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Conserved domains on  [gi|568961656|ref|XP_006511315|]
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coiled-coil domain-containing protein 33 isoform X1 [Mus musculus]

Protein Classification

C2 domain-containing protein( domain architecture ID 10033612)

C2 domain-containing protein may be a Ca2+-dependent membrane-targeting protein that binds a wide variety of substances including phospholipids, inositol polyphosphates, and intracellular proteins through its C2 domain

CATH:  2.60.40.150
Gene Ontology:  GO:0005544|GO:0005509
PubMed:  8976547|9632630
SCOP:  3000965

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
283-365 6.06e-07

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.60  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656  283 ITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKhspqamtSVTSEPTRAPVWGDTVNVEIqaEDTGREDLILKVMDNK 362
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFK-------TKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71

                  ...
gi 568961656  363 RKK 365
Cdd:cd00030    72 RFS 74
SMC_N super family cl47134
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
649-832 8.76e-06

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: 50.07  E-value: 8.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIE---------EQSRAEEENLAVSMKQ 719
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEEEVSRIEARLREIEQ 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   720 KLLLNELDMKRLRDRVQHLQNELI----RKNDREKELLLLYQAQQPQAAQLRRY-------------------------- 769
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlgdlkkerdeleaqlr 899
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961656   770 --QDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERKEPIpsnrPQGKPIMASGIPLGPVGETL 832
Cdd:TIGR02169  900 elERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELSLEDVQAEL 960
 
Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
283-365 6.06e-07

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.60  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656  283 ITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKhspqamtSVTSEPTRAPVWGDTVNVEIqaEDTGREDLILKVMDNK 362
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFK-------TKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71

                  ...
gi 568961656  363 RKK 365
Cdd:cd00030    72 RFS 74
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
649-832 8.76e-06

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: 50.07  E-value: 8.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIE---------EQSRAEEENLAVSMKQ 719
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEEEVSRIEARLREIEQ 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   720 KLLLNELDMKRLRDRVQHLQNELI----RKNDREKELLLLYQAQQPQAAQLRRY-------------------------- 769
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlgdlkkerdeleaqlr 899
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961656   770 --QDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERKEPIpsnrPQGKPIMASGIPLGPVGETL 832
Cdd:TIGR02169  900 elERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELSLEDVQAEL 960
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
282-366 1.15e-04

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 42.09  E-value: 1.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656    282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKHSpqamTSVTSEpTRAPVWGDTVNVEIQaeDTGREDLILKVMDN 361
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKK----TKVVKN-TLNPVWNETFEFEVP--PPELAELEIEVYDK 73

                    ....*
gi 568961656    362 KRKKE 366
Cdd:smart00239   74 DRFGR 78
C2 pfam00168
C2 domain;
282-363 1.97e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 38.84  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKaNKHSpqamTSVTSEpTRAPVWGDTVNVEIQAEDTgrEDLILKVMDN 361
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGK-QKKK----TKVVKN-TLNPVWNETFTFSVPDPEN--AVLEIEVYDY 73

                   ..
gi 568961656   362 KR 363
Cdd:pfam00168   74 DR 75
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
650-806 8.47e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 8.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   650 QEMEELQPRDVEMNNYRRAMQKMAEDILALK-KQANILEEENGMLRSHLSQQSIEEQSRAEEENLAVSMKQKLllneldM 728
Cdd:pfam13868  113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKERE------I 186
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961656   729 KRLRDRVQHLQNElirKNDREKELLLLYQAQQPQAAQLRRYQDKLQKMKALEDTVR-HQEKVIEKMEQILEERLCERKE 806
Cdd:pfam13868  187 ARLRAQQEKAQDE---KAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQaREEQIELKERRLAEEAEREEEE 262
 
Name Accession Description Interval E-value
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
283-365 6.06e-07

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 48.60  E-value: 6.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656  283 ITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKhspqamtSVTSEPTRAPVWGDTVNVEIqaEDTGREDLILKVMDNK 362
Cdd:cd00030     1 LRVTVIEARNLPAKDLNGKSDPYVKVSLGGKQKFK-------TKVVKNTLNPVWNETFEFPV--LDPESDTLTVEVWDKD 71

                  ...
gi 568961656  363 RKK 365
Cdd:cd00030    72 RFS 74
C2B_Synaptotagmin-like cd04050
C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
284-391 8.36e-07

C2 domain second repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the second C2 repeat, C2B, and has a type-I topology.


