Fermitin family pleckstrin homology (PH) domain; Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 307 PELFDYLRFIKPKRFTLKAFKRYWFTCRDLHLTLYKTREEAtqGAEPAHHINLRGCEVTPDVNIAQSKYGIKLEVPSAEG 386
Cdd:cd01237     1 PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEES--NGAPIQQINLKGCEVTPDVNVSQQKFCIKLLVPSPEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1947848041 387 MTEMMIRCDTEEQYAKWMAACRLAAKGRSLADSSYETEVKSIVAFLQ 433
Cdd:cd01237    79 MSEVWLRCDNEDQYAKWMAACRLASKGKTMADSSYDSEVSSILAFLS 125

first ubiquitin-like (Ubl) domain located at the N-terminus of coronavirus SARS-CoV non-structural protein 3 (Nsp3) and related proteins; This ubiquitin-like (Ubl) domain (Ubl1) is found at the N-terminus of coronavirus Nsp3, a large multi-functional multi-domain protein which is an essential component of the replication/transcription complex (RTC). The functions of Ubl1 in CoVs are related to single-stranded RNA (ssRNA) binding and to interacting with the nucleocapsid (N) protein. SARS-CoV Ubl1 has been shown to bind ssRNA having AUA patterns, and since the 5'-UTR of the SARS-CoV genome has a number of AUA repeats, it may bind there. In mouse hepatitis virus (MHV), this Ubl1 domain binds the cognate N protein. Adjacent to Ubl1 is a Glu-rich acidic region (also referred to as hypervariable region, HVR); Ubl1 together with HVR has been called Nsp3a. Currently, the function of HVR in CoVs is unknown. This model corresponds to one of two Ubl domains in Nsp3; the other is located N-terminal to the papain-like protease (PLpro) and is not represented by this model.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1947848041 167 ARNKLLRPRTLVERARINVAWLDSSLSIMEQGVREYDTLCLRFKFY 212
Cdd:cd17096    45 LRPPLYRPKSLVDKARLNSGWLDSSRSLMEQGVRENDTLLLRFKYY 90

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 392 IRCDtEEQYAKwMAACRLAAKGRSLADSSYETEVKSIVAFLQMQHpaltpaispsslninpddyvaprfLRKLKGK-LVQ 470
Cdd:pfam00373  28 LPCS-EEEALL-LAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL------------------------LRKMKSKeLEK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1947848041 471 RILEAHTNVKDLPLVDAKLSYIKAWQSLPEYGISLF 506
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117

Fermitin family pleckstrin homology (PH) domain; Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 307 PELFDYLRFIKPKRFTLKAFKRYWFTCRDLHLTLYKTREEAtqGAEPAHHINLRGCEVTPDVNIAQSKYGIKLEVPSAEG 386
Cdd:cd01237     1 PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEES--NGAPIQQINLKGCEVTPDVNVSQQKFCIKLLVPSPEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1947848041 387 MTEMMIRCDTEEQYAKWMAACRLAAKGRSLADSSYETEVKSIVAFLQ 433
Cdd:cd01237    79 MSEVWLRCDNEDQYAKWMAACRLASKGKTMADSSYDSEVSSILAFLS 125

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the kindlin family; The kindlin family is composed of Kindlin-1, 2 and 3, which are FERM domain-containing adaptor molecules that interact with the cytoplasmic component of integrins and regulate cell-matrix connections. Kindlins belong to the 4.1- ezrin-ridixin-moesin (FERM) domain containing protein family. They contain F1, F2 and F3 subdomains that typify FERM family members, and these subdomains are preceded by an N-terminal F0 subdomain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain. In addition, a distinctive feature of kindlins is the insertion of a pleckstrin homology (PH) subdomain into the F2 subdomain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1947848041 167 ARNKLLRPRTLVERARINVAWLDSSLSIMEQGVREYDTLCLRFKFY 212
Cdd:cd17096    45 LRPPLYRPKSLVDKARLNSGWLDSSRSLMEQGVRENDTLLLRFKYY 90

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 392 IRCDtEEQYAKwMAACRLAAKGRSLADSSYETEVKSIVAFLQMQHpaltpaispsslninpddyvaprfLRKLKGK-LVQ 470
Cdd:pfam00373  28 LPCS-EEEALL-LAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL------------------------LRKMKSKeLEK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1947848041 471 RILEAHTNVKDLPLVDAKLSYIKAWQSLPEYGISLF 506
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041  316 IKPKRFTLKAFKRYWFTCRDLHLTLYKTrEEATQGAEPAHHINLRGCEVTPDVNI--AQSKYGIKLEVPSAEgmtEMMIR 393
Cdd:smart00233   8 YKKSGGGKKSWKKRYFVLFNSTLLYYKS-KKDKKSYKPKGSIDLSGCTVREAPDPdsSKKPHCFEIKTSDRK---TLLLQ 83

                           90
                   ....*....|....*....
gi 1947848041  394 CDTEEQYAKWMAACRLAAK 412
Cdd:smart00233  84 AESEEEREKWVEALRKAIA 102

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.

