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Conserved domains on  [gi|1020532312|ref|XP_016105915|]
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PREDICTED: protein spire homolog 1-like [Sinocyclocheilus grahami]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
36-228 8.92e-100

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: 309.24  E-value: 8.92e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312  36 LCLEEILTLYSQPINEEQAWAVCYQCCRWLTQKQRRKetgGSPPGRIAGPGDVRIRKDGTVKLYQQSSPDKHI----PPS 111
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGLRQPTRRR---KQKFRRIRGPSDILLHRDGTVTLRFEASSDGPPkallPAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 112 TSIEIIESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMADTETD--CPDEGYEATEEEDEGDEELTEVSNIRGYR 189
Cdd:pfam16474  78 SETQVIQSLGVAIYKALDYGLKESEERELSPPLEQLIDLMTNGDDEDGGqeTDDEGYEADEEEEEEEDEEGTISSVRTFR 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1020532312 190 DIISLCTSHLPGPSDARNHYQAVCRALYAETKELRTFLE 228
Cdd:pfam16474 158 DVLKLCASHLPNPSDAPNHYQAVCRALFAETLELSTFLE 196
FYVE_SPIR1 cd15767
FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is ...
730-864 1.08e-38

FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


:

Pssm-ID: 277306  Cd Length: 79  Bit Score: 138.11  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 730 LKKGKLCFSCRTKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPISSLGPsilpkkestasaatekpsstsshk 809
Cdd:cd15767     1 LKKGKLCFSCRSKRFSLFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGP------------------------ 56
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1020532312 810 rhslqrtmsrsskhaerssskdelelpeqftaDWSSMEVCVDCKKFINDIISNSR 864
Cdd:cd15767    57 --------------------------------DWSTMEVCVDCKKFISDIISSSR 79
FYVE_like_SF super family cl28890
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
561-611 1.77e-19

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


The actual alignment was detected with superfamily member cd15767:

Pssm-ID: 333710  Cd Length: 79  Bit Score: 83.42  E-value: 1.77e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1020532312 561 LKKGKLCFSCRTKKFSLFTWSYTCQF-----CLFVHSAMKLPSKPHASLPISSLGP 611
Cdd:cd15767     1 LKKGKLCFSCRSKRFSLFTWSYTCQFckrpvCSQCCKKMRLPSKPYSTLPIFSLGP 56
WH2_Spire_1-2_r1 cd22065
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
250-281 2.73e-17

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: 75.85  E-value: 2.73e-17
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1020532312 250 DLNELQNADWARFWVQVMRDLRHGVKLKKVQE 281
Cdd:cd22065     1 ELDELQNTDWARLWVQVMRELRNGVKLKKVQE 32
WH2_Spire1_r2-like cd22078
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
290-321 1.64e-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: 70.64  E-value: 1.64e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1020532312 290 EFQLTPYEMLMDDIRSKRYKLRKVMVNGNIPP 321
Cdd:cd22078     1 EYELTPYEMLMDDIRSKRYTLRKVMVNGDIPP 32
WH2_Spire1-2_r3 cd22186
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
324-346 5.12e-08

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: 49.26  E-value: 5.12e-08
                          10        20
                  ....*....|....*....|...
gi 1020532312 324 KKSAHEIILEFIRSRPPLNPVSA 346
Cdd:cd22186     1 KKSAHELILDFIRSRPPLNPVSA 23
WH2_Spire1_r4 cd22080
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
355-378 1.03e-07

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 1; This family contains the fourth 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 4 of 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.


:

Pssm-ID: 409223  Cd Length: 24  Bit Score: 48.35  E-value: 1.03e-07
                          10        20
                  ....*....|....*....|....
gi 1020532312 355 RPPSLHERILEGIRSERKLRPVSP 378
Cdd:cd22080     1 RPRSLHERILEEIKAERKLRPVSP 24
 
Name Accession Description Interval E-value
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
36-228 8.92e-100

