmKKVLLEMEDQKNSYEQKAKEsLQKVLEEKMSAEQQLQSTQRS 308
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREEL------------EQAREELEQLEEELEQARSE-LEQLEEELEELNEQLQAAQAE 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 309 LALAEQKCEEWRSQYEALKEDWRKLGTQHRELESQLHVLQSKLQGADSRDLQMNQALQLLENEHQELQAKIELLQGDRDS 388
Cdd:COG4372    96 LAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953400674 389 SDTQHLQ---DQLKRSEEEKLTLMAKVQQLQGLLQNQSLQLQEQEKLLTKKDQALPLWSPKPSHNEVEPEGTGKEKEWDF 465
Cdd:COG4372   176 LSEAEAEqalDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEV 255
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953400674 466 RDQLQKKTLQLQAKEKECRELHSELDNLSDE 496
Cdd:COG4372   256 ILKEIEELELAILVEKDTEEEELEIAALELE 286
 
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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