NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|357933612|ref|NP_001239544|]
View 

alpha-(1,6)-fucosyltransferase isoform 2 [Mus musculus]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
FUT8_N_cat pfam19745
Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal ...
1-335 0e+00

Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal coiled-coil and the catalytic domains of the Alpha-(1,6)-fucosyltransferase (FUT8), an enzyme that catalyzes the transfer of a fucose residue in alpha 1-6 linkage to the N-Acetylglucosamine (GlcNAc) residue in N-glycans. The catalytic domain comprises two structures, an open sheet alpha/beta structure, which contains five helices and three beta- strands at the N-terminal, and a Rossmann fold that contains five helices and five beta-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases.


:

Pssm-ID: 466170 [Multi-domain]  Cd Length: 431  Bit Score: 689.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612    1 MTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLIL 80
Cdd:pfam19745  98 IADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQLHHVTYCFIVAYATNRTLIL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612   81 ESQNWRYATGGWETVFRPVSETCTDRSGLSTGHWSGEvNDKNIQVVELPIVDSLHPRPPYLPLAVPEDLADRLLRVHGDP 160
Cdd:pfam19745 178 DSKGWRYSKGGWESVFKPLSDTCTERSGAGASPWPGE-ENSDAQVVELPIVDSLNPRPPYLPLAIPADLAPRLLKLHGNP 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  161 AVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVDKKR 240
Cdd:pfam19745 257 PVWWVGQFLKYLMRPQASTQKFLEEAIEKLGFKKPIVGVHVRRTDKVGTEAAFHSIEEYMVWVEEYFQQLERRTRVDKRR 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  241 VYLATDDPTLLKEAKTKYSNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLH 320
Cdd:pfam19745 337 VYLATDDPKVIDEAKTKYPNYEVIGDPKIAKSAGLSSRYTDSSLRGIILDIHLLSLSDYLVCTFSSQVCRVAYELMQTRY 416
                         330
                  ....*....|....*
gi 357933612  321 PDASANFHSLDDIYY 335
Cdd:pfam19745 417 PDASDRFHSLDDIYY 431
SH3_Fut8 cd11792
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1, ...
343-397 5.26e-31

Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype. Fut8 is also implicated to play roles in aging and cancer metastasis. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212726  Cd Length: 55  Bit Score: 112.69  E-value: 5.26e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 357933612 343 NQIAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPSYKVRE 397
Cdd:cd11792    1 NQVAIYPHKPRNHDEIELRVGDIIGVAGNHWDGYSKGRNRRTGKTGLYPSYKVKD 55
 
Name Accession Description Interval E-value
FUT8_N_cat pfam19745
Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal ...
1-335 0e+00

Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal coiled-coil and the catalytic domains of the Alpha-(1,6)-fucosyltransferase (FUT8), an enzyme that catalyzes the transfer of a fucose residue in alpha 1-6 linkage to the N-Acetylglucosamine (GlcNAc) residue in N-glycans. The catalytic domain comprises two structures, an open sheet alpha/beta structure, which contains five helices and three beta- strands at the N-terminal, and a Rossmann fold that contains five helices and five beta-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases.


Pssm-ID: 466170 [Multi-domain]  Cd Length: 431  Bit Score: 689.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612    1 MTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLIL 80
Cdd:pfam19745  98 IADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQLHHVTYCFIVAYATNRTLIL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612   81 ESQNWRYATGGWETVFRPVSETCTDRSGLSTGHWSGEvNDKNIQVVELPIVDSLHPRPPYLPLAVPEDLADRLLRVHGDP 160
Cdd:pfam19745 178 DSKGWRYSKGGWESVFKPLSDTCTERSGAGASPWPGE-ENSDAQVVELPIVDSLNPRPPYLPLAIPADLAPRLLKLHGNP 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  161 AVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVDKKR 240
Cdd:pfam19745 257 PVWWVGQFLKYLMRPQASTQKFLEEAIEKLGFKKPIVGVHVRRTDKVGTEAAFHSIEEYMVWVEEYFQQLERRTRVDKRR 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  241 VYLATDDPTLLKEAKTKYSNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLH 320
Cdd:pfam19745 337 VYLATDDPKVIDEAKTKYPNYEVIGDPKIAKSAGLSSRYTDSSLRGIILDIHLLSLSDYLVCTFSSQVCRVAYELMQTRY 416
                         330
                  ....*....|....*
gi 357933612  321 PDASANFHSLDDIYY 335
Cdd:pfam19745 417 PDASDRFHSLDDIYY 431
Fut8_like cd11300
Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety ...
11-336 0e+00

Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety from GDP-fucose to the reducing terminal N-acetylglucosamine of the core structure of Asn-linked oligosaccharides, in a process termed core fucosylation. Core fucosylation is essential for the function of growth factor receptors. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


