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 1370638367 370 PELSDYLRFLKPKRFTLKQSKQFWFTCRDLHLTLYKSREEAaqGAEPVHHINLRGCEVTPEVNIAQGRYGIKLEVPSAEG 449
Cdd:cd01237     1 PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEES--NGAPIQQINLKGCEVTPDVNVSQQKFCIKLLVPSPEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370638367 450 MTEMFVRCNSEEQYAKWMAACRLAAKGRSLADSSYDSEVKSIIAFLQ 496
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 1370638367 230 LRPKSLIERARMNVAWLDSSLSIMEQGVREFDTLCLRFKFY 270
Cdd:cd17096    50 YRPKSLVDKARLNSGWLDSSRSLMEQGVRENDTLLLRFKYY 90

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

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370638367 459 SEEQYAKwMAACRLAAKGRSLADSSYDSEVKSIIAFLQMQHpapapainpssLDIIPEDYVSPRFLrkfkgkaKAHANVK 538
Cdd:pfam00373  31 SEEEALL-LAALQLQAEFGDYQPSSHTSEYLSLESFLPKQL-----------LRKMKSKELEKRVL-------EAHKNLR 91

                          90       100
                  ....*....|....*....|....*.
gi 1370638367 539 DLPLVDAKLSYIKAWQSLPEYGISLF 564
Cdd:pfam00373  92 GLSAEEAKLKYLQIAQSLPTYGVEFF 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 1370638367 370 PELSDYLRFLKPKRFTLKQSKQFWFTCRDLHLTLYKSREEAaqGAEPVHHINLRGCEVTPEVNIAQGRYGIKLEVPSAEG 449
Cdd:cd01237     1 PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEES--NGAPIQQINLKGCEVTPDVNVSQQKFCIKLLVPSPEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370638367 450 MTEMFVRCNSEEQYAKWMAACRLAAKGRSLADSSYDSEVKSIIAFLQ 496
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 1370638367 230 LRPKSLIERARMNVAWLDSSLSIMEQGVREFDTLCLRFKFY 270
Cdd:cd17096    50 YRPKSLVDKARLNSGWLDSSRSLMEQGVRENDTLLLRFKYY 90

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370638367 274 DLNPKY-DAVRINQIYEQAKWQLLNEEIDCTEEEMLMFAALQVQV 317
Cdd:pfam00373   1 DLELLLqDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQA 45

PH domain; PH stands for pleckstrin homology.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370638367 370 PELSDYLrfLKPKRFTLKQSKQFWFTCRDLHLTLYKSREeAAQGAEPVHHINLRGCEVTPEVNIAQG--RYGIKLEVPSA 447
Cdd:pfam00169   1 VVKEGWL--LKKGGGKKKSWKKRYFVLFDGSLLYYKDDK-SGKSKEPKGSISLSGCEVVEVVASDSPkrKFCFELRTGER 77

                          90       100
                  ....*....|....*....|....*...
gi 1370638367 448 EGMTEMFVRCNSEEQYAKWMAACRLAAK 475
Cdd:pfam00169  78 TGKRTYLLQAESEEERKDWIKAIQSAIR 105

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 1370638367 284 INQIYEQAKWQLLNEEIDCTEEEMLMFAALQVQVTL 319
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 1370638367 370 PELSDYLRFLKPKRFTLKQSKQFWFTCRDLHLTLYKSREEAaqGAEPVHHINLRGCEVTPEVNIAQGRYGIKLEVPSAEG 449
Cdd:cd01237     1 PELADYLKYFKPKKFTLKGYKRYWFVFKDTHLSYYKSKEES--NGAPIQQINLKGCEVTPDVNVSQQKFCIKLLVPSPEG 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370638367 450 MTEMFVRCNSEEQYAKWMAACRLAAKGRSLADSSYDSEVKSIIAFLQ 496
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 1370638367 230 LRPKSLIERARMNVAWLDSSLSIMEQGVREFDTLCLRFKFY 270
Cdd:cd17096    50 YRPKSLVDKARLNSGWLDSSRSLMEQGVRENDTLLLRFKYY 90

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

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370638367 274 DLNPKY-DAVRINQIYEQAKWQLLNEEIDCTEEEMLMFAALQVQV 317
Cdd:pfam00373   1 DLELLLqDEVTRHLLYLQAKDDILEGRLPCSEEEALLLAALQLQA 45

