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Conserved domains on  [gi|964111659|ref|XP_014761667|]
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protein spire isoform X5 [Drosophila ananassae]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
116-353 3.52e-33

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member smart00750:

Pssm-ID: 473864  Cd Length: 176  Bit Score: 125.21  E-value: 3.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659   116 VTLNNILDSFKAPLSEDQAWALIHQFISLYHKVAVeahhsaADYDAELPTRFELHFHRDGGVHFSgkdrlPPAQDqleqe 195
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELHR------QAKSGNILLTWDGLLKLDGSVAFK-----TPEQS----- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659   196 rnqelhtqessirgtlddsassssgdssaIIERAFdnnNHHHHHTPLVVSHRKIISELAQIVYTALDYNLPEDEECQMSQ 275
Cdd:smart00750  65 -----------------------------RPDPYF---MAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSA 112
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 964111659   276 ELESLFNFMTADETDDDCIDEGIDEGdkrwdddteeerndtKELEHIIETCRNHI-KPTLPENHYRAVCRALVTETIEL 353
Cdd:smart00750 113 ILEILLNGMPADDPRDRSNLEGVSAA---------------RSFEDFMRLCASRLpQRREAANHYLAHCRALFAETLEL 176
WH2_Spire1_r2-like cd22078
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
419-450 2.52e-15

second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 1 (Spir1), and related proteins; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) domain in human Spire family protein Spire-1 (also called Spir1) and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. It was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. The mammalian genome encodes two Spire proteins, namely Spire-1 (Spir1) and Spire-2 (Spir2). This model contains WH2 domain 2 of human Spire-1 protein. Major expression of both spire genes have been detected during embryogenesis in the developing nervous system). In addition, spire1 expression is found in the fetal liver, and in adult tissues, spire1 is mainly expressed in neuronal cells of the nervous system. Minor expression levels were detected in testis and spleen. Spire also acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. High levels of spire1 expression are restricted to the nervous system, oocytes, and testis. Since function of Spire-1 and Spire-2 in oocyte maturation is redundant, spire1 mutant mice are fertile, overall brain anatomy is not altered, and visual and motor functions remain normal; however, detailed behavioral studies of the spire1 mutant mice unveiled a very specific and highly significant phenotype in terms of fear learning in male mice. This family also contains the second of four tandem repeats of WH2 in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis.


:

Pssm-ID: 409221  Cd Length: 32  Bit Score: 69.87  E-value: 2.52e-15
                         10        20        30
                 ....*....|....*....|....*....|..
gi 964111659 419 EYELTPYEILMGDIRAKKYQLRKVMVNGDIPP 450
Cdd:cd22078    1 EYELTPYEMLMDDIRSKRYTLRKVMVNGDIPP 32
WH2_DmSpire_r1-like cd22067
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
381-407 2.15e-13

first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the first of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the first tandem WH2 domain of Spire (also called Spir-A or WH2-A).


:

Pssm-ID: 409210  Cd Length: 27  Bit Score: 64.21  E-value: 2.15e-13
                         10        20
                 ....*....|....*....|....*..
gi 964111659 381 QELAKLGFNDWARFWVQVIDELRRGVR 407
Cdd:cd22067    1 QELAKLGFNDWARFWVQVIDELRRGVR 27
WH2_DmSpire_r4 cd22069
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
484-512 7.31e-13

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the fourth of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the fourth tandem WH2 domain of Spire (also called Spir-D or WH2-A).


:

Pssm-ID: 409212  Cd Length: 29  Bit Score: 62.95  E-value: 7.31e-13
                         10        20
                 ....*....|....*....|....*....
gi 964111659 484 CTPSPREQLMESIRKGKELKQITPPEAPT 512
Cdd:cd22069    1 CEPSPREQLMESIRKGKELKQITPPEAAA 29
WH2_DmSpire_r3-like cd22068
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
452-477 2.65e-10

third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the third of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the third tandem WH2 domain of Spire (also called Spir-C or WH2-C), which plays a unique role whereby two critical residues have been identified for activity for binding to actin with positive cooperativity.