Pssm-ID: 211386 [Multi-domain]  Cd Length: 328  Bit Score: 587.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  11 DGAGDWREKEAKDLTELVQRRITYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATG 90
Cdd:cd11300    1 DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLILDSKGWRYSPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  91 GWETVFRPVSETCTDRSGLSTGHWSGEVNDKNIQVVELPIVDSLHPRPPYLPLAVPEDLADRLLRVHGDPAVWWVSQFVK 170
Cdd:cd11300   81 GWEKVFLPLSETCTDRSGDNTAVWWWEPTNSDVQVVKLPIIDSLHSRPPFLPLAVPEDLAERLERLHGDPRVWWIGQLLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 171 YLIRPQPWLEKEIEEATKKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQ--VDKKRVYLATDDP 248
Cdd:cd11300  161 YLMRPQPWLQDEIDEAKKELGFKHPIVGVHIRRTDKLGTEAAFHSLEEYMEHVEEWYDKYELRGPseKVKRRVYLATDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 249 TLLKEAKTKYSNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFH 328
Cdd:cd11300  241 SVFDEAKNKYPNYFFIGDPGISKSASLSTRYSDSSLKGIIIDIHLLSECDYLVCTFSSQVCRLAYELMQTRHPDASDRFH 320

                 ....*...
gi 357933612 329 SLDDIYYF 336
Cdd:cd11300  321 SLDDIYYY 328
SH3_Fut8 cd11792
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1, ...
343-397 5.26e-31

Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype. Fut8 is also implicated to play roles in aging and cancer metastasis. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212726  Cd Length: 55  Bit Score: 112.69  E-value: 5.26e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 357933612 343 NQIAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPSYKVRE 397
Cdd:cd11792    1 NQVAIYPHKPRNHDEIELRVGDIIGVAGNHWDGYSKGRNRRTGKTGLYPSYKVKD 55
SH3_9 pfam14604
Variant SH3 domain;
346-396 5.44e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 63.02  E-value: 5.44e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 357933612  346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRklGKTGLYPSYKVR 396
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIEESEDGWWEGINT--GRTGLVPANYVE 49
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
345-396 1.11e-07

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


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 48.30  E-value: 1.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 357933612   345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKlGKTGLYPSYKVR 396
Cdd:smart00326   6 RALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLGR-GKEGLFPSNYVE 56
 
Name Accession Description Interval E-value
FUT8_N_cat pfam19745
Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal ...
1-335 0e+00

Alpha-(1,6)-fucosyltransferase N- and catalytic domains; This entry represents the N-terminal coiled-coil and the catalytic domains of the Alpha-(1,6)-fucosyltransferase (FUT8), an enzyme that catalyzes the transfer of a fucose residue in alpha 1-6 linkage to the N-Acetylglucosamine (GlcNAc) residue in N-glycans. The catalytic domain comprises two structures, an open sheet alpha/beta structure, which contains five helices and three beta- strands at the N-terminal, and a Rossmann fold that contains five helices and five beta-strands at the C-terminal. The latter is conserved among the alpha1,2-, alpha1,6-, and protein O-fucosyltransferases and is similar to GT-B group glycosyltransferases.


Pssm-ID: 466170 [Multi-domain]  Cd Length: 431  Bit Score: 689.84  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612    1 MTDLYYLSQTDGAGDWREKEAKDLTELVQRRITYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLIL 80
Cdd:pfam19745  98 IADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQLHHVTYCFIVAYATNRTLIL 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612   81 ESQNWRYATGGWETVFRPVSETCTDRSGLSTGHWSGEvNDKNIQVVELPIVDSLHPRPPYLPLAVPEDLADRLLRVHGDP 160
Cdd:pfam19745 178 DSKGWRYSKGGWESVFKPLSDTCTERSGAGASPWPGE-ENSDAQVVELPIVDSLNPRPPYLPLAIPADLAPRLLKLHGNP 256
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  161 AVWWVSQFVKYLIRPQPWLEKEIEEATKKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQVDKKR 240
Cdd:pfam19745 257 PVWWVGQFLKYLMRPQASTQKFLEEAIEKLGFKKPIVGVHVRRTDKVGTEAAFHSIEEYMVWVEEYFQQLERRTRVDKRR 336
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  241 VYLATDDPTLLKEAKTKYSNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLH 320
Cdd:pfam19745 337 VYLATDDPKVIDEAKTKYPNYEVIGDPKIAKSAGLSSRYTDSSLRGIILDIHLLSLSDYLVCTFSSQVCRVAYELMQTRY 416
                         330
                  ....*....|....*
gi 357933612  321 PDASANFHSLDDIYY 335
Cdd:pfam19745 417 PDASDRFHSLDDIYY 431
Fut8_like cd11300
Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety ...
11-336 0e+00

Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety from GDP-fucose to the reducing terminal N-acetylglucosamine of the core structure of Asn-linked oligosaccharides, in a process termed core fucosylation. Core fucosylation is essential for the function of growth factor receptors. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


Pssm-ID: 211386 [Multi-domain]  Cd Length: 328  Bit Score: 587.29  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  11 DGAGDWREKEAKDLTELVQRRITYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATG 90
Cdd:cd11300    1 DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLILDSKGWRYSPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612  91 GWETVFRPVSETCTDRSGLSTGHWSGEVNDKNIQVVELPIVDSLHPRPPYLPLAVPEDLADRLLRVHGDPAVWWVSQFVK 170
Cdd:cd11300   81 GWEKVFLPLSETCTDRSGDNTAVWWWEPTNSDVQVVKLPIIDSLHSRPPFLPLAVPEDLAERLERLHGDPRVWWIGQLLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 171 YLIRPQPWLEKEIEEATKKLGFKHPVIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQLLARRMQ--VDKKRVYLATDDP 248
Cdd:cd11300  161 YLMRPQPWLQDEIDEAKKELGFKHPIVGVHIRRTDKLGTEAAFHSLEEYMEHVEEWYDKYELRGPseKVKRRVYLATDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 249 TLLKEAKTKYSNYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQADFLVCTFSSQVCRVAYEIMQTLHPDASANFH 328
Cdd:cd11300  241 SVFDEAKNKYPNYFFIGDPGISKSASLSTRYSDSSLKGIIIDIHLLSECDYLVCTFSSQVCRLAYELMQTRHPDASDRFH 320

                 ....*...
gi 357933612 329 SLDDIYYF 336
Cdd:cd11300  321 SLDDIYYY 328
SH3_Fut8 cd11792
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1, ...
343-397 5.26e-31

Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1,6-linkage of a fucose residue from a donor substrate to N-linked oligosaccharides on glycoproteins in a process called core fucosylation, which is crucial for growth factor receptor-mediated biological functions. Fut8-deficient mice show severe growth retardation, early death, and a pulmonary emphysema-like phenotype. Fut8 is also implicated to play roles in aging and cancer metastasis. It contains an N-terminal coiled-coil domain, a catalytic domain, and a C-terminal SH3 domain. The SH3 domain of Fut8 is located in the lumen and its role in glycosyl transfer is unclear. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212726  Cd Length: 55  Bit Score: 112.69  E-value: 5.26e-31
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 357933612 343 NQIAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPSYKVRE 397
Cdd:cd11792    1 NQVAIYPHKPRNHDEIELRVGDIIGVAGNHWDGYSKGRNRRTGKTGLYPSYKVKD 55
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
162-310 3.01e-15

GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


Pssm-ID: 211383  Cd Length: 206  Bit Score: 73.99  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 162 VWWVSQFVKYLIRPqPWLEKEIEEATKKLGFK--HPVIGVHVRRTDKVG------------TEAAFHPIEEYMVHVEEHF 227
Cdd:cd11296   39 ACPIRLVGKHLRFS-PEIRKLADRFVRKLLGLpgGPYLAVHLRRGDFEVecchlakwmgeyLEECLLSAEEIAEKIKELM 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 228 QLlarrmqVDKKRVYLATDDPT---LLKEAKTKYSNYEFISDNSISWSAGLHNRYteNSLRGVILDIHFLSQADFLVC-- 302
Cdd:cd11296  118 AE------RKLKVVYVATDEADreeLREELRKAGIRVVTKDDLLEDAELLELEKL--DNYLLSLVDQEICSRADVFIGtg 189
                        170
                 ....*....|
gi 357933612 303 --TFSSQVCR 310
Cdd:cd11296  190 fsTFSSNVAL 199
SH3_9 pfam14604
Variant SH3 domain;
346-396 5.44e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 63.02  E-value: 5.44e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 357933612  346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRklGKTGLYPSYKVR 396
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIEESEDGWWEGINT--GRTGLVPANYVE 49
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
166-312 3.32e-09

Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1,6-fucosyltransferase involved in the biosynthesis of the nodulation factor, a lipo-chitooligosaccharide formed by three-to-six beta-1,4-linked N-acetyl-d-glucosamine (GlcNAc) residues and a fatty acid acyl group attached to the nitrogen atom at the non-reducing end. NodZ transfers L-fucose from the GDP-beta-L-fucose donor to the reducing residue of the chitin oligosaccharide backbone, before the attachment of a fatty acid group. O-fucosyltransferase-like proteins are GDP-fucose dependent enzymes with similarities to the family 1 glycosyltransferases (GT1). They are soluble ER proteins that may be proteolytically cleaved from a membrane-associated preprotein, and are involved in the O-fucosylation of protein substrates, the core fucosylation of growth factor receptors, and other processes.


