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Conserved domains on  [gi|861634328|gb|KMQ91225|]
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tyrosine-protein phosphatase non-receptor type 14 [Lasius niger]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PTZ00178 PTZ00178
60S ribosomal protein L17; Provisional
230-393 3.30e-106

60S ribosomal protein L17; Provisional


:

Pssm-ID: 240306  Cd Length: 181  Bit Score: 311.23  E-value: 3.30e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 230 MGRYSHEPVNQTKSCKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVVDHKECVPFRRFNGGVGRCAQAKQFGTTQ 309
Cdd:PTZ00178   1 MVKYARKPQNPSKSAKAKGSDLRVHFKNTYETARAIKGMKLARAQKYLEDVLAKKRCVPFRRFNGGVGRTAQAKEFGHTQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 310 GRWPKKSAEFLLQLLKNAESNADYKGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEKEDVVAKA 389
Cdd:PTZ00178  81 GRWPEKSVKFVLSLLKNAEANAEAKGLDVEKLVISHVQVNRAPRGRRRTYRAHGRINPFMSSPCHIELIATEKDETVPKP 160

                 ....
gi 861634328 390 TEEE 393
Cdd:PTZ00178 161 KEAP 164
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
18-104 2.07e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


:

Pssm-ID: 340619  Cd Length: 85  Bit Score: 133.51  E-value: 2.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  18 KNQYVICVELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQLEKDAKNFTL 97
Cdd:cd17099    1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYV--NKKGQLRWVDLEKPLKKQLDKHAHEPLL 78

                 ....*..
gi 861634328  98 YLRVMYY 104
Cdd:cd17099   79 YFGVMFY 85
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
25-224 1.01e-36

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


:

Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 132.80  E-value: 1.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328    25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYiYCHNSPALRWVDMDKPLKRQLEKDAkNFTLYLRVMYY 104
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQF-EDPDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKFY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328   105 VTDVQFIQDEMTRYHY-YLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERH-TAECLQQCTFFPNDVikIDSGG 182
Cdd:smart00295  82 PPDPNQLKEDPTRLNLlYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQL--LDSRK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 861634328   183 QDSLLHTAICQYKSLTNVTQASAEELYISIVMQLEGYGNETF 224
Cdd:smart00295 160 LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
 
Name Accession Description Interval E-value
PTZ00178 PTZ00178
60S ribosomal protein L17; Provisional
230-393 3.30e-106

60S ribosomal protein L17; Provisional


Pssm-ID: 240306  Cd Length: 181  Bit Score: 311.23  E-value: 3.30e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 230 MGRYSHEPVNQTKSCKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVVDHKECVPFRRFNGGVGRCAQAKQFGTTQ 309
Cdd:PTZ00178   1 MVKYARKPQNPSKSAKAKGSDLRVHFKNTYETARAIKGMKLARAQKYLEDVLAKKRCVPFRRFNGGVGRTAQAKEFGHTQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 310 GRWPKKSAEFLLQLLKNAESNADYKGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEKEDVVAKA 389
Cdd:PTZ00178  81 GRWPEKSVKFVLSLLKNAEANAEAKGLDVEKLVISHVQVNRAPRGRRRTYRAHGRINPFMSSPCHIELIATEKDETVPKP 160

                 ....
gi 861634328 390 TEEE 393
Cdd:PTZ00178 161 KEAP 164
uL22_arch_euk TIGR01038
ribosomal protein uL22, eukaryotic/archaeal form; This model describes the ribosomal protein ...
233-382 1.10e-76

ribosomal protein uL22, eukaryotic/archaeal form; This model describes the ribosomal protein uL22 of the eukaryotic cytosol and of the Archaea, previously designated as L17, L22, and L23. The corresponding bacterial form of uL22 is described by a separate model. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273409  Cd Length: 148  Bit Score: 234.66  E-value: 1.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  233 YSHEPVNQTKSCKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVVDHKECVPFRRFNGGVGRCAQAkqFGTTQGRW 312
Cdd:TIGR01038   1 YSYKPEDPTKSAKARGRNLRISFKNARETCRAIRGMELDKARKYLEDVIAMKRAVPFRRYNGKVGHRAGL--WGWTAGRY 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  313 PKKSAEFLLQLLKNAESNADYKGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEK 382
Cdd:TIGR01038  79 PVKAAKFILKVLQNAEANAEYKGLDVEKLKIIHIQANKGPVIRRWMPRAFGRATPYNSSTTHIELVVEEK 148
Ribosomal_L22 pfam00237
Ribosomal protein L22p/L17e; This family includes L22 from prokaryotes and chloroplasts and ...
246-380 6.19e-42

Ribosomal protein L22p/L17e; This family includes L22 from prokaryotes and chloroplasts and L17 from eukaryotes.


Pssm-ID: 459725  Cd Length: 104  Bit Score: 143.31  E-value: 6.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  246 ARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVvdhkecvpfrrfnggvgrcaqakqfgttqgrwPKKSAEFLLQLLK 325
Cdd:pfam00237   1 AKARNLRISPKKARLVADLIRGMSVDEALAILKFS--------------------------------PKKAAKIVLKLLK 48
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 861634328  326 NAESNADYKGL-DVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILT 380
Cdd:pfam00237  49 SAIANAENKGNlDVDNLYISEIQVDKGPTLKRIRPRARGRAGPIRKRTSHITVVLK 104
Ribosomal_L22 cd00336
Ribosomal protein L22/L17e. L22 (L17 in eukaryotes) is a core protein of the large ribosomal ...
244-379 1.13e-39

Ribosomal protein L22/L17e. L22 (L17 in eukaryotes) is a core protein of the large ribosomal subunit. It is the only ribosomal protein that interacts with all six domains of 23S rRNA, and is one of the proteins important for directing the proper folding and stabilizing the conformation of 23S rRNA. L22 is the largest protein contributor to the surface of the polypeptide exit channel, the tunnel through which the polypeptide product passes. L22 is also one of six proteins located at the putative translocon binding site on the exterior surface of the ribosome.