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: 309.24  E-value: 8.92e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312  36 LCLEEILTLYSQPINEEQAWAVCYQCCRWLTQKQRRKetgGSPPGRIAGPGDVRIRKDGTVKLYQQSSPDKHI----PPS 111
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGLRQPTRRR---KQKFRRIRGPSDILLHRDGTVTLRFEASSDGPPkallPAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 112 TSIEIIESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMADTETD--CPDEGYEATEEEDEGDEELTEVSNIRGYR 189
Cdd:pfam16474  78 SETQVIQSLGVAIYKALDYGLKESEERELSPPLEQLIDLMTNGDDEDGGqeTDDEGYEADEEEEEEEDEEGTISSVRTFR 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1020532312 190 DIISLCTSHLPGPSDARNHYQAVCRALYAETKELRTFLE 228
Cdd:pfam16474 158 DVLKLCASHLPNPSDAPNHYQAVCRALFAETLELSTFLE 196
FYVE_SPIR1 cd15767
FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is ...
730-864 1.08e-38

FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277306  Cd Length: 79  Bit Score: 138.11  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 730 LKKGKLCFSCRTKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPISSLGPsilpkkestasaatekpsstsshk 809
Cdd:cd15767     1 LKKGKLCFSCRSKRFSLFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGP------------------------ 56
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1020532312 810 rhslqrtmsrsskhaerssskdelelpeqftaDWSSMEVCVDCKKFINDIISNSR 864
Cdd:cd15767    57 --------------------------------DWSTMEVCVDCKKFISDIISSSR 79
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
38-223 6.31e-38

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: 139.84  E-value: 6.31e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312   38 LEEILTLYSQPINEEQAWAVCYQCCRWLtqkqrRKETGGSPPGRIAGPGDVRIRKDGTVKLY--QQSSPDKHIPPSTSIE 115
Cdd:smart00750   3 LADILEVRGRPLNEEEIWAVCLQCLGAL-----RELHRQAKSGNILLTWDGLLKLDGSVAFKtpEQSRPDPYFMAPEVIQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312  116 I--------IESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMaDTETDCPDEGyeateeedegdeelteVSNIRG 187
Cdd:smart00750  78 GqsytekadIYSLGITLYEALDYELPYNEERELSAILEILLNGMPAD-DPRDRSNLEG----------------VSAARS 140
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1020532312  188 YRDIISLCTSHLPGPSDARNHYQAVCRALYAETKEL 223
Cdd:smart00750 141 FEDFMRLCASRLPQRREAANHYLAHCRALFAETLEL 176
FYVE_SPIR1 cd15767
FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is ...
561-611 1.77e-19

FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277306  Cd Length: 79  Bit Score: 83.42  E-value: 1.77e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1020532312 561 LKKGKLCFSCRTKKFSLFTWSYTCQF-----CLFVHSAMKLPSKPHASLPISSLGP 611
Cdd:cd15767     1 LKKGKLCFSCRSKRFSLFTWSYTCQFckrpvCSQCCKKMRLPSKPYSTLPIFSLGP 56
WH2_Spire_1-2_r1 cd22065
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
250-281 2.73e-17

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: 75.85  E-value: 2.73e-17
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1020532312 250 DLNELQNADWARFWVQVMRDLRHGVKLKKVQE 281
Cdd:cd22065     1 ELDELQNTDWARLWVQVMRELRNGVKLKKVQE 32
WH2_Spire1_r2-like cd22078
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
290-321 1.64e-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: 70.64  E-value: 1.64e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1020532312 290 EFQLTPYEMLMDDIRSKRYKLRKVMVNGNIPP 321
Cdd:cd22078     1 EYELTPYEMLMDDIRSKRYTLRKVMVNGDIPP 32
WH2_Spire1-2_r3 cd22186
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
324-346 5.12e-08

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: 49.26  E-value: 5.12e-08
                          10        20
                  ....*....|....*....|...
gi 1020532312 324 KKSAHEIILEFIRSRPPLNPVSA 346
Cdd:cd22186     1 KKSAHELILDFIRSRPPLNPVSA 23
WH2_Spire1_r4 cd22080
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
355-378 1.03e-07

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 1; This family contains the fourth 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 4 of 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.


