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Conserved domains on  [gi|58264064|ref|XP_569188|]
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Protein tyrosine kinase, putative [Cryptococcus neoformans var. neoformans JEC21]

Protein Classification

twinfilin-like domain-containing protein( domain architecture ID 10181689)

twinfilin-like domain-containing protein, similar to Entamoeba histolytica actin binding protein family protein; twinfilin-like domain-containing protein, similar to Phytophthora infestans cofilin/tropomyosin-type actin-binding protein; twinfilin-like domain-containing protein, similar to Phytophthora infestans cofilin/tropomyosin-type actin-binding protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 5-144 8.17e-40

N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


:

Pssm-ID: 200441  Cd Length: 139  Bit Score: 140.46  E-value: 8.17e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   5 SGIKVADDLTAAFTAALANPqDTRALVFIIDGESFKHHATVKPKGSYKDDIALVPEVLPSPKTPASFAYRLDSKdSGKWD 84
Cdd:cd11285   2 SGITASEELLDAFKSAKSSG-SVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK-SAGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064  85 WMMVTFVPDDAGVRAKMLQASSRSGLMKVLGANNFKHDWFATSISDLSPSALTAHLNHLS 144
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_gelsolin super family cl15697
Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization ...
 190-386 3.00e-21

Actin depolymerization factor/cofilin- and gelsolin-like domains; Actin depolymerization factor/cofilin-like domains are present in a family of essential eukaryotic actin regulatory proteins; these proteins enhance the turnover rate of actin and interact with actin monomers as well as actin filaments.


The actual alignment was detected with superfamily member cd11284:

Pssm-ID: 472830  Cd Length: 132  Bit Score: 89.21  E-value: 3.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064 190 KMNWGEGVVEALQKVAqrsDDGW-VVVLEIPSSNPgSIALLKSEAC-IPSQLTSKLPGKSPCYVFYSHPTPPStrnvpks 267
Cdd:cd11284   4 AFPVSEEAKDALSELA---SGGVnLVQLSIDLENE-TIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPHTYL------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064 268 psapigaprntfqgsqggvrvvnasfgspaveagenveseepepgasptqeetaeavgkGRVIFVYCCPSNSPVKYRMIY 347
Cdd:cd11284  73 -----------------------------------------------------------SSVVFIYSCPSGSKVKERMLY 93

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 58264064 348 STTVRGMQQDAIDKAGVEIVAKLETSDPSELTESHLKSS 386
Cdd:cd11284  94 ASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
 
Name Accession Description Interval E-value
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 5-144 8.17e-40

N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200441  Cd Length: 139  Bit Score: 140.46  E-value: 8.17e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   5 SGIKVADDLTAAFTAALANPqDTRALVFIIDGESFKHHATVKPKGSYKDDIALVPEVLPSPKTPASFAYRLDSKdSGKWD 84
Cdd:cd11285   2 SGITASEELLDAFKSAKSSG-SVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK-SAGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064  85 WMMVTFVPDDAGVRAKMLQASSRSGLMKVLGANNFKHDWFATSISDLSPSALTAHLNHLS 144
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 190-386 3.00e-21

C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200440  Cd Length: 132  Bit Score: 89.21  E-value: 3.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064 190 KMNWGEGVVEALQKVAqrsDDGW-VVVLEIPSSNPgSIALLKSEAC-IPSQLTSKLPGKSPCYVFYSHPTPPStrnvpks 267
Cdd:cd11284   4 AFPVSEEAKDALSELA---SGGVnLVQLSIDLENE-TIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPHTYL------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064 268 psapigaprntfqgsqggvrvvnasfgspaveagenveseepepgasptqeetaeavgkGRVIFVYCCPSNSPVKYRMIY 347
Cdd:cd11284  73 -----------------------------------------------------------SSVVFIYSCPSGSKVKERMLY 93

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 58264064 348 STTVRGMQQDAIDKAGVEIVAKLETSDPSELTESHLKSS 386
Cdd:cd11284  94 ASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 26-136 2.39e-12

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 63.75  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064    26 DTRALVFIIDGEsfKHHATVKPKGSYKDDIALVPEVLPSPKtpASFA-YRLDSKDSG---KWDWMMVTFVPDDAGVRAKM 101
Cdd:pfam00241  13 KTNWIIFKIDDD--KEEIVVEETGEGGLSYDEFLEELPDDE--PRYAvYRFEYTHDDgskRSKLVFITWCPDGAPIKRKM 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 58264064   102 LQASSRSGLMKVLgaNNFKHDWFATSISDLSPSAL 136
Cdd:pfam00241  89 LYASSKAALKREL--KGIHVEIQATDPSELTEEEI 121
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 47-136 2.63e-09