Pssm-ID: 238205  Cd Length: 105  Bit Score: 137.24  E-value: 1.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 244 CKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVvdhkecvpfrrfnggvgrcaqakqfgttqgrwPKKSAEFLLQL 323
Cdd:cd00336    1 AKAKGRYLRISPKKARLVARLIRGMSVDEALAQLEFV--------------------------------PKKAAKIILKL 48
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 861634328 324 LKNAESNADYKGL-DVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVIL 379
Cdd:cd00336   49 LKSAEANAENNGLdDPDKLYIKHIQVNKGPTLKRRRPRARGRANPIRKRTCHITVVL 105
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
18-104 2.07e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 133.51  E-value: 2.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  18 KNQYVICVELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQLEKDAKNFTL 97
Cdd:cd17099    1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYV--NKKGQLRWVDLEKPLKKQLDKHAHEPLL 78

                 ....*..
gi 861634328  98 YLRVMYY 104
Cdd:cd17099   79 YFGVMFY 85
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
25-224 1.01e-36

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 132.80  E-value: 1.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328    25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYiYCHNSPALRWVDMDKPLKRQLEKDAkNFTLYLRVMYY 104
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQF-EDPDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKFY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328   105 VTDVQFIQDEMTRYHY-YLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERH-TAECLQQCTFFPNDVikIDSGG 182
Cdd:smart00295  82 PPDPNQLKEDPTRLNLlYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQL--LDSRK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 861634328   183 QDSLLHTAICQYKSLTNVTQASAEELYISIVMQLEGYGNETF 224
Cdd:smart00295 160 LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
106-224 1.38e-26

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 102.73  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  106 TDVQFIQDEMTRYHYYLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERHTAECLQQCTFFPNDVIKidSGGQDS 185
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKE 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 861634328  186 LLHTAICQYKSLTNVTQASAEELYISIVMQLEGYGNETF 224
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
RplV COG0091
Ribosomal protein L22 [Translation, ribosomal structure and biogenesis]; Ribosomal protein L22 ...
245-382 2.52e-25

Ribosomal protein L22 [Translation, ribosomal structure and biogenesis]; Ribosomal protein L22 is part of the Pathway/BioSystem: Ribosome 50S subunit


Pssm-ID: 439861  Cd Length: 110  Bit Score: 99.35  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 245 KARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNvvdhkecvpfrrfnggvgrcaqakqfgttqgrWPKKSAEFLLQLL 324
Cdd:COG0091    4 KAKLRYVRISPRKARLVADLIRGKKVEEALAILEF--------------------------------SPKKAARIVLKVL 51
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 861634328 325 KNAESNADYK-GLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEK 382
Cdd:COG0091   52 KSAIANAENNnGLDVDNLVVKEIFVDKGPTLKRFRPRARGRATRIRKRTSHITVVVSEK 110
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
116-216 3.35e-24

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 95.78  E-value: 3.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 116 TRYHYYLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERHTAECLQQCTFFPNDVIKidSGGQDSLLHTAICQYK 195
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHK 78
                         90       100
                 ....*....|....*....|.
gi 861634328 196 SLTNVTQASAEELYISIVMQL 216
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
25-88 1.72e-12

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 61.84  E-value: 1.72e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 861634328   25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQL 88
Cdd:pfam09379   1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFL--DDNGEHRWLDLSKRLSKQA 62
 
Name Accession Description Interval E-value
PTZ00178 PTZ00178
60S ribosomal protein L17; Provisional
230-393 3.30e-106

60S ribosomal protein L17; Provisional


Pssm-ID: 240306  Cd Length: 181  Bit Score: 311.23  E-value: 3.30e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 230 MGRYSHEPVNQTKSCKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVVDHKECVPFRRFNGGVGRCAQAKQFGTTQ 309
Cdd:PTZ00178   1 MVKYARKPQNPSKSAKAKGSDLRVHFKNTYETARAIKGMKLARAQKYLEDVLAKKRCVPFRRFNGGVGRTAQAKEFGHTQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 310 GRWPKKSAEFLLQLLKNAESNADYKGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEKEDVVAKA 389
Cdd:PTZ00178  81 GRWPEKSVKFVLSLLKNAEANAEAKGLDVEKLVISHVQVNRAPRGRRRTYRAHGRINPFMSSPCHIELIATEKDETVPKP 160

                 ....
gi 861634328 390 TEEE 393
Cdd:PTZ00178 161 KEAP 164
uL22_arch_euk TIGR01038
ribosomal protein uL22, eukaryotic/archaeal form; This model describes the ribosomal protein ...
233-382 1.10e-76

ribosomal protein uL22, eukaryotic/archaeal form; This model describes the ribosomal protein uL22 of the eukaryotic cytosol and of the Archaea, previously designated as L17, L22, and L23. The corresponding bacterial form of uL22 is described by a separate model. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 273409  Cd Length: 148  Bit Score: 234.66  E-value: 1.10e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  233 YSHEPVNQTKSCKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVVDHKECVPFRRFNGGVGRCAQAkqFGTTQGRW 312
Cdd:TIGR01038   1 YSYKPEDPTKSAKARGRNLRISFKNARETCRAIRGMELDKARKYLEDVIAMKRAVPFRRYNGKVGHRAGL--WGWTAGRY 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  313 PKKSAEFLLQLLKNAESNADYKGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEK 382
Cdd:TIGR01038  79 PVKAAKFILKVLQNAEANAEYKGLDVEKLKIIHIQANKGPVIRRWMPRAFGRATPYNSSTTHIELVVEEK 148
rpl22p PRK04223
50S ribosomal protein L22P; Reviewed
229-381 8.11e-49

