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Conserved domains on  [gi|346320050|gb|EGX89651|]
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alpha-taxilin, putative [Cordyceps militaris CM01]

Protein Classification

taxilin( domain architecture ID 12101238)

taxilin is a myosin-like coiled-coil protein involved in intracellular vesicle traffic

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
70-364 1.43e-84

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


:

Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 261.81  E-value: 1.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   70 RATRDLVQQISKMDDS-QKIDHLTKRSSELLADMRRLEKENQKNRKRGDILQKERDINRTELSKTVGLKEKLEKLCRELQ 148
Cdd:pfam09728   1 KAARELMQLLNKLDSPeEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  149 RDNNKMKNENKELQAIQKRNTLSWDEKYATLLSKLEGYQEDKDIPRKQVVDMEMEelFRVRFKSFIEQYELRELHFHSQM 228
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEE--LREKLKSLIEQYELRELHFEKLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  229 RTKEIELQYHLSRF-----DRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNTYIDKLGEacnVKSALDQRDDIFAR 303
Cdd:pfam09728 159 KTKELEVQLAEAKLqqateEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEE---FQDTLNKSNEVFTT 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346320050  304 QRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQHWKNKMDIADRKTEKLMSII 364
Cdd:pfam09728 236 FKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLC 296
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
70-364 1.43e-84

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 261.81  E-value: 1.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   70 RATRDLVQQISKMDDS-QKIDHLTKRSSELLADMRRLEKENQKNRKRGDILQKERDINRTELSKTVGLKEKLEKLCRELQ 148
Cdd:pfam09728   1 KAARELMQLLNKLDSPeEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  149 RDNNKMKNENKELQAIQKRNTLSWDEKYATLLSKLEGYQEDKDIPRKQVVDMEMEelFRVRFKSFIEQYELRELHFHSQM 228
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEE--LREKLKSLIEQYELRELHFEKLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  229 RTKEIELQYHLSRF-----DRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNTYIDKLGEacnVKSALDQRDDIFAR 303
Cdd:pfam09728 159 KTKELEVQLAEAKLqqateEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEE---FQDTLNKSNEVFTT 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346320050  304 QRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQHWKNKMDIADRKTEKLMSII 364
Cdd:pfam09728 236 FKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLC 296
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
43-328 2.95e-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: 53.14  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050    43 LAARISQLEQ--DAAGEKDQELEIERE-VKRATRDLVQQISKMDdsQKIDHLTKRSSELLADMRRLEKENQKNRKRGDIL 119
Cdd:TIGR02168  689 LEEKIAELEKalAELRKELEELEEELEqLRKELEELSRQISALR--KDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   120 QKERDINRTELsktVGLKEKLEKLCRELQRDNNKMKNENKELQAIQKRNTLSwDEKYATLLSKLEGYQEDKDIPRKQVVD 199
Cdd:TIGR02168  767 EERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLESLERRIAATERRLED 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   200 MEMEelfRVRFKSFIEQYELRELHFHSQMRTKEIELQYHLSRFDRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNT 279
Cdd:TIGR02168  843 LEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 346320050   280 YIDKLGEACNVKSALDQR-----DDIFARQRKEMQDQAKKCKRLEKDNEALRRQ 328
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRidnlqERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
43-344 2.92e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  43 LAARISQLEQDAA-GEKDQELEIEREVKRAT------RDLVQQISKMDdsQKIDHLTKRSSELLADMRRLEKENQKNRKR 115
Cdd:COG1196  198 LERQLEPLERQAEkAERYRELKEELKELEAEllllklRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050 116 GDILQKERDINRTELSKtvgLKEKLEKLCRELQRDNNKMKNENKELQAIQKRNtLSWDEKYATLLSKLEGYQEDKDIPRK 195
Cdd:COG1196  276 LEELELELEEAQAEEYE---LLAELARLEQDIARLEERRRELEERLEELEEEL-AELEEELEELEEELEELEEELEEAEE 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050 196 QVVDMEMEElfrvrfksfiEQYELRELHFHSQMRTKEIELQYHLSRFDRDKKATEAELAKMRQLQTQVQTLSRSETQLRT 275
Cdd:COG1196  352 ELEEAEAEL----------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346320050 276 ELNTYIDKLGEAcnvKSALDQRDDIFARQRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQ 344
Cdd:COG1196  422 ELEELEEALAEL---EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
 
Name Accession Description Interval E-value
Taxilin pfam09728
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ...
70-364 1.43e-84

Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.


Pssm-ID: 462861 [Multi-domain]  Cd Length: 302  Bit Score: 261.81  E-value: 1.43e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   70 RATRDLVQQISKMDDS-QKIDHLTKRSSELLADMRRLEKENQKNRKRGDILQKERDINRTELSKTVGLKEKLEKLCRELQ 148
Cdd:pfam09728   1 KAARELMQLLNKLDSPeEKLAALCKKYAELLEEMKRLQKDLKKLKKKQDQLQKEKDQLQSELSKAILAKSKLEKLCRELQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  149 RDNNKMKNENKELQAIQKRNTLSWDEKYATLLSKLEGYQEDKDIPRKQVVDMEMEelFRVRFKSFIEQYELRELHFHSQM 228
Cdd:pfam09728  81 KQNKKLKEESKKLAKEEEEKRKELSEKFQSTLKDIQDKMEEKSEKNNKLREENEE--LREKLKSLIEQYELRELHFEKLL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  229 RTKEIELQYHLSRF-----DRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNTYIDKLGEacnVKSALDQRDDIFAR 303
Cdd:pfam09728 159 KTKELEVQLAEAKLqqateEEEKKAQEKEVAKARELKAQVQTLSETEKELREQLNLYVEKFEE---FQDTLNKSNEVFTT 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 346320050  304 QRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQHWKNKMDIADRKTEKLMSII 364
Cdd:pfam09728 236 FKKEMEKMSKKIKKLEKENLTWKRKWEKSNKALLEMAEERQKLKEELEKLQKKLEKLENLC 296
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
43-328 2.95e-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: 53.14  E-value: 2.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050    43 LAARISQLEQ--DAAGEKDQELEIERE-VKRATRDLVQQISKMDdsQKIDHLTKRSSELLADMRRLEKENQKNRKRGDIL 119
Cdd:TIGR02168  689 LEEKIAELEKalAELRKELEELEEELEqLRKELEELSRQISALR--KDLARLEAEVEQLEERIAQLSKELTELEAEIEEL 766
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   120 QKERDINRTELsktVGLKEKLEKLCRELQRDNNKMKNENKELQAIQKRNTLSwDEKYATLLSKLEGYQEDKDIPRKQVVD 199
Cdd:TIGR02168  767 EERLEEAEEEL---AEAEAEIEELEAQIEQLKEELKALREALDELRAELTLL-NEEAANLRERLESLERRIAATERRLED 842
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   200 MEMEelfRVRFKSFIEQYELRELHFHSQMRTKEIELQYHLSRFDRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNT 279
Cdd:TIGR02168  843 LEEQ---IEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEE 919
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 346320050   280 YIDKLGEACNVKSALDQR-----DDIFARQRKEMQDQAKKCKRLEKDNEALRRQ 328
Cdd:TIGR02168  920 LREKLAQLELRLEGLEVRidnlqERLSEEYSLTLEEAEALENKIEDDEEEARRR 973
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
43-344 2.92e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  43 LAARISQLEQDAA-GEKDQELEIEREVKRAT------RDLVQQISKMDdsQKIDHLTKRSSELLADMRRLEKENQKNRKR 115
Cdd:COG1196  198 LERQLEPLERQAEkAERYRELKEELKELEAEllllklRELEAELEELE--AELEELEAELEELEAELAELEAELEELRLE 275
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050 116 GDILQKERDINRTELSKtvgLKEKLEKLCRELQRDNNKMKNENKELQAIQKRNtLSWDEKYATLLSKLEGYQEDKDIPRK 195
Cdd:COG1196  276 LEELELELEEAQAEEYE---LLAELARLEQDIARLEERRRELEERLEELEEEL-AELEEELEELEEELEELEEELEEAEE 351
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050 196 QVVDMEMEElfrvrfksfiEQYELRELHFHSQMRTKEIELQYHLSRFDRDKKATEAELAKMRQLQTQVQTLSRSETQLRT 275
Cdd:COG1196  352 ELEEAEAEL----------AEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEE 421
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 346320050 276 ELNTYIDKLGEAcnvKSALDQRDDIFARQRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQ 344
Cdd:COG1196  422 ELEELEEALAEL---EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELA 487
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
85-351 1.61e-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: 1.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050    85 SQKIDHLTKRSSELLADMRRLEKENQKNRKRGDILQKERDINRTEL----SKTVGLKEKLEKLCRELQRDNNKMKNENKE 160
Cdd:TIGR02168  676 RREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELeelsRQISALRKDLARLEAEVEQLEERIAQLSKE 755
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   161 LQAIQKRNTLSWDEKYATLLSKLEGYQEDKDIPRKQVVDMEMEELFRVRFKSFIEQYELRELHFHSQMRTkeieLQYHLS 240
Cdd:TIGR02168  756 LTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER----LESLER 831
