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Conserved domains on  [gi|2093825691|ref|NP_001152843|]
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hydrocephalus-inducing protein homolog [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
 2017-2216 6.18e-78

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


:

Pssm-ID: 465383  Cd Length: 199  Bit Score: 257.76  E-value: 6.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2017 IIIHGAPLTGKTSAAVALSRHYGTACLSIDSLVMEAISDRNSSAGLRARELCLRAAIEQSHKETEEAGQST-----DPSA 2091
Cdd:pfam17213    2 IIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAavvpgQPTT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2092 PQLGAEP--RHSLETSQSSSGDKTSlhsisSRSRASAATGRRKSDNHASQSQKQQ-LTDPTGSQGSSSShrflvLPCVPT 2168
Cdd:pfam17213   82 YRLSVEAltKHTSEGTLVGPESKIS-----KGKRGSVVSGKGKADSHGTGSQKQHhQHQSETPQISSSP-----PPAGPI 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2093825691 2169 QQWLSIGDSAAGEVGLMSCVLPEDVLGAILSERLQLSDCYQGVVFDGL 2216
Cdd:pfam17213  152 QRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 509-608 2.09e-16

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


:

Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 77.70  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691  509 EGLIPPGGLQhIHISFCSTILGQFTEEFGVTVHGCPQPVTLTVrGCVIGPTFHFDVPSLCFgDVSFGFPHTLSCRLSNTS 588
Cdd:pfam15780    2 VLLLAPFSRQ-PFVCFGDVPVGTSAERLLTVVNPSEEPAEVKV-SKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78

                           90       100
                   ....*....|....*....|
gi 2093825691  589 LVPMTFSLRIPGDGSGAPSV 608
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 2433-2528 6.95e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.60  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2433 QEEAK--EKALSDSEKM---LAMRFKIYEASQKdiahilsnwdrvqgvlvsswSQEEAWQRAEEQNTHLSSRRSRKDREK 2507
Cdd:pfam20492   19 EEETKkaQEELEESEETaeeLEEERRQAEEEAE--------------------RLEQKRQEAEEEKERLEESAEMEAEEK 78

                           90       100
                   ....*....|....*....|.
gi 2093825691 2508 ERLEKERqeRERQEKLKALEE 2528
Cdd:pfam20492   79 EQLEAEL--AEAQEEIARLEE 97
choice_anch_D super family cl44405
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long ...
 4385-4434 2.26e-03

choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM.


The actual alignment was detected with superfamily member NF012200:

Pssm-ID: 467954 [Multi-domain]  Cd Length: 107  Bit Score: 40.68  E-value: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2093825691 4385 TVEVQGKGAEMKVDVVEPHGKVVKLGALSVGQTVKKTVTIANNSVAPLTF 4434
Cdd:NF012200     2 TVALTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTI 51
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
 2017-2216 6.18e-78

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 257.76  E-value: 6.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2017 IIIHGAPLTGKTSAAVALSRHYGTACLSIDSLVMEAISDRNSSAGLRARELCLRAAIEQSHKETEEAGQST-----DPSA 2091
Cdd:pfam17213    2 IIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAavvpgQPTT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2092 PQLGAEP--RHSLETSQSSSGDKTSlhsisSRSRASAATGRRKSDNHASQSQKQQ-LTDPTGSQGSSSShrflvLPCVPT 2168
Cdd:pfam17213   82 YRLSVEAltKHTSEGTLVGPESKIS-----KGKRGSVVSGKGKADSHGTGSQKQHhQHQSETPQISSSP-----PPAGPI 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2093825691 2169 QQWLSIGDSAAGEVGLMSCVLPEDVLGAILSERLQLSDCYQGVVFDGL 2216
Cdd:pfam17213  152 QRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 509-608 2.09e-16

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 77.70  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691  509 EGLIPPGGLQhIHISFCSTILGQFTEEFGVTVHGCPQPVTLTVrGCVIGPTFHFDVPSLCFgDVSFGFPHTLSCRLSNTS 588
Cdd:pfam15780    2 VLLLAPFSRQ-PFVCFGDVPVGTSAERLLTVVNPSEEPAEVKV-SKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78

                           90       100
                   ....*....|....*....|
gi 2093825691  589 LVPMTFSLRIPGDGSGAPSV 608
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 2433-2528 6.95e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.60  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2433 QEEAK--EKALSDSEKM---LAMRFKIYEASQKdiahilsnwdrvqgvlvsswSQEEAWQRAEEQNTHLSSRRSRKDREK 2507
Cdd:pfam20492   19 EEETKkaQEELEESEETaeeLEEERRQAEEEAE--------------------RLEQKRQEAEEEKERLEESAEMEAEEK 78

