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Conserved domains on  [gi|573890034|ref|XP_006632780|]
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PREDICTED: alpha-(1,6)-fucosyltransferase isoform X1 [Lepisosteus oculatus]

Protein Classification

Graphical summary

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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 ...
68-500 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 catalyses 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: 437577  Cd Length: 431  Bit Score: 763.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034   68 RIPEGPIDQGPgAAGRVRILEEQLIKAKEQIESFRRSSGDaGPGQNQEKLRRKVENGVKELWYFIRSELKKLTHAE-PGE 146
Cdd:pfam19745   1 RLRRSEESKGI-ANGQLDSLEDQLVKAKQQIEDYKPSAAN-GPSLEHEVLRRRLDNGIQELWYYLSSELKKLRKEIdRES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  147 LQKHTEGLLEDLGHQQRSIMTDLYYLSQSDGAGEWREKEAKDLSDLVQNRISYLQNPKDCSKARKLVCNINKGCGYGCQL 226
Cdd:pfam19745  79 LANHINEILDLLAEHKRSLIADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  227 HHVVYCFMIAYGTQRTLILESQNWRYATSGWETVFKPVSDTCTDRTGASTGHWSGEaNDKDVQVVELPIVDSLHPRPPYL 306
Cdd:pfam19745 159 HHVTYCFIVAYATERTLILDSKGWRYSKGGWESVFKPLSDTCTERDGAGASPWPGE-ENSDAQVVELPIVDSLNPRPPYL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  307 PLAIPEDLADRLDRLHGDPSVWWVSQFVKYLIRPQSWLEKEIEEATRKLGFKHPIIGVHVRRTDKVGTEAAFHPIEEYMV 386
Cdd:pfam19745 238 PLAIPADLAPRLLKLHGNPPVWWVGQFLKYLMRPQASTQKFLEEAIEKLGFKKPIVGVHVRRTDKVGTEAAFHSIEEYMV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  387 HVEEHFQSLALRTHVDKKRVYLATDDPSLLQEAKAKYQDYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQTDFLV 466
Cdd:pfam19745 318 WVEEYFQQLERRTRVDKRRVYLATDDPKVIDEAKTKYPNYEVIGDPKIAKSAGLSSRYTDSSLRGIILDIHLLSLSDYLV 397
                         410       420       430
                  ....*....|....*....|....*....|....
gi 573890034  467 CTFSSQVCRVAYEIMQTLHPDASSYFHSLDDIYY 500
Cdd:pfam19745 398 CTFSSQVCRVAYELMQTRYPDASDRFHSLDDIYY 431
SH3_Fut8 cd11792
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1, ...
508-562 2.90e-29

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: 109.60  E-value: 2.90e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 573890034 508 NQIAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYPSYKVKE 562
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 ...
68-500 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 catalyses 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: 437577  Cd Length: 431  Bit Score: 763.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034   68 RIPEGPIDQGPgAAGRVRILEEQLIKAKEQIESFRRSSGDaGPGQNQEKLRRKVENGVKELWYFIRSELKKLTHAE-PGE 146
Cdd:pfam19745   1 RLRRSEESKGI-ANGQLDSLEDQLVKAKQQIEDYKPSAAN-GPSLEHEVLRRRLDNGIQELWYYLSSELKKLRKEIdRES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  147 LQKHTEGLLEDLGHQQRSIMTDLYYLSQSDGAGEWREKEAKDLSDLVQNRISYLQNPKDCSKARKLVCNINKGCGYGCQL 226
Cdd:pfam19745  79 LANHINEILDLLAEHKRSLIADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  227 HHVVYCFMIAYGTQRTLILESQNWRYATSGWETVFKPVSDTCTDRTGASTGHWSGEaNDKDVQVVELPIVDSLHPRPPYL 306
Cdd:pfam19745 159 HHVTYCFIVAYATERTLILDSKGWRYSKGGWESVFKPLSDTCTERDGAGASPWPGE-ENSDAQVVELPIVDSLNPRPPYL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  307 PLAIPEDLADRLDRLHGDPSVWWVSQFVKYLIRPQSWLEKEIEEATRKLGFKHPIIGVHVRRTDKVGTEAAFHPIEEYMV 386
Cdd:pfam19745 238 PLAIPADLAPRLLKLHGNPPVWWVGQFLKYLMRPQASTQKFLEEAIEKLGFKKPIVGVHVRRTDKVGTEAAFHSIEEYMV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  387 HVEEHFQSLALRTHVDKKRVYLATDDPSLLQEAKAKYQDYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQTDFLV 466
Cdd:pfam19745 318 WVEEYFQQLERRTRVDKRRVYLATDDPKVIDEAKTKYPNYEVIGDPKIAKSAGLSSRYTDSSLRGIILDIHLLSLSDYLV 397
                         410       420       430
                  ....*....|....*....|....*....|....
gi 573890034  467 CTFSSQVCRVAYEIMQTLHPDASSYFHSLDDIYY 500
Cdd:pfam19745 398 CTFSSQVCRVAYELMQTRYPDASDRFHSLDDIYY 431
Fut8_like cd11300
Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety ...
176-501 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  Cd Length: 328  Bit Score: 593.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 176 DGAGEWREKEAKDLSDLVQNRISYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATS 255
Cdd:cd11300    1 DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLILDSKGWRYSPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 256 GWETVFKPVSDTCTDRTGASTGHWSGEANDKDVQVVELPIVDSLHPRPPYLPLAIPEDLADRLDRLHGDPSVWWVSQFVK 335
Cdd:cd11300   81 GWEKVFLPLSETCTDRSGDNTAVWWWEPTNSDVQVVKLPIIDSLHSRPPFLPLAVPEDLAERLERLHGDPRVWWIGQLLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 336 YLIRPQSWLEKEIEEATRKLGFKHPIIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQSLALRTH--VDKKRVYLATDDP 413
Cdd:cd11300  161 YLMRPQPWLQDEIDEAKKELGFKHPIVGVHIRRTDKLGTEAAFHSLEEYMEHVEEWYDKYELRGPseKVKRRVYLATDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 414 SLLQEAKAKYQDYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQTDFLVCTFSSQVCRVAYEIMQTLHPDASSYFH 493
Cdd:cd11300  241 SVFDEAKNKYPNYFFIGDPGISKSASLSTRYSDSSLKGIIIDIHLLSECDYLVCTFSSQVCRLAYELMQTRHPDASDRFH 320

                 ....*...
gi 573890034 494 SLDDIYYF 501
Cdd:cd11300  321 SLDDIYYY 328
SH3_Fut8 cd11792
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1, ...
508-562 2.90e-29

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: 109.60  E-value: 2.90e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 573890034 508 NQIAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYPSYKVKE 562
Cdd:cd11792    1 NQVAIYPHKPRNHDEIELRVGDIIGVAGNHWDGYSKGRNRRTGKTGLYPSYKVKD 55
SH3_9 pfam14604
Variant SH3 domain;
511-561 9.93e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 62.63  E-value: 9.93e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 573890034  511 AIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRkiGRTGLYPSYKVK 561
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIEESEDGWWEGINT--GRTGLVPANYVE 49
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
510-561 3.77e-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: 47.15  E-value: 3.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 573890034   510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKiGRTGLYPSYKVK 561
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 ...
68-500 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 catalyses 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: 437577  Cd Length: 431  Bit Score: 763.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034   68 RIPEGPIDQGPgAAGRVRILEEQLIKAKEQIESFRRSSGDaGPGQNQEKLRRKVENGVKELWYFIRSELKKLTHAE-PGE 146
Cdd:pfam19745   1 RLRRSEESKGI-ANGQLDSLEDQLVKAKQQIEDYKPSAAN-GPSLEHEVLRRRLDNGIQELWYYLSSELKKLRKEIdRES 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  147 LQKHTEGLLEDLGHQQRSIMTDLYYLSQSDGAGEWREKEAKDLSDLVQNRISYLQNPKDCSKARKLVCNINKGCGYGCQL 226
Cdd:pfam19745  79 LANHINEILDLLAEHKRSLIADIEKLSKADGAEEWRKKELKDLSDLVQKRLDHLQNPEDCSKARKLICNLNKGCGFGCQL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  227 HHVVYCFMIAYGTQRTLILESQNWRYATSGWETVFKPVSDTCTDRTGASTGHWSGEaNDKDVQVVELPIVDSLHPRPPYL 306
Cdd:pfam19745 159 HHVTYCFIVAYATERTLILDSKGWRYSKGGWESVFKPLSDTCTERDGAGASPWPGE-ENSDAQVVELPIVDSLNPRPPYL 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  307 PLAIPEDLADRLDRLHGDPSVWWVSQFVKYLIRPQSWLEKEIEEATRKLGFKHPIIGVHVRRTDKVGTEAAFHPIEEYMV 386
Cdd:pfam19745 238 PLAIPADLAPRLLKLHGNPPVWWVGQFLKYLMRPQASTQKFLEEAIEKLGFKKPIVGVHVRRTDKVGTEAAFHSIEEYMV 317
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034  387 HVEEHFQSLALRTHVDKKRVYLATDDPSLLQEAKAKYQDYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQTDFLV 466
Cdd:pfam19745 318 WVEEYFQQLERRTRVDKRRVYLATDDPKVIDEAKTKYPNYEVIGDPKIAKSAGLSSRYTDSSLRGIILDIHLLSLSDYLV 397
                         410       420       430
                  ....*....|....*....|....*....|....
gi 573890034  467 CTFSSQVCRVAYEIMQTLHPDASSYFHSLDDIYY 500
Cdd:pfam19745 398 CTFSSQVCRVAYELMQTRYPDASDRFHSLDDIYY 431
Fut8_like cd11300
Alpha 1-6-fucosyltransferase; Alpha 1,6-fucosyltransferase (Fut8) transfers a fucose moiety ...
176-501 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  Cd Length: 328  Bit Score: 593.84  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 176 DGAGEWREKEAKDLSDLVQNRISYLQNPKDCSKARKLVCNINKGCGYGCQLHHVVYCFMIAYGTQRTLILESQNWRYATS 255
Cdd:cd11300    1 DGDSEWRRKELKKLSKLVQKRIHKLQNPKDCSKAKKLVCNLNKGCGFGCQLHHVVYCLIVAYGTNRTLILDSKGWRYSPG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 256 GWETVFKPVSDTCTDRTGASTGHWSGEANDKDVQVVELPIVDSLHPRPPYLPLAIPEDLADRLDRLHGDPSVWWVSQFVK 335
Cdd:cd11300   81 GWEKVFLPLSETCTDRSGDNTAVWWWEPTNSDVQVVKLPIIDSLHSRPPFLPLAVPEDLAERLERLHGDPRVWWIGQLLK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 336 YLIRPQSWLEKEIEEATRKLGFKHPIIGVHVRRTDKVGTEAAFHPIEEYMVHVEEHFQSLALRTH--VDKKRVYLATDDP 413
Cdd:cd11300  161 YLMRPQPWLQDEIDEAKKELGFKHPIVGVHIRRTDKLGTEAAFHSLEEYMEHVEEWYDKYELRGPseKVKRRVYLATDDP 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 414 SLLQEAKAKYQDYEFISDNSISWSAGLHNRYTENSLRGVILDIHFLSQTDFLVCTFSSQVCRVAYEIMQTLHPDASSYFH 493
Cdd:cd11300  241 SVFDEAKNKYPNYFFIGDPGISKSASLSTRYSDSSLKGIIIDIHLLSECDYLVCTFSSQVCRLAYELMQTRHPDASDRFH 320

                 ....*...
gi 573890034 494 SLDDIYYF 501
Cdd:cd11300  321 SLDDIYYY 328
SH3_Fut8 cd11792
Src homology 3 domain of Alpha1,6-fucosyltransferase (Fut8); Fut8 catalyzes the alpha1, ...
508-562 2.90e-29

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: 109.60  E-value: 2.90e-29
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 573890034 508 NQIAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYPSYKVKE 562
Cdd:cd11792    1 NQVAIYPHKPRNHDEIELRVGDIIGVAGNHWDGYSKGRNRRTGKTGLYPSYKVKD 55
O-FucT_like cd11296
GDP-fucose protein O-fucosyltransferase and related proteins; O-fucosyltransferase-like ...
314-475 9.01e-14

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: 70.52  E-value: 9.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 314 LADRLDR---LHGDpSVWWVSQFVKYLIRPqSWLEKEIEEATRKLGFK--HPIIGVHVRRTDKVG------------TEA 376
Cdd:cd11296   24 LAILLGRtlvLPLC-LACPIRLVGKHLRFS-PEIRKLADRFVRKLLGLpgGPYLAVHLRRGDFEVecchlakwmgeyLEE 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 377 AFHPIEEYMVHVEEHFQSLALrthvdkKRVYLATDDPS---LLQEAKAKYQDYEFISDNSISWSAGLHNRYteNSLRGVI 453
Cdd:cd11296  102 CLLSAEEIAEKIKELMAERKL------KVVYVATDEADreeLREELRKAGIRVVTKDDLLEDAELLELEKL--DNYLLSL 173
                        170       180
                 ....*....|....*....|....*.
gi 573890034 454 LDIHFLSQTDFLVC----TFSSQVCR 475
Cdd:cd11296  174 VDQEICSRADVFIGtgfsTFSSNVAL 199
SH3_9 pfam14604
Variant SH3 domain;
511-561 9.93e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 62.63  E-value: 9.93e-13
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 573890034  511 AIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRkiGRTGLYPSYKVK 561
Cdd:pfam14604   1 ALYPYEPKDDDELSLQRGDVITVIEESEDGWWEGINT--GRTGLVPANYVE 49
SH3_SH3RF2_3 cd11784
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ...
510-560 6.79e-09

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: 52.09  E-value: 6.79e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 573890034 510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYPSYKV 560
Cdd:cd11784    3 VALHSYSAHRPEELELQKGEGVRVLGKFQEGWLRGLSLVTGRVGIFPSNYV 53
NodZ_like cd11548
Alpha 1,6-fucosyltransferase similar to Bradyrhizobium NodZ; Bradyrhizobium NodZ is an alpha 1, ...
331-477 1.33e-08

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  Cd Length: 287  Bit Score: 56.22  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 573890034 331 SQFVKYLIRPQSWLEKEIEEATRKLgFKHPIIGVHVRRTDKvgtEAAFHPIEEYMVHVEEhfqslALRT----HVDKKrV 406
Cdd:cd11548  138 KCYLYRLFTPKQEVRAAVRKLYAKL-FGRPTIGVHIRTTDH---KDSLFIKLSPLHRVVD-----ALRKkvalHKDAT-I 207
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 573890034 407 YLATDDPSLLQEAKAKYQDYEFISDnsisWSAGLHNRYTENSLRGV---ILDIHFLSQTDFLVCTFSSQVCRVA 477
Cdd:cd11548  208 FLATDSAEVKDELKRLFPDVVVTPK----EFPPHGERSASDGLEGAedaLIDMYLLARCDHLIGSRFSTFSRMA 277
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
510-561 3.77e-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: 47.15  E-value: 3.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 573890034   510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKiGRTGLYPSYKVK 561
Cdd:smart00326   6 RALYDYTAQDPDELSFKKGDIITVLEKSDDGWWKGRLGR-GKEGLFPSNYVE 56
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
510-557 5.99e-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: 43.61  E-value: 5.99e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 573890034 510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKiGRTGLYPS 557
Cdd:cd00174    3 RALYDYEAQDDDELSFKKGDIITVLEKDDDGWWEGELNG-GREGLFPA 49
SH3_SH3RF_3 cd11783
Third Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), SH3RF3, and ...
510-556 4.26e-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  Cd Length: 55  Bit Score: 41.23  E-value: 4.26e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 573890034 510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYP 556
Cdd:cd11783    3 VALYPYKPQKPDELELRKGEMYTVTEKCQDGWFKGTSLRTGQSGVFP 49
SH3_SH3RF_C cd11785
C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), ...
511-557 9.16e-05

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: 40.14  E-value: 9.16e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 573890034 511 AIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYPS 557
Cdd:cd11785    4 VIVPYPPQSEAELELKEGDIVFVHKKREDGWFKGTLQRTGKTGLFPG 50
SH3_UBASH3 cd11791
Src homology 3 domain of Ubiquitin-associated and SH3 domain-containing proteins, also called ...
511-556 1.82e-04

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: 39.59  E-value: 1.82e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 573890034 511 AIYPHHPRTGEEIPLEPGDVIGVA----GNHWDGYSKGINRKIGRTGLYP 556
Cdd:cd11791    4 VLYPYTPQEEDELELVPGDYIYVSpeelDSSSDGWVEGTSWLTGCSGLLP 53
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
510-557 1.95e-04

SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal transduction related to cytoskeletal organisation. 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: 39.11  E-value: 1.95e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 573890034  510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINrKIGRTGLYPS 557
Cdd:pfam00018   1 VALYDYTAQEPDELSFKKGDIIIVLEKSEDGWWKGRN-KGGKEGLIPS 47
SH3_SH3RF1_3 cd11926
Third Src Homology 3 domain of SH3 domain containing ring finger 1, an E3 ubiquitin-protein ...
510-556 4.79e-04

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  Cd Length: 55  Bit Score: 38.41  E-value: 4.79e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 573890034 510 IAIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRKIGRTGLYP 556
Cdd:cd11926    3 VAIYPYTPRKEDELELRKGEMFLVFERCQDGWFKGTSMHTSKIGVFP 49
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
511-562 8.28e-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: 37.71  E-value: 8.28e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 573890034 511 AIYPHHPRTGEEIPLEPGDVIGVAGNHWDGYSKGINRkiGRTGLYPSYKVKE 562
Cdd:cd11823    4 ALYSYTANREDELSLQPGDIIEVHEKQDDGWWLGELN--GKKGIFPATYVEE 53
SH3_JIP1_like cd11801
Src homology 3 domain of JNK-interacting proteins 1 and 2, and similar domains; ...
511-562 2.53e-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: 36.13  E-value: 2.53e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 573890034 511 AIYPHHPRTGEEIPLEPGDVIGV---AGNHWdgySKGINRKIGRTGLYPSYKVKE 562
Cdd:cd11801    4 ALHKFIPRHEDEIELDIGDPVYVeqeADDLW---CEGTNLRTGQRGIFPAAYVVE 55
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
511-556 5.22e-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: 35.41  E-value: 5.22e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 573890034 511 AIYPHHPRTGEEIPLEPGDVIGVAGNH-----WDGYSKGinrkiGRTGLYP 556
Cdd:cd11836    4 ALYAFEARNPDEISFQPGDIIQVDESQvaepgWLAGELK-----GKTGWFP 49
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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