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   241 RFDRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNTYIDKLGEACNVKSALDQRddiFARQRKEMQDQAKKCKRLEK 320
Cdd:TIGR02168  832 RIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEA---LALLRSELEELSEELRELES 908
                          250       260       270
                   ....*....|....*....|....*....|.
gi 346320050   321 DNEALRRQKEATAANIIRMAEERQHWKNKMD 351
Cdd:TIGR02168  909 KRSELRRELEELREKLAQLELRLEGLEVRID 939
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
41-344 1.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.16  E-value: 1.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  41 RLLAARISQLEQDAAGEKDQELEIEREVKRATRDLVQ-QISKMDdsQKIDHLTKRSSELLADMRRLEKENQKNRKRGDIL 119
Cdd:COG1196  230 LLLKLRELEAELEELEAELEELEAELEELEAELAELEaELEELR--LELEELELELEEAQAEEYELLAELARLEQDIARL 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050 120 QKERDINRTELSKtvgLKEKLEKLCRELQRDNNKMKNENKELQAIQKRNTLSwDEKYATLLSKLEGYQEdkdiprkqvvD 199
Cdd:COG1196  308 EERRRELEERLEE---LEEELAELEEELEELEEELEELEEELEEAEEELEEA-EAELAEAEEALLEAEA----------E 373
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050 200 MEMEELFRVRFKSFIEQYELRELHFHSQMRTKEIELQYHLSRFDRDKKATEAELAKMRQLQTQVQTLSRSETQLRTELNT 279
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAE 453
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 346320050 280 YIDKLGEACNVKSALDQRDDIFARQRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQ 344
Cdd:COG1196  454 LEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAG 518
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
48-387 2.03e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 2.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050    48 SQLEQDAAGEKDQELEIEREVKRATRDLVQQISKMDD-SQKIDHLTKRSSELLADMRRLEKEnqknrkrgdiLQKERDIN 126
Cdd:pfam15921  331 SELREAKRMYEDKIEELEKQLVLANSELTEARTERDQfSQESGNLDDQLQKLLADLHKREKE----------LSLEKEQN 400
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   127 RTELSKTVGLKEKLEKLCRELQRDNNKMKNENKELQAIQKRNTLSWDEKYATLLSKLEGYQEDKDIPRKQVVDMEMeelf 206
Cdd:pfam15921  401 KRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLEKVSSLTAQLESTKEM---- 476
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   207 rvrFKSFIEQYELRELHFHSQMRTKEiELQYHLSRFDRDKKATEAELAKMR-QLQTQVQTLSrsetQLRTELNTYIDKLG 285
Cdd:pfam15921  477 ---LRKVVEELTAKKMTLESSERTVS-DLTASLQEKERAIEATNAEITKLRsRVDLKLQELQ----HLKNEGDHLRNVQT 548
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050   286 EACNVKSALDQRDDIFARQRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQHWKNKMDIADRKTEKLMSIIQ 365
Cdd:pfam15921  549 ECEALKLQMAEKDKVIEILRQQIENMTQLVGQHGRTAGAMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIRELEARVS 628
                          330       340
                   ....*....|....*....|..
gi 346320050   366 QMQQQGRKVPSAMESTLESCKN 387
Cdd:pfam15921  629 DLELEKVKLVNAGSERLRAVKD 650
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
119-349 7.01e-03

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 38.93  E-value: 7.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  119 LQKERDINRTELSKTVGLKEKLEKLCRELQRDNNKMKNENKELQAI-QKRNTLSWDEKYATLLSKLEGYQEDKDIpRKQV 197
Cdd:pfam05483 399 FKNNKEVELEELKKILAEDEKLLDEKKQFEKIAEELKGKEQELIFLlQAREKEIHDLEIQLTAIKTSEEHYLKEV-EDLK 477
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 346320050  198 VDMEMEELFRVRFKSFIEQYELRELHFHSQMRTKEIELQYHLSRFDRDKKATEAELakmrqlqTQVQTLSRSETQLRTEL 277
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEERML-------KQIENLEEKEMNLRDEL 550
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 346320050  278 NTYIDKLGEACN-VKSALDQRDDIFARQRKEMQDQAKKCKRLEKDNEALRRQKEATAANIIRMAEERQHWKNK 349
Cdd:pfam05483 551 ESVREEFIQKGDeVKCKLDKSEENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEELHQENKALKKK 623
 
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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