Pssm-ID: 409223  Cd Length: 24  Bit Score: 48.35  E-value: 1.03e-07
                          10        20
                  ....*....|....*....|....
gi 1020532312 355 RPPSLHERILEGIRSERKLRPVSP 378
Cdd:cd22080     1 RPRSLHERILEEIKAERKLRPVSP 24
 
Name Accession Description Interval E-value
KIND pfam16474
Kinase non-catalytic C-lobe domain; The KIND domain (kinase non-catalytic C-lobe domain) ...
36-228 8.92e-100

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: 309.24  E-value: 8.92e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312  36 LCLEEILTLYSQPINEEQAWAVCYQCCRWLTQKQRRKetgGSPPGRIAGPGDVRIRKDGTVKLYQQSSPDKHI----PPS 111
Cdd:pfam16474   1 LSLEEILKSYEQPINEEQAWAVCYQCCRGLRQPTRRR---KQKFRRIRGPSDILLHRDGTVTLRFEASSDGPPkallPAR 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 112 TSIEIIESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMADTETD--CPDEGYEATEEEDEGDEELTEVSNIRGYR 189
Cdd:pfam16474  78 SETQVIQSLGVAIYKALDYGLKESEERELSPPLEQLIDLMTNGDDEDGGqeTDDEGYEADEEEEEEEDEEGTISSVRTFR 157
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1020532312 190 DIISLCTSHLPGPSDARNHYQAVCRALYAETKELRTFLE 228
Cdd:pfam16474 158 DVLKLCASHLPNPSDAPNHYQAVCRALFAETLELSTFLE 196
FYVE_SPIR1 cd15767
FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is ...
730-864 1.08e-38

FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277306  Cd Length: 79  Bit Score: 138.11  E-value: 1.08e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 730 LKKGKLCFSCRTKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPISSLGPsilpkkestasaatekpsstsshk 809
Cdd:cd15767     1 LKKGKLCFSCRSKRFSLFTWSYTCQFCKRPVCSQCCKKMRLPSKPYSTLPIFSLGP------------------------ 56
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1020532312 810 rhslqrtmsrsskhaerssskdelelpeqftaDWSSMEVCVDCKKFINDIISNSR 864
Cdd:cd15767    57 --------------------------------DWSTMEVCVDCKKFISDIISSSR 79
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
38-223 6.31e-38

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: 139.84  E-value: 6.31e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312   38 LEEILTLYSQPINEEQAWAVCYQCCRWLtqkqrRKETGGSPPGRIAGPGDVRIRKDGTVKLY--QQSSPDKHIPPSTSIE 115
Cdd:smart00750   3 LADILEVRGRPLNEEEIWAVCLQCLGAL-----RELHRQAKSGNILLTWDGLLKLDGSVAFKtpEQSRPDPYFMAPEVIQ 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312  116 I--------IESLGIMIYKALDYGLKEHEERELSPPLEQLIDLMTNMaDTETDCPDEGyeateeedegdeelteVSNIRG 187
Cdd:smart00750  78 GqsytekadIYSLGITLYEALDYELPYNEERELSAILEILLNGMPAD-DPRDRSNLEG----------------VSAARS 140
                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1020532312  188 YRDIISLCTSHLPGPSDARNHYQAVCRALYAETKEL 223
Cdd:smart00750 141 FEDFMRLCASRLPQRREAANHYLAHCRALFAETLEL 176
FYVE_SPIR2 cd15768
FYVE-related domain found in protein spire homolog 2 (Spire2) and similar proteins; Spire2 is ...
730-860 3.13e-20

FYVE-related domain found in protein spire homolog 2 (Spire2) and similar proteins; Spire2 is encoded by gene spir-2, which is expressed in the nervous system and highly expressed in the colonic epithelium. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire2 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277307  Cd Length: 112  Bit Score: 86.87  E-value: 3.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 730 LKKGKLCFSCRTKkFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPISSLGPSILPKKESTASAATEKPSSTSSHK 809
Cdd:cd15768     1 LKKGKICCCCRVK-FPLFSWPSNCLFCKRSVCSSCSMKMKMPSKKLAHIPVYTVGFESPPRSTSAKANARRWTDSLHGPS 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1020532312 810 RHSLqrtmsrsskhaerssskdELELPEQFTADWSSMEVCVDCKKFINDII 860
Cdd:cd15768    80 WRSV------------------EEEFPHIYAQGSVLKDVCSDCTGFVADVV 112
FYVE_SPIR1 cd15767
FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is ...
561-611 1.77e-19

FYVE-related domain found in protein spire homolog 1 (Spire1) and similar proteins; Spire1 is encoded by gene spir-1, which is primarily found to be expressed in the developing nervous system and in neuronal cells of the adult brain, as well as in the fetal liver and in the adult spleen. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire1 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277306  Cd Length: 79  Bit Score: 83.42  E-value: 1.77e-19
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1020532312 561 LKKGKLCFSCRTKKFSLFTWSYTCQF-----CLFVHSAMKLPSKPHASLPISSLGP 611
Cdd:cd15767     1 LKKGKLCFSCRSKRFSLFTWSYTCQFckrpvCSQCCKKMRLPSKPYSTLPIFSLGP 56
WH2_Spire_1-2_r1 cd22065
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
250-281 2.73e-17

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: 75.85  E-value: 2.73e-17
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1020532312 250 DLNELQNADWARFWVQVMRDLRHGVKLKKVQE 281
Cdd:cd22065     1 ELDELQNTDWARLWVQVMRELRNGVKLKKVQE 32
WH2_Spire1_r2-like cd22078
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
290-321 1.64e-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: 70.64  E-value: 1.64e-15
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1020532312 290 EFQLTPYEMLMDDIRSKRYKLRKVMVNGNIPP 321
Cdd:cd22078     1 EYELTPYEMLMDDIRSKRYTLRKVMVNGDIPP 32
FYVE_SPIR cd15748
FYVE-related domain found in Spir proteins, Spire1 and Spire2; Spir proteins were originally ...
732-766 4.80e-14

FYVE-related domain found in Spir proteins, Spire1 and Spire2; Spir proteins were originally discovered as the protein products of the Drosophila spire gene. They are Jun N-terminal kinase (JNK)-interacting proteins that have exclusively been identified in metazoans. They may play roles in membrane trafficking and cortical filament crosslinking. This family includes Spire1 and Spire2, which function as new essential factors in asymmetric division of oocytes. They mediate asymmetric spindle positioning by assembling a cytoplasmic actin network. They are also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, they cooperate synergistically with Fmn2 to assemble F-actin in oocytes. Both Spire1 and Spire2 contain an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. Their FYVE domains resemble FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically bind the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277287  Cd Length: 42  Bit Score: 66.97  E-value: 4.80e-14
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1020532312 732 KGKLCFSCRTKKFSLFTWSYTCQFCKRPVCSQCCK 766
Cdd:cd15748     1 KGKVCFCCKKKKFSFFTWPNTCKLCKRVVCSKCCR 35
WH2_Spire2_r2 cd22079
second tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
292-321 2.04e-12

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: 61.85  E-value: 2.04e-12
                          10        20        30
                  ....*....|....*....|....*....|
gi 1020532312 292 QLTPYEMLMDDIRSKRYKLRKVMVNGNIPP 321
Cdd:cd22079     1 QLTPFEMLMQDIRARKYKLRKVMVDGDIPP 30
FYVE_SPIR2 cd15768
FYVE-related domain found in protein spire homolog 2 (Spire2) and similar proteins; Spire2 is ...
561-640 5.89e-09

FYVE-related domain found in protein spire homolog 2 (Spire2) and similar proteins; Spire2 is encoded by gene spir-2, which is expressed in the nervous system and highly expressed in the colonic epithelium. It functions as a new essential factor in asymmetric division of oocytes. It mediates asymmetric spindle positioning by assembling a cytoplasmic actin network. It is also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, it cooperates synergistically with Fmn2 to assemble F-actin in oocytes. Spire2 contains an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. The FYVE domain resembles a FYVE-related domain that is structurally similar to the canonical FYVE domains but lacks the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically binds the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277307  Cd Length: 112  Bit Score: 54.52  E-value: 5.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1020532312 561 LKKGKLCFSCRTKkFSLFTWSYTCQFC-LFVHSA----MKLPSKPHASLPISSLGPSILPKKESTASAATEKPSSTSSHK 635
Cdd:cd15768     1 LKKGKICCCCRVK-FPLFSWPSNCLFCkRSVCSScsmkMKMPSKKLAHIPVYTVGFESPPRSTSAKANARRWTDSLHGPS 79

                  ....*
gi 1020532312 636 RHSLQ 640
Cdd:cd15768    80 WRSVE 84
WH2_Spire1-2_r3 cd22186
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
324-346 5.12e-08

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: 49.26  E-value: 5.12e-08
                          10        20
                  ....*....|....*....|...
gi 1020532312 324 KKSAHEIILEFIRSRPPLNPVSA 346
Cdd:cd22186     1 KKSAHELILDFIRSRPPLNPVSA 23
WH2_Spire1_r4 cd22080
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
355-378 1.03e-07

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 1; This family contains the fourth 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 4 of 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.


Pssm-ID: 409223  Cd Length: 24  Bit Score: 48.35  E-value: 1.03e-07
                          10        20
                  ....*....|....*....|....
gi 1020532312 355 RPPSLHERILEGIRSERKLRPVSP 378
Cdd:cd22080     1 RPRSLHERILEEIKAERKLRPVSP 24
FYVE_SPIR cd15748
FYVE-related domain found in Spir proteins, Spire1 and Spire2; Spir proteins were originally ...
563-587 1.06e-07

FYVE-related domain found in Spir proteins, Spire1 and Spire2; Spir proteins were originally discovered as the protein products of the Drosophila spire gene. They are Jun N-terminal kinase (JNK)-interacting proteins that have exclusively been identified in metazoans. They may play roles in membrane trafficking and cortical filament crosslinking. This family includes Spire1 and Spire2, which function as new essential factors in asymmetric division of oocytes. They mediate asymmetric spindle positioning by assembling a cytoplasmic actin network. They are also required for polar body extrusion by promoting assembly of the cleavage furrow. Moreover, they cooperate synergistically with Fmn2 to assemble F-actin in oocytes. Both Spire1 and Spire2 contain an N-terminal protein-interaction KIND domain, WH2 actin-binding domains, a Rab GTPase-interaction Spir-box, and a C-terminal FYVE membrane-binding domain. Their FYVE domains resemble FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a binding pocket that specifically bind the phospholipid phosphatidylinositol 3-phosphate (PtdIns3P or PI3P).


Pssm-ID: 277287  Cd Length: 42  Bit Score: 48.87  E-value: 1.06e-07
                          10        20
                  ....*....|....*....|....*
gi 1020532312 563 KGKLCFSCRTKKFSLFTWSYTCQFC 587
Cdd:cd15748     1 KGKVCFCCKKKKFSFFTWPNTCKLC 25
WH2_DmSpire_r1-like cd22067
first tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
249-275 1.16e-05

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: 42.64  E-value: 1.16e-05
                          10        20
                  ....*....|....*....|....*..
gi 1020532312 249 RDLNELQNADWARFWVQVMRDLRHGVK 275
Cdd:cd22067     1 QELAKLGFNDWARFWVQVIDELRRGVR 27
FYVE_like_SF cd00065
FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger ...
736-780 2.41e-05

