FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1298 GSAFFEVKQTTDPNYPEMLLIAINKHGVSLIHPQTKDILVTHPFTRISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 1377
Cdd:cd13199      1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80

                           90
                   ....*....|....*.
gi 2035224584 1378 DDLLTSYISLMLTNMN 1393
Cdd:cd13199     81 DDLLTSYISLLLSNMK 96

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1088 QIFHKVYFPDDTDEAFEVDSSTRAKDFCQNISQRLNLRSSEGFSLFVKIADKVISVPEGDFFFDFVRHLTDWIRKARPTR 1167
Cdd:cd17093      1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80

                           90
                   ....*....|....*...
gi 2035224584 1168 DGITPQFSYQVFFMKKLW 1185
Cdd:cd17093     81 DGPKPSLTYQVFFMRKLW 98

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  693 LLFSRFYEAYRNSGPNLPKNDVIIAVNWTGVYVVDDQEQVLLELSFPEITTVSSQKTNKVFTQTFSLNTVRGEEFTFQSP 772
Cdd:cd13198      1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRDGGQSFTLTTIQGEEFVFQSP 80

                           90
                   ....*....|....*....
gi 2035224584  773 NAEDIRDLVVYFLEGLKKR 791
Cdd:cd13198     81 NAEDIAELVNYFLEGLRKR 99

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  1090 FHKVYFPDDTDEAFEVDSSTRAKDFCQNISQRLNLRSSEGFSLFVKIADKVISvpegdfffdfvrhltDWIRKARPTRDG 1169
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDEDLR---------------HWLDPAKTLLDQ 65

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  1170 ITPQFSYQVFFMKKLWTNTV--PGKDRNAdLIFHFHQELPKLIRGYHKCSKEEAAKLAALVYRVRFGESKQEL--QAIPQ 1245
Cdd:smart00295   66 DVKSEPLTLYFRVKFYPPDPnqLKEDPTR-LNLLYLQVRNDILEGRLPCPEEEALLLAALALQAEFGDYDEELhdLRGEL 144

                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|....*..
gi 2035224584  1246 MLRELIPADLGKIQSANDWKRSIVAAYNQDAGMTPEDAKITFLKIVYRWPTFGSAFF 1302
Cdd:smart00295  145 SLKRFLPKQLLDSRKLKEWRERIVELHKELIGLSPEEAKLKYLELARKLPTYGVELF 201

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   483 MLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVsslgsggdhvmdaISQCEQYAKEQGAQER 562
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   563 N-APWRLFFRKEIFAPWHE-PTEDQVATNLIYQQVVRGVKFGEYRCDKEEdLAMIAAQQYFIEFNsDMNLERLLTLLPN- 639
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEEE-ALLLAALALQAEFG-DYDEELHDLRGELs 145

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035224584   640 ---YIPDyCLTGVEKAvDRWAASVVQAFKKsyYVKEKIPTLKVKedVVSYAKfKWPLLFSRFY 699
Cdd:smart00295  146 lkrFLPK-QLLDSRKL-KEWRERIVELHKE--LIGLSPEEAKLK--YLELAR-KLPTYGVELF 201

Calmodulin-binding motif; Short calmodulin-binding motif containing conserved Ile and Gln residues.

                            10        20
                    ....*....|....*....|...
gi 2035224584    13 RLKAATIIVQKYWKGYIQRQRYK 35
Cdd:smart00015    1 RLTRAAIIIQAAWRGYLARKRYK 23

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1298 GSAFFEVKQTTDPNYPEMLLIAINKHGVSLIHPQTKDILVTHPFTRISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 1377
Cdd:cd13199      1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80

                           90
                   ....*....|....*.
gi 2035224584 1378 DDLLTSYISLMLTNMN 1393
Cdd:cd13199     81 DDLLTSYISLLLSNMK 96

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1088 QIFHKVYFPDDTDEAFEVDSSTRAKDFCQNISQRLNLRSSEGFSLFVKIADKVISVPEGDFFFDFVRHLTDWIRKARPTR 1167
Cdd:cd17093      1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80

                           90
                   ....*....|....*...
gi 2035224584 1168 DGITPQFSYQVFFMKKLW 1185
Cdd:cd17093     81 DGPKPSLTYQVFFMRKLW 98