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in kindlin-2 (KIND2); KIND2, also termed fermitin family homolog 2 (FERMT2), or mitogen-inducible gene 2 protein (MIG-2), or Pleckstrin homology (PH) domain-containing family C member 1, is an adaptor protein that is widely distributed and is particularly abundant in adherent cells. It binds to the integrin beta cytoplasmic tail to promote integrin activation. It promotes carcinogenesis through regulation of cell-cell and cell-extracellular matrix adhesion. KIND2 also plays an important role in cardiac development. KIND2 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        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370638367 213 SLAHSPATPSPDARNRQL-RPKSLIERARMNVAWLDSSLSIMEQGVREFDTLCLRFKFY 270
Cdd:cd17184    43 SLLRKPRDPTKKKKLAKMyKPQSLLDKAKINQGWLDSSRSLMEQDVKENEALLLRFKYY 101

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 1370638367 228 RQLRPKSLIERARMNVAWLDSSLSIMEQGVREFDTLCLRFKFY 270
Cdd:cd17185    49 KLYRPSSVTDKTQIHSRWLDSSRSLMQQGVQEGDRLWLRFKYY 91

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 1370638367  370 PELSDYLRFLKPKRFtlKQSKQFWFTCRDLHLTLYKSrEEAAQGAEPVHHINLRGCEVTPEVNI--AQGRYGIKLEVPSA 447
Cdd:smart00233   1 VIKEGWLYKKSGGGK--KSWKKRYFVLFNSTLLYYKS-KKDKKSYKPKGSIDLSGCTVREAPDPdsSKKPHCFEIKTSDR 77

                           90       100
                   ....*....|....*....|....*...
gi 1370638367  448 EgmtEMFVRCNSEEQYAKWMAACRLAAK 475
Cdd:smart00233  78 K---TLLLQAESEEEREKWVEALRKAIA 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 1370638367 284 INQIYEQAKWQLLNEEIDCTEEEMLMFAALQVQVTL 319
Cdd:cd14473     2 RYLLYLQVKRDILEGRLPCSEETAALLAALALQAEY 37

TBC1 domain family member 2A pleckstrin homology (PH) domain; TBC1D2A (also called PARIS-1/Prostate antigen recognized and identified by SEREX 1 and ARMUS) contains a PH domain and a TBC-type GTPase catalytic domain. TBC1D2A integrates signaling between Arf6, Rac1, and Rab7 during junction disassembly. Activated Rac1 recruits TBC1D2A to locally inactivate Rab7 via its C-terminal TBC/RabGAP domain and facilitate E-cadherin degradation in lysosomes. The TBC1D2A PH domain mediates localization at cell-cell contacts and coprecipitates with cadherin complexes. 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 1370638367 371 ELSDYLRFLKPKRFTLKQSKQFWFTCRDLHLTLYKSREEaaQGAEPVHHINLRGCEVTPEVNIAQGRYGIK-------LE 443
Cdd:cd01265     1 RLCGYLNKLETRGLGLKGWKRRWFVLDESKCQLYYYRSP--QDATPLGSIDLSGAAFSYDPEAEPGQFEIHtpgrvhiLK 78

                  ....*....
gi 1370638367 444 VPSAEGMTE 452
Cdd:cd01265    79 ASTRQAMLY 87

Boi family Pleckstrin homology domain; Yeast Boi proteins Boi1 and Boi2 are functionally redundant and important for cell growth with Boi mutants displaying defects in bud formation and in the maintenance of cell polarity.They appear to be linked to Rho-type GTPase, Cdc42 and Rho3. Boi1 and Boi2 display two-hybrid interactions with the GTP-bound ("active") form of Cdc42, while Rho3 can suppress of the lethality caused by deletion of Boi1 and Boi2. These findings suggest that Boi1 and Boi2 are targets of Cdc42 that promote cell growth in a manner that is regulated by Rho3. Boi proteins contain a N-terminal SH3 domain, followed by a SAM (sterile alpha motif) domain, a proline-rich region, which mediates binding to the second SH3 domain of Bem1, and C-terminal PH domain. The PH domain is essential for its function in cell growth and is important for localization to the bud, while the SH3 domain is needed for localization to the neck. 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 1370638367 374 DYLRFLKPKRFTLKQSKQFWFTCRDLHLTLYKSREEA-AQGaepvhHINLRGCEVTP--EVNIAQGRYGIKLeVPSAEGM 450
Cdd:cd13316     1 DHSGWMKKRGERYGTWKTRYFVLKGTRLYYLKSENDDkEKG-----LIDLTGHRVVPddSNSPFRGSYGFKL-VPPAVPK 74

                          90
                  ....*....|....*....
gi 1370638367 451 TEMFVrCNSEEQYAKWMAA 469
Cdd:cd13316    75 VHYFA-VDEKEELREWMKA 92