:

Pssm-ID: 409211  Cd Length: 26  Bit Score: 55.49  E-value: 2.65e-10
                         10        20
                 ....*....|....*....|....*.
gi 964111659 452 VKKDAHAMILEFIRSRPPLRKASERQ 477
Cdd:cd22068    1 VKKDAHAMILEFIRSRPPLKKASDRQ 26
 
Name Accession Description Interval E-value
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
116-353 3.52e-33

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 125.21  E-value: 3.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659   116 VTLNNILDSFKAPLSEDQAWALIHQFISLYHKVAVeahhsaADYDAELPTRFELHFHRDGGVHFSgkdrlPPAQDqleqe 195
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELHR------QAKSGNILLTWDGLLKLDGSVAFK-----TPEQS----- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659   196 rnqelhtqessirgtlddsassssgdssaIIERAFdnnNHHHHHTPLVVSHRKIISELAQIVYTALDYNLPEDEECQMSQ 275
Cdd:smart00750  65 -----------------------------RPDPYF---MAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSA 112
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 964111659   276 ELESLFNFMTADETDDDCIDEGIDEGdkrwdddteeerndtKELEHIIETCRNHI-KPTLPENHYRAVCRALVTETIEL 353
Cdd:smart00750 113 ILEILLNGMPADDPRDRSNLEGVSAA---------------RSFEDFMRLCASRLpQRREAANHYLAHCRALFAETLEL 176
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
116-357 3.73e-25

Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) evolved from a catalytic protein kinase fold and functions as an interaction domain. In SPIRE1 (protein spire homolog 1) this domain interacts with FMN2 (formin-2).


Pssm-ID: 465129  Cd Length: 196  Bit Score: 103.15  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659  116 VTLNNILDSFKAPLSEDQAWALIHQFISLYhkvaVEAHHSAADYDAELPTRFELHFHRDGGVHfsgkdrlppaqdqleqe 195
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGL----RQPTRRRKQKFRRIRGPSDILLHRDGTVT----------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659  196 rnqeLHTQESSirgtlddsassssgdssaiierafdnnNHHHHHTPLVVSHRKIISELAQIVYTALDYNLPEDEECQMSQ 275
Cdd:pfam16474  60 ----LRFEASS---------------------------DGPPKALLPARSETQVIQSLGVAIYKALDYGLKESEERELSP 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659  276 ELESLFNFMTADETDDD---CIDEGIdEGDKRWDDDTEEERND--TKELEHIIETCRNHIK-PTLPENHYRAVCRALVTE 349
Cdd:pfam16474 109 PLEQLIDLMTNGDDEDGgqeTDDEGY-EADEEEEEEEDEEGTIssVRTFRDVLKLCASHLPnPSDAPNHYQAVCRALFAE 187

                  ....*...
gi 964111659  350 TIELRVFL 357
Cdd:pfam16474 188 TLELSTFL 195
WH2_Spire1_r2-like cd22078
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
419-450 2.52e-15

second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 1 (Spir1), and related proteins; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) domain in human Spire family protein Spire-1 (also called Spir1) and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. It was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. The mammalian genome encodes two Spire proteins, namely Spire-1 (Spir1) and Spire-2 (Spir2). This model contains WH2 domain 2 of human Spire-1 protein. Major expression of both spire genes have been detected during embryogenesis in the developing nervous system). In addition, spire1 expression is found in the fetal liver, and in adult tissues, spire1 is mainly expressed in neuronal cells of the nervous system. Minor expression levels were detected in testis and spleen. Spire also acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. High levels of spire1 expression are restricted to the nervous system, oocytes, and testis. Since function of Spire-1 and Spire-2 in oocyte maturation is redundant, spire1 mutant mice are fertile, overall brain anatomy is not altered, and visual and motor functions remain normal; however, detailed behavioral studies of the spire1 mutant mice unveiled a very specific and highly significant phenotype in terms of fear learning in male mice. This family also contains the second of four tandem repeats of WH2 in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis.