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  693 LLFSRFYEAYRNSGPNLPKNDVIIAVNWTGVYVVDDQEQVLLELSFPEITTVSSQKTNKVFTQTFSLNTVRGEEFTFQSP 772
Cdd:cd13198      1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRDGGQSFTLTTIQGEEFVFQSP 80

                           90
                   ....*....|....*....
gi 2035224584  773 NAEDIRDLVVYFLEGLKKR 791
Cdd:cd13198     81 NAEDIAELVNYFLEGLRKR 99

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  378 LHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP-------GYAPY 450
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevgKYAQF 80

                           90       100
                   ....*....|....*....|....*
gi 2035224584  451 CEDRLKRTFNNGTRNQPPSWLELQA 475
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  984 TDHIFDGPLKHEILRDETYCQMMKQLTDNRNRLSEERGWELMWLATGLFSCSQSLLKELTMFLR-------SRRHPISQD 1056
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpsREVGKYAQF 80

                           90       100
                   ....*....|....*....|....*
gi 2035224584 1057 SLQRLQKTLRNGQRKYPPHQVEVEA 1081
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   483 MLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVsslgsggdhvmdaISQCEQYAKEQGAQER 562
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   563 N-APWRLFFRKEIFAPWHE-PTEDQVATNLIYQQVVRGVKFGEYRCDKEEdLAMIAAQQYFIEFNsDMNLERLLTLLPN- 639
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEEE-ALLLAALALQAEFG-DYDEELHDLRGELs 145

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035224584   640 ---YIPDyCLTGVEKAvDRWAASVVQAFKKsyYVKEKIPTLKVKedVVSYAKfKWPLLFSRFY 699
Cdd:smart00295  146 lkrFLPK-QLLDSRKL-KEWRERIVELHKE--LIGLSPEEAKLK--YLELAR-KLPTYGVELF 201

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        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1200 FHFHQELPKLIRGYHKCSKEEAAKLAALVYRVRFGE-SKQELQAIPQMLRELIPADLGKIQSANDWKRSIVAAYNQDAGM 1278
Cdd:cd14473      4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDyDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83

                           90
                   ....*....|....*.
gi 2035224584 1279 TPEDAKITFLKIVYRW 1294
Cdd:cd14473     84 SPAEAKLKYLKIARKL 99

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035224584   791 RSKFVIALQDYKAPGEGssFLTFLKGDLIILEEDStgetvlNSGWCVGRCERTQEkGDFPAEtvYV 856
Cdd:smart00326    1 EGPQVRALYDYTAQDPD--ELSFKKGDIITVLEKS------DDGWWKGRLGRGKE-GLFPSN--YV 55

MAEBL; Provisional

                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2035224584   85 KIKFEQKRHVEALRlKKKEERELKDAGNKRAKEIAEQHYRERIYQLERK--EMEIEMEERKIVEEKKNKINEAARKADE 161
Cdd:PTZ00121  1424 KKKAEEKKKADEAK-KKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKadEAKKKAEEAKKADEAKKKAEEAKKKADE 1501

ATP synthase archaeal, H subunit; he A1/A0 ATP synthase is homologous to the V-type (V1/V0, vacuolar) ATPase, but functions in the ATP synthetic direction as does the F1/F0 ATPase of bacteria. The hydrophilic A1 "stalk" complex (AhaABCDEFG) is the site of ATP generation and is coupled to the membrane-embedded proton translocating A0 complex. It is unclear precisely where AhaH fits into these complexes.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   84 KKIKFEQKRHVEALRLKKKEERELKDAGNKRAKEIAEQHYRE------RIyqLERKEMEIEMEERKIVEEKKNKINEAAR 157
Cdd:TIGR02926    2 EEIKKAEEDAEELIEEAEEERKQRIAEAREEARELLEEAEEEasklgeEI--IKEAEEEIEKEAEKIREEGEKEIEAMKS 79

                   ....
gi 2035224584  158 KADE 161
Cdd:TIGR02926   80 KAKE 83

Protein of unknown function (DUF6033); This family of proteins is functionally uncharacterized. This family of proteins is primarily found in Clostridia. Proteins in this family are typically between 212 and 271 amino acids in length.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   89 EQKRHVEALRLKKKEERELKdagnkrAKEIAEQHYRERIYQLERKEMEIEMEERKIVEEKKNKINEAAR--KADEPV-DD 165
Cdd:pfam19498  119 AQKERIEKKRAKKKEEKKAE------EKKAEKKKREERLEKAKEEKEETVTVTASSIEELLKKIKDYYYnvKSDSVLtEE 192