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 54.98  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064     47 PKGSYKDDIALVPEvlpspKTPASFAYRLDS--KDSGKWDWMMVTFVPDDAGVRAKMLQASSRSGLMKVLGanNFKHDWF 124
Cdd:smart00102  38 TEDSYDEFVEELPE-----DECRYALYDYKFttEESKKSKIVFIFWSPDGAPVKSKMLYASSKDTLKKELG--GIQVEVQ 110

                           90
                   ....*....|..
gi 58264064    125 ATSISDLSPSAL 136
Cdd:smart00102 111 ATDEDDLDEEAL 122
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 197-385 1.04e-07

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 50.65  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   197 VVEALQKVAQRSDDGWVVvLEIpSSNPGSIALLKSEA--CIPSQLTSKLPGKSPCYVFYSHptppstrnvpkspsapiga 274
Cdd:pfam00241   1 CKEAYQELRSDKKTNWII-FKI-DDDKEEIVVEETGEggLSYDEFLEELPDDEPRYAVYRF------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   275 prnTFQGSQGGVRVvnasfgspaveagenveseepepgasptqeetaeavgkgRVIFVYCCPSNSPVKYRMIYSTTVRGM 354
Cdd:pfam00241  60 ---EYTHDDGSKRS---------------------------------------KLVFITWCPDGAPIKRKMLYASSKAAL 97

                         170       180       190
                  ....*....|....*....|....*....|.
gi 58264064   355 QQdAIDKAGVEIvaklETSDPSELTESHLKS 385
Cdd:pfam00241  98 KR-ELKGIHVEI----QATDPSELTEEEILE 123
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 318-387 2.83e-06

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 46.51  E-value: 2.83e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064    318 EETAEAVGKGRVIFVYCCPSNSPVKYRMIYSTTVRGMQQdAIDKAGVEIVAkletSDPSELTESHLKSSL 387
Cdd:smart00102  62 KFTTEESKKSKIVFIFWSPDGAPVKSKMLYASSKDTLKK-ELGGIQVEVQA----TDEDDLDEEALKEKL 126
 
Name Accession Description Interval E-value
ADF_Twf-N_like cd11285
N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 5-144 8.17e-40

N-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200441  Cd Length: 139  Bit Score: 140.46  E-value: 8.17e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   5 SGIKVADDLTAAFTAALANPqDTRALVFIIDGESFKHHATVKPKGSYKDDIALVPEVLPSPKTPASFAYRLDSKdSGKWD 84
Cdd:cd11285   2 SGITASEELLDAFKSAKSSG-SVRAIKITIENEELVPDATIETTGSWEQDFDLLVLPLLEEKEPCYILYRLDSK-SAGYE 79

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064  85 WMMVTFVPDDAGVRAKMLQASSRSGLMKVLGANNFKHDWFATSISDLSPSALTAHLNHLS 144
Cdd:cd11285  80 WVFISFVPDSAPVRQKMLYASTRATLKRELGSNHIKDELFATELEELTLEGYEKHLKHEA 139
ADF_Twf-C_like cd11284
C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor ...
 190-386 3.00e-21

C-terminal ADF domain of twinfilin and related proteins; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. Twinfilin contains two ADF domains, and inhibits the assembly of actin filaments by strongly interacting with monomeric ADP-actin (ADP-G-actin) in a 1:1 stochiometry (with it's C-terminal ADF domain, Twf-C) and inhibiting the actin monomer's nucleotide exchange. Mammalian twinfilin may also cap the barbed ends of F-actin filaments and prevent further assembly (or disassembly), in a process which requires both ADF domains. The N-terminal ADF domain (Twf-N) binds G-actin with a lower affinity than Twf-C; Twf-C can also bind F-actin. During capping, Twf-N may interact with the terminal actin subunit, and Twf-C may bind between two adjacent subunits at the side of the filament.


Pssm-ID: 200440  Cd Length: 132  Bit Score: 89.21  E-value: 3.00e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064 190 KMNWGEGVVEALQKVAqrsDDGW-VVVLEIPSSNPgSIALLKSEAC-IPSQLTSKLPGKSPCYVFYSHPTPPStrnvpks 267
Cdd:cd11284   4 AFPVSEEAKDALSELA---SGGVnLVQLSIDLENE-TIELVSSSSIsIPDDLSSLIPSDHPRYHFYRYPHTYL------- 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064 268 psapigaprntfqgsqggvrvvnasfgspaveagenveseepepgasptqeetaeavgkGRVIFVYCCPSNSPVKYRMIY 347
Cdd:cd11284  73 -----------------------------------------------------------SSVVFIYSCPSGSKVKERMLY 93

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 58264064 348 STTVRGMQQDAIDKAGVEIVAKLETSDPSELTESHLKSS 386
Cdd:cd11284  94 ASSKSGLLNHAEDEGKIEIDKKIEIGDPDELTESFLSDE 132
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 26-136 2.39e-12