Pssm-ID: 176015 [Multi-domain]  Cd Length: 105  Bit Score: 48.33  E-value: 8.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656  284 TVTLYGATNLPAGKDGSEPWPYVVVKT--TSEKankhspqamtSVTSEPTRAPVWGDTVNVEIQaeDTGREDLILKVMDN 361
Cdd:cd04050     3 FVYLDSAKNLPLAKSTKEPSPYVELTVgkTTQK----------SKVKERTNNPVWEEGFTFLVR--NPENQELEIEVKDD 70
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 568961656  362 KRKKELVSYDIPIKYL-----RIFHPyQFKLEKSE 391
Cdd:cd04050    71 KTGKSLGSLTLPLSELlkepdLTLDQ-PFPLDNSG 104
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
649-832 8.76e-06

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: 50.07  E-value: 8.76e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   649 TQEMEELQPRDVEMNNYRRAMQKMAEDILALKKQANILEEENGMLRSHLSQQSIE---------EQSRAEEENLAVSMKQ 719
Cdd:TIGR02169  740 EELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLSHSRIPeiqaelsklEEEVSRIEARLREIEQ 819
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   720 KLLLNELDMKRLRDRVQHLQNELI----RKNDREKELLLLYQAQQPQAAQLRRY-------------------------- 769
Cdd:TIGR02169  820 KLNRLTLEKEYLEKEIQELQEQRIdlkeQIKSIEKEIENLNGKKEELEEELEELeaalrdlesrlgdlkkerdeleaqlr 899
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568961656   770 --QDKLQKMKALEDTVRHQEKVIEKMEQILEERLCERKEPIpsnrPQGKPIMASGIPLGPVGETL 832
Cdd:TIGR02169  900 elERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPK----GEDEEIPEEELSLEDVQAEL 960
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
282-366 1.15e-04

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 42.09  E-value: 1.15e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656    282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKANKHSpqamTSVTSEpTRAPVWGDTVNVEIQaeDTGREDLILKVMDN 361
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGKSDPYVKVSLDGDPKEKKK----TKVVKN-TLNPVWNETFEFEVP--PPELAELEIEVYDK 73

                    ....*
gi 568961656    362 KRKKE 366
Cdd:smart00239   74 DRFGR 78
C2 pfam00168
C2 domain;
282-363 1.97e-03

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 38.84  E-value: 1.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   282 TITVTLYGATNLPAGKDGSEPWPYVVVKTTSEKaNKHSpqamTSVTSEpTRAPVWGDTVNVEIQAEDTgrEDLILKVMDN 361
Cdd:pfam00168    2 RLTVTVIEAKNLPPKDGNGTSDPYVKVYLLDGK-QKKK----TKVVKN-TLNPVWNETFTFSVPDPEN--AVLEIEVYDY 73

                   ..
gi 568961656   362 KR 363
Cdd:pfam00168   74 DR 75
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
630-887 2.02e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.35  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   630 LDENLGAIRESWSMSSLDSTQEMEELQPRDVEMNNYRRAMQKMAEDI-------LALKKQANILEEENGMLRSHL--SQQ 700
Cdd:TIGR02168  237 LREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIeelqkelYALANEISRLEQQKQILRERLanLER 316
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   701 SIEEQSRAEEENLAVSMKQKLLLNELDMK--RLRDRVQHLQNELIRKNDREKELLLLYQAQQPQAAQLRR-YQDKLQKMK 777
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEELAELEEKleELKEELESLEAELEELEAELEELESRLEELEEQLETLRSkVAQLELQIA 396
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   778 ALEDTVRHQEKVIEKMEQILEERLCERKEPIPsnRPQGKPIMASGIPLGPVGETLAvdlysMLLAENTRLRTELEKNRQQ 857
Cdd:TIGR02168  397 SLNNEIERLEARLERLEDRRERLQQEIEELLK--KLEEAELKELQAELEELEEELE-----ELQEELERLEEALEELREE 469
                          250       260       270
                   ....*....|....*....|....*....|
gi 568961656   858 SAPIILQQQALPVDPRELGAGGDLAERLQD 887
Cdd:TIGR02168  470 LEEAEQALDAAERELAQLQARLDSLERLQE 499
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
650-806 8.47e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 39.52  E-value: 8.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568961656   650 QEMEELQPRDVEMNNYRRAMQKMAEDILALK-KQANILEEENGMLRSHLSQQSIEEQSRAEEENLAVSMKQKLllneldM 728
Cdd:pfam13868  113 EDQAEAEEKLEKQRQLREEIDEFNEEQAEWKeLEKEEEREEDERILEYLKEKAEREEEREAEREEIEEEKERE------I 186
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568961656   729 KRLRDRVQHLQNElirKNDREKELLLLYQAQQPQAAQLRRYQDKLQKMKALEDTVR-HQEKVIEKMEQILEERLCERKE 806
Cdd:pfam13868  187 ARLRAQQEKAQDE---KAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQaREEQIELKERRLAEEAEREEEE 262
 
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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