                           90
                   ....*....|
gi 2035224584  166 SKLVEAMFDF 175
Cdd:pfam19498  193 EKGVGQQFDF 202

FERM domain C-lobe, repeat 2, of Myosin VII (MyoVII, Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1298 GSAFFEVKQTTDPNYPEMLLIAINKHGVSLIHPQTKDILVTHPFTRISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 1377
Cdd:cd13199      1 GSAFFEVKQTTDPSLPEILLIAINKNGVSLIDPKTKEILATHPFSKISNWSSGNTYFHMTIGNLVRGSKLLCETSLGYKM 80

                           90
                   ....*....|....*.
gi 2035224584 1378 DDLLTSYISLMLTNMN 1393
Cdd:cd13199     81 DDLLTSYISLLLSNMK 96

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 2, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the second FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1088 QIFHKVYFPDDTDEAFEVDSSTRAKDFCQNISQRLNLRSSEGFSLFVKIADKVISVPEGDFFFDFVRHLTDWIRKARPTR 1167
Cdd:cd17093      1 QIFHKVYFPDDTDEAFEVDSSTRARDLCQNIASRLGLKSSEGFSLFVKIADKVISLPEGDFFFDFIRHLTDWIKKARPTK 80

                           90
                   ....*....|....*...
gi 2035224584 1168 DGITPQFSYQVFFMKKLW 1185
Cdd:cd17093     81 DGPKPSLTYQVFFMRKLW 98

FERM domain C-lobe, repeat 1, of Myosin VII (MyoVII/Myo7); MyoVII, a MyTH-FERM myosin, is an actin-based motor protein essential for a variety of biological processes in the actin cytoskeleton function. Mutations in MyoVII leads to problems in sensory perception: deafness and blindness in humans (Usher Syndrome), retinal defects and deafness in mice (shaker 1), and aberrant auditory and vestibular function in zebrafish. Myosin VIIAs have plus (barbed) end-directed motor activity on actin filaments and a characteristic actin-activated ATPase activity. MyoVII consists of a conserved spectrin-like, SH3 subdomain N-terminal region, a motor/head region, a neck made of 4-5 IQ motifs, and a tail consisting of a coiled-coil domain, followed by a tandem repeat of myosin tail homology 4 (MyTH4) domains and partial FERM domains that are separated by an SH3 subdomain and are thought to mediate dimerization and binding to other proteins or cargo. Members include: MyoVIIa, MyoVIIb, and MyoVII members that do not have distinct myosin VIIA and myosin VIIB genes. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs) , the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  693 LLFSRFYEAYRNSGPNLPKNDVIIAVNWTGVYVVDDQEQVLLELSFPEITTVSSQKTNKVFTQTFSLNTVRGEEFTFQSP 772
Cdd:cd13198      1 LLFSRFFEATKFSGPSLPKSEVIIAVNWTGIYFVDEQEQVLLELSFPEITGVSSSRGKRDGGQSFTLTTIQGEEFVFQSP 80

                           90
                   ....*....|....*....
gi 2035224584  773 NAEDIRDLVVYFLEGLKKR 791
Cdd:cd13198     81 NAEDIAELVNYFLEGLRKR 99

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  378 LHFIIGHGILRAELRDEIYCQICKQLTNNPSKSSHARGWILLSLCVGCFAPSEKFVSYLRAFIREGPP-------GYAPY 450
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKRHADdpsrevgKYAQF 80

                           90       100
                   ....*....|....*....|....*
gi 2035224584  451 CEDRLKRTFNNGTRNQPPSWLELQA 475
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105

MyTH4 domain; Domain in myosin and kinesin tails, present twice in myosin-VIIa, and also present in 3 other myosins.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  984 TDHIFDGPLKHEILRDETYCQMMKQLTDNRNRLSEERGWELMWLATGLFSCSQSLLKELTMFLR-------SRRHPISQD 1056
Cdd:pfam00784    1 AQNILQKGLKRPELRDEIYCQLIKQTTNNPKPESLLRGWQLLALCLGTFPPSKKLLKYLLKFLKrhaddpsREVGKYAQF 80

                           90       100
                   ....*....|....*....|....*
gi 2035224584 1057 SLQRLQKTLRNGQRKYPPHQVEVEA 1081
Cdd:pfam00784   81 CLKRLKRTLKNGGRKYPPSREEIEA 105

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.

