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Conserved domains on  [gi|2024511933|ref|XP_040532052|]
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coiled-coil domain-containing protein 141 isoform X2 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 133-357 1.99e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 50.14  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  133 FFENALEFAVKIDQVEDFLKNAQEFDNIDNLRELLLQQEHHTKELLEKSlallNKSHELTEFIEEFKREGPNANTEVIQG 212
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHE----ERVEALNELGEQLIEEGHPDAEEIQER 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  213 AQSSCLKIDSLLELLQDRRRQLDRSLKHQRQgLEQVLQICLW-HQQENQVTSwykknirdyihkQNLGSSLLENEELLKE 291
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQF-FRDADDLEQWlEEKEAALAS------------EDLGKDLESVEELLKK 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024511933  292 HKEMEVRLKEWSSTVEQLEAEAVKILLSEDYTEKEHLNLSSQKIHLLRGEVCCHMEERKALLQEAN 357
Cdd:cd00176    148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 857-1080 8.21e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  857 LNVSVKNLKQELARLECDSINWSSKADKYEEELSQ-HFQYHIYQEEINELRESFKDLKKKFNNLKFNYTKKTEKARNLKA 935
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  936 LKIQI-QQVDTYPEKIQILKKKIDNLEKRL--VDTATNEPNVRVFLGSVSELQKQLNDFGIVVEDYKQNL-GLTEHLQLM 1011
Cdd:TIGR02168  387 KVAQLeLQIASLNNEIERLEARLERLEDRRerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALEEL 466

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024511933 1012 MEECQFCFEDVSATVIRVGKYSAECKTREAMETLYKQFNKFIeSTVPQQEEKFQQIIDLAKQLYGFEEG 1080
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEG 534
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 133-357 1.99e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.14  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  133 FFENALEFAVKIDQVEDFLKNAQEFDNIDNLRELLLQQEHHTKELLEKSlallNKSHELTEFIEEFKREGPNANTEVIQG 212
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHE----ERVEALNELGEQLIEEGHPDAEEIQER 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  213 AQSSCLKIDSLLELLQDRRRQLDRSLKHQRQgLEQVLQICLW-HQQENQVTSwykknirdyihkQNLGSSLLENEELLKE 291
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQF-FRDADDLEQWlEEKEAALAS------------EDLGKDLESVEELLKK 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024511933  292 HKEMEVRLKEWSSTVEQLEAEAVKILLSEDYTEKEHLNLSSQKIHLLRGEVCCHMEERKALLQEAN 357
Cdd:cd00176    148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 857-1080 8.21e-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: 43.89  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  857 LNVSVKNLKQELARLECDSINWSSKADKYEEELSQ-HFQYHIYQEEINELRESFKDLKKKFNNLKFNYTKKTEKARNLKA 935
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  936 LKIQI-QQVDTYPEKIQILKKKIDNLEKRL--VDTATNEPNVRVFLGSVSELQKQLNDFGIVVEDYKQNL-GLTEHLQLM 1011
Cdd:TIGR02168  387 KVAQLeLQIASLNNEIERLEARLERLEDRRerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALEEL 466

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024511933 1012 MEECQFCFEDVSATVIRVGKYSAECKTREAMETLYKQFNKFIeSTVPQQEEKFQQIIDLAKQLYGFEEG 1080
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEG 534
 
Name Accession Description Interval E-value
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 133-357 1.99e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.14  E-value: 1.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  133 FFENALEFAVKIDQVEDFLKNAQEFDNIDNLRELLLQQEHHTKELLEKSlallNKSHELTEFIEEFKREGPNANTEVIQG 212
Cdd:cd00176      5 FLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKKHEALEAELAAHE----ERVEALNELGEQLIEEGHPDAEEIQER 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  213 AQSSCLKIDSLLELLQDRRRQLDRSLKHQRQgLEQVLQICLW-HQQENQVTSwykknirdyihkQNLGSSLLENEELLKE 291
Cdd:cd00176     81 LEELNQRWEELRELAEERRQRLEEALDLQQF-FRDADDLEQWlEEKEAALAS------------EDLGKDLESVEELLKK 147

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024511933  292 HKEMEVRLKEWSSTVEQLEAEAVKILLSEDYTEKEHLNLSSQKIHLLRGEVCCHMEERKALLQEAN 357
Cdd:cd00176    148 HKELEEELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEAL 213
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 52-238 2.17e-05

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 47.06  E-value: 2.17e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933   52 EIGSNQDETRKLLQDHELLLTKLKALEDKVWDLLHEADKAAEENKEKSQVYDAMAETLGDAWDTLIIMLEKRQALLELTM 131
Cdd:cd00176     27 DYGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEAL 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  132 ---VFFENALEFAVKIDQVEDFLKNAQEFDNIDNLRELLLQQEHHTKELLEKSlallNKSHELTEFIEEFKREGPNANTE 208
Cdd:cd00176    107 dlqQFFRDADDLEQWLEEKEAALASEDLGKDLESVEELLKKHKELEEELEAHE----PRLKSLNELAEELLEEGHPDADE 182

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024511933  209 VIQGAQSSCL-KIDSLLELLQDRRRQLDRSL 238
Cdd:cd00176    183 EIEEKLEELNeRWEELLELAEERQKKLEEAL 213
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 857-1080 8.21e-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: 43.89  E-value: 8.21e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  857 LNVSVKNLKQELARLECDSINWSSKADKYEEELSQ-HFQYHIYQEEINELRESFKDLKKKFNNLKFNYTKKTEKARNLKA 935
Cdd:TIGR02168  307 LRERLANLERQLEELEAQLEELESKLDELAEELAElEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRS 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024511933  936 LKIQI-QQVDTYPEKIQILKKKIDNLEKRL--VDTATNEPNVRVFLGSVSELQKQLNDFGIVVEDYKQNL-GLTEHLQLM 1011
Cdd:TIGR02168  387 KVAQLeLQIASLNNEIERLEARLERLEDRRerLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELeRLEEALEEL 466

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024511933 1012 MEECQFCFEDVSATVIRVGKYSAECKTREAMETLYKQFNKFIeSTVPQQEEKFQQIIDLAKQLYGFEEG 1080
Cdd:TIGR02168  467 REELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGV-KALLKNQSGLSGILGVLSELISVDEG 534
 
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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