50S ribosomal protein L22P; Reviewed


Pssm-ID: 179794  Cd Length: 153  Bit Score: 162.73  E-value: 8.11e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 229 AMGRYSHEpVNQTKSCKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVVDHKECVPFRRFNGGVGRcaQAKQFGTT 308
Cdd:PRK04223   2 ARINYSVK-ADPEKTAKAMGRELPISPKHSVEIAREIRGMKLDEAKAYLEDVIALKRAVPFKRHNKKVGH--RKGIDGWP 78
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 861634328 309 QGRWPKKSAEFLLQLLKNAESNADYKGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTE 381
Cdd:PRK04223  79 AGRYPVKAAKAFLKLLENAEANAEYKGLDTEKLVIVHIAAHKGRVIKGYMPRAFGRATPKNTETVNIEVILEE 151
Ribosomal_L22 pfam00237
Ribosomal protein L22p/L17e; This family includes L22 from prokaryotes and chloroplasts and ...
246-380 6.19e-42

Ribosomal protein L22p/L17e; This family includes L22 from prokaryotes and chloroplasts and L17 from eukaryotes.


Pssm-ID: 459725  Cd Length: 104  Bit Score: 143.31  E-value: 6.19e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  246 ARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVvdhkecvpfrrfnggvgrcaqakqfgttqgrwPKKSAEFLLQLLK 325
Cdd:pfam00237   1 AKARNLRISPKKARLVADLIRGMSVDEALAILKFS--------------------------------PKKAAKIVLKLLK 48
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 861634328  326 NAESNADYKGL-DVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILT 380
Cdd:pfam00237  49 SAIANAENKGNlDVDNLYISEIQVDKGPTLKRIRPRARGRAGPIRKRTSHITVVLK 104
Ribosomal_L22 cd00336
Ribosomal protein L22/L17e. L22 (L17 in eukaryotes) is a core protein of the large ribosomal ...
244-379 1.13e-39

Ribosomal protein L22/L17e. L22 (L17 in eukaryotes) is a core protein of the large ribosomal subunit. It is the only ribosomal protein that interacts with all six domains of 23S rRNA, and is one of the proteins important for directing the proper folding and stabilizing the conformation of 23S rRNA. L22 is the largest protein contributor to the surface of the polypeptide exit channel, the tunnel through which the polypeptide product passes. L22 is also one of six proteins located at the putative translocon binding site on the exterior surface of the ribosome.


Pssm-ID: 238205  Cd Length: 105  Bit Score: 137.24  E-value: 1.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 244 CKARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNVvdhkecvpfrrfnggvgrcaqakqfgttqgrwPKKSAEFLLQL 323
Cdd:cd00336    1 AKAKGRYLRISPKKARLVARLIRGMSVDEALAQLEFV--------------------------------PKKAAKIILKL 48
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 861634328 324 LKNAESNADYKGL-DVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVIL 379
Cdd:cd00336   49 LKSAEANAENNGLdDPDKLYIKHIQVNKGPTLKRRRPRARGRANPIRKRTCHITVVL 105
FERM_F1_PTPN14_like cd17099
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
18-104 2.07e-38

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptors PTPN14, PTPN21, and similar proteins; This family includes tyrosine-protein phosphatase non-receptors PTPN14 and PTPN21, both of which are protein-tyrosine phosphatase (PTP). They belong to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation.


Pssm-ID: 340619  Cd Length: 85  Bit Score: 133.51  E-value: 2.07e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  18 KNQYVICVELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQLEKDAKNFTL 97
Cdd:cd17099    1 KNSFVVRIQLLDNTVLECTLSPESTGQDCLEYVAQRLELREIEYFGLRYV--NKKGQLRWVDLEKPLKKQLDKHAHEPLL 78

                 ....*..
gi 861634328  98 YLRVMYY 104
Cdd:cd17099   79 YFGVMFY 85
B41 smart00295
Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in ...
25-224 1.01e-36

Band 4.1 homologues; Also known as ezrin/radixin/moesin (ERM) protein domains. Present in myosins, ezrin, radixin, moesin, protein tyrosine phosphatases. Plasma membrane-binding domain. These proteins play structural and regulatory roles in the assembly and stabilization of specialized plasmamembrane domains. Some PDZ domain containing proteins bind one or more of this family. Now includes JAKs.


Pssm-ID: 214604 [Multi-domain]  Cd Length: 201  Bit Score: 132.80  E-value: 1.01e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328    25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYiYCHNSPALRWVDMDKPLKRQLEKDAkNFTLYLRVMYY 104
Cdd:smart00295   4 VYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQF-EDPDEDLRHWLDPAKTLLDQDVKSE-PLTLYFRVKFY 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328   105 VTDVQFIQDEMTRYHY-YLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERH-TAECLQQCTFFPNDVikIDSGG 182
Cdd:smart00295  82 PPDPNQLKEDPTRLNLlYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELHdLRGELSLKRFLPKQL--LDSRK 159
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 861634328   183 QDSLLHTAICQYKSLTNVTQASAEELYISIVMQLEGYGNETF 224
Cdd:smart00295 160 LKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201
FERM_M pfam00373
FERM central domain; This domain is the central structural domain of the FERM domain.
106-224 1.38e-26

FERM central domain; This domain is the central structural domain of the FERM domain.