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   483 MLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVsslgsggdhvmdaISQCEQYAKEQGAQER 562
Cdd:smart00295    1 VLKVYLLDGTTLEFEVDSSTTAEELLETVCRKLGIRESEYFGLQFEDPDED-------------LRHWLDPAKTLLDQDV 67

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584   563 N-APWRLFFRKEIFAPWHE-PTEDQVATNLIYQQVVRGVKFGEYRCDKEEdLAMIAAQQYFIEFNsDMNLERLLTLLPN- 639
Cdd:smart00295   68 KsEPLTLYFRVKFYPPDPNqLKEDPTRLNLLYLQVRNDILEGRLPCPEEE-ALLLAALALQAEFG-DYDEELHDLRGELs 145

                           170       180       190       200       210       220
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2035224584   640 ---YIPDyCLTGVEKAvDRWAASVVQAFKKsyYVKEKIPTLKVKedVVSYAKfKWPLLFSRFY 699
Cdd:smart00295  146 lkrFLPK-QLLDSRKL-KEWRERIVELHKE--LIGLSPEEAKLK--YLELAR-KLPTYGVELF 201

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        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1200 FHFHQELPKLIRGYHKCSKEEAAKLAALVYRVRFGE-SKQELQAIPQMLRELIPADLGKIQSANDWKRSIVAAYNQDAGM 1278
Cdd:cd14473      4 LLYLQVKRDILEGRLPCSEETAALLAALALQAEYGDyDPSEHKPKYLSLKRFLPKQLLKQRKPEEWEKRIVELHKKLRGL 83

                           90
                   ....*....|....*.
gi 2035224584 1279 TPEDAKITFLKIVYRW 1294
Cdd:cd14473     84 SPAEAKLKYLKIARKL 99

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain, F1 sub-domain, found in Dictyostelium discoideum Myosin-VIIa (DdMyo7) and similar proteins; DdMyo7, also termed Myosin-I heavy chain, or class VII unconventional myosin, or M7, plays a role in adhesion in Dictyostelium where it is a component of a complex of proteins that serve to link membrane receptors to the underlying actin cytoskeleton. It interacts with talinA, an actin-binding protein with a known role in cell-substrate adhesion. DdMyo7 is required for phagocytosis. It is also essential for the extension of filopodia, plasma membrane protrusions filled with parallel bundles of F-actin. Members in this family contain a myosin motor domain, two MyTH4 domains, two FERM (Band 4.1, ezrin, radixin, moesin) domains, and two Pleckstrin homology (PH) domains. Some family members contain an extra SH3 domain. Each 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).

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  480 KPIMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLK-DQFGFSLYIALFDKVSSLGSgGDHVMDAISQCEQYAKEQG 558
Cdd:cd17208      2 RPIVARFYFLDGQFKALEFDSAATAAEVLEQLKQKIGLRsTADGFALYEVFGGIERAILP-EEKVADVLSKWEKLQRTMA 80

                           90
                   ....*....|....*..
gi 2035224584  559 AQERNAPWRLFFRKEIF 575
Cdd:cd17208     81 SCAAQQAVKFVFKKRLF 97

FERM (Four.1 protein, Ezrin, Radixin, Moesin) domain 1, F1 sub-domain, found in Myosin-VIIa, Myosin-VIIb, and similar proteins; This family includes two nontraditional members of the myosin superfamily, myosin-VIIa and myosin-VIIb. Myosin-VIIa, also termed myosin-7a (Myo7a), has been implicated in the structural organization of hair bundles at the apex of sensory hair cells (SHCs) where it serves mechanotransduction in the process of hearing and balance. Mutations in the MYO7A gene may be associated with Usher Syndrome type 1B (USH1B) and nonsyndromic hearing loss (DFNB2, DFNA11). Myosin-VIIb, also termed myosin-7b (Myo7b), is a high duty ratio motor adapted for generating and maintaining tension. It associates with harmonin and ANKS4B to form a stable ternary complex for anchoring microvilli tip-link cadherins. Like other unconventional myosins, myosin-VII is composed of a conserved motor head, a neck region and a tail region containing two MyTH4 domains, a SH3 domain, and two FERM domains. The FERM domain is made up of three sub-domains, F1, F2, and F3. The family corresponds to the F1 sub-domain of the first FERM domain, which is also called the N-terminal ubiquitin-like structural domain of the FERM domain (FERM_N).

                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2035224584 1093 VYFPDDTDEAFEVDSSTRAKDFCQNISQRLNLRSSEGFSLFVKIADKVISVPEG-DFFFDFV 1153
Cdd:cd17092      6 VTFMDGSTKTVEVDSATTARELCRQLAEKLGLKDTFGFSLYIALFDKVSSLGSGtDHVMDAI 67

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        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  587 ATNLIYQQVVRGVKFGEYRCDkEEDLAMIAAQQYFIEFNsDMNLERLL---TLLPNYIPDYCLTGVEKavDRWAASVVQA 663
Cdd:cd14473      1 TRYLLYLQVKRDILEGRLPCS-EETAALLAALALQAEYG-DYDPSEHKpkyLSLKRFLPKQLLKQRKP--EEWEKRIVEL 76

                   ....*....
gi 2035224584  664 FKKSYYVKE 672
Cdd:cd14473     77 HKKLRGLSP 85

FERM domain C-lobe of Myosin XV (MyoXV/Myo15); MyoXV, a MyTH-FERM myosin, are actin-based motor proteins essential for a variety of biological processes in actin cytoskeleton function. Specifically MyoXV functions in the actin organization in hair cells of the organ of Corti. Mutations in Human MyoXVa causes non-syndromic deafness, DFNB3 and the mouse shaker-2 mutation. MyoXV consists of a N-terminal motor/head region, a neck made of 1-3 IQ motifs, and a tail that consists of either a myosin tail homology 4 (MyTH4) domains, followed by an SH3 domain, and a MyTH-FERM domains as in rat Myo15 or two MyTH-FERM domains separated by a SH3 domain as in human Myo15A. The MyTH-FERM domains are thought to mediate dimerization and binding to other proteins or cargo. The FERM domain has a cloverleaf tripart structure composed of: (1) FERM_N (A-lobe or F1); (2) FERM_M (B-lobe, or F2); and (3) FERM_C (C-lobe or F3). The C-lobe/F3 within the FERM domain is part of the PH domain family. 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 (PTPs), the tyrosine kinases FAK and JAK, in addition to other proteins involved in signaling. This domain is structurally similar to the PH and PTB domains and consequently is capable of binding to both peptides and phospholipids at different sites.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584 1298 GSAFFEVKQTTDPNYPEMLLIAINKHGVSLIHPQTKDILVTHPFT------RISNWSSGNTYFHMTIGNLVRGSKLLCET 1371
Cdd:cd13201      1 GSNFFYVQRVSDPRLPGPCLLALNREGLHFLDPKTHETLLRIPLKevqstrKLRPLEDGTPFLDIKYGNLMQQRTIRLET 80

                           90       100
                   ....*....|....*....|
gi 2035224584 1372 SLGYKMDDLLTSYISLMLTN 1391
Cdd:cd13201     81 DQAHEISRLIAQYIEEASEN 100

Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences containing proline and hydrophobic amino acids. Pro-containing polypeptides may bind to SH3 domains in 2 different binding orientations.

                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2035224584   791 RSKFVIALQDYKAPGEGssFLTFLKGDLIILEEDStgetvlNSGWCVGRCERTQEkGDFPAEtvYV 856
Cdd:smart00326    1 EGPQVRALYDYTAQDPD--ELSFKKGDIITVLEKS------DDGWWKGRLGRGKE-GLFPSN--YV 55

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.

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2035224584  482 IMLPITFMDGNTKTLLADSATTARELCNQLSDKIGLKDQFGFSLYIALFDKVS-SLGSgGDHVMDAISqceqyakeqgaq 560
Cdd:cd01765      1 ISCRVRLLDGTELTLEVSKKATGQELFDKVCEKLNLLEKDYFGLFYEDNDGQKhWLDL-DKKISKQLK------------ 67

                           90
                   ....*....|..
gi 2035224584  561 eRNAPWRLFFRK 572
Cdd:cd01765     68 -RSGPYQFYFRV 78

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organization. First described in the Src cytoplasmic tyrosine kinase. The structure is a partly opened beta barrel.