                           90       100
                   ....*....|....*....|.
gi 2093825691 2508 ERLEKERqeRERQEKLKALEE 2528
Cdd:pfam20492   79 EQLEAEL--AEAQEEIARLEE 97
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 2468-2576 8.13e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.57  E-value: 8.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2468 NWDRVQgvlvsswSQEEAWQRAEEQNTHLSSRRSRKDREKERLEKERQERERQEKLKALEEsQAQAGKGAEGSAKGQDvg 2547
Cdd:PRK09510    63 QYNRQQ-------QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQK-- 132

                           90       100
                   ....*....|....*....|....*....
gi 2093825691 2548 vpcldiqvlDAEDAIGKILESGKLPPAEQ 2576
Cdd:PRK09510   133 ---------QAEEAAAKAAAAAKAKAEAE 152
choice_anch_D NF012200
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long ...
 4385-4434 2.26e-03

choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM.


Pssm-ID: 467954 [Multi-domain]  Cd Length: 107  Bit Score: 40.68  E-value: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2093825691 4385 TVEVQGKGAEMKVDVVEPHGKVVKLGALSVGQTVKKTVTIANNSVAPLTF 4434
Cdd:NF012200     2 TVALTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTI 51
 
Name Accession Description Interval E-value
Hydin_ADK pfam17213
Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to ...
 2017-2216 6.18e-78

Hydin Adenylate kinase-like domain; This domain found in the Hydin protein is homologous to adenylate kinases.


Pssm-ID: 465383  Cd Length: 199  Bit Score: 257.76  E-value: 6.18e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2017 IIIHGAPLTGKTSAAVALSRHYGTACLSIDSLVMEAISDRNSSAGLRARELCLRAAIEQSHKETEEAGQST-----DPSA 2091
Cdd:pfam17213    2 IIVHGAPLSGKTATAVTLAKHYGAACLTIDSIVLEAISDGNSIAGLRARELCARAAIEQSEREAEEAAQEAavvpgQPTT 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2092 PQLGAEP--RHSLETSQSSSGDKTSlhsisSRSRASAATGRRKSDNHASQSQKQQ-LTDPTGSQGSSSShrflvLPCVPT 2168
Cdd:pfam17213   82 YRLSVEAltKHTSEGTLVGPESKIS-----KGKRGSVVSGKGKADSHGTGSQKQHhQHQSETPQISSSP-----PPAGPI 151

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2093825691 2169 QQWLSIGDSAAGEVGLMSCVLPEDVLGAILSERLQLSDCYQGVVFDGL 2216
Cdd:pfam17213  152 QRRLSVSASVGGEEGLMSCVLPEDLLVEILAERIQLNDCHRGVVFDGL 199
ASH pfam15780
Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal ...
 509-608 2.09e-16

Abnormal spindle-like microcephaly-assoc'd, ASPM-SPD-2-Hydin; The ASH domain or N-terminal domain of abnormal spindle-like microcephaly-associated protein are found in proteins associated with cilia, flagella, the centrosome and the Golgi complex. The domain is also found in Hydin and OCRL whose deficiencies are associated with hydrocephalus and Lowe oculocerebrorenal syndrome (OCRL), respectively. The fact that Human ASPM protein carries an ASH domain indicates possible roles for ASPM in sperm flagellar or in ependymal cells' cilia. The presence of ASH in centrosomal and ciliary proteins indicates that ASPM may possess roles not only in mitotic spindle regulation, but also in ciliary and flagellar function.


Pssm-ID: 464865 [Multi-domain]  Cd Length: 98  Bit Score: 77.70  E-value: 2.09e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691  509 EGLIPPGGLQhIHISFCSTILGQFTEEFGVTVHGCPQPVTLTVrGCVIGPTFHFDVPSLCFgDVSFGFPHTLSCRLSNTS 588
Cdd:pfam15780    2 VLLLAPFSRQ-PFVCFGDVPVGTSAERLLTVVNPSEEPAEVKV-SKVPAPTKGFSVSPLEF-TVQPGESQTLTVTWTPTE 78

                           90       100
                   ....*....|....*....|
gi 2093825691  589 LVPMTFSLRIPGDGSGAPSV 608
Cdd:pfam15780   79 EGAVRETLQFTVNDVGKHQV 98
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 2433-2528 6.95e-04

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 42.60  E-value: 6.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2433 QEEAK--EKALSDSEKM---LAMRFKIYEASQKdiahilsnwdrvqgvlvsswSQEEAWQRAEEQNTHLSSRRSRKDREK 2507
Cdd:pfam20492   19 EEETKkaQEELEESEETaeeLEEERRQAEEEAE--------------------RLEQKRQEAEEEKERLEESAEMEAEEK 78