Pssm-ID: 459788 [Multi-domain]  Cd Length: 117  Bit Score: 102.73  E-value: 1.38e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  106 TDVQFIQDEMTRYHYYLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERHTAECLQQCTFFPNDVIKidSGGQDS 185
Cdd:pfam00373   1 DLELLLQDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQAEFGDYQPSSHTSEYLSLESFLPKQLLR--KMKSKE 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 861634328  186 LLHTAICQYKSLTNVTQASAEELYISIVMQLEGYGNETF 224
Cdd:pfam00373  79 LEKRVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117
RplV COG0091
Ribosomal protein L22 [Translation, ribosomal structure and biogenesis]; Ribosomal protein L22 ...
245-382 2.52e-25

Ribosomal protein L22 [Translation, ribosomal structure and biogenesis]; Ribosomal protein L22 is part of the Pathway/BioSystem: Ribosome 50S subunit


Pssm-ID: 439861  Cd Length: 110  Bit Score: 99.35  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 245 KARGSNLRVHFKNTHETARAIKNMALRRAQKYLKNvvdhkecvpfrrfnggvgrcaqakqfgttqgrWPKKSAEFLLQLL 324
Cdd:COG0091    4 KAKLRYVRISPRKARLVADLIRGKKVEEALAILEF--------------------------------SPKKAARIVLKVL 51
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 861634328 325 KNAESNADYK-GLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILTEK 382
Cdd:COG0091   52 KSAIANAENNnGLDVDNLVVKEIFVDKGPTLKRFRPRARGRATRIRKRTSHITVVVSEK 110
FERM_B-lobe cd14473
FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C ...
116-216 3.35e-24

FERM domain B-lobe; The FERM domain has a cloverleaf tripart structure (FERM_N, FERM_M, FERM_C/N, alpha-, and C-lobe/A-lobe, B-lobe, C-lobe/F1, F2, F3). The FERM domain is found in the cytoskeletal-associated proteins such as ezrin, moesin, radixin, 4.1R, and merlin. These proteins provide a link between the membrane and cytoskeleton and are involved in signal transduction pathways. The FERM domain is also found in protein tyrosine phosphatases, the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the pleckstrin homology (PH) and phosphotyrosine binding (PTB) domains and consequently is capable of binding to both peptides and phospholipids at different sites.


Pssm-ID: 271216  Cd Length: 99  Bit Score: 95.78  E-value: 3.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 116 TRYHYYLQLKSDILEDRIHCNPRQACLLASYSMQAEFGNYSPERHTAECLQQCTFFPNDVIKidSGGQDSLLHTAICQYK 195
Cdd:cd14473    1 TRYLLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDYDPSEHKPKYLSLKRFLPKQLLK--QRKPEEWEKRIVELHK 78
                         90       100
                 ....*....|....*....|.
gi 861634328 196 SLTNVTQASAEELYISIVMQL 216
Cdd:cd14473   79 KLRGLSPAEAKLKYLKIARKL 99
FERM_F1_PTPN14 cd17191
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
18-105 1.59e-20

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 14 (PTPN14) and similar proteins; PTPN14, also termed protein-tyrosine phosphatase pez, or PTPD2, or PTP36, is a widely expressed non-transmembrane cytosolic protein tyrosine phosphatase (PTP). It belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN14 plays a role in the nucleus during cell proliferation. It forms a complex with Kibra and LATS1 proteins and negatively regulates the key Hippo pathway protein Yes-associated protein (YAP) oncogenic function by controlling its localization. It specifically regulates p130 Crk-associated substrate (p130Cas) phosphorylation at tyrosine residue 128 (Y128) in colorectal cancer (CRC) cells. Moreover, PTPN14 may be a critical enzyme in regulating endothelial cell function. It plays a crucial role in organogenesis by inducing transforming growth factor beta (TGFbeta) and epithelial-mesenchymal transition (EMT). It also acts as a modifier of angiogenesis and hereditary haemorrhagic telangiectasia. It regulates the lymphatic function and choanal development through the interaction with the vascular endothelial growth factor receptor 3 (VEGFR3), a receptor tyrosine kinase essential for lymphangiogenesis. Furthermore, PTPN14 functions as a regulator of cell motility through its action on cell-cell adhesion. Beta-Catenin, a central component of adherens junctions, has been identified as a PTPN14 substrate. PTPN14 works as a novel sperm-motility biomarker and a potential mitochondrial protein.


Pssm-ID: 340711  Cd Length: 87  Bit Score: 85.48  E-value: 1.59e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  18 KNQYVICVELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQLEKDAKNFTL 97
Cdd:cd17191    1 KNCFVTRIRLLDSNVIECTLSVESTGQECLEAVAQRLELRETHYFGLWFL--SKSQQARWVELEKPLKKQLDKFANEPLL 78

                 ....*...
gi 861634328  98 YLRVMYYV 105
Cdd:cd17191   79 FFGVMFYV 86
FERM_F1_PTPN21 cd17192
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
18-105 1.22e-18

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 21 (PTPN21) and similar proteins; PTPN21, also termed protein-tyrosine phosphatase D1 (PTPD1), is a cytosolic non-receptor protein-tyrosine phosphatase (PTP) that belongs to the FERM family of PTPs characterized by a conserved N-terminal FERM domain and a C-terminal PTP catalytic domain with an intervening sequence containing an acidic region and a putative SH3 domain-binding sequence. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN21 interacts with a Tec tyrosine kinase family member, the epithelial and endothelial tyrosine kinase (Etk, also known as Bmx), modulates Stat3 activation, and plays a role in the regulation of cell growth and differentiation. It also associates with and activates Src tyrosine kinase, and directs epidermal growth factor (EGF)/Src signaling to the nucleus through activating ERK1/2- and Elk1-dependent gene transcription. PTPD1-Src complex interacts a protein kinase A-anchoring protein AKAP121 to forms a PTPD1-Src-AKAP121 complex, which is required for efficient maintenance of mitochondrial membrane potential and ATP oxidative synthesis. As a novel component of the endocytic pathway, PTPN21 supports EGF receptor stability and mitogenic signaling in bladder cancer cells. Moreover, PTPD1 regulates focal adhesion kinase (FAK) autophosphorylation and cell migration through modulating Src-FAK signaling at adhesion sites.


