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Conserved domains on  [gi|1958742591|ref|XP_038952586|]
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coiled-coil domain-containing protein 68 isoform X1 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
85-297 7.36e-05

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


The actual alignment was detected with superfamily member TIGR02169:

Pssm-ID: 481474 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 7.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591   85 RLDLLLESMRRKDQQLLEMNKENEVLQIKLEASREAGAAALR--NAAQRLFDNYQTQSEDLEKK-----HKDSKHVLQVN 157
Cdd:TIGR02169  703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELEARieeleEDLHKLEEALN 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  158 KLEKEQtLKQRAKNLSQLSEKLGEKHEQIVGlenRVQRMENEKKALLERKLCLESKLlqlksnaanskscQHLQTEISIL 237
Cdd:TIGR02169  783 DLEARL-SHSRIPEIQAELSKLEEEVSRIEA---RLREIEQKLNRLTLEKEYLEKEI-------------QELQEQRIDL 845
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  238 QEQICHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQNEELKTKV 297
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-297 7.36e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 7.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591   85 RLDLLLESMRRKDQQLLEMNKENEVLQIKLEASREAGAAALR--NAAQRLFDNYQTQSEDLEKK-----HKDSKHVLQVN 157
Cdd:TIGR02169  703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELEARieeleEDLHKLEEALN 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  158 KLEKEQtLKQRAKNLSQLSEKLGEKHEQIVGlenRVQRMENEKKALLERKLCLESKLlqlksnaanskscQHLQTEISIL 237
Cdd:TIGR02169  783 DLEARL-SHSRIPEIQAELSKLEEEVSRIEA---RLREIEQKLNRLTLEKEYLEKEI-------------QELQEQRIDL 845
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  238 QEQICHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQNEELKTKV 297
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
140-203 6.83e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 6.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958742591 140 SEDLEKKHKDSKHVLQVNKLEKEQTLKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKAL 203
Cdd:PRK05771   63 RSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
107-298 3.31e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 107 NEVLQIKLEASREAGAAALRNAAQRLfdnyQTQSEDLEKkhkdskhvlQVNKLEKEQTLKQRAKNLSQLSEKLGEKHEQI 186
Cdd:COG3206   155 NALAEAYLEQNLELRREEARKALEFL----EEQLPELRK---------ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 187 VGLENRVQRMENEKKALLERKLCLESKL---LQLKSNAANSKSCQHLQTEISILQEQICHLQFVIHSQHQNLRNIIQEME 263
Cdd:COG3206   222 SELESQLAEARAELAEAEARLAALRAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958742591 264 GLKNTLKEQDKKI--------ENLKEKVTVLEAQNEELKTKVA 298
Cdd:COG3206   302 ALRAQLQQEAQRIlasleaelEALQAREASLQAQLAQLEARLA 344
 
Name Accession Description Interval E-value
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-297 7.36e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 44.67  E-value: 7.36e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591   85 RLDLLLESMRRKDQQLLEMNKENEVLQIKLEASREAGAAALR--NAAQRLFDNYQTQSEDLEKK-----HKDSKHVLQVN 157
Cdd:TIGR02169  703 RLDELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEdlSSLEQEIENVKSELKELEARieeleEDLHKLEEALN 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  158 KLEKEQtLKQRAKNLSQLSEKLGEKHEQIVGlenRVQRMENEKKALLERKLCLESKLlqlksnaanskscQHLQTEISIL 237
Cdd:TIGR02169  783 DLEARL-SHSRIPEIQAELSKLEEEVSRIEA---RLREIEQKLNRLTLEKEYLEKEI-------------QELQEQRIDL 845
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  238 QEQICHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQNEELKTKV 297
Cdd:TIGR02169  846 KEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKI 905
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
85-295 2.69e-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: 42.74  E-value: 2.69e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591   85 RLDLLLESMRRKDQQLLEMNKENEVLQIKLEASREAGAAALRNAAQRLFDnYQTQSEDLEKKHKDSKHVLQvnklEKEQT 164
Cdd:TIGR02168  299 RLEQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEE-LKEELESLEAELEELEAELE----ELESR 373
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  165 LKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKALLERKLCLESKLLQLKSNAANSKScQHLQTEISILQEQICHL 244
Cdd:TIGR02168  374 LEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAEL-KELQAELEELEEELEEL 452
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958742591  245 QFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQNEELKT 295
Cdd:TIGR02168  453 QEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEG 503
PRK05771 PRK05771
V-type ATP synthase subunit I; Validated
140-203 6.83e-04