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 63.75  E-value: 2.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064    26 DTRALVFIIDGEsfKHHATVKPKGSYKDDIALVPEVLPSPKtpASFA-YRLDSKDSG---KWDWMMVTFVPDDAGVRAKM 101
Cdd:pfam00241  13 KTNWIIFKIDDD--KEEIVVEETGEGGLSYDEFLEELPDDE--PRYAvYRFEYTHDDgskRSKLVFITWCPDGAPIKRKM 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 58264064   102 LQASSRSGLMKVLgaNNFKHDWFATSISDLSPSAL 136
Cdd:pfam00241  89 LYASSKAALKREL--KGIHVEIQATDPSELTEEEI 121
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 47-136 2.63e-09

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 54.98  E-value: 2.63e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064     47 PKGSYKDDIALVPEvlpspKTPASFAYRLDS--KDSGKWDWMMVTFVPDDAGVRAKMLQASSRSGLMKVLGanNFKHDWF 124
Cdd:smart00102  38 TEDSYDEFVEELPE-----DECRYALYDYKFttEESKKSKIVFIFWSPDGAPVKSKMLYASSKDTLKKELG--GIQVEVQ 110

                           90
                   ....*....|..
gi 58264064    125 ATSISDLSPSAL 136
Cdd:smart00102 111 ATDEDDLDEEAL 122
Cofilin_ADF pfam00241
Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin ...
 197-385 1.04e-07

Cofilin/tropomyosin-type actin-binding protein; Severs actin filaments and binds to actin monomers.


Pssm-ID: 459727  Cd Length: 123  Bit Score: 50.65  E-value: 1.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   197 VVEALQKVAQRSDDGWVVvLEIpSSNPGSIALLKSEA--CIPSQLTSKLPGKSPCYVFYSHptppstrnvpkspsapiga 274
Cdd:pfam00241   1 CKEAYQELRSDKKTNWII-FKI-DDDKEEIVVEETGEggLSYDEFLEELPDDEPRYAVYRF------------------- 59

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064   275 prnTFQGSQGGVRVvnasfgspaveagenveseepepgasptqeetaeavgkgRVIFVYCCPSNSPVKYRMIYSTTVRGM 354
Cdd:pfam00241  60 ---EYTHDDGSKRS---------------------------------------KLVFITWCPDGAPIKRKMLYASSKAAL 97

                         170       180       190
                  ....*....|....*....|....*....|.
gi 58264064   355 QQdAIDKAGVEIvaklETSDPSELTESHLKS 385
Cdd:pfam00241  98 KR-ELKGIHVEI----QATDPSELTEEEILE 123
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 86-136 1.24e-07

Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging.


Pssm-ID: 200442  Cd Length: 133  Bit Score: 50.63  E-value: 1.24e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 58264064  86 MMVTFVPDDAGVRAKMLQASSRSGLMKVLgaNNFKHDWFATSISDLSPSAL 136
Cdd:cd11286  81 VFISWCPDTAPIKSKMLYASSKDALKKKL--NGIKKEIQATDLSELSEEEI 129
ADF_cofilin_like cd11286
Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor ...
 319-385 1.45e-06

Cofilin, Destrin, and related actin depolymerizing factors; Actin depolymerization factor/cofilin-like domains (ADF domains) are present in a family of essential eukaryotic actin regulatory proteins. These proteins enhance the turnover rate of actin, and interact with actin monomers (G-actin) as well as actin filaments (F-actin), typically with a preference for ADP-G-actin subunits. The basic function of cofilin is to promote disassembly of aged actin filaments. Vertebrates have three isoforms of cofilin: cofilin-1 (Cfl1, non-muscle cofilin), cofilin-2 (muscle cofilin), and ADF (destrin). When bound to actin monomers, cofilins inhibit their spontaneous exchange of nucleotides. The cooperative binding to (aged) ADP-F-actin induces a local change in the actin filament structure and further promotes aging.


Pssm-ID: 200442  Cd Length: 133  Bit Score: 47.55  E-value: 1.45e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 58264064 319 ETAEAVGKGRVIFVYCCPSNSPVKYRMIYSTTvrgmqQDAIDKAGVEIVAKLETSDPSELTESHLKS 385
Cdd:cd11286  70 ETKDGGKRSKLVFISWCPDTAPIKSKMLYASS-----KDALKKKLNGIKKEIQATDLSELSEEEILE 131
ADF smart00102
Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin ...
 318-387 2.83e-06

Actin depolymerisation factor/cofilin -like domains; Severs actin filaments and binds to actin monomers.


Pssm-ID: 214516  Cd Length: 127  Bit Score: 46.51  E-value: 2.83e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 58264064    318 EETAEAVGKGRVIFVYCCPSNSPVKYRMIYSTTVRGMQQdAIDKAGVEIVAkletSDPSELTESHLKSSL 387
Cdd:smart00102  62 KFTTEESKKSKIVFIFWSPDGAPVKSKMLYASSKDTLKK-ELGGIQVEVQA----TDEDDLDEEALKEKL 126
 
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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