Pssm-ID: 340712  Cd Length: 87  Bit Score: 80.07  E-value: 1.22e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  18 KNQYVICVELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPalRWVDMDKPLKRQLEKDAKNFTL 97
Cdd:cd17192    1 KSCLVARIQLLNNEFVEFTLSVESTGQECLEAVAQRLELREITYFSLWYYNKQNQQ--RWVDLEKPLKKQLDKYALEPTV 78

                 ....*...
gi 861634328  98 YLRVMYYV 105
Cdd:cd17192   79 YFGVVFYV 86
FERM_F0_F1 cd01765
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found ...
25-103 3.12e-14

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F0 sub-domain and F1 sub-domain, found in FERM (Four.1/Ezrin/Radixin/Moesin) family proteins; FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain is present at the N-terminus of a large and diverse group of proteins that mediate linkage of the cytoskeleton to the plasma membrane. FERM-containing proteins are ubiquitous components of the cytocortex and are involved in cell transport, cell structure and signaling functions. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N), which is structurally similar to ubiquitin.


Pssm-ID: 340464  Cd Length: 80  Bit Score: 67.61  E-value: 3.12e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQLeKDAKNFTLYLRVMY 103
Cdd:cd01765    5 VRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYE--DNDGQKHWLDLDKKISKQL-KRSGPYQFYFRVKF 80
FERM_N pfam09379
FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the ...
25-88 1.72e-12

FERM N-terminal domain; This domain is the N-terminal ubiquitin-like structural domain of the FERM domain.


Pssm-ID: 430570  Cd Length: 63  Bit Score: 61.84  E-value: 1.72e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 861634328   25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQL 88
Cdd:pfam09379   1 VRLLDGTVLEFDVQPKATGQVLLDQVCNHLNLKEKDYFGLQFL--DDNGEHRWLDLSKRLSKQA 62
FERM_F1_PTPN3_like cd17100
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
22-105 6.40e-10

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3) and similar proteins; This family includes two tyrosine-protein phosphatase non-receptors, PTPN3 and PTPN4, both of which belong to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340620  Cd Length: 86  Bit Score: 55.39  E-value: 6.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  22 VIC-VELLDATsiECTLSID--SVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSP-ALRWVDMDKPLKRQLeKDAKNFTL 97
Cdd:cd17100    2 VRCiVHFLDDT--EQTFEVEkrDKGQVLLDKVFNHLELVEKDYFGLQFSDDSPATdSMRWLDPLKPIRKQI-KGGPPYYL 78

                 ....*...
gi 861634328  98 YLRVMYYV 105
Cdd:cd17100   79 NFRVKFYV 86
FERM_F1_FRMD3 cd17102
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
25-104 1.15e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 3 (FRMD3) and similar proteins; FRMD3, also termed band 4.1-like protein 4O, or ovary type protein 4.1 (4.1O), belongs to the 4.1 protein superfamily, which share the highly conserved membrane-association FERM domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). FRMD3 is involved in maintaining cell shape and integrity. It also functions as a tumour suppressor in non-small cell lung carcinoma (NSCLC). Some single nucleotide polymorphisms (SNPs) located in FRMD3 have been associated with diabetic kidney disease (DKD) in different ethnicities.


Pssm-ID: 340622  Cd Length: 82  Bit Score: 54.56  E-value: 1.15e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATS-IECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSpaLRWVDMDKPLKRQLeKDAKNFTLYLRVMY 103
Cdd:cd17102    5 IRLLDDSEvICCEFKKDTKGQFLLDYVCNYLNLLEKDYFGLRYVDTEKQ--RHWLDPNKSIYKQL-KGVPPYVLCFRVKF 81

                 .
gi 861634328 104 Y 104
Cdd:cd17102   82 Y 82
FERM_F1_EPB41L4A cd17107
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
25-107 2.45e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4A (EPB41L4A) and similar proteins; EPB41L4A, also termed protein NBL4, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4A is an important component of the beta-catenin/Tcf pathway. It may be related to determination of cell polarity or proliferation.


Pssm-ID: 340627  Cd Length: 91  Bit Score: 53.89  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDAT----SIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYiyCHNSPALRWVDMDKPLKRQLEKDAKNFTLYLR 100
Cdd:cd17107    7 IVLLDESelilTIQQDGIKSSKGSVVLDVVFQHLNLLETDYFGLRY--IDRQHQTHWLDPAKTLSEQLKLIGPPYTLYFG 84

                 ....*..
gi 861634328 101 VMYYVTD 107
Cdd:cd17107   85 VKFYAED 91
FERM_F1_FARP1_like cd17098
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and ...
25-107 3.54e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM, RhoGEF and pleckstrin domain-containing protein 1 (FARP1) and similar proteins; This family includes the F1 sub-domain of FERM, RhoGEF and pleckstrin domain-containing proteins FARP1, FARP2, and FERM domain-containing protein 7 (FRMD7). FARP1, also termed chondrocyte-derived ezrin-like protein (CDEP), or pleckstrin homology (PH) domain-containing family C member 2 (PLEKHC2), is a neuronal activator of the RhoA GTPase. It promotes outgrowth of developing motor neuron dendrites. It also regulates excitatory synapse formation and morphology, as well as activates the GTPase Rac1 to promote F-actin assembly. FARP2, also termed FERM domain including RhoGEF (FIR), or Pleckstrin homology (PH) domain-containing family C member 3, is a Dbl-family guanine nucleotide exchange factor (GEF) that activates Rac1 or Cdc42 in response to upstream signals, suggesting roles in regulating processes such as neuronal axon guidance and bone homeostasis. It is also a key molecule involved in the response of neuronal growth cones to class-3 semaphorins. FRMD7 plays an important role in neuronal development and is involved in the regulation of F-actin, neurofilament, and microtubule dynamics. All family members contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340618  Cd Length: 85  Bit Score: 53.37  E-value: 3.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPAlrWVDMDKPLKRQLeKDAKNFTLYLRVMYY 104
Cdd:cd17098    5 VQMLDDTVHIFQVQQKALGEVLFDQVCKHLNLLESDYFGLEFTDPEGNKC--WLDPEKPILRQV-KRPKDVVFKFVVKFY 81