                           90       100
                   ....*....|....*....|.
gi 2093825691 2508 ERLEKERqeRERQEKLKALEE 2528
Cdd:pfam20492   79 EQLEAEL--AEAQEEIARLEE 97
tolA PRK09510
cell envelope integrity inner membrane protein TolA; Provisional
 2468-2576 8.13e-04

cell envelope integrity inner membrane protein TolA; Provisional


Pssm-ID: 236545 [Multi-domain]  Cd Length: 387  Bit Score: 45.57  E-value: 8.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2468 NWDRVQgvlvsswSQEEAWQRAEEQNTHLSSRRSRKDREKERLEKERQERERQEKLKALEEsQAQAGKGAEGSAKGQDvg 2547
Cdd:PRK09510    63 QYNRQQ-------QQQKSAKRAEEQRKKKEQQQAEELQQKQAAEQERLKQLEKERLAAQEQ-KKQAEEAAKQAALKQK-- 132

                           90       100
                   ....*....|....*....|....*....
gi 2093825691 2548 vpcldiqvlDAEDAIGKILESGKLPPAEQ 2576
Cdd:PRK09510   133 ---------QAEEAAAKAAAAAKAKAEAE 152
choice_anch_D NF012200
choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long ...
 4385-4434 2.26e-03

choice-of-anchor D domain; This HMM describes a repeat domain just over 100 amino acids long and usually found in tandem copies. Members appear to be extracellular proteins that have some C-terminal anchoring domain, such as type IX secrection (T9SS) or PEP-CTERM.


Pssm-ID: 467954 [Multi-domain]  Cd Length: 107  Bit Score: 40.68  E-value: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 2093825691 4385 TVEVQGKGAEMKVDVVEPHGKVVKLGALSVGQTVKKTVTIANNSVAPLTF 4434
Cdd:NF012200     2 TVALTGNGVAAADPSITPSPASIDFGNVRVGDTASQTVTITNTGTAALTI 51
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
2432-2528 2.52e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 44.28  E-value: 2.52e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2432 EQEEAKEKaLSDSEKMLAMRFKIYEASQKDIAHILSNWDrvqgvlvsswsqEEAWQRAEEQNTHLSSRRSRKDREKERLE 2511
Cdd:PRK03918   620 ELKKLEEE-LDKAFEELAETEKRLEELRKELEELEKKYS------------EEEYEELREEYLELSRELAGLRAELEELE 686

                           90
                   ....*....|....*....
gi 2093825691 2512 KERQERERQ-EKLKA-LEE 2528
Cdd:PRK03918   687 KRREEIKKTlEKLKEeLEE 705
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 2482-2538 2.85e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 41.56  E-value: 2.85e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2093825691 2482 QEEAWQRAEEQnthlssRRSRKD-----REKERLEKERQERERQEKLKAL-EESQAQAGKGAE 2538
Cdd:pfam05672   59 REEEARRLEEE------RRREEEerqrkAEEEAEEREQREQEEQERLQKQkEEAEAKAREEAE 115
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 2432-2532 3.13e-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: 43.37  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2093825691 2432 EQEEAKEKALSDSEKMLAMRFKIYEASQKDIAHILsnwDRVQGVLVSSwsQEEAWQRAEEQNTHLSSR----RSRKDREK 2507
Cdd:pfam13868  148 EEEREEDERILEYLKEKAEREEEREAEREEIEEEK---EREIARLRAQ--QEKAQDEKAERDELRAKLyqeeQERKERQK 222

                           90       100
                   ....*....|....*....|....*
gi 2093825691 2508 ERLEKERQERERQEKLKALEESQAQ 2532
Cdd:pfam13868  223 EREEAEKKARQRQELQQAREEQIEL 247
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 2488-2533 5.81e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.79  E-value: 5.81e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2093825691 2488 RAEEQNTHLSSRRsRKDRE-KERLEKERQERERQEKLKaLEESQAQA 2533
Cdd:pfam05672    8 DAEEAARILAEKR-RQAREqREREEQERLEKEEEERLR-KEELRRRA 52
MAP7 pfam05672
MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is ...
 2482-2530 7.43e-03

MAP7 (E-MAP-115) family; The organization of microtubules varies with the cell type and is presumably controlled by tissue-specific microtubule-associated proteins (MAPs). The 115-kDa epithelial MAP (E-MAP-115/MAP7) has been identified as a microtubule-stabilising protein predominantly expressed in cell lines of epithelial origin. The binding of this microtubule associated protein is nucleotide independent.


Pssm-ID: 461709 [Multi-domain]  Cd Length: 153  Bit Score: 40.41  E-value: 7.43e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 2093825691 2482 QEEAWQRAEEQNTHLSSRRSRKDREKERLEKERQERERQEKLKALEESQ 2530
Cdd:pfam05672   38 EEEERLRKEELRRRAEEERARREEEARRLEEERRREEEERQRKAEEEAE 86
 
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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