                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1947848041 226 INQIYEQAKWQLLNEEIDCTEEEMLMFAALQVQVTL 261
Cdd:cd14473     2 RYLLYLQVKRDILEGRLPCSEETAALLAALALQAEY 37

Fermitin family pleckstrin homology (PH) domain; Fermitin functions as a mediator of integrin inside-out signalling. The recruitment of Fermitin proteins and Talin to the membrane mediates the terminal event of integrin signalling, via interaction with integrin beta subunits. Fermatin has FERM domain interrupted with a pleckstrin homology (PH) domain. Fermitin family homologs (Fermt1, 2, and 3, also known as Kindlins) are each encoded by a different gene. In mammalian studies, Fermt1 is generally expressed in epithelial cells, Fermt2 is expressed inmuscle tissues, and Fermt3 is expressed in hematopoietic lineages. Specifically Fermt2 is expressed in smooth and striated muscle tissues in mice and in the somites (a trunk muscle precursor) and neural crest in Xenopus embryos. As such it has been proposed that Fermt2 plays a role in cardiomyocyte and neural crest differentiation. Expression of mammalian Fermt3 is associated with hematopoietic lineages: the anterior ventral blood islands, vitelline veins, and early myeloid cells. In Xenopus embryos this expression, also include the notochord and cement gland. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 307 PELFDYLRFIKPKRFTLKAFKRYWFTCRDLHLTLYKTREEAtqGAEPAHHINLRGCEVTPDVNIAQSKYGIKLEVPSAEG 386
Cdd:cd01237     1 PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEES--NGAPIQQINLKGCEVTPDVNVSQQKFCIKLLVPSPEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1947848041 387 MTEMMIRCDTEEQYAKWMAACRLAAKGRSLADSSYETEVKSIVAFLQ 433
Cdd:cd01237    79 MSEVWLRCDNEDQYAKWMAACRLASKGKTMADSSYDSEVSSILAFLS 125

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in the kindlin family; The kindlin family is composed of Kindlin-1, 2 and 3, which are FERM domain-containing adaptor molecules that interact with the cytoplasmic component of integrins and regulate cell-matrix connections. Kindlins belong to the 4.1- ezrin-ridixin-moesin (FERM) domain containing protein family. They contain F1, F2 and F3 subdomains that typify FERM family members, and these subdomains are preceded by an N-terminal F0 subdomain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F1 domain. In addition, a distinctive feature of kindlins is the insertion of a pleckstrin homology (PH) subdomain into the F2 subdomain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1947848041 167 ARNKLLRPRTLVERARINVAWLDSSLSIMEQGVREYDTLCLRFKFY 212
Cdd:cd17096    45 LRPPLYRPKSLVDKARLNSGWLDSSRSLMEQGVRENDTLLLRFKYY 90

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-1 (KIND1); KIND1, also termed Kindlerin, or Kindler syndrome protein, or fermitin family homolog 1 (FERMT1), or Unc-112-related protein 1 (URP1), is an integrin-interacting protein that has been implicated in cell adhesion, proliferation, polarity, and motility. It is essential for maintaining the structure of cell-matrix adhesion, such as focal adhesions and podosomes. KIND1 is expressed primarily in epithelial cells. Loss or mutations of KIND1 gene may cause the Kindler syndrome (KS), an autosomal recessive skin disorder with an intriguing progressive phenotype comprising skin blistering, photosensitivity, progressive poikiloderma with extensive skin atrophy, and propensity to skin cancer. KIND1 forms a molecular complex with the key transforming growth factor (TGF)-beta/Smad3 signaling components including type I TGFbeta receptor (TbetaRI), Smad3 and Smad anchor for receptor activation (SARA) to control the activation of TGF-beta/Smad3 signaling pathway. KIND1 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1947848041 170 KLLRPRTLVERARINVAWLDSSLSIMEQGVREYDTLCLRFKFY 212
Cdd:cd17183    51 KMYQPRTLLDKAKLNAGWLDSSRSLMEQGIQEDDQLLLRFKYY 93

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 392 IRCDtEEQYAKwMAACRLAAKGRSLADSSYETEVKSIVAFLQMQHpaltpaispsslninpddyvaprfLRKLKGK-LVQ 470
Cdd:pfam00373  28 LPCS-EEEALL-LAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL------------------------LRKMKSKeLEK 81

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1947848041 471 RILEAHTNVKDLPLVDAKLSYIKAWQSLPEYGISLF 506
Cdd:pfam00373  82 RVLEAHKNLRGLSAEEAKLKYLQIAQSLPTYGVEFF 117