V-type ATP synthase subunit I; Validated


Pssm-ID: 235600 [Multi-domain]  Cd Length: 646  Bit Score: 41.45  E-value: 6.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958742591 140 SEDLEKKHKDSKHVLQVNKLEKEQTLKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKAL 203
Cdd:PRK05771   63 RSYLPKLNPLREEKKKVSVKSLEELIKDVEEELEKIEKEIKELEEEISELENEIKELEQEIERL 126
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
159-295 8.97e-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: 41.20  E-value: 8.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  159 LEKEQTLKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKALLERKLCLESKLLQLKSNAANskscqhLQTEISILQ 238
Cdd:TIGR02168  673 LERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLAR------LEAEVEQLE 746
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958742591  239 EQICHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQNEELKT 295
Cdd:TIGR02168  747 ERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALRE 803
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
136-298 9.53e-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: 41.20  E-value: 9.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  136 YQTQSEDLEKKHK----DSKHVLQVNKLEKEQTLKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEK-------KALL 204
Cdd:TIGR02168  215 YKELKAELRELELallvLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelYALA 294
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  205 ERKLCLESKLLQLKSNAANS-KSCQHLQTEISILQEQICHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKV 283
Cdd:TIGR02168  295 NEISRLEQQKQILRERLANLeRQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRL 374
                          170
                   ....*....|....*
gi 1958742591  284 TVLEAQNEELKTKVA 298
Cdd:TIGR02168  375 EELEEQLETLRSKVA 389
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
107-298 3.31e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 107 NEVLQIKLEASREAGAAALRNAAQRLfdnyQTQSEDLEKkhkdskhvlQVNKLEKEQTLKQRAKNLSQLSEKLGEKHEQI 186
Cdd:COG3206   155 NALAEAYLEQNLELRREEARKALEFL----EEQLPELRK---------ELEEAEAALEEFRQKNGLVDLSEEAKLLLQQL 221
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 187 VGLENRVQRMENEKKALLERKLCLESKL---LQLKSNAANSKSCQHLQTEISILQEQICHLQFVIHSQHQNLRNIIQEME 263
Cdd:COG3206   222 SELESQLAEARAELAEAEARLAALRAQLgsgPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIA 301
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1958742591 264 GLKNTLKEQDKKI--------ENLKEKVTVLEAQNEELKTKVA 298
Cdd:COG3206   302 ALRAQLQQEAQRIlasleaelEALQAREASLQAQLAQLEARLA 344
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
74-296 3.71e-03

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 39.23  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  74 QNGLDSTtdPTRLDLLLESMRRKDQQLLEMNKENEVLQIKLEASReagaaalrnaaQRLFDNYQTQSEDLEkkhkdskHV 153
Cdd:COG3206   204 KNGLVDL--SEEAKLLLQQLSELESQLAEARAELAEAEARLAALR-----------AQLGSGPDALPELLQ-------SP 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 154 LQVNKLEKEQTLKQRaknLSQLSEKLGEKHEQIVGLENRVQRMENEKKALLERKLcleskllqlksnaanskscQHLQTE 233
Cdd:COG3206   264 VIQQLRAQLAELEAE---LAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRIL-------------------ASLEAE 321
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958742591 234 ISILQEQIchlqfvihsqhQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQNEELKTK 296
Cdd:COG3206   322 LEALQARE-----------ASLQAQLAQLEARLAELPELEAELRRLEREVEVARELYESLLQR 373
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
165-297 5.59e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 37.60  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 165 LKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKALLERKLCLESKLLQLKSN---AANSKSCQHLQTEISILQEQI 241
Cdd:COG1579    33 LAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQLGNVRNNkeyEALQKEIESLKRRISDLEDEI 112
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 242 CHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQ----DKKIENLKEKVTVLEAQNEELKTKV 297
Cdd:COG1579   113 LELMERIEELEEELAELEAELAELEAELEEKkaelDEELAELEAELEELEAEREELAAKI 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
134-293 8.11e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 8.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 134 DNYQTQSEDLEKK---HKDSKHVLQVNKLEKEQTLKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKALLERKlcl 210
Cdd:COG1196   235 RELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERR--- 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591 211 eskllqlksnaanskscQHLQTEISILQEQICHLQFVIHSQHQNLRNIIQEMEGLKNTLKEQDKKIENLKEKVTVLEAQN 290
Cdd:COG1196   312 -----------------RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL 374

                  ...
gi 1958742591 291 EEL 293
Cdd:COG1196   375 AEA 377
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
85-311 8.41e-03

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 38.13  E-value: 8.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591   85 RLDLLLESMRRKDQQLLEMNKENEvLQIKLEASREAGAAALRNAAQRLFDNYQTQSEDLEKKHKDskhvlqvnkLEKEqt 164
Cdd:TIGR02169  823 RLTLEKEYLEKEIQELQEQRIDLK-EQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGD---------LKKE-- 890
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958742591  165 LKQRAKNLSQLSEKLGEKHEQIVGLENRVQRMENEKKALLERKLCLESKLLQLKSNAANSKSCQHLQTEISILQEQICHL 244
Cdd:TIGR02169  891 RDELEAQLRELERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRAL 970
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958742591  245 QFVihsqhqNLRnIIQEMEGLKNTLKEqdkkienLKEKVTVLEAQNEELKTKVAHWTESPRTSVSKA 311
Cdd:TIGR02169  971 EPV------NML-AIQEYEEVLKRLDE-------LKEKRAKLEEERKAILERIEEYEKKKREVFMEA 1023
 
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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