                 ...
gi 861634328 105 VTD 107
Cdd:cd17098   82 TPD 84
FERM_F1_MYLIP cd17104
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ...
25-104 5.21e-09

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in E3 ubiquitin-protein ligase MYLIP and similar proteins; MYLIP, also termed inducible degrader of the LDL-receptor (Idol), or myosin regulatory light chain interacting protein (MIR), is an E3 ubiquitin-protein ligase that mediates ubiquitination and subsequent proteasomal degradation of myosin regulatory light chain (MRLC), LDLR, VLDLR and LRP8. Its activity depends on E2 ubiquitin-conjugating enzymes of the UBE2D family, including UBE2D1, UBE2D2, UBE2D3, and UBE2D4. MYLIP stimulates clathrin-independent endocytosis and acts as a sterol-dependent inhibitor of cellular cholesterol uptake by binding directly to the cytoplasmic tail of the LDLR and promoting its ubiquitination via the UBE2D1/E1 complex. The ubiquitinated LDLR then enters the multivesicular body (MVB) protein-sorting pathway and is shuttled to the lysosome for degradation. Moreover, MYLIP has been identified as a novel ERM-like protein that affects cytoskeleton interactions regulating cell motility, such as neurite outgrowth. The ERM proteins includes ezrin, radixin, and moesin, which are cytoskeletal effector proteins linking actin to membrane-bound proteins at the cell surface. MYLIP contains a FERM-domain and a C-terminal C3HC4-type RING-HC finger. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340624  Cd Length: 81  Bit Score: 52.66  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPAlrWVDMDKPLKRQLEKDAKnFTLYLRVMYY 104
Cdd:cd17104    5 VSQPDSVVIEVEVDPKANGQECLDKVCQKLGIIEKDYFGLQYTGPKGERL--WLNLRNRISRQLPGPPP-YRLRLRVKFF 81
PRK12279 PRK12279
50S ribosomal protein L22/unknown domain fusion protein; Provisional
313-394 3.93e-08

50S ribosomal protein L22/unknown domain fusion protein; Provisional


Pssm-ID: 138835 [Multi-domain]  Cd Length: 311  Bit Score: 54.70  E-value: 3.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328 313 PKKSAEFLLQLLKNAESNADY--KGLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVILT----EKEDVV 386
Cdd:PRK12279  40 PKKFAPIVLKLLNSAISNVQHnsKDMDPSKLYIYKIVANQGPTMKRTLPRAKGSADQLFKRTTHLEIVLSddvnEREKEL 119

                 ....*...
gi 861634328 387 AKATEEEP 394
Cdd:PRK12279 120 AAIKAKKS 127
rplV_bact TIGR01044
ribosomal protein L22, bacterial type; This model decribes bacterial and chloroplast ribosomal ...
311-379 6.97e-08

ribosomal protein L22, bacterial type; This model decribes bacterial and chloroplast ribosomal protein L22. [Protein synthesis, Ribosomal proteins: synthesis and modification]


Pssm-ID: 130116  Cd Length: 103  Bit Score: 50.21  E-value: 6.97e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 861634328  311 RW-PKKSAEFLLQLLKNAESNADYK-GLDVDRLVVEHIQVNHAPCLRRRTYRAHGRINPYMSSPCHIEVIL 379
Cdd:TIGR01044  33 RFtPKKASPIIEKVLASAIANAEHNyGLDANNLVVVTAFVDEGPTLKRIRPRAKGRASRIRKRTSHITVVV 103
FERM_F1_EPB41L5_like cd17108
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
22-104 1.33e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5) and similar proteins; This family includes FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins, EPB41L5 and EPB41L4B. EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer. Both EPB41L5 and EPB41L4B contain a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340628  Cd Length: 81  Bit Score: 48.89  E-value: 1.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  22 VIC-VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPalRWVDMDKPLKRQLeKDAKNFTLYLR 100
Cdd:cd17108    1 IQCkVILLDGTDLSIELPKKAKGQELYEQVFYHLDLIEKDYFGLQFMDAAQVQ--HWLDPTKKIKKQV-KIGPPYTLRFR 77

                 ....
gi 861634328 101 VMYY 104
Cdd:cd17108   78 VKFY 81
FERM_F1_EPB41L5 cd17205
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
25-107 2.01e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like 5 (EPB41L5); EPB41L5 is a mesenchymal-specific protein that is an integral component of the ARF6-based pathway. It is normally induced during epithelial-mesenchymal transition (EMT) by an EMT-related transcriptional factor, ZEB1, which drives ARF6-based invasion, metastasis and drug resistance. EPB41L5 also binds to paxillin to enhance integrin/paxillin association, and thus promotes focal adhesion dynamics. Moreover, EPB41L5 acts as a substrate for the E3 ubiquitin ligase Mind bomb 1 (Mib1), which is essential for activation of Notch signaling. EPB41L5 is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340725  Cd Length: 86  Bit Score: 48.50  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPalRWVDMDKPLKRQLeKDAKNFTLYLRVMYY 104
Cdd:cd17205    7 VSLLDGTDVSVDLPKKAKGQELFEQIMYHLDLIEKDYFGLRFMDSAQVA--HWLDVTKSIKKQV-KIGPPYCLHLRVKFY 83

                 ...
gi 861634328 105 VTD 107
Cdd:cd17205   84 SSE 86
FERM_F1_EPB41L4B cd17204
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band ...
25-107 6.43e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte band 4.1-like protein 4B (EPB41L4B); EPB41L4B, also termed FERM-containing protein CG1, or expressed in high metastatic cells (Ehm2), or Lulu2, is a member of the band 4.1/Nbl4 (novel band 4.1-like protein 4) group of the FERM protein superfamily. It contains a FERM domain that is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). EPB41L4B is a positive regulator of keratinocyte adhesion and motility, suggesting a role in wound healing. It also promotes cancer metastasis in melanoma, prostate cancer and breast cancer.