Pssm-ID: 211389 [Multi-domain]  Cd Length: 287  Bit Score: 57.38  E-value: 3.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 166 SQFVKYLIRPQPWLEKEIEEATKKLgFKHPVIGVHVRRTDKvgtEAAFHPIEEYMVHVEEhfQLLARRMQVDKKRVYLAT 245
Cdd:cd11548  138 KCYLYRLFTPKQEVRAAVRKLYAKL-FGRPTIGVHIRTTDH---KDSLFIKLSPLHRVVD--ALRKKVALHKDATIFLAT 211
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 357933612 246 DDPTLLKEAKTKYSNYEFISDnsisWSAGLHNRYTENSLRGV---ILDIHFLSQADFLVCTFSSQVCRVA 312
Cdd:cd11548  212 DSAEVKDELKRLFPDVVVTPK----EFPPHGERSASDGLEGAedaLIDMYLLARCDHLIGSRFSTFSRMA 277
SH3_SH3RF2_3 cd11784
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ...
345-395 1.87e-08

Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called POSHER (POSH-eliminating RING protein) or HEPP1 (heart protein phosphatase 1-binding protein). It acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation of SH3RF1 (or POSH), a scaffold protein that is required for pro-apoptotic JNK activation. It may also play a role in cardiac functions together with protein phosphatase 1. SH3RF2 contains an N-terminal RING finger domain and three SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF2. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212718  Cd Length: 55  Bit Score: 50.55  E-value: 1.87e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357933612 345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPSYKV 395
Cdd:cd11784    3 VALHSYSAHRPEELELQKGEGVRVLGKFQEGWLRGLSLVTGRVGIFPSNYV 53
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
345-396 1.11e-07

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


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 48.30  E-value: 1.11e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 357933612   345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKlGKTGLYPSYKVR 396
Cdd:smart00326   6 RALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLGR-GKEGLFPSNYVE 56
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
345-392 1.99e-06

Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction domains that bind proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. Thus, they are referred to as proline-recognition domains (PRDs). SH3 domains are less selective and show more diverse specificity compared to other PRDs. They have been shown to bind peptide sequences that lack the PxxP motif; examples include the PxxDY motif of Eps8 and the RKxxYxxY sequence in SKAP55. SH3 domain containing proteins play versatile and diverse roles in the cell, including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies, among others. Many members of this superfamily are adaptor proteins that associate with a number of protein partners, facilitating complex formation and signal transduction.


Pssm-ID: 212690 [Multi-domain]  Cd Length: 51  Bit Score: 44.38  E-value: 1.99e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 357933612 345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKlGKTGLYPS 392
Cdd:cd00174    3 RALYDYEAQDDDELSFKKGDIITVLEKDDDGWWEGELNG-GREGLFPA 49
SH3_SH3RF_C cd11785
C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), ...
346-392 4.60e-06

C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the fourth SH3 domain, located at the C-terminus of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212719  Cd Length: 55  Bit Score: 43.61  E-value: 4.60e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPS 392
Cdd:cd11785    4 VIVPYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRTGKTGLFPG 50
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
345-391 1.77e-05

Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and similar domains; SH3RF1 (or POSH) and SH3RF3 (or POSH2) are scaffold proteins that function as E3 ubiquitin-protein ligases. They contain an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle of SH3RF1 and SH3RF3, and similar domains. SH3RF1 plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF3 interacts with p21-activated kinase 2 (PAK2) and GTP-loaded Rac1. It may play a role in regulating JNK mediated apoptosis in certain conditions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212717 [Multi-domain]  Cd Length: 55  Bit Score: 42.00  E-value: 1.77e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 357933612 345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYP 391
Cdd:cd11783    3 VALYPYKPQKPDELELRKGEMYTVTEKCQDGWFKGTSLRTGQSGVFP 49
SH3_SH3RF1_3 cd11926
Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ...
345-391 3.69e-05

Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ligase; SH3RF1 is also called POSH (Plenty of SH3s) or SH3MD2 (SH3 multiple domains protein 2). It is a scaffold protein that acts as an E3 ubiquitin-protein ligase. It plays a role in calcium homeostasis through the control of the ubiquitin domain protein Herp. It may also have a role in regulating death receptor mediated and JNK mediated apoptosis. SH3RF1 also enhances the ubiquitination of ROMK1 potassium channel resulting in its increased endocytosis. It contains an N-terminal RING finger domain and four SH3 domains. This model represents the third SH3 domain, located in the middle, of SH3RF1. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212859 [Multi-domain]  Cd Length: 55  Bit Score: 41.11  E-value: 3.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 357933612 345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYP 391
Cdd:cd11926    3 VAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFP 49
SH3_UBASH3 cd11791
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called ...
346-391 5.08e-05

Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called TULA (T cell Ubiquitin LigAnd) family of proteins; UBASH3 or TULA proteins are also referred to as Suppressor of T cell receptor Signaling (STS) proteins. They contain an N-terminal UBA domain, a central SH3 domain, and a C-terminal histidine phosphatase domain. They bind c-Cbl through the SH3 domain and to ubiquitin via UBA. In some vertebrates, there are two TULA family proteins, called UBASH3A (also called TULA or STS-2) and UBASH3B (also called TULA-2 or STS-1), which show partly overlapping as well as distinct functions. UBASH3B is widely expressed while UBASH3A is only found in lymphoid cells. UBASH3A facilitates apoptosis induced in T cells through its interaction with the apoptosis-inducing factor AIF. UBASH3B is an active phosphatase while UBASH3A is not. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212725 [Multi-domain]  Cd Length: 59  Bit Score: 40.75  E-value: 5.08e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVA----GNHWDGYSKGINRKLGKTGLYP 391
Cdd:cd11791    4 VLYPYTPQEEDELELVPGDYIYVSpeelDSSSDGWVEGTSWLTGCSGLLP 53
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
345-392 6.16e-05

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


Pssm-ID: 394975 [Multi-domain]  Cd Length: 47  Bit Score: 40.26  E-value: 6.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 357933612  345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINrKLGKTGLYPS 392
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRN-KGGKEGLIPS 47
SH3_Shank cd11832
Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins; Shank ...
345-393 1.61e-04

Src homology 3 domain of SH3 and multiple ankyrin repeat domains (Shank) proteins; Shank proteins carry scaffolding functions through multiple sites of protein-protein interaction in its domain architecture, including ankyrin (ANK) repeats, a long proline rich region, as well as SH3, PDZ, and SAM domains. They bind a variety of membrane and cytosolic proteins, and exist in alternatively spliced isoforms. They are highly enriched in postsynaptic density (PSD) where they interact with the cytoskeleton and with postsynaptic membrane receptors including NMDA and glutamate receptors. They are crucial in the construction and organization of the PSD and dendritic spines of excitatory synapses. There are three members of this family (Shank1, Shank2, Shank3) which show distinct and cell-type specific patterns of expression. Shank1 is brain-specific; Shank2 is found in neurons, glia, endocrine cells, liver, and kidney; Shank3 is widely expressed. The SH3 domain of Shank binds GRIP, a scaffold protein that binds AMPA receptors and Eph receptors/ligands. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212766  Cd Length: 50  Bit Score: 38.96  E-value: 1.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 357933612 345 IAVYPHKPRTEEEIPMEPGDIIGV----AGNHWDGYSKginrklGKTGLYPSY 393
Cdd:cd11832    3 IAVKSYSPQEEGEISLHKGDRVKVlsigEGGFWEGSVR------GRTGWFPSD 49
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
346-397 2.50e-04

Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called SH3 domain-containing kinase-binding protein 1 (SH3KBP1) or CD2-binding protein 3 (CD2BP3) or Ruk, is an adaptor protein that is involved in the downregulation of receptor tyrosine kinases by facilitating endocytosis through interaction with endophilin-associated ubiquitin ligase Cbl proteins. It is also important in many other cellular processes including vesicle-mediated transport, cytoskeletal remodelling, apoptosis, cell adhesion and migration, and viral infection, among others. CIN85 exists as multiple variants from alternative splicing; the main variant contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CIN85. SH3B has been shown to bind Cbl proline-rich peptides and ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212988 [Multi-domain]  Cd Length: 53  Bit Score: 38.82  E-value: 2.50e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRklGKTGLYPSYKVRE 397
Cdd:cd12055    4 VAFSYLPQNEDELELKVGDIIEVVGEVEEGWWEGVLN--GKTGMFPSNFIKE 53
SH3_Vinexin_3 cd11918
Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain ...
346-391 3.92e-04

Third (or C-terminal) Src Homology 3 domain of Vinexin, also called Sorbin and SH3 domain containing 3 (Sorbs3); Vinexin is also called Sorbs3, SH3P3, and SH3-containing adapter molecule 1 (SCAM-1). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. Vinexin was first identified as a vinculin binding protein; it is co-localized with vinculin at cell-ECM and cell-cell adhesion sites. There are several splice variants of vinexin: alpha, which contains the SoHo and three SH3 domains and displays tissue-specific expression; and beta, which contains only the three SH3 domains and is widely expressed. Vinexin alpha stimulates the accumulation of F-actin at focal contact sites. Vinexin also promotes keratinocyte migration and wound healing. The SH3 domains of vinexin have been reported to bind a number of ligands including vinculin, WAVE2, DLG5, Abl, and Cbl. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212851 [Multi-domain]  Cd Length: 58  Bit Score: 38.40  E-value: 3.92e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYP 391
Cdd:cd11918    6 AVYQYRPQNEDELELREGDRVDVMQQCDDGWFVGVSRRTQKFGTFP 51
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
346-397 6.51e-04

Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in endothelial and epithelial cells and is involved in the regulation, trafficking and targeting of endothelial NOS (eNOS). It facilitates the endocytosis of eNOS by coordinating the functions of dynamin and the Wiskott-Aldrich syndrome protein (WASP). Increased expression of Nostrin may be correlated to preeclampsia. Nostrin contains an N-terminal F-BAR domain and a C-terminal SH3 domain. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212757 [Multi-domain]  Cd Length: 53  Bit Score: 37.32  E-value: 6.51e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRklGKTGLYPSYKVRE 397
Cdd:cd11823    4 ALYSYTANREDELSLQPGDIIEVHEKQDDGWWLGELN--GKKGIFPATYVEE 53
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
346-391 1.07e-03

First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212770 [Multi-domain]  Cd Length: 55  Bit Score: 36.95  E-value: 1.07e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNH-----WDGYSKGinrklGKTGLYP 391
Cdd:cd11836    4 ALYAFEARNPDEISFQPGDIIQVDESQvaepgWLAGELK-----GKTGWFP 49
SH3_Intersectin1_1 cd11987
First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
346-392 1.09e-03

First Src homology 3 domain (or SH3A) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor protein that functions in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. It plays a role in clathrin-coated pit (CCP) formation. It binds to many proteins through its multidomain structure and facilitate the assembly of multimeric complexes. ITSN1 localizes in membranous organelles, CCPs, the Golgi complex, and may be involved in the cell membrane trafficking system. It exists in alternatively spliced short and long isoforms. The short isoform contains two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoform, in addition, contains RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. The first SH3 domain (or SH3A) of ITSN1 has been shown to bind many proteins including Sos1, dynamin1/2, CIN85, c-Cbl, PI3K-C2, SHIP2, N-WASP, and CdGAP, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212920 [Multi-domain]  Cd Length: 55  Bit Score: 36.90  E-value: 1.09e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHwDGYSKGINRKL-GKTGLYPS 392
Cdd:cd11987    4 ALYPFEARSHDEITIQPGDIVMVDESQ-TGEPGWLGGELkGKTGWFPA 50
SH3_CD2AP_2 cd12054
Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ...
347-397 1.32e-03

Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ligand with Multiple SH3 domains) or METS1 (Mesenchyme-to-Epithelium Transition protein with SH3 domains), is a cytosolic adaptor protein that plays a role in regulating the cytoskeleton. It is critical in cell-to-cell union necessary for kidney function. It also stabilizes the contact between a T cell and antigen-presenting cells. It is primarily expressed in podocytes at the cytoplasmic face of the slit diaphragm and serves as a linker anchoring podocin and nephrin to the actin cytoskeleton. CD2AP contains three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP to bind various protein partners and assemble complexes that have been implicated in many different functions. This alignment model represents the second SH3 domain (SH3B) of CD2AP. SH3B binds to c-Cbl in a site (TPSSRPLR is the core binding motif) distinct from the c-Cbl/SH3A binding site. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212987 [Multi-domain]  Cd Length: 55  Bit Score: 36.87  E-value: 1.32e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357933612 347 VYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRklGKTGLYPSYKVRE 397
Cdd:cd12054    6 LFEYVPQNEDELELKVGDIIDINEEVEEGWWSGTLN--GKSGLFPSNFVKE 54
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
346-397 1.86e-03

Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This subfamily is composed of the second SH3 domain (SH3B) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3B of both proteins have been shown to bind to Cbl. In the case of CD2AP, its SH3B binds to Cbl at a site distinct from the c-Cbl/SH3A binding site. The CIN85 SH3B also binds ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212807 [Multi-domain]  Cd Length: 53  Bit Score: 36.16  E-value: 1.86e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGinRKLGKTGLYPSYKVRE 397
Cdd:cd11874    4 VLFSYTPQNEDELELKVGDTIEVLGEVEEGWWEG--KLNGKVGVFPSNFVKE 53
SH3_Sorbs1_3 cd11916
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), ...
346-396 2.70e-03

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 1 (Sorbs1), also called ponsin; Sorbs1 is also called ponsin, SH3P12, or CAP (c-Cbl associated protein). It is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It binds Cbl and plays a major role in regulating the insulin signaling pathway by enhancing insulin-induced phosphorylation of Cbl. Sorbs1, like vinexin, localizes at cell-ECM and cell-cell adhesion sites where it binds vinculin, paxillin, and afadin. It may function in the control of cell motility. Other interaction partners of Sorbs1 include c-Abl, Sos, flotillin, Grb4, ataxin-7, filamin C, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212849 [Multi-domain]  Cd Length: 59  Bit Score: 36.12  E-value: 2.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPSYKVR 396
Cdd:cd11916    6 ALYSYAPQNDDELELRDGDIVDVMEKCDDGWFVGTSRRTKQFGTFPGNYVK 56
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
346-393 3.15e-03

Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific Angiogenesis Inhibitor 1-Associated Protein 2 (BAIAP2)-Like proteins, and similar proteins; Proteins in this family include IRSp53, BAIAP2L1, BAIAP2L2, and similar proteins. They all contain an Inverse-Bin/Amphiphysin/Rvs (I-BAR) or IMD domain in addition to the SH3 domain. IRSp53, also known as BAIAP2, is a scaffolding protein that takes part in many signaling pathways including Cdc42-induced filopodia formation, Rac-mediated lamellipodia extension, and spine morphogenesis. IRSp53 exists as multiple splicing variants that differ mainly at the C-termini. BAIAP2L1, also called IRTKS (Insulin Receptor Tyrosine Kinase Substrate), serves as a substrate for the insulin receptor and binds the small GTPase Rac. It plays a role in regulating the actin cytoskeleton and colocalizes with F-actin, cortactin, VASP, and vinculin. IRSp53 and IRTKS also mediate the recruitment of effector proteins Tir and EspFu, which regulate host cell actin reorganization, to bacterial attachment sites. BAIAP2L2 co-localizes with clathrin plaques but its function has not been determined. The SH3 domains of IRSp53 and IRTKS have been shown to bind the proline-rich C-terminus of EspFu. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212713 [Multi-domain]  Cd Length: 57  Bit Score: 35.76  E-value: 3.15e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNH-WDGYSKGINRKLGKTGLYP-SY 393
Cdd:cd11779    5 ALYPHAAGGETQLSFEEGDVITLLGPEpRDGWHYGENERSGRRGWFPiAY 54
SH3_CIP4_Bzz1_like cd11777
Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains; This subfamily ...
346-396 4.77e-03

Src Homology 3 domain of Cdc42-Interacting Protein 4, Bzz1 and similar domains; This subfamily is composed of Cdc42-Interacting Protein 4 (CIP4) and similar proteins such as Formin Binding Protein 17 (FBP17) and FormiN Binding Protein 1-Like (FNBP1L), as well as yeast Bzz1 (or Bzz1p). CIP4 and FNBP1L are Cdc42 effectors that bind Wiskott-Aldrich syndrome protein (WASP) and function in endocytosis. CIP4 and FBP17 bind to the Fas ligand and may be implicated in the inflammatory response. CIP4 may also play a role in phagocytosis. Bzz1 is also a WASP/Las17-interacting protein involved in endocytosis and trafficking to the vacuole. It physically interacts with type I myosins and functions in the early steps of endocytosis. Members of this subfamily contain an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs) domain as well as at least one C-terminal SH3 domain. Bzz1 contains a second SH3 domain at the C-terminus. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212711 [Multi-domain]  Cd Length: 55  Bit Score: 35.28  E-value: 4.77e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIG-VAGNHWDGYSKgINRKLGKTGLYPSYKVR 396
Cdd:cd11777    4 ALYAFVGSSEGTISMTEGEKLSlVEEDKGDGWTR-VRRDTGEEGYVPTSYIR 54
SH3_JIP1_like cd11801
Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; ...
352-397 5.01e-03

Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; JNK-interacting proteins (JIPs) function as scaffolding proteins for c-Jun N-terminal kinase (JNK) signaling pathways. They bind to components of Mitogen-activated protein kinase (MAPK) pathways such as JNK, MKK, and several MAP3Ks such as MLK and DLK. There are four JIPs (JIP1-4); all contain a JNK binding domain. JIP1 and JIP2 also contain SH3 and Phosphotyrosine-binding (PTB) domains. Both are highly expressed in the brain and pancreatic beta-cells. JIP1 functions as an adaptor linking motor to cargo during axonal transport and also is involved in regulating insulin secretion. JIP2 form complexes with fibroblast growth factor homologous factors (FHFs), which facilitates activation of the p38delta MAPK. The SH3 domain of JIP1 homodimerizes at the interface usually involved in proline-rich ligand recognition, despite the lack of this motif in the domain itself. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212735  Cd Length: 55  Bit Score: 34.98  E-value: 5.01e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 357933612 352 PRTEEEIPMEPGDIIGV---AGNHWdgySKGINRKLGKTGLYPSYKVRE 397
Cdd:cd11801   10 PRHEDEIELDIGDPVYVeqeADDLW---CEGTNLRTGQRGIFPAAYVVE 55
SH3_Sorbs2_3 cd11917
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), ...
346-396 7.68e-03