Pssm-ID: 409221  Cd Length: 32  Bit Score: 69.87  E-value: 2.52e-15
                         10        20        30
                 ....*....|....*....|....*....|..
gi 964111659 419 EYELTPYEILMGDIRAKKYQLRKVMVNGDIPP 450
Cdd:cd22078    1 EYELTPYEMLMDDIRSKRYTLRKVMVNGDIPP 32
WH2_DmSpire_r1-like cd22067
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
381-407 2.15e-13

first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the first of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the first tandem WH2 domain of Spire (also called Spir-A or WH2-A).


Pssm-ID: 409210  Cd Length: 27  Bit Score: 64.21  E-value: 2.15e-13
                         10        20
                 ....*....|....*....|....*..
gi 964111659 381 QELAKLGFNDWARFWVQVIDELRRGVR 407
Cdd:cd22067    1 QELAKLGFNDWARFWVQVIDELRRGVR 27
WH2_DmSpire_r4 cd22069
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
484-512 7.31e-13

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the fourth of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the fourth tandem WH2 domain of Spire (also called Spir-D or WH2-A).


Pssm-ID: 409212  Cd Length: 29  Bit Score: 62.95  E-value: 7.31e-13
                         10        20
                 ....*....|....*....|....*....
gi 964111659 484 CTPSPREQLMESIRKGKELKQITPPEAPT 512
Cdd:cd22069    1 CEPSPREQLMESIRKGKELKQITPPEAAA 29
WH2_DmSpire_r3-like cd22068
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
452-477 2.65e-10

third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the third of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the third tandem WH2 domain of Spire (also called Spir-C or WH2-C), which plays a unique role whereby two critical residues have been identified for activity for binding to actin with positive cooperativity.


Pssm-ID: 409211  Cd Length: 26  Bit Score: 55.49  E-value: 2.65e-10
                         10        20
                 ....*....|....*....|....*.
gi 964111659 452 VKKDAHAMILEFIRSRPPLRKASERQ 477
Cdd:cd22068    1 VKKDAHAMILEFIRSRPPLKKASDRQ 26
 
Name Accession Description Interval E-value
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
116-353 3.52e-33

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 125.21  E-value: 3.52e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659   116 VTLNNILDSFKAPLSEDQAWALIHQFISLYHKVAVeahhsaADYDAELPTRFELHFHRDGGVHFSgkdrlPPAQDqleqe 195
Cdd:smart00750   1 VSLADILEVRGRPLNEEEIWAVCLQCLGALRELHR------QAKSGNILLTWDGLLKLDGSVAFK-----TPEQS----- 64
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659   196 rnqelhtqessirgtlddsassssgdssaIIERAFdnnNHHHHHTPLVVSHRKIISELAQIVYTALDYNLPEDEECQMSQ 275
Cdd:smart00750  65 -----------------------------RPDPYF---MAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSA 112
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 964111659   276 ELESLFNFMTADETDDDCIDEGIDEGdkrwdddteeerndtKELEHIIETCRNHI-KPTLPENHYRAVCRALVTETIEL 353
Cdd:smart00750 113 ILEILLNGMPADDPRDRSNLEGVSAA---------------RSFEDFMRLCASRLpQRREAANHYLAHCRALFAETLEL 176
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
116-357 3.73e-25

Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) evolved from a catalytic protein kinase fold and functions as an interaction domain. In SPIRE1 (protein spire homolog 1) this domain interacts with FMN2 (formin-2).


Pssm-ID: 465129  Cd Length: 196  Bit Score: 103.15  E-value: 3.73e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659  116 VTLNNILDSFKAPLSEDQAWALIHQFISLYhkvaVEAHHSAADYDAELPTRFELHFHRDGGVHfsgkdrlppaqdqleqe 195
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGL----RQPTRRRKQKFRRIRGPSDILLHRDGTVT----------------- 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659  196 rnqeLHTQESSirgtlddsassssgdssaiierafdnnNHHHHHTPLVVSHRKIISELAQIVYTALDYNLPEDEECQMSQ 275
Cdd:pfam16474  60 ----LRFEASS---------------------------DGPPKALLPARSETQVIQSLGVAIYKALDYGLKESEERELSP 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 964111659  276 ELESLFNFMTADETDDD---CIDEGIdEGDKRWDDDTEEERND--TKELEHIIETCRNHIK-PTLPENHYRAVCRALVTE 349
Cdd:pfam16474 109 PLEQLIDLMTNGDDEDGgqeTDDEGY-EADEEEEEEEDEEGTIssVRTFRDVLKLCASHLPnPSDAPNHYQAVCRALFAE 187

                  ....*...
gi 964111659  350 TIELRVFL 357
Cdd:pfam16474 188 TLELSTFL 195
WH2_Spire1_r2-like cd22078
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
419-450 2.52e-15

second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 1 (Spir1), and related proteins; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) domain in human Spire family protein Spire-1 (also called Spir1) and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. It was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. The mammalian genome encodes two Spire proteins, namely Spire-1 (Spir1) and Spire-2 (Spir2). This model contains WH2 domain 2 of human Spire-1 protein. Major expression of both spire genes have been detected during embryogenesis in the developing nervous system). In addition, spire1 expression is found in the fetal liver, and in adult tissues, spire1 is mainly expressed in neuronal cells of the nervous system. Minor expression levels were detected in testis and spleen. Spire also acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. High levels of spire1 expression are restricted to the nervous system, oocytes, and testis. Since function of Spire-1 and Spire-2 in oocyte maturation is redundant, spire1 mutant mice are fertile, overall brain anatomy is not altered, and visual and motor functions remain normal; however, detailed behavioral studies of the spire1 mutant mice unveiled a very specific and highly significant phenotype in terms of fear learning in male mice. This family also contains the second of four tandem repeats of WH2 in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis.


Pssm-ID: 409221  Cd Length: 32  Bit Score: 69.87  E-value: 2.52e-15
                         10        20        30
                 ....*....|....*....|....*....|..
gi 964111659 419 EYELTPYEILMGDIRAKKYQLRKVMVNGDIPP 450
Cdd:cd22078    1 EYELTPYEMLMDDIRSKRYTLRKVMVNGDIPP 32
WH2_DmSpire_r1-like cd22067
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
381-407 2.15e-13

first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the first of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the first tandem WH2 domain of Spire (also called Spir-A or WH2-A).


Pssm-ID: 409210  Cd Length: 27  Bit Score: 64.21  E-value: 2.15e-13
                         10        20
                 ....*....|....*....|....*..
gi 964111659 381 QELAKLGFNDWARFWVQVIDELRRGVR 407
Cdd:cd22067    1 QELAKLGFNDWARFWVQVIDELRRGVR 27
WH2_Spire_1-2_r1 cd22065
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
382-412 2.83e-13

first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homologs 1 and 2; This family contains the first tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) domain in human Spire family proteins Spire-1 (also called Spir1) and Spire-2 (Spir2) and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. It was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. The mammalian genome encodes two Spire proteins, namely Spire-1 and Spire-2. This model contains WH2 domain 1 of human Spire-1 and Spire-2 . Major expression of both spire genes have been detected during embryogenesis in the developing nervous system). In addition, spire1 expression is found in the fetal liver, while spire2 expression is seen in early stages of intestinal development. In adult tissues, the spire2 gene shows a rather broad expression pattern, which includes the epithelial cells of the digestive tract, testical spermatocytes, and neuronal cells of the nervous system. In contrast, spire1 is mainly expressed in neuronal cells of the nervous system. Minor expression levels were detected in testis and spleen. Spire also acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. High levels of spire1 expression are restricted to the nervous system, oocytes, and testis. Since function of Spire-1 and Spire-2 in oocyte maturation is redundant, spire1 mutant mice are fertile, overall brain anatomy is not altered, and visual and motor functions remain normal; however, detailed behavioral studies of the spire1 mutant mice unveiled a very specific and highly significant phenotype in terms of fear learning in male mice.


Pssm-ID: 409208  Cd Length: 32  Bit Score: 63.91  E-value: 2.83e-13
                         10        20        30
                 ....*....|....*....|....*....|.
gi 964111659 382 ELAKLGFNDWARFWVQVIDELRRGVRLKKSN 412
Cdd:cd22065    1 ELDELQNTDWARLWVQVMRELRNGVKLKKVQ 31
WH2_DmSpire_r4 cd22069
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
484-512 7.31e-13

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the fourth of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the fourth tandem WH2 domain of Spire (also called Spir-D or WH2-A).


Pssm-ID: 409212  Cd Length: 29  Bit Score: 62.95  E-value: 7.31e-13
                         10        20
                 ....*....|....*....|....*....
gi 964111659 484 CTPSPREQLMESIRKGKELKQITPPEAPT 512
Cdd:cd22069    1 CEPSPREQLMESIRKGKELKQITPPEAAA 29
WH2_Spire2_r2 cd22079
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
421-450 4.09e-11

second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 2; This family contains the second tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) domain in human Spire family protein Spire-2 (also called Spir2) and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. It was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. The mammalian genome encodes two Spire proteins, namely Spire-1 (Spir1) and Spire-2 (Spir2). This model contains WH2 domain 2 of human Spire-2. Major expression of both spire genes have been detected during embryogenesis in the developing nervous system). In addition, spire2 expression is seen in early stages of intestinal development. In adult tissues, the spire2 gene shows a rather broad expression pattern, which includes the epithelial cells of the digestive tract, testical spermatocytes, and neuronal cells of the nervous system. Spire also acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage.


Pssm-ID: 409222  Cd Length: 30  Bit Score: 57.61  E-value: 4.09e-11
                         10        20        30
                 ....*....|....*....|....*....|
gi 964111659 421 ELTPYEILMGDIRAKKYQLRKVMVNGDIPP 450
Cdd:cd22079    1 QLTPFEMLMQDIRARKYKLRKVMVDGDIPP 30
WH2_DmSpire_r3-like cd22068
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
452-477 2.65e-10

third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in Drosophila melanogaster Spire, and similar proteins; This family contains the third of four tandem repeats of Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) in Drosophila melanogaster Spire (also called Spir), an actin nucleator essential for establishing an actin mesh during oogenesis. Spire was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire promotes dissociation of the actin nucleator Cappuccino (Capu) from the barbed end of actin filaments. Spire is involved in intracellular vesicle transport along actin fibers, providing a link between actin cytoskeleton dynamics and intracellular transport. Drosophila Spire contains four tandem WH2 domains which appear to function by determining the size of filament nuclei according to the number of WH2 repeats, suggesting that the WH2 domains of Spire line up actin subunits along a filament strand of the actin double helix, thereby generating nuclei for actin assembly. This model contains the third tandem WH2 domain of Spire (also called Spir-C or WH2-C), which plays a unique role whereby two critical residues have been identified for activity for binding to actin with positive cooperativity.


Pssm-ID: 409211  Cd Length: 26  Bit Score: 55.49  E-value: 2.65e-10
                         10        20
                 ....*....|....*....|....*.
gi 964111659 452 VKKDAHAMILEFIRSRPPLRKASERQ 477
Cdd:cd22068    1 VKKDAHAMILEFIRSRPPLKKASDRQ 26
WH2_Spire1-2_r3 cd22186
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
453-475 2.15e-05