Pssm-ID: 340724  Cd Length: 84  Bit Score: 46.73  E-value: 6.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMDKPLKRQLeKDAKNFTLYLRVMYY 104
Cdd:cd17204    5 VLLLDGTDVSVELPKHAKGQDLFDQIVYHLDLVETDYFGLQFM--DAAQVAHWLDHTKPIKKQI-KIGPPYTLHFRIKYY 81

                 ...
gi 861634328 105 VTD 107
Cdd:cd17204   82 SSE 84
FERM_F1_EPB41 cd17105
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
25-107 7.66e-07

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1 (EPB41) and similar proteins; EPB41, also termed protein 4.1 (P4.1), or 4.1R, or Band 4.1, or EPB4.1, belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41 is a widely expressed cytoskeletal phosphoprotein that stabilizes the spectrin-actin cytoskeleton and anchors the cytoskeleton to the cell membrane. EPB41 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340625  Cd Length: 83  Bit Score: 46.73  E-value: 7.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLrYIYchNSPALR-WVDMDKPLKRQLEKDAKNFTlyLRVMY 103
Cdd:cd17105    5 VSLLDDTVYECEVEKHAKGQDLFKKVCEHLNLLEEDYFGL-AIW--DSPTSKtWLDPAKEIKKQVHGGPWEFT--FNVKF 79

                 ....
gi 861634328 104 YVTD 107
Cdd:cd17105   80 YPPD 83
FERM_F1_EPB41L2 cd17202
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
22-107 3.39e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 2 (EPB41L2) and similar proteins; EPB41L2, also termed generally expressed protein 4.1 (4.1G), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L2 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340722  Cd Length: 84  Bit Score: 44.96  E-value: 3.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  22 VIC-VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLryIYCHNSPALRWVDMDKPLKRQLEKDAKNFTlyLR 100
Cdd:cd17202    2 VLCkVTLLDGTEYSCDLEKRAKGQVLFDKVCEHLNLLEKDYFGL--LYQVSANQKNWLDSTKEIKRQIRRLPWLFT--FN 77

                 ....*..
gi 861634328 101 VMYYVTD 107
Cdd:cd17202   78 VKFYPPD 84
FERM_F1_EPB41L1 cd17201
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
22-107 6.67e-06

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 1 (EPB41L1) and similar proteins; EPB41L1, also termed neuronal protein 4.1 (4.1N), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. It is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. It suppresses hypoxia-induced epithelial-mesenchymal transition in epithelial ovarian cancer (EOC) cells. The down-regulation of EPB41L1 expression is a critical step for non-small cell lung cancer (NSCLC) development. Moreover, EPB41L1 functions as a linker protein between inositol 1,4,5-trisphosphate receptor type1 (IP3R1) and actin filaments in neurons. EPB41L1 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340721  Cd Length: 84  Bit Score: 44.10  E-value: 6.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  22 VIC-VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLryIYCHNSPALRWVDMDKPLKRQLEKDAKNFTlyLR 100
Cdd:cd17201    2 AICkVTLLDGSEYECEVEKHARGQVLFDTVCEHLNLLEKDYFGL--TFCDTESQKNWLDPSKEIKKQIRSGPWHFA--FT 77

                 ....*..
gi 861634328 101 VMYYVTD 107
Cdd:cd17201   78 VKFYPPD 84
FERM_F1_PTPN4 cd17194
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
22-105 5.35e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 4 (PTPN4); PTPN4, also termed protein-tyrosine phosphatase MEG1 (MEG) or PTPase-MEG1, belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN4 protects cells against apoptosis. It associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN4-p38gamma complex that promotes cellular signaling, preventing cell death induction. It also inhibits tyrosine phosphorylation and subsequent cytoplasm translocation of TRIF-related adaptor molecule (TRAM, also known as TICAM2), resulting in the disturbance of TRAM-TRIF interaction. Moreover, PTPN4 negatively regulates cell proliferation and motility through dephosphorylation of CrkI.


Pssm-ID: 340714  Cd Length: 84  Bit Score: 41.44  E-value: 5.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  22 VIC-VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRyIYCHNSPALRWVDMDKPLKRQLEKDAKnFTLYLR 100
Cdd:cd17194    2 VVCnILLLDNTVQAFKVNKHDQGQVLLDLVFKHLDLTERDYFGLQ-LADDSTDNPRWLDPNKPIRKQLKRGSP-HNLNFR 79

                 ....*
gi 861634328 101 VMYYV 105
Cdd:cd17194   80 VKFFV 84
FERM_F1_PTPN3 cd17193
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein ...
22-105 7.21e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in tyrosine-protein phosphatase non-receptor type 3 (PTPN3); PTPN3, also termed protein-tyrosine phosphatase H1 (PTP-H1), belongs to the non-transmembrane FERM-containing protein-tyrosine phosphatase (PTP) subfamily characterized by a conserved N-terminal FERM domain, a PDZ domain, and a C-terminal PTP catalytic domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). PTPN3 associates with the mitogen-activated protein kinase p38gamma (also known as MAPK12) to form a PTPN3-p38gamma complex that promotes Ras-induced oncogenesis. It may also act as a tumor suppressor in lung cancer through its modulation of epidermal growth factor receptor (EGFR) signaling. Moreover, PTPN3 shows sensitizing effect to anti-estrogens. It dephosphorylates the tyrosine kinase EGFR, disrupts its interaction with the nuclear estrogen receptor, and increases breast cancer sensitivity to small molecule tyrosine kinase inhibitors (TKIs). It also cooperates with vitamin D receptor to stimulate breast cancer growth through their mutual stabilization.


Pssm-ID: 340713  Cd Length: 84  Bit Score: 40.99  E-value: 7.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  22 VIC-VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRyiycHNSPAL---RWVDMDKPLKRQLeKDAKNFTL 97
Cdd:cd17193    2 VICnVHFLDGSVQSFKVNKQDTGQVLLDMAYNHLGLTEREYFGLQ----HNEDSVdspRWLEPSKPIRKQL-KGGFPCSL 76

                 ....*...
gi 861634328  98 YLRVMYYV 105
Cdd:cd17193   77 HFRVRFFI 84
FERM_F1_EPB41L cd17106
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
25-107 7.24e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like proteins; The family includes erythrocyte membrane protein band 4.1-like proteins EPB41L1/4.1N, EPB41L2/4.1G, and EPB41L3/4.1B. They belong to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L1 is a cytoskeleton-associated protein that may serve as a tumor suppressor in solid tumors. EPB41L2 is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 also acts as a tumor suppressor implicated in a variety of meningiomas and carcinomas. Members in this family contain a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340626  Cd Length: 84  Bit Score: 41.27  E-value: 7.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPalRWVDMDKPLKRQLEKDAKNFtlYLRVMYY 104
Cdd:cd17106    6 VLLLDGTEYTCEVEKRAKGQVLFDKVCEHLNLLEKDYFGLTYRDAQDQK--NWLDPAKEIKKQIRSGPWLF--SFNVKFY 81

                 ...
gi 861634328 105 VTD 107
Cdd:cd17106   82 PPD 84
FERM_F1_ERM_like cd17097
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family ...
43-104 7.39e-05

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the ERM family proteins; The ezrin-radixin-moesin (ERM) family includes a group of closely related cytoskeletal proteins that play an essential role in microvilli formation, T-cell activation, and tumor metastasis through providing a regulated linkage between F-actin and membrane-associated proteins. These proteins may also function in signaling cascades that regulate the assembly of actin stress fibers. The ERM proteins consist of an N-terminal FERM domain, a coiled-coil (CC) domain and a C-terminal tail segment (C-tail) containing a well-defined actin-binding motif. They exist in two states, a dormant state in which the FERM domain binds to its own C-terminal tail and thereby precludes binding of some partner proteins, and an activated state, in which the FERM domain binds to one of many membrane binding proteins and the C-terminal tail binds to F-actin. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N). Merlin, which is highly related to the members of the ezrin, radixin, and moesin (ERM) protein family that are directly attached to and functionally linked with NHE1, is included in this family.


Pssm-ID: 340617  Cd Length: 83  Bit Score: 41.11  E-value: 7.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 861634328  43 GQECLNNVTQRLGLGQPEFFGLRYIYCHNSPAlrWVDMDKPLKRQLEKDAKNFTLYLRVMYY 104
Cdd:cd17097   22 GRELFDLVCRTIGLRETWYFGLQYENKKGRVA--WLKPDKKVLTQDVSKNNTLKFFFLVKFY 81
FERM_F1_EPB41L3 cd17203
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte ...
25-107 1.46e-04

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in erythrocyte membrane protein band 4.1-like protein 3 (EPB41L3) and similar proteins; EPB41L3, also termed 4.1B, or differentially expressed in adenocarcinoma of the lung protein 1 (DAL-1), belongs to the skeletal protein 4.1 family that is involved in cellular processes such as cell adhesion, migration and signaling. EPB41L3 is a tumor suppressor that has been implicated in a variety of meningiomas and carcinomas. EPB41L3 contains a FERM domain, a spectrin and actin binding (SAB) domain, and a C-terminal domain. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340723  Cd Length: 84  Bit Score: 40.31  E-value: 1.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIYCHNSPalRWVDMDKPLKRQLEKDAKNFTlyLRVMYY 104
Cdd:cd17203    6 VTLLDGSEYTCEVEKRSKGQVLFDKVCEHLNLLEKDYFGLTYRDSENQK--NWLDPAKEIKKQIRSGAWQFS--FNVKFY 81

                 ...
gi 861634328 105 VTD 107
Cdd:cd17203   82 PPD 84
FERM_F1_FRMD1 cd17197
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
23-105 1.21e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 1 (FRMD1); FRMD1 is an uncharacterized FERM domain-containing protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340717  Cd Length: 98  Bit Score: 37.86  E-value: 1.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  23 ICVELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALrWVDMDKPLKRQLEKDAKN-------- 94
Cdd:cd17197    4 ICVLLPNKEQLSLTVGVKATGQELFQQVCELLKIKEAHFFGLSVV--KNNEHI-FMDLEQKLSKYFPKEWKKetgkgtek 80
                         90
                 ....*....|....*
gi 861634328  95 ----FTLYLRVMYYV 105
Cdd:cd17197   81 fsipFVACFRVQYYV 95
FERM_F1_FRMD4B cd17200
FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM ...
25-108 5.19e-03

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in FERM domain-containing protein 4B (FRMD4B); FRMD4B, also termed GRP1-binding protein GRSP1, interacts with the coil-coil domain of ARF exchange factor GRP1 to form the Grsp1-Grp1 complex that co-localizes with cortical actin rich regions in response to stimulation of CHO-T cells with insulin or epidermal growth factor (EGF). FRMD4B contains a FERM protein interaction domain as well as two coiled coil domains and may therefore function as a scaffolding protein. The FERM domain is made up of three sub-domains, F1, F2, and F3. This family corresponds to the F1 sub-domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).


Pssm-ID: 340720  Cd Length: 89  Bit Score: 36.02  E-value: 5.19e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 861634328  25 VELLDATSIECTLSIDSVGQECLNNVTQRLGLGQPEFFGLRYIycHNSPALRWVDMD-KPLKRQLEKDAKNFTLYLRVMY 103
Cdd:cd17200    7 VHLLDDRKLELLVQPKLLSRELLDLVASHFNLKEKEYFGITFI--DDTGQSNWLQLDhRVLDHDLPKKSGPVTLYFAVRF 84

                 ....*
gi 861634328 104 YVTDV 108
Cdd:cd17200   85 YIESI 89
 
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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