FYVE domain like superfamily; FYVE domain is a 60-80 residue double zinc finger motif-containing module named after the four proteins, Fab1, YOTB, Vac1, and EEA1. The canonical FYVE domains are distinguished from other zinc fingers by three signature sequences: an N-terminal WxxD motif (x for any residue), the central basic R(R/K)HHCRxCG patch, and a C-terminal RVC motif, which form a compact phosphatidylinositol 3-phosphate (PtdIns3P, also termed PI3P)-binding site. They are found in many membrane trafficking regulators, including EEA1, Hrs, Vac1p, Vps27p, and FENS-1, which locate to early endosomes, specifically bind PtdIns3P, and play important roles in vesicular traffic and in signal transduction. Some proteins, such as rabphilin-3A and alpha-Rab3-interacting molecules (RIMs), are also involved in membrane trafficking and bind to members of the Rab subfamily of GTP hydrolases. However, they contain FYVE-related domains that are structurally similar to the canonical FYVE domains but lack the three signature sequences. At this point, they may not bind to phosphoinositides. In addition, this superfamily also contains the third group of proteins, caspase-associated ring proteins CARP1 and CARP2. They do not localize to membranes in the cell and are involved in the negative regulation of apoptosis, specifically targeting two initiator caspases, caspase 8 and caspase 10, which are distinguished from other FYVE-type proteins. Moreover, these proteins have an altered sequence in the basic ligand binding patch and lack the WxxD motif that is conserved only in phosphoinositide binding FYVE domains. Thus they constitute a family of unique FYVE-type domains called FYVE-like domains. The FYVE domain is structurally similar to the RING domain and the PHD finger. This superfamily also includes ADDz zinc finger domain, which is a PHD-like zinc finger motif that contains two parts, a C2-C2 and a PHD-like zinc finger.


Pssm-ID: 277249 [Multi-domain]  Cd Length: 52  Bit Score: 42.52  E-value: 2.41e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1020532312 736 CFSCRtKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKPHASLPI 780
Cdd:cd00065     2 CMLCG-KKFSLFRRRHHCRRCGRVFCSKCSSKKLPLPSFGSGKPV 45
WH2_DmSpire_r3-like cd22068
third tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat found in ...
324-348 4.15e-05

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: 41.24  E-value: 4.15e-05
                          10        20
                  ....*....|....*....|....*
gi 1020532312 324 KKSAHEIILEFIRSRPPLNPVSARK 348
Cdd:cd22068     2 KKDAHAMILEFIRSRPPLKKASDRQ 26
WH2_Spire cd22066
second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) ...
324-345 9.63e-05

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: 39.88  E-value: 9.63e-05
                          10        20
                  ....*....|....*....|..
gi 1020532312 324 KKSAHEIILEFIRSRPPLNPVS 345
Cdd:cd22066     1 QKSPHEMILEFIRSRPPLKKVS 22
WH2_Spire cd22066
second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) ...
292-314 2.01e-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: 36.41  E-value: 2.01e-03
                          10        20
                  ....*....|....*....|...
gi 1020532312 292 QLTPYEMLMDDIRsKRYKLRKVM 314
Cdd:cd22066     1 QKSPHEMILEFIR-SRPPLKKVS 22
WH2_Spire cd22066
second, third, and fourth, tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) ...
356-377 2.98e-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: 35.64  E-value: 2.98e-03
                          10        20
                  ....*....|....*....|..
gi 1020532312 356 PPSLHERILEGIRSERKLRPVS 377
Cdd:cd22066     1 QKSPHEMILEFIRSRPPLKKVS 22
WH2_Spire2_r4 cd22081
fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein ...
358-376 8.45e-03

fourth tandem Wiskott-Aldrich Syndrome Homology (WASP) region 2 (WH2 motif) repeat of protein Spire homolog 2; This family contains the fourth 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 4 of 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: 409224  Cd Length: 22  Bit Score: 34.56  E-value: 8.45e-03
                          10
                  ....*....|....*....
gi 1020532312 358 SLHERILEGIRSERKLRPV 376
Cdd:cd22081     3 SLHEKILEEIKQERKLRPV 21
FYVE_RUFY4 cd15745
FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar ...
735-774 9.61e-03

FYVE-related domain found in RUN and FYVE domain-containing protein 4 (RUFY4) and similar proteins; RUFY4 belongs to the FUFY protein family which is characterized by the presence of an N-terminal RUN domain and a C-terminal FYVE domain. The FYVE domain of RUFY4 resembles the FYVE-related domain as it lacks the WxxD motif (x for any residue). The biological function of RUFY4 still remains unclear.


Pssm-ID: 277284 [Multi-domain]  Cd Length: 52  Bit Score: 35.17  E-value: 9.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1020532312 735 LCFSCRtKKFSLFTWSYTCQFCKRPVCSQCCKKMKLPSKP 774
Cdd:cd15745     1 ACAICA-KAFSLFRRKYVCRLCGGVVCHSCSSEDLVLSVP 39
 
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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