third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homologs 1 and 2; This family contains the third tandem Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) domain in human Spire family protein Spire-1 (also called Spir1) and Spire-2 (Spir2) and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. It was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. The mammalian genome encodes two Spire proteins, namely Spire-1 (Spir1) and Spire-2 (Spir2). This model contains WH2 domain 3 of human Spire-1 and Spire-2 . Major expression of both spire genes have been detected during embryogenesis in the developing nervous system). In addition, spire1 expression is found in the fetal liver, while spire2 expression is seen in early stages of intestinal development. In adult tissues, the spire2 gene shows a rather broad expression pattern, which includes the epithelial cells of the digestive tract, testical spermatocytes, and neuronal cells of the nervous system. In contrast, spire1 is mainly expressed in neuronal cells of the nervous system. Minor expression levels were detected in testis and spleen. Spire also acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. High levels of spire1 expression are restricted to the nervous system, oocytes, and testis. Since function of Spire-1 and Spire-2 in oocyte maturation is redundant, spire1 mutant mice are fertile, overall brain anatomy is not altered, and visual and motor functions remain normal; however, detailed behavioral studies of the spire1 mutant mice unveiled a very specific and highly significant phenotype in terms of fear learning in male mice.


Pssm-ID: 409226  Cd Length: 23  Bit Score: 41.56  E-value: 2.15e-05
                         10        20
                 ....*....|....*....|...
gi 964111659 453 KKDAHAMILEFIRSRPPLRKASE 475
Cdd:cd22186    1 KKSAHELILDFIRSRPPLNPVSA 23
WH2_Spire cd22066
second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) ...
453-474 1.59e-04

second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeats of protein Spire; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) repeats 2-4 in human Spire (also called Spir), Drosophila Spire, and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. This WH2-containing actin nucleator was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. Several spire gene family members have been identified, including paralogs Spire-1 (Spir1) and Spire-2 (Spir2) in higher eukaryotes. Spire acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. Spire-1 and Spire-2 encode a modified Fab1/YOTB/Vac1/EEA1 (FYVE)-type zinc finger membrane-binding domain at their C-termini that promiscuously interacts with negatively charged lipids and the interaction of these proteins with additional factors may provide the specificity for its targeting to the correct subpopulation of vesicles.


Pssm-ID: 409209  Cd Length: 22  Bit Score: 39.11  E-value: 1.59e-04
                         10        20
                 ....*....|....*....|..
gi 964111659 453 KKDAHAMILEFIRSRPPLRKAS 474
Cdd:cd22066    1 QKSPHEMILEFIRSRPPLKKVS 22
WH2_Spire cd22066
second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) ...
486-506 4.51e-03

second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeats of protein Spire; This family contains the Wiskott-Aldrich syndrome protein (WASP)-homology domain 2 (WH2) repeats 2-4 in human Spire (also called Spir), Drosophila Spire, and related proteins. Spire is an actin nucleator essential for establishing an actin mesh during oogenesis. This WH2-containing actin nucleator was first identified as a Drosophila maternal effect gene essential to establishment of both the anterior/posterior and dorsal/ventral body axes in developing oocytes and embryos. It has been found to sever filaments and sequester monomers in addition to nucleating new filaments; it remains associated with the slow-growing pointed end of the new filament. Spire is involved in intracellular vesicle transport along actin fibers, providing a novel link between actin cytoskeleton dynamics and intracellular transport. It is required for asymmetric spindle positioning and asymmetric cell division during oocyte meiosis. Spire contains four tandem WH2 domains. Several spire gene family members have been identified, including paralogs Spire-1 (Spir1) and Spire-2 (Spir2) in higher eukaryotes. Spire acts in the nucleus where, together with Spire-1 and Spire-2, it promotes assembly of nuclear actin filaments in response to DNA damage in order to facilitate movement of chromatin and repair factors after DNA damage. Spire-1 and Spire-2 encode a modified Fab1/YOTB/Vac1/EEA1 (FYVE)-type zinc finger membrane-binding domain at their C-termini that promiscuously interacts with negatively charged lipids and the interaction of these proteins with additional factors may provide the specificity for its targeting to the correct subpopulation of vesicles.


Pssm-ID: 409209  Cd Length: 22  Bit Score: 34.87  E-value: 4.51e-03
                         10        20
                 ....*....|....*....|.
gi 964111659 486 PSPREQLMESIRKGKELKQIT 506
Cdd:cd22066    2 KSPHEMILEFIRSRPPLKKVS 22
 
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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