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-3 (KIND3); KIND3, also termed fermitin family homolog 3 (FERMT3), or MIG2-like protein, or Unc-112-related protein 2, is an adaptor protein that expressed primarily in hematopoietic cells. It plays a central role in cell adhesion in hematopoietic cells, and also promotes integrin activation, clustering and outside-in signaling. KIND3, together with talin-1, contributes essentially to the activation of beta2-integrins in neutrophils. In addition, KIND3 interacts with the ribosome and regulates c-Myc expression required for proliferation of chronic myeloid leukemia cells. Mutations in the KIND3 gene cause leukocyte adhesion deficiency type III (LAD III), which is characterized by high susceptibility to infections, spontaneous and episodic bleedings, and osteopetrosis. KIND3 consists of an atypical FERM domain that is made up of F1, F2 and F3 domains, as well as an N-terminal region, which precedes the FERM domain and has been referred to as the F0 domain. This family corresponds to the F1 domain.

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1947848041 170 KLLRPRTLVERARINVAWLDSSLSIMEQGVREYDTLCLRFKFY 212
Cdd:cd17185    49 KLYRPSSVTDKTQIHSRWLDSSRSLMQQGVQEGDRLWLRFKYY 91

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 316 IKPKRFTLKAFKRYWFTCRDLHLTLYKTREeATQGAEPAHHINLRGCEVTPDVNIAQS--KYGIKLEVPSAEGMTEMMIR 393
Cdd:pfam00169   8 LKKGGGKKKSWKKRYFVLFDGSLLYYKDDK-SGKSKEPKGSISLSGCEVVEVVASDSPkrKFCFELRTGERTGKRTYLLQ 86

                          90
                  ....*....|....*....
gi 1947848041 394 CDTEEQYAKWMAACRLAAK 412
Cdd:pfam00169  87 AESEEERKDWIKAIQSAIR 105

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 317 KPKRFTLKAFKRYWFTCRDLHLTLYKTREEATQgaEPAHHINLRG-CEVTPDVNIaQSKYGIKLEVPSAEGMTemmIRCD 395
Cdd:cd00821     7 KRGGGGLKSWKKRWFVLFEGVLLYYKSKKDSSY--KPKGSIPLSGiLEVEEVSPK-ERPHCFELVTPDGRTYY---LQAD 80

                          90
                  ....*....|..
gi 1947848041 396 TEEQYAKWMAAC 407
Cdd:cd00821    81 SEEERQEWLKAL 92

Phosphoinositol 3-phosphate binding proteins 1, 2, and 3 pleckstrin homology (PH) domain; PEPP1 (also called PLEKHA4/PH domain-containing family A member 4 and RHOXF1/Rhox homeobox family member 1), and related homologs PEPP2 (also called PLEKHA5/PH domain-containing family A member 5) and PEPP3 (also called PLEKHA6/PH domain-containing family A member 6), have PH domains that interact specifically with PtdIns(3,4)P3. Other proteins that bind PtdIns(3,4)P3 specifically are: TAPP1 (tandem PH-domain-containing protein-1) and TAPP2], PtdIns3P AtPH1, and Ptd- Ins(3,5)P2 (centaurin-beta2). All of these proteins contain at least 5 of the 6 conserved amino acids that make up the putative phosphatidylinositol 3,4,5- trisphosphate-binding motif (PPBM) located at their N-terminus. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1947848041 322 TLKAFKRYWFTCRDLHLTLYKTREEAT-QGAEPAHHINLRGCEVTPDVNiaqSKYGIKLEVPsaeGMTEMMIRCDTEEQY 400
Cdd:cd13248    20 GLKNWRKRWFVLKDNCLYYYKDPEEEKaLGSILLPSYTISPAPPSDEIS---RKFAFKAEHA---NMRTYYFAADTAEEM 93

                          90
                  ....*....|.
gi 1947848041 401 AKWMAACRLAA 411
Cdd:cd13248    94 EQWMNAMSLAA 104

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Talin and similar proteins; Talin is a cytoskeletal protein that activates integrins and couples them to cytoskeletal actin. Talin consists of an N-terminal head and a C-terminal rod. The talin head harbors a FERM (Band 4.1, ezrin, radixin, moesin) domain made up of F1, F2 and F3 domains, as well as an N-terminal region that precedes the FERM domain and has been referred to as the F0 domain. Both F0 and F1 domains have similar ubiquitin-like folds. This family corresponds to the F0 domain that is joined to the F1 domain in a novel fixed orientation by an extensive charged interface. It is required for maximal integrin-activation, by interacting with other FA components; no binding partner has yet been found for it.

                          10        20
                  ....*....|....*....|....*
gi 1947848041 187 WLDSSLSIMEQGVREYDTLCLRFKF 211
Cdd:cd17090    87 WLDHDQTLREQGVDEDETLLLRRKF 111