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing 2 (Sorbs2), also called Arg-binding protein 2 (ArgBP2); Sorbs2 or ArgBP2 is an adaptor protein containing one sorbin homology (SoHo) and three SH3 domains. It regulates actin-dependent processes including cell adhesion, morphology, and migration. It is expressed in many tissues and is abundant in the heart. Like vinexin, it is found in focal adhesion where it interacts with vinculin and afadin. It also localizes in epithelial cell stress fibers and in cardiac muscle cell Z-discs. Sorbs2 has been implicated to play roles in the signaling of c-Arg, Akt, and Pyk2. Other interaction partners of Sorbs2 include c-Abl, flotillin, spectrin, dynamin 1/2, synaptojanin, PTP-PEST, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212850 [Multi-domain]  Cd Length: 61  Bit Score: 34.58  E-value: 7.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYPSYKVR 396
Cdd:cd11917    9 ALYNYMPRNEDELELREGDVIDVMEKCDDGWFVGTSRRTKFFGTFPGNYVK 59
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
345-397 7.72e-03

Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor proteins that function in exo- and endocytosis, actin cytoskeletal reorganization, and signal transduction. They are essential for initiating clathrin-coated pit formation. They bind to many proteins through their multidomain structure and facilitate the assembly of multimeric complexes. Vertebrates contain two ITSN proteins, ITSN1 and ITSN2, which exist in alternatively spliced short and long isoforms. The short isoforms contain two Eps15 homology domains (EH1 and EH2), a coiled-coil region and five SH3 domains (SH3A-E), while the long isoforms, in addition, contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin homology (PH) and C2 domains. ITSN1 and ITSN2 are both widely expressed, with variations depending on tissue type and stage of development. The fifth SH3 domain (or SH3E) of ITSN1 has been shown to bind many protein partners including SGIP1, Sos1, dynamin1/2, CIN85, c-Cbl, SHIP2, N-WASP, and synaptojanin-1, among others. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 34.31  E-value: 7.72e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 357933612 345 IAVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKG-INrklGKTGLYPSYKVRE 397
Cdd:cd11840    3 IALFPYTAQNEDELSFQKGDIINVLSKDDPDWWRGeLN---GQTGLFPSNYVEP 53
SH3_Sorbs_3 cd11780
Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) ...
346-391 8.85e-03

Third (or C-terminal) Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar domains; This family, also called the vinexin family, is composed predominantly of adaptor proteins containing one sorbin homology (SoHo) and three SH3 domains. Members include the third SH3 domains of Sorbs1 (or ponsin), Sorbs2 (or ArgBP2), Vinexin (or Sorbs3), and similar domains. They are involved in the regulation of cytoskeletal organization, cell adhesion, and growth factor signaling. Members of this family bind multiple partners including signaling molecules like c-Abl, c-Arg, Sos, and c-Cbl, as well as cytoskeletal molecules such as vinculin and afadin. They may have overlapping functions. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212714 [Multi-domain]  Cd Length: 55  Bit Score: 34.20  E-value: 8.85e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVAGNHWDGYSKGINRKLGKTGLYP 391
Cdd:cd11780    4 ALYSYTPQNEDELELREGDIVYVMEKCDDGWFVGTSERTGLFGTFP 49
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
346-397 9.70e-03

Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine nucleotide exchange factors (GEFs), which activate small GTPases by exchanging bound GDP for free GTP. They act as GEFs for both Cdc42 and Rac 1, and have been implicated in cell motility, adhesion, neurite outgrowth, and cell polarity. Vertebrates contain two proteins from the PIX subfamily, alpha-PIX and beta-PIX. Alpha-PIX, also called ARHGEF6, is localized in dendritic spines where it regulates spine morphogenesis. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. Beta-PIX play roles in regulating neuroendocrine exocytosis, focal adhesion maturation, cell migration, synaptic vesicle localization, and insulin secretion. PIX proteins contain an N-terminal SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains, and a C-terminal leucine-zipper domain for dimerization. The SH3 domain of PIX binds to an atypical PxxxPR motif in p21-activated kinases (PAKs) with high affinity. The binding of PAKs to PIX facilitate the localization of PAKs to focal complexes and also localizes PAKs to PIX targets Cdc43 and Rac, leading to the activation of PAKs. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212810 [Multi-domain]  Cd Length: 53  Bit Score: 34.21  E-value: 9.70e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 357933612 346 AVYPHKPRTEEEIPMEPGDIIGVA----GNHWDGYSKGinrklgKTGLYPSYKVRE 397
Cdd:cd11877    4 AKFNFEGTNEDELSFDKGDIITVTqvveGGWWEGTLNG------KTGWFPSNYVKE 53
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH