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Conserved domains on  [gi|2024466778|ref|XP_040543502|]
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peripheral-type benzodiazepine receptor-associated protein 1 isoform X8 [Gallus gallus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1546-1607 1.87e-41

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212945  Cd Length: 62  Bit Score: 146.28  E-value: 1.87e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1546 IFVALFDYDPVSMSPNPDAAEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd12012      1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1687-1746 8.40e-37

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212946  Cd Length: 61  Bit Score: 133.27  E-value: 8.40e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1687 SMVAVFDYNPKESSPNADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12013      1 RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLE 60
SH3 super family cl17036
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 662-705 3.70e-24

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.


The actual alignment was detected with superfamily member cd12014:

Pssm-ID: 473055  Cd Length: 62  Bit Score: 97.04  E-value: 3.70e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778  662 VFLARYSYNPF-DGPNENPEAELPLTAGEYIYIYGDMDEDGFFEG 705
Cdd:cd12014      1 VFVARYSYNPLrDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEG 45
sbcc super family cl31020
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 337-535 8.90e-11

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


The actual alignment was detected with superfamily member TIGR00618:

Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 67.30  E-value: 8.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLEFELKKKRKKCEnlehEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESENAdlklqVV 416
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQE----EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA-----VT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  417 LVTKERDSVIQRnqgLQTKLENLEQVLKHMRDVAERRQllEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLLE 496
Cdd:TIGR00618  304 QIEQQAQRIHTE---LQSKMRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024466778  497 ARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTS 535
Cdd:TIGR00618  379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS 417
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-524 1.33e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


:

Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  129 EEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVVTAPVPLKGSSLELCKKAFArQRAKDLTEQASALLAKDKQIEALQ 208
Cdd:COG4717     91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  209 QECRELQAKLIAGKGDPRCLNVVEFDRL-----------------LRESQKEVLRLQRQIA-LKNFKECLRPSK------ 264
Cdd:COG4717    170 AELAELQEELEELLEQLSLATEEELQDLaeeleelqqrlaeleeeLEEAQEELEELEEELEqLENELEAAALEErlkear 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  265 -GSSGGSLPSAASCPGPALNACSKDSPAAKEVCSGGPALGGAAHGKVEpgvLPLGPALEGHENFPPKNAVADQESSQQIQ 343
Cdd:COG4717    250 lLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLA 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  344 QLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSEnaRLAEENLQLNEKAGwagqVESEnADLkLQVVLVTKERD 423
Cdd:COG4717    327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAG----VEDE-EEL-RAALEQAEEYQ 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  424 SVIQRNQGLQTKLENLEQVLKHMRDVAERRQlLEAEHKEALLVLQEKQEEVRRLQQAQAEAKR-----EHEGAVQLLEAR 498
Cdd:COG4717    399 ELKEELEELEEQLEELLGELEELLEALDEEE-LEEELEELEEELEELEEELEELREELAELEAeleqlEEDGELAELLQE 477

                          410       420       430
                   ....*....|....*....|....*....|...
gi 2024466778  499 VKDLEDQCRSQTEQFS-------LLSQELKQFR 524
Cdd:COG4717    478 LEELKAELRELAEEWAalklaleLLEEAREEYR 510
 
Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1546-1607 1.87e-41

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212945  Cd Length: 62  Bit Score: 146.28  E-value: 1.87e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1546 IFVALFDYDPVSMSPNPDAAEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd12012      1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1687-1746 8.40e-37

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212946  Cd Length: 61  Bit Score: 133.27  E-value: 8.40e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1687 SMVAVFDYNPKESSPNADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12013      1 RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLE 60
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 662-705 3.70e-24

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212947  Cd Length: 62  Bit Score: 97.04  E-value: 3.70e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778  662 VFLARYSYNPF-DGPNENPEAELPLTAGEYIYIYGDMDEDGFFEG 705
Cdd:cd12014      1 VFVARYSYNPLrDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEG 45
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1685-1746 2.17e-11

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: 60.63  E-value: 2.17e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778  1685 PRSMVAVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQ-QRGLVPSNFLE 1746
Cdd:smart00326    2 GPQVRALYDYTAQDPD-------ELSFKKGDIITVL-EKSDDGWWKGRLGRgKEGLFPSNYVE 56
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 337-535 8.90e-11

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 67.30  E-value: 8.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLEFELKKKRKKCEnlehEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESENAdlklqVV 416
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQE----EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA-----VT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  417 LVTKERDSVIQRnqgLQTKLENLEQVLKHMRDVAERRQllEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLLE 496
Cdd:TIGR00618  304 QIEQQAQRIHTE---LQSKMRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024466778  497 ARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTS 535
Cdd:TIGR00618  379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS 417
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 336-522 1.95e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKagwAGQVESENADLKLQV 415
Cdd:COG1196    270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEEELEELEEEL 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLL 495
Cdd:COG1196    347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                          170       180
                   ....*....|....*....|....*..
gi 2024466778  496 EARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG1196    427 EEALAELEEEEEEEEEALEEAAEEEAE 453
SH3_9 pfam14604
Variant SH3 domain;
1690-1746 2.29e-10

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 57.24  E-value: 2.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKEsspnadaEAELTFSAGDIITVfGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:pfam14604    1 ALYPYEPKD-------DDELSLQRGDVITV-IEESEDGWWEGINTGRTGLVPANYVE 49
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1543-1605 6.20e-10

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: 56.39  E-value: 6.20e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024466778  1543 GIRIFVALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDaDGFYRGEC-AGREGYIPCNMV 1605
Cdd:smart00326    1 EGPQVRALYDYTAQD--------PDELSFKKGDIITVLEKSD-DGWWKGRLgRGKEGLFPSNYV 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-524 1.33e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  129 EEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVVTAPVPLKGSSLELCKKAFArQRAKDLTEQASALLAKDKQIEALQ 208
Cdd:COG4717     91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  209 QECRELQAKLIAGKGDPRCLNVVEFDRL-----------------LRESQKEVLRLQRQIA-LKNFKECLRPSK------ 264
Cdd:COG4717    170 AELAELQEELEELLEQLSLATEEELQDLaeeleelqqrlaeleeeLEEAQEELEELEEELEqLENELEAAALEErlkear 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  265 -GSSGGSLPSAASCPGPALNACSKDSPAAKEVCSGGPALGGAAHGKVEpgvLPLGPALEGHENFPPKNAVADQESSQQIQ 343
Cdd:COG4717    250 lLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLA 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  344 QLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSEnaRLAEENLQLNEKAGwagqVESEnADLkLQVVLVTKERD 423
Cdd:COG4717    327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAG----VEDE-EEL-RAALEQAEEYQ 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  424 SVIQRNQGLQTKLENLEQVLKHMRDVAERRQlLEAEHKEALLVLQEKQEEVRRLQQAQAEAKR-----EHEGAVQLLEAR 498
Cdd:COG4717    399 ELKEELEELEEQLEELLGELEELLEALDEEE-LEEELEELEEELEELEEELEELREELAELEAeleqlEEDGELAELLQE 477

                          410       420       430
                   ....*....|....*....|....*....|...
gi 2024466778  499 VKDLEDQCRSQTEQFS-------LLSQELKQFR 524
Cdd:COG4717    478 LEELKAELRELAEEWAalklaleLLEEAREEYR 510
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1547-1608 1.96e-09

Variant 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: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 54.91  E-value: 1.96e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1547 FVALFDYDPVSMSPnpdaaeeeLPFKEGQILKVCgDKDADGFYRGECAGREGYIPCNMVSEV 1608
Cdd:pfam07653    2 GRVIFDYVGTDKNG--------LTLKKGDVVKVL-GKDNDGWWEGETGGRVGLVPSTAVEEI 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-483 4.80e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  111 SSLTEENSLLRRSCFPETEEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVVTAPVPLKGSSLELCK-----KAFARQ 185
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  186 RAKDLTEQASALLAKDKQIEALQQECRELQAKLIAGKGDprclnvvefdrllRESQKEVLRlQRQIALKNFKECLRpskg 265
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------------IEELEAQIE-QLKEELKALREALD---- 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  266 ssggslpsaascpgpALNACSKDspaakevcsggpaLGGAAHGKVEpgvlplgpALEGHENfppknAVADQEssQQIQQL 345
Cdd:TIGR02168  807 ---------------ELRAELTL-------------LNEEAANLRE--------RLESLER-----RIAATE--RRLEDL 843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  346 EFELKKKRKKCENLEHEVRKKHKRCKELEIQLQ----EVQSENARLAEENLQLNEKAGWAGQVESENADLKLQVVLVTKE 421
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778  422 RDSVIQRNQGLQTKLENL-EQVLKHMRDVAErrqLLEAEHKEALLVLQEKQEEVRRLQQAQAE 483
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLqERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLENKIKE 983
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 336-546 5.10e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.65  E-value: 5.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEfelKKKRKKCENLEHEVRKKHKRCKELE---IQLQEVQSENARLaEENLQLNEKAGWA------GQVES 406
Cdd:pfam05483  264 EESRDKANQLE---EKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQKAL-EEDLQIATKTICQlteekeAQMEE 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  407 ENADLKLQVVLVTKERDSVIQRNQGLQT---KLENLEQVLK-----------HMRDVAERRQLLEAEHKEALLVLQEKQ- 471
Cdd:pfam05483  340 LNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKiitmelqkkssELEEMTKFKNNKEVELEELKKILAEDEk 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  472 --EEVRRLQQAQAEAKREHEGAVQLLEAR---VKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTSTLVTSELPLAL 546
Cdd:pfam05483  420 llDEKKQFEKIAEELKGKEQELIFLLQARekeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
mukB PRK04863
chromosome partition protein MukB;
426-529 2.21e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  426 IQRNQGLQTKLENLEQVLKHmRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQL------LEARV 499
Cdd:PRK04863   489 VSRSEAWDVARELLRRLREQ-RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELeqlqeeLEARL 567

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024466778  500 KDLEDQCRSQTEQFSLLSQELKQFRLQTGK 529
Cdd:PRK04863   568 ESLSESVSEARERRMALRQQLEQLQARIQR 597
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-526 9.02e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 9.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   98 KLLSALEDLRHRCSSLTEENSLLRRSC------FPETEEKVKHLKRKNAELAVIAKRLEErARKLQEANLKVVTAPVPLK 171
Cdd:PRK03918   228 KEVKELEELKEEIEELEKELESLEGSKrkleekIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  172 GSSLELCK-KAFARQRAKDLTEQASALLAKDKQIEALQQECRELQAKLIAGKGDPRCLN-----VVEFDRL-LRESQKEV 244
Cdd:PRK03918   307 DELREIEKrLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakakKEELERLkKRLTGLTP 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  245 LRLQRQI-ALKNFKECLRPSK---GSSGGSLPSAASCPGPALNACSKdspaAKEVCsggPALGGaahgkvepgvlplgPA 320
Cdd:PRK03918   387 EKLEKELeELEKAKEEIEEEIskiTARIGELKKEIKELKKAIEELKK----AKGKC---PVCGR--------------EL 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  321 LEGHENFPPKNAVAD-QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEI--QLQEVQSENARLAEENLQ---- 393
Cdd:PRK03918   446 TEEHRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLEELEkkae 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  394 ----LNEKA-GWAGQVESENADLKlQVVLVTKERDSVIQRNQGLQTKLENLEQVL-----KHMRDVAERRQLLEAEHKEA 463
Cdd:PRK03918   526 eyekLKEKLiKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEPFYNEY 604

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778  464 LLVL---QEKQEEVRRLQQAQAEAKR------EHEGAVQLLEARVKDL-----EDQCRSQTEQFSLLSQELKQFRLQ 526
Cdd:PRK03918   605 LELKdaeKELEREEKELKKLEEELDKafeelaETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAE 681
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 87-513 5.39e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   87 ADYSFLVSQNMKLLSALEDLRHRCSSLTeensllrrSCFPETEEKVKHL-KRKNAELAVIAKrLEERARKLQEANLKVVT 165
Cdd:pfam01576  138 EDILLLEDQNSKLSKERKLLEERISEFT--------SNLAEEEEKAKSLsKLKNKHEAMISD-LEERLKKEEKGRQELEK 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  166 APVPLKGSSLELckkafaRQRAKDLTEQASALLAKdkqieaLQQECRELQAKLiaGKGDPRCLNVVEFDRLLRESQKEVL 245
Cdd:pfam01576  209 AKRKLEGESTDL------QEQIAELQAQIAELRAQ------LAKKEEELQAAL--ARLEEETAQKNNALKKIRELEAQIS 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  246 RLQRQIALknfkECLRPSKGSSggslpsAASCPGPALNAC------SKDSPAAKEvcsggpalggAAHGKVEPGVLPLGP 319
Cdd:pfam01576  275 ELQEDLES----ERAARNKAEK------QRRDLGEELEALkteledTLDTTAAQQ----------ELRSKREQEVTELKK 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  320 ALE----GHE----NFPPKNAVADQESSQQIQQLE---FELKKKRKKCE----NLEHEVR--------KKHKRcKELEIQ 376
Cdd:pfam01576  335 ALEeetrSHEaqlqEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALEsenaELQAELRtlqqakqdSEHKR-KKLEGQ 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  377 LQEVQSENARLAEENLQLNEKAGwAGQVESENA-----DLKLQVVLVTKERDSViqrNQGLQTKLENLEQVLKHMRDVAE 451
Cdd:pfam01576  414 LQELQARLSESERQRAELAEKLS-KLQSELESVssllnEAEGKNIKLSKDVSSL---ESQLQDTQELLQEETRQKLNLST 489

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778  452 RRQLLEAEhKEALLVLQEKQEEVRR--------LQQAQAEAKREHE---GAVQLLEARVKDLEDQCRSQTEQF 513
Cdd:pfam01576  490 RLRQLEDE-RNSLQEQLEEEEEAKRnverqlstLQAQLSDMKKKLEedaGTLEALEEGKKRLQRELEALTQQL 561
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 404-549 1.63e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   404 VESENADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRD--------VAERRQLLEAEHKEALLVLQEKQEEVR 475
Cdd:smart00787  156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdpteldrAKEKLKKLLQEIMIKVKKLEELEEELQ 235

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024466778   476 RLQQAQAEAKREhegaVQLLEARVKDLEDQcRSQTEQFSLLsqELKQFRLQTGKIDLLTSTLVTSELPLALCSS 549
Cdd:smart00787  236 ELESKIEDLTNK----KSELNTEIAEAEKK-LEQCRGFTFK--EIEKLKEQLKLLQSLTGWKITKLSGNTLSMT 302
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 335-411 4.83e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 4.83e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778  335 DQESSQQIQQLEFELKKKRKKCENLEHEVrkkhkrcKELEIQLQEVQSENARLAEENLQLNEKagwAGQVESENADL 411
Cdd:cd22887      6 LQELEKRLAELEAELASLEEEIKDLEEEL-------KEKNKANEILNDELIALQIENNLLEEK---LRKLQEENDEL 72
 
Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1546-1607 1.87e-41

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212945  Cd Length: 62  Bit Score: 146.28  E-value: 1.87e-41
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1546 IFVALFDYDPVSMSPNPDAAEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd12012      1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1687-1746 8.40e-37

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212946  Cd Length: 61  Bit Score: 133.27  E-value: 8.40e-37
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1687 SMVAVFDYNPKESSPNADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12013      1 RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLE 60
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 1688-1747 5.12e-28

Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212785  Cd Length: 62  Bit Score: 108.17  E-value: 5.12e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1688 MVAVFDYNPKESSPNADAEAELTFSAGDIITVFGSMDDDGFYYGELNQ-QRGLVPSNFLEA 1747
Cdd:cd11851      2 MVALYDYNPETMSPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGgRKGLVPSNFVQE 62
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 662-705 3.70e-24

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212947  Cd Length: 62  Bit Score: 97.04  E-value: 3.70e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778  662 VFLARYSYNPF-DGPNENPEAELPLTAGEYIYIYGDMDEDGFFEG 705
Cdd:cd12014      1 VFVARYSYNPLrDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEG 45
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 1546-1607 1.11e-23

Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212785  Cd Length: 62  Bit Score: 95.85  E-value: 1.11e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778 1546 IFVALFDYDPVSMSPNPDAaEEELPFKEGQILKVCGDKDADGFYRGE-CAGREGYIPCNMVSE 1607
Cdd:cd11851      1 LMVALYDYNPETMSPNDDP-EEELSFHAGDVVRVYGPMDEDGFYYGElEGGRKGLVPSNFVQE 62
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1689-1746 1.75e-21

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212947  Cd Length: 62  Bit Score: 89.33  E-value: 1.75e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1689 VAVFDYNPKESSPNADAEAELTFSAGDIITVFGSMDDDGFYYGEL-NQQRGLVPSNFLE 1746
Cdd:cd12014      3 VARYSYNPLRDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELlDGRRGLVPSNFVE 61
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1689-1746 3.65e-21

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212945  Cd Length: 62  Bit Score: 88.50  E-value: 3.65e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1689 VAVFDYNPKESSPNADA-EAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12012      3 VALFDYDPLTMSPNPDAaEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVS 61
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1546-1607 8.76e-18

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212946  Cd Length: 61  Bit Score: 78.96  E-value: 8.76e-18
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1546 IFVALFDYDPVSMSPNPDAaEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd12013      1 RMVALFDYDPRESSPNVDA-EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 662-705 3.82e-16

Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212785  Cd Length: 62  Bit Score: 74.27  E-value: 3.82e-16
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778  662 VFLARYSYNPFDG-PNENPEAELPLTAGEYIYIYGDMDEDGFFEG 705
Cdd:cd11851      1 LMVALYDYNPETMsPNDDPEEELSFHAGDVVRVYGPMDEDGFYYG 45
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1546-1605 1.67e-15

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212947  Cd Length: 62  Bit Score: 72.39  E-value: 1.67e-15
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1546 IFVALFDYDPVSMSPNpDAAEEELPFKEGQILKVCGDKDADGFYRGECA-GREGYIPCNMV 1605
Cdd:cd12014      1 VFVARYSYNPLRDSPN-ENPEAELPLNAGDYVYVYGDMDEDGFYEGELLdGRRGLVPSNFV 60
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1685-1746 2.17e-11

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: 60.63  E-value: 2.17e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778  1685 PRSMVAVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQ-QRGLVPSNFLE 1746
Cdd:smart00326    2 GPQVRALYDYTAQDPD-------ELSFKKGDIITVL-EKSDDGWWKGRLGRgKEGLFPSNYVE 56
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 665-705 6.97e-11

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212946  Cd Length: 61  Bit Score: 59.32  E-value: 6.97e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024466778  665 ARYSYNPFD-GPNENPEAELPLTAGEYIYIYGDMDEDGFFEG 705
Cdd:cd12013      4 ALFDYDPREsSPNVDAEVELSFRAGDIITVFGEMDEDGFYYG 45
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 337-535 8.90e-11

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 67.30  E-value: 8.90e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLEFELKKKRKKCEnlehEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESENAdlklqVV 416
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREAQE----EQLKKQQLLKQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKA-----VT 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  417 LVTKERDSVIQRnqgLQTKLENLEQVLKHMRDVAERRQllEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLLE 496
Cdd:TIGR00618  304 QIEQQAQRIHTE---LQSKMRSRAKLLMKRAAHVKQQS--SIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLT 378

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024466778  497 ARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTS 535
Cdd:TIGR00618  379 QHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTS 417
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1688-1744 1.78e-10

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: 57.86  E-value: 1.78e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1688 MVAVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELN-QQRGLVPSNF 1744
Cdd:cd00174      2 ARALYDYEAQDDD-------ELSFKKGDIITVL-EKDDDGWWEGELNgGREGLFPANY 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 336-522 1.95e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 66.11  E-value: 1.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKagwAGQVESENADLKLQV 415
Cdd:COG1196    270 EELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE---LEELEEELEELEEEL 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLL 495
Cdd:COG1196    347 EEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEEL 426

                          170       180
                   ....*....|....*....|....*..
gi 2024466778  496 EARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG1196    427 EEALAELEEEEEEEEEALEEAAEEEAE 453
SH3_9 pfam14604
Variant SH3 domain;
1690-1746 2.29e-10

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 57.24  E-value: 2.29e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKEsspnadaEAELTFSAGDIITVfGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:pfam14604    1 ALYPYEPKD-------DDELSLQRGDVITV-IEESEDGWWEGINTGRTGLVPANYVE 49
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1688-1746 3.40e-10

Variant 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: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 57.22  E-value: 3.40e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNPkeSSPNadaeaELTFSAGDIITVFGsMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:pfam07653    2 GRVIFDYVG--TDKN-----GLTLKKGDVVKVLG-KDNDGWWEGETGGRVGLVPSTAVE 52
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 343-522 4.03e-10

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 64.96  E-value: 4.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  343 QQLEfELKKKRKKCE-----NLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESENADLKLQVVL 417
Cdd:COG1196    200 RQLE-PLERQAEKAEryrelKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEE 278

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  418 VTKERDSVIQRNQGLQTKLENLEQVLKH----MRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQ 493
Cdd:COG1196    279 LELELEEAQAEEYELLAELARLEQDIARleerRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEA 358

                          170       180
                   ....*....|....*....|....*....
gi 2024466778  494 LLEARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG1196    359 ELAEAEEALLEAEAELAEAEEELEELAEE 387
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1543-1605 6.20e-10

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: 56.39  E-value: 6.20e-10
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024466778  1543 GIRIFVALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDaDGFYRGEC-AGREGYIPCNMV 1605
Cdd:smart00326    1 EGPQVRALYDYTAQD--------PDELSFKKGDIITVLEKSD-DGWWKGRLgRGKEGLFPSNYV 55
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
129-524 1.33e-09

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 63.25  E-value: 1.33e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  129 EEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVVTAPVPLKGSSLELCKKAFArQRAKDLTEQASALLAKDKQIEALQ 208
Cdd:COG4717     91 AELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELP-ERLEELEERLEELRELEEELEELE 169

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  209 QECRELQAKLIAGKGDPRCLNVVEFDRL-----------------LRESQKEVLRLQRQIA-LKNFKECLRPSK------ 264
Cdd:COG4717    170 AELAELQEELEELLEQLSLATEEELQDLaeeleelqqrlaeleeeLEEAQEELEELEEELEqLENELEAAALEErlkear 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  265 -GSSGGSLPSAASCPGPALNACSKDSPAAKEVCSGGPALGGAAHGKVEpgvLPLGPALEGHENFPPKNAVADQESSQQIQ 343
Cdd:COG4717    250 lLLLIAAALLALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREK---ASLGKEAEELQALPALEELEEEELEELLA 326

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  344 QLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSEnaRLAEENLQLNEKAGwagqVESEnADLkLQVVLVTKERD 423
Cdd:COG4717    327 ALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAG----VEDE-EEL-RAALEQAEEYQ 398

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  424 SVIQRNQGLQTKLENLEQVLKHMRDVAERRQlLEAEHKEALLVLQEKQEEVRRLQQAQAEAKR-----EHEGAVQLLEAR 498
Cdd:COG4717    399 ELKEELEELEEQLEELLGELEELLEALDEEE-LEEELEELEEELEELEEELEELREELAELEAeleqlEEDGELAELLQE 477

                          410       420       430
                   ....*....|....*....|....*....|...
gi 2024466778  499 VKDLEDQCRSQTEQFS-------LLSQELKQFR 524
Cdd:COG4717    478 LEELKAELRELAEEWAalklaleLLEEAREEYR 510
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1547-1608 1.96e-09

Variant 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: 429575 [Multi-domain]  Cd Length: 54  Bit Score: 54.91  E-value: 1.96e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1547 FVALFDYDPVSMSPnpdaaeeeLPFKEGQILKVCgDKDADGFYRGECAGREGYIPCNMVSEV 1608
Cdd:pfam07653    2 GRVIFDYVGTDKNG--------LTLKKGDVVKVL-GKDNDGWWEGETGGRVGLVPSTAVEEI 54
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 336-522 2.82e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 62.26  E-value: 2.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAgwAGQVESENADLKlqv 415
Cdd:COG1196    312 RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL--AEAEEELEELAE--- 386

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 vlvtkERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLL 495
Cdd:COG1196    387 -----ELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461

                          170       180
                   ....*....|....*....|....*..
gi 2024466778  496 EARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG1196    462 LELLAELLEEAALLEAALAELLEELAE 488
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 336-522 5.90e-09

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 61.11  E-value: 5.90e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSE----NARLAEENLQLNEKAGWAGQVESENADL 411
Cdd:COG1196    242 EELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEeyelLAELARLEQDIARLEERRRELEERLEEL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  412 KLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMR----DVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKRE 487
Cdd:COG1196    322 EEELAELEEELEELEEELEELEEELEEAEEELEEAEaelaEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQ 401

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 2024466778  488 HEGAVQLLEARVKDLEdqcRSQTEQFSLLSQELKQ 522
Cdd:COG1196    402 LEELEEAEEALLERLE---RLEEELEELEEALAEL 433
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 340-527 7.46e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 7.46e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  340 QQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAgwagqvesenADLKLQVVLVT 419
Cdd:TIGR02168  239 EELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEI----------SRLEQQKQILR 308

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  420 KERDSVIQRNQGLQTKLENLEQVLKHMRD-----------VAERRQLLEAEHKEALLVLQE-------KQEEVRRLQQAQ 481
Cdd:TIGR02168  309 ERLANLERQLEELEAQLEELESKLDELAEelaeleekleeLKEELESLEAELEELEAELEElesrleeLEEQLETLRSKV 388

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 2024466778  482 AEAKRE---HEGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQFRLQT 527
Cdd:TIGR02168  389 AQLELQiasLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE 437
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 336-531 8.45e-09

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 60.80  E-value: 8.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSEnarlaEENLQLNEKAGWAGQVESENADLKLQV 415
Cdd:TIGR04523  249 SNTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-----ISDLNNQKEQDWNKELKSELKNQEKKL 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSVIQRNQGLQTKLENLEQVLKHmrdvaerrqlLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREhegaVQLL 495
Cdd:TIGR04523  324 EEIQNQISQNNKIISQLNEQISQLKKELTN----------SESENSEKQRELEEKQNEIEKLKKENQSYKQE----IKNL 389

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024466778  496 EARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKID 531
Cdd:TIGR04523  390 ESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1546-1603 1.11e-08

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: 52.85  E-value: 1.11e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1546 IFVALFDYDPvsmspnpdAAEEELPFKEGQILKVCgDKDADGFYRGECA-GREGYIPCN 1603
Cdd:cd00174      1 YARALYDYEA--------QDDDELSFKKGDIITVL-EKDDDGWWEGELNgGREGLFPAN 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 127-541 1.42e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  127 ETEEKVKHLKRKnAELAVIAKRLEERARKLQEANLkvvtapvplkgsslelckkafarqrAKDLTEQASALLAKDKQIEA 206
Cdd:TIGR02168  197 ELERQLKSLERQ-AEKAERYKELKAELRELELALL-------------------------VLRLEELREELEELQEELKE 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  207 LQQECRELQAKLIAGKGDPRCLN--VVEFDRLLRESQKEVLRLQRQIA-LKNFKECLRPSKGSSGGSLPsaascpgpALN 283
Cdd:TIGR02168  251 AEEELEELTAELQELEEKLEELRleVSELEEEIEELQKELYALANEISrLEQQKQILRERLANLERQLE--------ELE 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  284 ACSKDSPAAKEVcsggpalggaahgkvepgvlplgpaleghenfppknavaDQESSQQIQQLEFELKkkrKKCENLEHEV 363
Cdd:TIGR02168  323 AQLEELESKLDE---------------------------------------LAEELAELEEKLEELK---EELESLEAEL 360

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  364 RKKHKRCKELEIQLQEVQSENARLAEENLQLNEkagwagQVESENADLKLQVVLVT---KERDSVIQRNQGLQTKLENLE 440
Cdd:TIGR02168  361 EELEAELEELESRLEELEEQLETLRSKVAQLEL------QIASLNNEIERLEARLErleDRRERLQQEIEELLKKLEEAE 434

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  441 QVLKHMRDVAERRQLLEAEHKEALLV--LQEKQEEVRRLQQAQAEAKREHegavQLLEARVKDLEDQcRSQTEQFSLLSQ 518
Cdd:TIGR02168  435 LKELQAELEELEEELEELQEELERLEeaLEELREELEEAEQALDAAEREL----AQLQARLDSLERL-QENLEGFSEGVK 509

                          410       420
                   ....*....|....*....|...
gi 2024466778  519 ELKQFRLQTGKIDLLTSTLVTSE 541
Cdd:TIGR02168  510 ALLKNQSGLSGILGVLSELISVD 532
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 336-505 1.42e-08

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 57.24  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLaEENLQlnekagwagQVESENADLKLQV 415
Cdd:COG1579     13 QELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRL-ELEIE---------EVEARIKKYEEQL 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSviqrnQGLQTKLENLEqvlkhmrdvaERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLL 495
Cdd:COG1579     83 GNVRNNKEY-----EALQKEIESLK----------RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147

                          170
                   ....*....|
gi 2024466778  496 EARVKDLEDQ 505
Cdd:COG1579    148 DEELAELEAE 157
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 127-533 1.60e-08

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 59.95  E-value: 1.60e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  127 ETEEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVvtapvplkgsslelckkafaRQRAKDLTEQASALLAKDKQIEA 206
Cdd:COG1196    226 EAELLLLKLRELEAELEELEAELEELEAELEELEAEL--------------------AELEAELEELRLELEELELELEE 285

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  207 LQQECRELQAKLIAGKGDprcLNVVEfdRLLRESQKEVLRLQRQIALKNFKEclrpskgssggslpsaascpgpalnacs 286
Cdd:COG1196    286 AQAEEYELLAELARLEQD---IARLE--ERRRELEERLEELEEELAELEEEL---------------------------- 332

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  287 kdspaakevcsggpalggaahgkvepgvlplgpaleghenfppknavadQESSQQIQQLEFELKKKRKKCENLEHEVRKK 366
Cdd:COG1196    333 -------------------------------------------------EELEEELEELEEELEEAEEELEEAEAELAEA 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  367 HKRCKELEIQLQEVQSENARLAEENLQ-LNEKAGWAGQVESENADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKH 445
Cdd:COG1196    364 EEALLEAEAELAEAEEELEELAEELLEaLRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  446 MRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLLEARVKDLEDQcrSQTEQFSLLSQELKQFRL 525
Cdd:COG1196    444 LEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADY--EGFLEGVKAALLLAGLRG 521


                   ....*...
gi 2024466778  526 QTGKIDLL 533
Cdd:COG1196    522 LAGAVAVL 529
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1548-1602 1.75e-08

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: 52.21  E-value: 1.75e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1548 VALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDaDGFYRGEC-AGREGYIPC 1602
Cdd:pfam00018    1 VALYDYTAQE--------PDELSFKKGDIIIVLEKSE-DGWWKGRNkGGKEGLIPS 47
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1689-1746 2.62e-08

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: 51.65  E-value: 2.62e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11840      3 IALFPYT-------AQNEDELSFQKGDIINVL-SKDDPDWWRGELNGQTGLFPSNYVE 52
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
340-530 2.91e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 58.63  E-value: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  340 QQIQQLEFELKKKRKKcenlEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLnEKAGWAGQVESENADLKlqvvlvt 419
Cdd:COG4717     71 KELKELEEELKEAEEK----EEEYAELQEELEELEEELEELEAELEELREELEKL-EKLLQLLPLYQELEALE------- 138

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  420 KERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLV--------LQEKQEEVRRLQQAQAEAKREHEGA 491
Cdd:COG4717    139 AELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQlslateeeLQDLAEELEELQQRLAELEEELEEA 218

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 2024466778  492 ---VQLLEARVKDLEDQCRSQTEQFSLlsQELKQFRLQTGKI 530
Cdd:COG4717    219 qeeLEELEEELEQLENELEAAALEERL--KEARLLLLIAAAL 258
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1548-1605 5.88e-08

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212738 [Multi-domain]  Cd Length: 52  Bit Score: 50.82  E-value: 5.88e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1548 VALFDYDPvsmspnpdAAEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMV 1605
Cdd:cd11804      3 VAKHDFKA--------TAEDELSFKKGSILKVLNMEDDPNWYKAELDGKEGLIPKNYI 52
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 1548-1606 6.46e-08

N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212881 [Multi-domain]  Cd Length: 54  Bit Score: 50.58  E-value: 6.46e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1548 VALFDYdpvsmspnPDAAEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVS 1606
Cdd:cd11948      3 VALYSF--------QATESDELPFQKGDILKILNMEDDQNWYKAELQGREGYIPKNYIK 53
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 662-705 6.57e-08

Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. 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: 212945  Cd Length: 62  Bit Score: 50.75  E-value: 6.57e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024466778  662 VFLARYSYNPFD-GPNENP-EAELPLTAGEYIYIYGDMDEDGFFEG 705
Cdd:cd12012      1 LFVALFDYDPLTmSPNPDAaEEELPFKEGQLIKVYGDKDADGFYLG 46
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
342-526 6.66e-08

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 57.47  E-value: 6.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  342 IQQLEfELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLnekagwagqvesenaDLKLQVVLVTKE 421
Cdd:COG4717     70 LKELK-ELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKL---------------EKLLQLLPLYQE 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  422 RDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEAllvLQEKQEEVRRLQQAQAEAKREHEGAVQLLEARVKD 501
Cdd:COG4717    134 LEALEAELAELPERLEELEERLEELRELEEELEELEAELAEL---QEELEELLEQLSLATEEELQDLAEELEELQQRLAE 210

                          170       180
                   ....*....|....*....|....*
gi 2024466778  502 LEDQCRSQTEQFSLLSQELKQFRLQ 526
Cdd:COG4717    211 LEEELEEAQEELEELEEELEQLENE 235
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 342-522 6.74e-08

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 57.77  E-value: 6.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  342 IQQLEFELKKKRKKCENLEHEVRkkHKRCKELEIQLQEVQSE----NARLAEENLQLNEKAGWAGQVESENADLKLQVVL 417
Cdd:TIGR02169  767 IEELEEDLHKLEEALNDLEARLS--HSRIPEIQAELSKLEEEvsriEARLREIEQKLNRLTLEKEYLEKEIQELQEQRID 844

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  418 VTKERDSVIQRNQGLQTKLENLEQVLKHMRdvAERRQlLEAEHKEallvLQEKQEEVRRLQQAQAEAKREHEGAVQLLEA 497
Cdd:TIGR02169  845 LKEQIKSIEKEIENLNGKKEELEEELEELE--AALRD-LESRLGD----LKKERDELEAQLRELERKIEELEAQIEKKRK 917

                          170       180
                   ....*....|....*....|....*
gi 2024466778  498 RVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:TIGR02169  918 RLSELKAKLEALEEELSEIEDPKGE 942
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 1689-1746 8.09e-08

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: 50.42  E-value: 8.09e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1689 VAVFDYNPKEsspnadaEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11823      3 KALYSYTANR-------EDELSLQPGDIIEVH-EKQDDGWWLGELNGKKGIFPATYVE 52
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 1690-1746 8.23e-08

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) 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. SH3C of both proteins have been shown to bind to 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: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 50.43  E-value: 8.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1690 AVFDYNPKesspnadAEAELTFSAGDIITVFG-SMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11875      4 VLFDYEAE-------NEDELTLREGDIVTILSkDCEDKGWWKGELNGKRGVFPDNFVE 54
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 1688-1744 1.44e-07

Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is 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. Together with other proteins, it induces membrane scission in yeast. Bzz1 contains an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), a central coiled-coil, and two C-terminal SH3 domains. This model represents the second 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: 212712 [Multi-domain]  Cd Length: 51  Bit Score: 49.42  E-value: 1.44e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1688 MVAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNF 1744
Cdd:cd11778      2 VEALYDYE-------AQGDDEISIRVGDRIAVIRGDDGSGWTYGEINGVKGLFPTSY 51
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
 1686-1751 1.88e-07

Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal sorting complex required for transport (ESCRT-0) and is involved in sorting ubiquitinated cargo proteins from the endosome. It may also be involved in the regulation of IL2 and GM-CSF mediated signaling, and has been implicated in neural cell survival. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. 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: 212897 [Multi-domain]  Cd Length: 55  Bit Score: 49.56  E-value: 1.88e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1686 RSMVAVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFleaVTSD 1751
Cdd:cd11964      1 RKVRAIYDFEAAEDN-------ELTFKAGDIITILDDSDPN-WWKGETPQGTGLFPSNF---VTAD 55
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
 1703-1746 3.13e-07

Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar proteins; This subfamily is composed of Rho GTPase activating proteins (GAPs) with similarity to GRAF. Members contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, a Rho GAP domain, and a C-terminal SH3 domain. Although vertebrates harbor four Rho GAPs in the GRAF subfamily including GRAF, GRAF2, GRAF3, and Oligophrenin-1 (OPHN1), only three are included in this model. OPHN1 contains the BAR, PH and GAP domains, but not the C-terminal SH3 domain. GRAF and GRAF2 show GAP activity towards RhoA and Cdc42. GRAF influences Rho-mediated cytoskeletal rearrangements and binds focal adhesion kinase. GRAF2 regulates caspase-activated p21-activated protein kinase-2. The SH3 domain of GRAF and GRAF2 binds PKNbeta, a target of the small GTPase Rho. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212815 [Multi-domain]  Cd Length: 54  Bit Score: 48.83  E-value: 3.13e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 2024466778 1703 ADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11882     10 AEDESELSFEPGQIITNVQPSDEPGWLEGTLNGRTGLIPENYVE 53
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
340-513 3.73e-07

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 55.31  E-value: 3.73e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  340 QQIQQLE---FELKKKRKKCENLEHEVRKKHKRCKEL------EIQLQEVQSENARLAEENLQLNEKAGWAGQVESENAD 410
Cdd:COG4913    617 AELAELEeelAEAEERLEALEAELDALQERREALQRLaeyswdEIDVASAEREIAELEAELERLDASSDDLAALEEQLEE 696

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  411 LKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALL---VLQEKQEEVRRLQQAQAEAKRE 487
Cdd:COG4913    697 LEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELRALLeerFAAALGDAVERELRENLEERID 776

                          170       180
                   ....*....|....*....|....*.
gi 2024466778  488 HegavqlLEARVKDLEDQCRSQTEQF 513
Cdd:COG4913    777 A------LRARLNRAEEELERAMRAF 796
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
 1692-1746 4.06e-07

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) 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. SH3C of both proteins have been shown to bind to 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: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 48.62  E-value: 4.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1692 FDYNPKesspnadAEAELTFSAGDIITVFG-SMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12142      6 FDYNPV-------APDELALKKGDVIEVISkETEDEGWWEGELNGRRGFFPDNFVM 54
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 337-535 4.10e-07

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 55.03  E-value: 4.10e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLnekagwagqvESENADLKLQVV 416
Cdd:TIGR04523  332 QNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNL----------ESQINDLESKIQ 401

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  417 LVTKErdsviqrNQGLQTKLENLEQvlkhmrdvaeRRQLLEAEHKEaLLVLQEKQ-EEVRRLQQAQAEAK---REHEGAV 492
Cdd:TIGR04523  402 NQEKL-------NQQKDEQIKKLQQ----------EKELLEKEIER-LKETIIKNnSEIKDLTNQDSVKEliiKNLDNTR 463

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2024466778  493 QLLEARVKDLEDQCRSQTEQFSLLSQELKQfrlQTGKIDLLTS 535
Cdd:TIGR04523  464 ESLETQLKVLSRSINKIKQNLEQKQKELKS---KEKELKKLNE 503
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 336-545 5.58e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 54.00  E-value: 5.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSEnARLAEENLQLNEKagwagQVESENADLKLQV 415
Cdd:COG4942     30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQE-LAALEAELAELEK-----EIAELRAELEAQK 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVtKERDSVIQRNqGLQTKLENL---------EQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKR 486
Cdd:COG4942    104 EEL-AELLRALYRL-GRQPPLALLlspedfldaVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLA 181

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778  487 EHEGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTSTLVTSELPLA 545
Cdd:COG4942    182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAAAA 240
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1546-1603 5.62e-07

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 47.96  E-value: 5.62e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1546 IFVALFDYDPVsmspnpdaAEEELPFKEGQILKVCGDKDADGFY-RGECAGREGYIPCN 1603
Cdd:cd11845      1 IYVALYDYEAR--------TDDDLSFKKGDRLQILDDSDGDWWLaRHLSTGKEGYIPSN 51
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 334-524 7.12e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 7.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  334 ADQESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENArlaeenlqlnekagwagqvesenadlKL 413
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELE--------------------------QL 717

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  414 QVVLVTKERDSVIQRNQglqtklenLEQVLKHMRDVAERRQLLEAEHKEALlvlQEKQEEVRRLQQAQAEAKrEHEGAVQ 493
Cdd:TIGR02168  718 RKELEELSRQISALRKD--------LARLEAEVEQLEERIAQLSKELTELE---AEIEELEERLEEAEEELA-EAEAEIE 785

                          170       180       190
                   ....*....|....*....|....*....|.
gi 2024466778  494 LLEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:TIGR02168  786 ELEAQIEQLKEELKALREALDELRAELTLLN 816
SH3_Eve1_5 cd11818
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1703-1744 9.41e-07

Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. 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: 212752 [Multi-domain]  Cd Length: 50  Bit Score: 47.09  E-value: 9.41e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024466778 1703 ADAEAELTFSAGDIITVFGSMDDDGFyYGELNQQRGLVPSNF 1744
Cdd:cd11818     10 GENEDELSFKAGDIITELESIDEEWM-SGELRGKSGIFPKNF 50
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 332-524 9.58e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 53.23  E-value: 9.58e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  332 AVADQESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSE----NARLAEENLQLNEKAGWAGQVESE 407
Cdd:COG4942     12 ALAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRiaalARRIRALEQELAALEAELAELEKE 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  408 NADLKLQVVLVTK---ERDSVIQRNqGLQTKLENL---EQVLKHMRDVAERRQLLEAeHKEALLVLQEKQEEVRRLQQAQ 481
Cdd:COG4942     92 IAELRAELEAQKEelaELLRALYRL-GRQPPLALLlspEDFLDAVRRLQYLKYLAPA-RREQAEELRADLAELAALRAEL 169

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 2024466778  482 AEAKREHEGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:COG4942    170 EAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELA 212
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1690-1746 9.77e-07

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically 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: 212739 [Multi-domain]  Cd Length: 53  Bit Score: 47.24  E-value: 9.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11805      4 ALYDFNPQEPG-------ELEFRRGDIITVLDSSDPD-WWKGELRGRVGIFPANYVQ 52
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
336-498 1.04e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 52.98  E-value: 1.04e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLnekagwagqvESENADLKLQV 415
Cdd:COG4372     76 EQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQL----------EAQIAELQSEI 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQL--LEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQ 493
Cdd:COG4372    146 AEREEELKELEEQLESLQEELAALEQELQALSEAEAEQALdeLLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKD 225


                   ....*
gi 2024466778  494 LLEAR 498
Cdd:COG4372    226 SLEAK 230
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
 1689-1746 1.52e-06

Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. They localize to sites of actin polymerization in epithelial adherens junction and immune synapses, as well as to the leading edge of lamellipodia. Vertebrates contain two Abi proteins, Abi1 and Abi2. Abi1 displays a wide expression pattern while Abi2 is highly expressed in the eye and brain. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212760 [Multi-domain]  Cd Length: 52  Bit Score: 46.55  E-value: 1.52e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11826      3 VALYDYT-------ADKDDELSFQEGDIIYVT-KKNDDGWYEGVLNGVTGLFPGNYVE 52
SH3_CIN85_1 cd12052
First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 1692-1745 1.69e-06

First Src Homology 3 domain (SH3A) 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 first SH3 domain (SH3A) of CIN85; SH3A binds to internal proline-rich motifs within the proline-rich region. This intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. SH3A has also been shown to bind ubiquitin and to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic end of the cell adhesion protein CD2. 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: 212985 [Multi-domain]  Cd Length: 53  Bit Score: 46.81  E-value: 1.69e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024466778 1692 FDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFL 1745
Cdd:cd12052      6 FDYK-------AQHEDELTITVGDIITKI-KKDDGGWWEGEIKGRRGLFPDNFV 51
SH3_PACSIN cd11843
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ...
 1690-1746 1.73e-06

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) proteins; PACSINs, also called Synaptic dynamin-associated proteins (Syndapins), act as regulators of cytoskeletal and membrane dynamics. They bind both dynamin and Wiskott-Aldrich syndrome protein (WASP), and may provide direct links between the actin cytoskeletal machinery through WASP and dynamin-dependent endocytosis. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain 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: 212777 [Multi-domain]  Cd Length: 53  Bit Score: 46.64  E-value: 1.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11843      4 ALYDYEGQESD-------ELSFKAGDILTKLEEEDEQGWCKGRLDGRVGLYPANYVE 53
SH3_Sla1p_2 cd11774
Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1687-1745 1.97e-06

Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. 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: 212708 [Multi-domain]  Cd Length: 52  Bit Score: 46.30  E-value: 1.97e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1687 SMVAVFDYNpKESspnadaEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFL 1745
Cdd:cd11774      1 QAKALYDYD-KQT------EEELSFNEGDTLDVYDDSDSDWILVGFNGTQFGFVPANYI 52
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 1690-1748 2.23e-06

Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, 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: 212737 [Multi-domain]  Cd Length: 55  Bit Score: 46.48  E-value: 2.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1690 AVFDYNPKEsspnadaEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLEAV 1748
Cdd:cd11803      5 ALYDFEPEN-------EGELGFKEGDIITLTNQIDEN-WYEGMVNGQSGFFPVNYVEVL 55
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1689-1742 2.33e-06

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: 46.04  E-value: 2.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024466778 1689 VAVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQ-QRGLVPS 1742
Cdd:pfam00018    1 VALYDYTAQEPD-------ELSFKKGDIIIVL-EKSEDGWWKGRNKGgKEGLIPS 47
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 327-522 2.52e-06

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 51.75  E-value: 2.52e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  327 FPPKNAVAD---QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEkagwagQ 403
Cdd:COG3883      7 AAPTPAFADpqiQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAEAEA------E 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  404 VESENADLKlqvvlvtkERDSVIQRNQGLQTKLE------NLEQVLKHMRDVaerRQLLEAEhKEALLVLQEKQEEVRRL 477
Cdd:COG3883     81 IEERREELG--------ERARALYRSGGSVSYLDvllgseSFSDFLDRLSAL---SKIADAD-ADLLEELKADKAELEAK 148

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778  478 QQAQAEAKREHEGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG3883    149 KAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAEEAA 193
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
317-526 2.68e-06

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 51.83  E-value: 2.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  317 LGPALEGHENFPPKNAVADQESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSE----NARLAEENL 392
Cdd:COG4372      8 VGKARLSLFGLRPKTGILIAALSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSEleqlEEELEELNE 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  393 QLNEKAGWAGQVESENADLKlqvvlvtkerdsviQRNQGLQTKLENLEQvlkhmrdvaeRRQLLEAEHKEallvLQEKQE 472
Cdd:COG4372     88 QLQAAQAELAQAQEELESLQ--------------EEAEELQEELEELQK----------ERQDLEQQRKQ----LEAQIA 139

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024466778  473 EVRRLQQAQAEAKREHEGAVQLLEARVKDLEDQCRSQTEQFslLSQELKQFRLQ 526
Cdd:COG4372    140 ELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAE--AEQALDELLKE 191
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 1689-1746 3.23e-06

Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, also called CD2 Binding Protein 1 (CD2BP1), is mainly expressed in hematopoietic cells. It is a binding partner of the cell surface receptor CD2 and PTP-PEST, a tyrosine phosphatase which functions in cell motility and Rac1 regulation. It also plays a role in the activation of the Wiskott-Aldrich syndrome protein (WASP), which couples actin rearrangement and T cell activation. Mutations in the gene encoding PSTPIP1 cause the autoinflammatory disorder known as PAPA (pyogenic sterile arthritis, pyoderma gangrenosum, and acne) syndrome. PSTPIP1 contains an N-terminal F-BAR domain, PEST motifs, 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: 212758 [Multi-domain]  Cd Length: 53  Bit Score: 45.83  E-value: 3.23e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1689 VAVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11824      3 SVLYDYTAQEDD-------ELSISKGDVVAVI-EKGEDGWWTVERNGQKGLVPGTYLE 52
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1690-1747 3.39e-06

Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or SH3P2, is a signaling protein containing SH3 and ankyrin-repeat domains. It acts through a Src-related pathway to enhance the formation of osteoclasts and bone resorption. It also acts as a negative regulator of cell motility. 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: 212706 [Multi-domain]  Cd Length: 53  Bit Score: 45.75  E-value: 3.39e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLEA 1747
Cdd:cd11772      4 ALYDYEAQHPD-------ELSFEEGDLLYIS-DKSDPNWWKATCGGKTGLIPSNYVEE 53
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 1549-1607 3.96e-06

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) 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. SH3C of both proteins have been shown to bind to 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: 212808 [Multi-domain]  Cd Length: 55  Bit Score: 45.80  E-value: 3.96e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778 1549 ALFDYDPvsmspnpdAAEEELPFKEGQIL----KVCGDKdadGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11875      4 VLFDYEA--------ENEDELTLREGDIVtilsKDCEDK---GWWKGELNGKRGVFPDNFVEP 55
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1689-1745 4.31e-06

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The N-terminal SH3 domain of GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212738 [Multi-domain]  Cd Length: 52  Bit Score: 45.43  E-value: 4.31e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFL 1745
Cdd:cd11804      3 VAKHDFK-------ATAEDELSFKKGSILKVLNMEDDPNWYKAELDGKEGLIPKNYI 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 111-483 4.80e-06

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 51.98  E-value: 4.80e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  111 SSLTEENSLLRRSCFPETEEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVVTAPVPLKGSSLELCK-----KAFARQ 185
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKdlarlEAEVEQ 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  186 RAKDLTEQASALLAKDKQIEALQQECRELQAKLIAGKGDprclnvvefdrllRESQKEVLRlQRQIALKNFKECLRpskg 265
Cdd:TIGR02168  745 LEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAE-------------IEELEAQIE-QLKEELKALREALD---- 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  266 ssggslpsaascpgpALNACSKDspaakevcsggpaLGGAAHGKVEpgvlplgpALEGHENfppknAVADQEssQQIQQL 345
Cdd:TIGR02168  807 ---------------ELRAELTL-------------LNEEAANLRE--------RLESLER-----RIAATE--RRLEDL 843

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  346 EFELKKKRKKCENLEHEVRKKHKRCKELEIQLQ----EVQSENARLAEENLQLNEKAGWAGQVESENADLKLQVVLVTKE 421
Cdd:TIGR02168  844 EEQIEELSEDIESLAAEIEELEELIEELESELEallnERASLEEALALLRSELEELSEELRELESKRSELRRELEELREK 923

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778  422 RDSVIQRNQGLQTKLENL-EQVLKHMRDVAErrqLLEAEHKEALLVLQEKQEEVRRLQQAQAE 483
Cdd:TIGR02168  924 LAQLELRLEGLEVRIDNLqERLSEEYSLTLE---EAEALENKIEDDEEEARRRLKRLENKIKE 983
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
317-524 4.86e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.84  E-value: 4.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  317 LGPALEGHENFppKNAVADQESSQQI------QQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQsenARLAEE 390
Cdd:COG4913    254 LEPIRELAERY--AAARERLAELEYLraalrlWFAQRRLELLEAELEELRAELARLEAELERLEARLDALR---EELDEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  391 NLQLNEKAGwaGQVEsenaDLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALlvlqek 470
Cdd:COG4913    329 EAQIRGNGG--DRLE----QLEREIERLERELEERERRRARLEALLAALGLPLPASAEEFAALRAEAAALLEAL------ 396

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024466778  471 QEEVRRLQQAQAEAKREHEGavqlLEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:COG4913    397 EEELEALEEALAEAEAALRD----LRRELRELEAEIASLERRKSNIPARLLALR 446
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 336-546 5.10e-06

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 51.65  E-value: 5.10e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEfelKKKRKKCENLEHEVRKKHKRCKELE---IQLQEVQSENARLaEENLQLNEKAGWA------GQVES 406
Cdd:pfam05483  264 EESRDKANQLE---EKTKLQDENLKELIEKKDHLTKELEdikMSLQRSMSTQKAL-EEDLQIATKTICQlteekeAQMEE 339

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  407 ENADLKLQVVLVTKERDSVIQRNQGLQT---KLENLEQVLK-----------HMRDVAERRQLLEAEHKEALLVLQEKQ- 471
Cdd:pfam05483  340 LNKAKAAHSFVVTEFEATTCSLEELLRTeqqRLEKNEDQLKiitmelqkkssELEEMTKFKNNKEVELEELKKILAEDEk 419

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  472 --EEVRRLQQAQAEAKREHEGAVQLLEAR---VKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTSTLVTSELPLAL 546
Cdd:pfam05483  420 llDEKKQFEKIAEELKGKEQELIFLLQARekeIHDLEIQLTAIKTSEEHYLKEVEDLKTELEKEKLKNIELTAHCDKLLL 499
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
331-526 5.56e-06

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 51.56  E-value: 5.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  331 NAVAD-----------QESSQQIQQLEFELKKKRKKCENLEHEV---RKKHK-------------RCKELEIQLQEVQSE 383
Cdd:COG3206    155 NALAEayleqnlelrrEEARKALEFLEEQLPELRKELEEAEAALeefRQKNGlvdlseeaklllqQLSELESQLAEARAE 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  384 NARLAEENLQLNEKAGWAGQVESENADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEA 463
Cdd:COG3206    235 LAEAEARLAALRAQLGSGPDALPELLQSPVIQQLRAQLAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQRI 314

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778  464 LLVLQEKQEEVRRLQQAQAEAKREHEGAVQLL---EARVKDLEDQCRSQTEQFSLLSQELKQFRLQ 526
Cdd:COG3206    315 LASLEAELEALQAREASLQAQLAQLEARLAELpelEAELRRLEREVEVARELYESLLQRLEEARLA 380
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 1689-1746 6.40e-06

Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, Abp1 (actin-binding protein 1), hematopoietic lineage cell-specific protein 1 (HS1), and similar proteins. These proteins are involved in regulating actin dynamics through direct or indirect interaction with the Arp2/3 complex, which is required to initiate actin polymerization. They all contain at least one C-terminal SH3 domain. Cortactin and HS1 bind Arp2/3 and actin through an N-terminal region that contains an acidic domain and several copies of a repeat domain found in cortactin and HS1. Abp1 binds actin via an N-terminal actin-depolymerizing factor (ADF) homology domain. Yeast Abp1 binds Arp2/3 directly through two acidic domains. Mammalian Abp1 does not directly interact with Arp2/3; instead, it regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. The C-terminal region of these proteins acts as an adaptor or scaffold that can connect membrane trafficking and signaling proteins that bind the SH3 domain within the actin network. 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: 212753 [Multi-domain]  Cd Length: 54  Bit Score: 45.00  E-value: 6.40e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQ-QRGLVPSNFLE 1746
Cdd:cd11819      3 KALYDYQ-------AAEDNEISFVEGDIITQI-EQIDEGWWLGVNAKgQKGLFPANYVE 53
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 336-537 6.54e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 6.54e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSE----NARLAEENLQlnEKAGWAGQVESENADL 411
Cdd:TIGR02169  733 EKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEAlndlEARLSHSRIP--EIQAELSKLEEEVSRI 810

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  412 KLQVVLVTKERDSVIQRNQGLQTKLENLEQvlkHMRDVAERRQLLEAEHKEALLVLQEKQEEVRrlqqaqaeakrEHEGA 491
Cdd:TIGR02169  811 EARLREIEQKLNRLTLEKEYLEKEIQELQE---QRIDLKEQIKSIEKEIENLNGKKEELEEELE-----------ELEAA 876

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 2024466778  492 VQLLEARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTSTL 537
Cdd:TIGR02169  877 LRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSEL 922
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
 1690-1746 6.59e-06

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: 45.02  E-value: 6.59e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKesspNADaeaELTFSAGDIITVFGSmDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11874      4 VLFSYTPQ----NED---ELELKVGDTIEVLGE-VEEGWWEGKLNGKVGVFPSNFVK 52
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 341-524 8.22e-06

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 51.22  E-value: 8.22e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  341 QIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEI----------------------QLQEVQSENARL----AEENLQL 394
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLTEEISELEKRLEEIEQlleelnkkikdlgeeeqlrvkeKIGELEAEIASLersiAEKEREL 317

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  395 NEKAGWAGQVESE-------NADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHM--------RDVAERRQLLEA- 458
Cdd:TIGR02169  318 EDAEERLAKLEAEidkllaeIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVdkefaetrDELKDYREKLEKl 397

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778  459 --EHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQ---LLEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:TIGR02169  398 krEINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKLEQLAADLSKYE 468
SH3_Abi2 cd11972
Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It ...
 1688-1749 8.52e-06

Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It regulates actin cytoskeletal reorganization at adherens junctions and dendritic spines, which is important in cell morphogenesis, migration, and cognitive function. Mice deficient with Abi2 show defects in orientation and migration of lens fibers, neuronal migration, dendritic spine morphology, as well as deficits in learning and memory. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212905 [Multi-domain]  Cd Length: 61  Bit Score: 45.00  E-value: 8.52e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1688 MVAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLEAVT 1749
Cdd:cd11972      5 VVAIYDYT-------KDKEDELSFQEGAIIYVI-KKNDDGWYEGVMNGVTGLFPGNYVESIM 58
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
348-531 8.78e-06

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 51.07  E-value: 8.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  348 ELKKKRKKCENLEhEVRKKHKRCKELEIQLQEVQSENARL----AEENLQLNEKA-----GWAGQVESENADLKLQVVLV 418
Cdd:COG4913    243 ALEDAREQIELLE-PIRELAERYAAARERLAELEYLRAALrlwfAQRRLELLEAEleelrAELARLEAELERLEARLDAL 321

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  419 TKERDSVIQ--RNQGLQtKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEK----QEEVRRLQQAQAEAKREHEGAV 492
Cdd:COG4913    322 REELDELEAqiRGNGGD-RLEQLEREIERLERELEERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEEL 400

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 2024466778  493 QLLEARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKID 531
Cdd:COG4913    401 EALEEALAEAEAALRDLRRELRELEAEIASLERRKSNIP 439
SH3_GRB2_N cd11946
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
 1565-1605 9.00e-06

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. Its N-terminal SH3 domain binds to Sos and Sos-derived proline-rich peptides. 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: 212879 [Multi-domain]  Cd Length: 56  Bit Score: 44.63  E-value: 9.00e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2024466778 1565 AEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMV 1605
Cdd:cd11946     13 ADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYI 53
SH3_CD2AP-like_1 cd11873
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ...
 1688-1746 1.00e-05

First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This subfamily is composed of the first SH3 domain (SH3A) 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. SH3A of both proteins bind to an atypical PXXXPR motif at the C-terminus of Cbl and the cytoplasmic domain of the cell adhesion protein CD2. CIN85 SH3A binds to internal proline-rich motifs within the proline-rich region; this intramolecular interaction serves as a regulatory mechanism to keep CIN85 in a closed conformation, preventing the recruitment of other proteins. CIN85 SH3A has also been shown to bind 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: 212806 [Multi-domain]  Cd Length: 53  Bit Score: 44.56  E-value: 1.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11873      2 VIVEFDYD-------AEEPDELTLKVGDIITNV-KKMEEGWWEGTLNGKRGMFPDNFVK 52
SH3_GRB2_N cd11946
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
 1688-1746 1.00e-05

N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. Its N-terminal SH3 domain binds to Sos and Sos-derived proline-rich peptides. 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: 212879 [Multi-domain]  Cd Length: 56  Bit Score: 44.63  E-value: 1.00e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNPKesspnADAEAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11946      1 MEAIAKYDFK-----ATADDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIE 54
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 1549-1605 1.07e-05

Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain three endophilin-A isoforms (A1, A2, and A3). Endophilin-A proteins are enriched in the brain and play multiple roles in receptor-mediated endocytosis. They tubulate membranes and regulate calcium influx into neurons to trigger the activation of the endocytic machinery. They are also involved in the sorting of plasma membrane proteins, actin filament assembly, and the uncoating of clathrin-coated vesicles for fusion with endosomes. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, 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: 212737 [Multi-domain]  Cd Length: 55  Bit Score: 44.56  E-value: 1.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1549 ALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDaDGFYRGECAGREGYIPCNMV 1605
Cdd:cd11803      5 ALYDFEPEN--------EGELGFKEGDIITLTNQID-ENWYEGMVNGQSGFFPVNYV 52
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 341-522 1.29e-05

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 48.49  E-value: 1.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  341 QIQQLEFELKKKRKKCENLEHEVRKKHKRCKELE-----IQLQEVQSENaRLAEENLQLNEKAGWAGQVESENADLKLQV 415
Cdd:pfam00261   44 RIQLLEEELERTEERLAEALEKLEEAEKAADESErgrkvLENRALKDEE-KMEILEAQLKEAKEIAEEADRKYEEVARKL 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSVIQRNQGLQTKLENLEQvlkHMRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQ--AQAEAKREH-EGAV 492
Cdd:pfam00261  123 VVVEGDLERAEERAELAESKIVELEE---ELKVVGNNLKSLEASEEKASEREDKYEEQIRFLTEklKEAETRAEFaERSV 199

                          170       180       190
                   ....*....|....*....|....*....|
gi 2024466778  493 QLLEARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:pfam00261  200 QKLEKEVDRLEDELEAEKEKYKAISEELDQ 229
SH3_FCHSD_2 cd11762
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 1690-1746 1.31e-05

Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. 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: 212696 [Multi-domain]  Cd Length: 57  Bit Score: 44.31  E-value: 1.31e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1690 AVFDYNpkesspnADAEAELTFSAGDIITVFGSMD---DDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11762      4 ALYDYE-------AQSDEELSFPEGAIIRILRKDDngvDDGWWEGEFNGRVGVFPSLVVE 56
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 1689-1746 1.62e-05

N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor protein that is highly expressed in lymphoid tissues. It acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. It has been identified as a regulator of TGFbeta signaling in diabetic kidney tubules and may have a role in the pathogenesis of the disease. GRAP contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212881 [Multi-domain]  Cd Length: 54  Bit Score: 44.04  E-value: 1.62e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1689 VAVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11948      3 VALYSFQATESD-------ELPFQKGDILKILNMEDDQNWYKAELQGREGYIPKNYIK 53
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 340-537 1.75e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 49.63  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  340 QQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGwagQVESEnadlklqvvlvT 419
Cdd:TIGR04523  468 TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIE---KLESE-----------K 533

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  420 KERDSVIQRnqgLQTKLENLEQVLKhmrdvaerRQLLEAEhkeallvLQEKQEEVRRLQQAQAEAKREHEGAVQLL---E 496
Cdd:TIGR04523  534 KEKESKISD---LEDELNKDDFELK--------KENLEKE-------IDEKNKEIEELKQTQKSLKKKQEEKQELIdqkE 595

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2024466778  497 ARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKIDLLTSTL 537
Cdd:TIGR04523  596 KEKKDLIKEIEEKEKKISSLEKELEKAKKENEKLSSIIKNI 636
SH3_FCHSD2_2 cd11894
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain ...
 1549-1607 1.96e-05

Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. 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: 212827  Cd Length: 56  Bit Score: 43.77  E-value: 1.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1549 ALFDYDpvsmspnpDAAEEELPFKEGQILKVCG--DKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11894      4 ALYDYE--------GQTDDELSFPEGAIIRILNkeNQDDDGFWEGEFNGRIGVFPSVLVEE 56
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 337-487 2.07e-05

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 47.20  E-value: 2.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLaeenLQLNEKAGWAgqvesENADLKLQVV 416
Cdd:pfam15619   57 ELPQLIARHNEEVRVLRERLRRLQEKERDLERKLKEKEAELLRLRDQLKRL----EKLSEDKNLA-----EREELQKKLE 127

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778  417 LVTKERDSVIQRNQGLQTKLENLEQVLKHMRdVAERRQlleaeHKEALLVLQEKQEEVRRLQQAQAEAKRE 487
Cdd:pfam15619  128 QLEAKLEDKDEKIQDLERKLELENKSFRRQL-AAEKKK-----HKEAQEEVKILQEEIERLQQKLKEKERE 192
mukB PRK04863
chromosome partition protein MukB;
426-529 2.21e-05

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 49.57  E-value: 2.21e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  426 IQRNQGLQTKLENLEQVLKHmRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQL------LEARV 499
Cdd:PRK04863   489 VSRSEAWDVARELLRRLREQ-RHLAEQLQQLRMRLSELEQRLRQQQRAERLLAEFCKRLGKNLDDEDELeqlqeeLEARL 567

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024466778  500 KDLEDQCRSQTEQFSLLSQELKQFRLQTGK 529
Cdd:PRK04863   568 ESLSESVSEARERRMALRQQLEQLQARIQR 597
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 1702-1746 2.42e-05

N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212880 [Multi-domain]  Cd Length: 52  Bit Score: 43.25  E-value: 2.42e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778 1702 NADAEAELTFSAGDIITVFGSmdDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11947      9 TASGEDELSFKKGDVLKILSS--DDIWFKAELNGEEGYVPKNFVD 51
SH3_MLK1-3 cd12059
Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine ...
 1690-1744 3.55e-05

Src Homology 3 domain of Mixed Lineage Kinases 1, 2, and 3; MLKs 1, 2, and 3 are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Little is known about the specific function of MLK1, also called MAP3K9. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. MLK2, also called MAP3K10, is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK3, also called MAP3K11, is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. It also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and thus, impacts inflammation and immunity. MLKs contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. 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: 212992 [Multi-domain]  Cd Length: 58  Bit Score: 43.22  E-value: 3.55e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1690 AVFDYNpkesspnADAEAELTFSAGDIITVFgSMD-----DDGFYYGELNQQRGLVPSNF 1744
Cdd:cd12059      4 AVFDYE-------ASAEDELTLRRGDRVEVL-SKDsavsgDEGWWTGKINDRVGIFPSNY 55
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
 1686-1747 3.69e-05

Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. There are two vertebrate STAMs, STAM1 and STAM2, which may be functionally redundant; vertebrate STAMs contain ITAM motifs. They are part of the endosomal sorting complex required for transport (ESCRT-0). STAM2 deficiency in mice did not cause any obvious abnormality, while STAM1 deficiency resulted in growth retardation. Loss of both STAM1 and STAM2 in mice proved lethal, indicating that STAMs are important for embryonic development. 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: 212754 [Multi-domain]  Cd Length: 54  Bit Score: 42.84  E-value: 3.69e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1686 RSMVAVFDYNPKEsspnadaEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLEA 1747
Cdd:cd11820      1 RKVRALYDFEAAE-------DNELTFKAGEIITVLDDSDPN-WWKGSNHRGEGLFPANFVTA 54
SH3_FCHSD2_2 cd11894
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain ...
 1690-1746 3.90e-05

Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. 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: 212827  Cd Length: 56  Bit Score: 43.00  E-value: 3.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1690 AVFDYNpkesspnADAEAELTFSAGDIITVFG--SMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11894      4 ALYDYE-------GQTDDELSFPEGAIIRILNkeNQDDDGFWEGEFNGRIGVFPSVLVE 55
SH3_MPP7 cd12033
Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); ...
 1690-1742 4.31e-05

Src Homology 3 domain of Membrane Protein, Palmitoylated 7 (or MAGUK p55 subfamily member 7); MPP7 is a scaffolding protein that binds to DLG1 and promotes tight junction formation and epithelial cell polarity. Mutations in the MPP7 gene may be associated with the pathogenesis of diabetes and extreme bone mineral density. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212966  Cd Length: 61  Bit Score: 43.09  E-value: 4.31e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSPNADAEAELTFSAGDIITVFgSMDDDGFYY----GELNQQRGLVPS 1742
Cdd:cd12033      4 ALFDYNPNEDKAIPCKEAGLSFKKGDILQIM-SQDDATWWQakheGDANPRAGLIPS 59
SH3_SH3RF_1 cd11786
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ...
 1690-1746 4.56e-05

First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the first SH3 domain of SH3RF1 (or POSH), SH3RF2 (or POSHER), SH3RF3 (POSH2), and similar domains. Members of this family are scaffold proteins that function as E3 ubiquitin-protein ligases. They all contain an N-terminal RING finger domain and multiple SH3 domains; SH3RF1 and SH3RF3 have four SH3 domains while SH3RF2 has three. 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. SH3RF2 acts as an anti-apoptotic regulator of the JNK pathway by binding to and promoting the degradation 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: 212720 [Multi-domain]  Cd Length: 53  Bit Score: 42.73  E-value: 4.56e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11786      4 ALYNYEGKEPG-------DLSFKKGDIILLRKRIDEN-WYHGECNGKQGFFPASYVQ 52
SH3_Cortactin cd11959
Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src ...
 1687-1747 4.57e-05

Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src kinase. It is an actin regulatory protein that binds to the Arp2/3 complex and stabilizes branched actin filaments. It is involved in cellular processes that affect cell motility, adhesion, migration, endocytosis, and invasion. It is expressed ubiquitously except in hematopoietic cells, where the homolog hematopoietic lineage cell-specific 1 (HS1) is expressed instead. Cortactin contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region interacts with the Arp2/3 complex and F-actin, and is crucial in regulating branched actin assembly. Cortactin also serves as a scaffold and provides a bridge to the actin cytoskeleton for membrane trafficking and signaling proteins that bind to its SH3 domain. Binding partners for the SH3 domain of cortactin include dynamin2, N-WASp, MIM, FGD1, 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: 212892 [Multi-domain]  Cd Length: 53  Bit Score: 42.40  E-value: 4.57e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1687 SMVAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLEA 1747
Cdd:cd11959      1 TAVALYDYQ-------AADDDEISFDPDDIITNI-EMIDEGWWRGVCRGKYGLFPANYVEL 53
SH3_Sla1p_2 cd11774
Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1549-1605 4.80e-05

Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates endocytosis by playing a role as an adaptor protein in coupling components of the actin cytoskeleton to the endocytic machinery. It interacts with Abp1p, Las17p and Pan1p, which are activator proteins of actin-related protein 2/3 (Arp2/3). Sla1p contains multiple domains including three SH3 domains, a SAM (sterile alpha motif) domain, and a Sla1 homology domain 1 (SHD1), which binds to the NPFXD motif that is found in many integral membrane proteins such as the Golgi-localized Arf-binding protein Lsb5p and the P4-ATPases, Drs2p and Dnf1p. 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: 212708 [Multi-domain]  Cd Length: 52  Bit Score: 42.45  E-value: 4.80e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1549 ALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMV 1605
Cdd:cd11774      4 ALYDYDKQT--------EEELSFNEGDTLDVYDDSDSDWILVGFNGTQFGFVPANYI 52
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
 1550-1605 4.84e-05

Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; N-terminal SH3 domain of the uncharacterized protein SH3 domain-containing protein 21, and similar uncharacterized domains, it belongs to the CD2AP-like_3 subfamily of proteins. The CD2AP-like_3 subfamily is composed of the third SH3 domain (SH3C) 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. SH3C of both proteins have been shown to bind to 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: 213018 [Multi-domain]  Cd Length: 55  Bit Score: 42.45  E-value: 4.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1550 LFDYDPVsmspnpdaAEEELPFKEGQILKVCGDKDAD-GFYRGECAGREGYIPCNMV 1605
Cdd:cd12142      5 LFDYNPV--------APDELALKKGDVIEVISKETEDeGWWEGELNGRRGFFPDNFV 53
SH3_Abi1 cd11971
Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of ...
 1688-1753 4.84e-05

Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of actin cytoskeletal reorganization through interactions with many protein complexes. It is part of WAVE, a nucleation-promoting factor complex, that links Rac 1 activation to actin polymerization causing lamellipodia protrusion at the plasma membrane. Abi1 interact with formins to promote protrusions at the leading edge of motile cells. It also is a target of alpha4 integrin, regulating membrane protrusions at sites of integrin engagement. Abi proteins are adaptor proteins serving as binding partners and substrates of Abl tyrosine kinases. They are involved in regulating actin cytoskeletal reorganization and play important roles in membrane-ruffling, endocytosis, cell motility, and cell migration. Abi proteins contain a homeobox homology domain, a proline-rich region, and a SH3 domain. The SH3 domain of Abi binds to a PxxP motif in Abl. 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: 212904 [Multi-domain]  Cd Length: 59  Bit Score: 42.70  E-value: 4.84e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1688 MVAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLEAVTSDGD 1753
Cdd:cd11971      2 VVAIYDYS-------KDKDDELSFMEGAIIYVI-KKNDDGWYEGVCNGVTGLFPGNYVESIMHYAD 59
SH3_CD2AP_1 cd12053
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1706-1748 4.87e-05

First Src Homology 3 domain (SH3A) 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 first SH3 domain (SH3A) of CD2AP. SH3A binds to the PXXXPR motif present in c-Cbl and the cytoplasmic domain of cell adhesion protein CD2. Its interaction with CD2 anchors CD2 at sites of cell contact. 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: 212986  Cd Length: 56  Bit Score: 42.52  E-value: 4.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024466778 1706 EAELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLEAV 1748
Cdd:cd12053     13 EDELTIRVGEIIRNVKKLEEEGWLEGELNGRRGMFPDNFVKEI 55
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
336-524 5.11e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 48.52  E-value: 5.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARL------AEENLQLNEkagWAGQVESENA 409
Cdd:PRK03918   234 EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELkelkekAEEYIKLSE---FYEEYLDELR 310

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  410 DLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQeKQEEVRRLQQAQA-EAKREH 488
Cdd:PRK03918   311 EIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKA-KKEELERLKKRLTgLTPEKL 389

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024466778  489 EGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:PRK03918   390 EKELEELEKAKEEIEEEISKITARIGELKKEIKELK 425
SH3_DNMBP_N3 cd11796
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
 1703-1745 5.68e-05

Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. 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: 212730  Cd Length: 51  Bit Score: 42.34  E-value: 5.68e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024466778 1703 ADAEAELTFSAGDIITVFGSMDDdGFYYGELNQQRGLVPSNFL 1745
Cdd:cd11796     10 AQLDEELDLREGDVVTITGILDK-GWFRGELNGRRGIFPEGFV 51
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 332-522 5.86e-05

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 47.98  E-value: 5.86e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  332 AVADQESSQQIQQLEFELKKKRKKCENLEHEVRK-KHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESENAD 410
Cdd:pfam15964  441 ASQEMDVTKVCGEMRYQLNQTKMKKDEAEKEHREyRTKTGRQLEIKDQEIEKLGLELSESKQRLEQAQQDAARAREECLK 520

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  411 L-------KLQVVLVTKERDSV---------------IQRNQGLQTKLENLEQvlKHMRDVAERRQLLEAEH------KE 462
Cdd:pfam15964  521 LtellgesEHQLHLTRLEKESIqqsfsneakaqalqaQQREQELTQKMQQMEA--QHDKTVNEQYSLLTSQNtfiaklKE 598

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024466778  463 ALLVLQEKQEEV---RRLQQAQAEAKREH-EGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:pfam15964  599 ECCTLAKKLEEItqkSRSEVEQLSQEKEYlQDRLEKLQKRNEELEEQCVQHGRMHERMKQRLRQ 662
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 336-527 5.93e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 48.09  E-value: 5.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKagwAGQVESENADLKLQV 415
Cdd:TIGR04523  380 QSYKQEIKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSE---IKDLTNQDSVKELII 456

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSviqrnqgLQTKLENLEQVLKHMR-DVAERRQLLEAEHKEALLVLQEKQ---EEVRRLQQAQAEAKREhega 491
Cdd:TIGR04523  457 KNLDNTRES-------LETQLKVLSRSINKIKqNLEQKQKELKSKEKELKKLNEEKKeleEKVKDLTKKISSLKEK---- 525

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 2024466778  492 VQLLEARVKDLEDQCRSQTEQFSLLSQELKQFRLQT 527
Cdd:TIGR04523  526 IEKLESEKKEKESKISDLEDELNKDDFELKKENLEK 561
SH3_FCHSD_2 cd11762
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 1549-1607 6.01e-05

Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of FCH and double SH3 domains protein 1 (FCHSD1) and FCHSD2. These proteins have a common domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. They have only been characterized in silico and their functions remain unknown. This group also includes the insect protein, nervous wreck, which acts as a regulator of synaptic growth signaling. 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: 212696 [Multi-domain]  Cd Length: 57  Bit Score: 42.38  E-value: 6.01e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1549 ALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDA---DGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11762      4 ALYDYEAQS--------DEELSFPEGAIIRILRKDDNgvdDGWWEGEFNGRVGVFPSLVVEE 57
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 336-522 6.74e-05

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 47.71  E-value: 6.74e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRkkhkrckELEIQLQEVQSENARLAE--ENLQLNEKagwagQVESENADLKL 413
Cdd:TIGR04523  366 EEKQNEIEKLKKENQSYKQEIKNLESQIN-------DLESKIQNQEKLNQQKDEqiKKLQQEKE-----LLEKEIERLKE 433

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  414 QVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRdvaERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREhegaVQ 493
Cdd:TIGR04523  434 TIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLE---TQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEE----KK 506

                          170       180
                   ....*....|....*....|....*....
gi 2024466778  494 LLEARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:TIGR04523  507 ELEEKVKDLTKKISSLKEKIEKLESEKKE 535
DivIVA pfam05103
DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum ...
 418-524 7.08e-05

DivIVA protein; The Bacillus subtilis divIVA1 mutation causes misplacement of the septum during cell division, resulting in the formation of small, circular, anucleate mini-cells. Inactivation of divIVA produces a mini-cell phenotype, whereas overproduction of DivIVA results in a filamentation phenotype. These proteins appear to contain coiled-coils.


Pssm-ID: 428304 [Multi-domain]  Cd Length: 131  Bit Score: 44.48  E-value: 7.08e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  418 VTKERDSVIQRNQGLQTKLENLEQVLKHMRDvaerrqlLEAEHKEALLVLQEKQEEVRR---------LQQAQAEAKREH 488
Cdd:pfam05103   30 VAEDYEALIRENAELKEKIEELEEKLAHYKN-------LEETLQNTLILAQETAEEVKAnaqkeaeliIKEAEAKAERIV 102

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 2024466778  489 EGAvqllEARVKDLEDqcrsQTEQfslLSQELKQFR 524
Cdd:pfam05103  103 DDA----NNEVKKIND----EIEE---LKRQRRQFR 127
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
 1690-1748 7.29e-05

C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic protein that binds focal adhesion proteins and is involved in cell signaling, migration, and proliferation. It is overexpressed in several cancer cells including breast, ovarian, bladder, and liver. In cancer cells, it can be found in the nucleus; its degree of nuclear localization correlates with tumor size and poor prognosis. Lasp1 is a 36kD protein containing an N-terminal LIM domain, two nebulin repeats, 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: 212867 [Multi-domain]  Cd Length: 59  Bit Score: 42.29  E-value: 7.29e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1690 AVFDYNpkesspnADAEAELTFSAGDIITVFGSMdDDGFYYG--ELNQQRGLVPSNFLEAV 1748
Cdd:cd11934      7 AVYDYN-------AADEDEVSFQDGDTIVNVQQI-DDGWMYGtvERTGDTGMLPANYVEAI 59
SH3_FCHSD1_2 cd11895
Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain ...
 1549-1608 7.33e-05

Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain structure consisting of an N-terminal F-BAR (FES-CIP4 Homology and Bin/Amphiphysin/Rvs), two SH3, and C-terminal proline-rich domains. It has only been characterized in silico and its function is unknown. 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: 212828  Cd Length: 58  Bit Score: 42.26  E-value: 7.33e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778 1549 ALFDYDpvSMSPnpdaaeEELPFKEGQILKV---CGDKDADGFYRGECAGREGYIPCNMVSEV 1608
Cdd:cd11895      4 ALYSYT--GQSP------EELSFPEGALIRLlprAQDGVDDGFWRGEFGGRVGVFPSLLVEEL 58
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 1548-1607 7.49e-05

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: 41.94  E-value: 7.49e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1548 VALFDYDPvsmspnpdAAEEELPFKEGQILKVcGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11823      3 KALYSYTA--------NREDELSLQPGDIIEV-HEKQDDGWWLGELNGKKGIFPATYVEE 53
SH3_Blk cd12009
Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of ...
 1548-1606 7.56e-05

Src homology 3 domain of Blk Protein Tyrosine Kinase; Blk is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. It is expressed specifically in B-cells and is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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: 212942 [Multi-domain]  Cd Length: 54  Bit Score: 42.11  E-value: 7.56e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1548 VALFDYDPVSmspnpdaaEEELPFKEGQILKV-CGDKDAdGFYRGECAGREGYIPCNMVS 1606
Cdd:cd12009      3 IAQYDFVPSN--------ERDLQLKKGEKLQVlKSDGEW-WLAKSLTTGKEGYIPSNYVA 53
SH3_VAV1_2 cd11976
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ...
 1568-1607 7.63e-05

C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly in the hematopoietic system and it plays an important role in the development and activation of B and T cells. It is activated by tyrosine phosphorylation to function as a guanine nucleotide exchange factor (GEF) for Rho GTPases following cell surface receptor activation, triggering various effects such as cytoskeletal reorganization, transcription regulation, cell cycle progression, and calcium mobilization. It also serves as a scaffold protein and has been shown to interact with Ku70, Socs1, Janus kinase 2, SIAH2, S100B, Abl gene, ZAP-70, SLP76, and Syk, among others. VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The C-terminal SH3 domain of Vav1 interacts with a wide variety of proteins including cytoskeletal regulators (zyxin), RNA-binding proteins (Sam68), transcriptional regulators, viral proteins, and dynamin 2. 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: 212909 [Multi-domain]  Cd Length: 54  Bit Score: 41.85  E-value: 7.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024466778 1568 ELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11976     15 ELSLKEGDIIKILNKKGQQGWWRGEIYGRVGWFPANYVEE 54
SH3_CRK_N cd11758
N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor ...
 1549-1607 7.93e-05

N-terminal Src Homology 3 domain of Ct10 Regulator of Kinase adaptor proteins; CRK adaptor proteins consists of SH2 and SH3 domains, which bind tyrosine-phosphorylated peptides and proline-rich motifs, respectively. They function downstream of protein tyrosine kinases in many signaling pathways started by various extracellular signals, including growth and differentiation factors. Cellular CRK (c-CRK) contains a single SH2 domain, followed by N-terminal and C-terminal SH3 domains. It is involved in the regulation of many cellular processes including cell growth, motility, adhesion, and apoptosis. CRK has been implicated in the malignancy of various human cancers. The N-terminal SH3 domain of CRK binds a number of target proteins including DOCK180, C3G, SOS, and cABL. The CRK family includes two alternatively spliced protein forms, CRKI and CRKII, that are expressed by the CRK gene, and the CRK-like (CRKL) protein, which is expressed by a distinct gene (CRKL). 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: 212692 [Multi-domain]  Cd Length: 55  Bit Score: 41.96  E-value: 7.93e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1549 ALFDYdpvsmspnPDAAEEELPFKEGQILKVCgDKDADGFYRGECA-GREGYIPCNMVSE 1607
Cdd:cd11758      5 ALFDF--------PGNDDEDLPFKKGEILTVI-RKPEEQWWNARNSeGKTGMIPVPYVEK 55
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
98-526 9.02e-05

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 47.37  E-value: 9.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   98 KLLSALEDLRHRCSSLTEENSLLRRSC------FPETEEKVKHLKRKNAELAVIAKRLEErARKLQEANLKVVTAPVPLK 171
Cdd:PRK03918   228 KEVKELEELKEEIEELEKELESLEGSKrkleekIRELEERIEELKKEIEELEEKVKELKE-LKEKAEEYIKLSEFYEEYL 306

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  172 GSSLELCK-KAFARQRAKDLTEQASALLAKDKQIEALQQECRELQAKLIAGKGDPRCLN-----VVEFDRL-LRESQKEV 244
Cdd:PRK03918   307 DELREIEKrLSRLEEEINGIEERIKELEEKEERLEELKKKLKELEKRLEELEERHELYEeakakKEELERLkKRLTGLTP 386

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  245 LRLQRQI-ALKNFKECLRPSK---GSSGGSLPSAASCPGPALNACSKdspaAKEVCsggPALGGaahgkvepgvlplgPA 320
Cdd:PRK03918   387 EKLEKELeELEKAKEEIEEEIskiTARIGELKKEIKELKKAIEELKK----AKGKC---PVCGR--------------EL 445

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  321 LEGHENFPPKNAVAD-QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEI--QLQEVQSENARLAEENLQ---- 393
Cdd:PRK03918   446 TEEHRKELLEEYTAElKRIEKELKEIEEKERKLRKELRELEKVLKKESELIKLKELaeQLKELEEKLKKYNLEELEkkae 525

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  394 ----LNEKA-GWAGQVESENADLKlQVVLVTKERDSVIQRNQGLQTKLENLEQVL-----KHMRDVAERRQLLEAEHKEA 463
Cdd:PRK03918   526 eyekLKEKLiKLKGEIKSLKKELE-KLEELKKKLAELEKKLDELEEELAELLKELeelgfESVEELEERLKELEPFYNEY 604

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778  464 LLVL---QEKQEEVRRLQQAQAEAKR------EHEGAVQLLEARVKDL-----EDQCRSQTEQFSLLSQELKQFRLQ 526
Cdd:PRK03918   605 LELKdaeKELEREEKELKKLEEELDKafeelaETEKRLEELRKELEELekkysEEEYEELREEYLELSRELAGLRAE 681
Tropomyosin pfam00261
Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 ...
 368-507 9.12e-05

Tropomyosin; Tropomyosin is an alpha-helical protein that forms a coiled-coil structure of 2 parallel helices containing 2 sets of 7 alternating actin binding sites. The protein is best known for its role in regulating the interaction between actin and myosin in muscle contraction, but is also involved in the organization and dynamics of the cytoskeleton in non-muscle cells. There are multiple cell-specific isoforms, expressed by alternative promoters and alternative RNA processing of at least four genes. Muscle isoforms of tropomyosin are characterized by having 284 amino acid residues and a highly conserved N-terminal region, whereas non-muscle forms are generally smaller and are heterogeneous in their N-terminal region.


Pssm-ID: 459736 [Multi-domain]  Cd Length: 235  Bit Score: 45.79  E-value: 9.12e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  368 KRCKELEIQLQEVQsENARLAEENLQLNEKAgwAGQVESENADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLK--- 444
Cdd:pfam00261    1 KKMQQIKEELDEAE-ERLKEAMKKLEEAEKR--AEKAEAEVAALNRRIQLLEEELERTEERLAEALEKLEEAEKAADese 77

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024466778  445 HMRDVAERRQL--------LEAEHKEALLVLQE---KQEEV-RRLQQAQAEAKREHEGAvQLLEARVKDLEDQCR 507
Cdd:pfam00261   78 RGRKVLENRALkdeekmeiLEAQLKEAKEIAEEadrKYEEVaRKLVVVEGDLERAEERA-ELAESKIVELEEELK 151
SH3_ASPP2 cd11953
Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2; ASPP2 is the full ...
 1546-1605 9.13e-05

Src Homology 3 (SH3) domain of Apoptosis Stimulating of p53 protein 2; ASPP2 is the full length form of the previously-identified tumor supressor, p53-binding protein 2 (p53BP2). ASPP2 activates the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73). It plays a central role in regulating apoptosis and cell growth; ASPP2-deficient mice show postnatal death. Downregulated expression of ASPP2 is frequently found in breast tumors, lung cancer, and diffuse large B-cell lymphoma where it is correlated with a poor clinical outcome. ASPP2 contains a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain at its C-terminal half. The SH3 domain and the ANK repeats of ASPP2 contribute to the p53 binding site; they bind to the DNA binding domain of p53. 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: 212886 [Multi-domain]  Cd Length: 57  Bit Score: 41.86  E-value: 9.13e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1546 IFVALFDYDPvsmsPNPDaaeeELPFKEGQILKVCGDKDADG--FYRGECAGREGYIPCNMV 1605
Cdd:cd11953      2 VVYALWDYEG----ESDD----ELSFKEGDCMTILRREDEDEteWWWARLNDKEGYVPRNLL 55
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1548-1607 9.46e-05

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: 41.63  E-value: 9.46e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1548 VALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDADgFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11840      3 IALFPYTAQN--------EDELSFQKGDIINVLSKDDPD-WWRGELNGQTGLFPSNYVEP 53
YqiK COG2268
Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];
348-497 9.64e-05

Uncharacterized membrane protein YqiK, contains Band7/PHB/SPFH domain [Function unknown];


Pssm-ID: 441869 [Multi-domain]  Cd Length: 439  Bit Score: 47.17  E-value: 9.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  348 ELKKKRKKCENL-----EHEVRKKHKRCKELEIQlQEVQSENARLAEENlqlNEKAgwagqveSENADLKLQVVLVTKER 422
Cdd:COG2268    196 EIIRDARIAEAEaeretEIAIAQANREAEEAELE-QEREIETARIAEAE---AELA-------KKKAEERREAETARAEA 264

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  423 DsviqrnQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVR-----RLQQAQAEAKREHEGAVQLLEA 497
Cdd:COG2268    265 E------AAYEIAEANAEREVQRQLEIAEREREIELQEKEAEREEAELEADVRkpaeaEKQAAEAEAEAEAEAIRAKGLA 338
SH3_Intersectin2_5 cd11996
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 1688-1746 9.89e-05

Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) 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. ITSN2 also functions as a specific GEF for Cdc42 activation in epithelial morphogenesis, and is required in mitotic spindle orientation. 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 fifth SH3 domain (or SH3E) of ITSN2 is expected to bind protein partners, similar to ITSN1 which 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: 212929 [Multi-domain]  Cd Length: 54  Bit Score: 41.89  E-value: 9.89e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11996      3 VIAMYDYT-------ANNEDELSFSKGQLINVLNKDDPD-WWQGEINGVTGLFPSNYVK 53
TMF_TATA_bd pfam12325
TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil ...
 403-512 1.14e-04

TATA element modulatory factor 1 TATA binding; This is the C-terminal conserved coiled coil region of a family of TATA element modulatory factor 1 proteins conserved in eukaryotes. The proteins bind to the TATA element of some RNA polymerase II promoters and repress their activity. by competing with the binding of TATA binding protein. TMF1_TATA_bd is the most conserved part of the TMFs. TMFs are evolutionarily conserved golgins that bind Rab6, a ubiquitous ras-like GTP-binding Golgi protein, and contribute to Golgi organization in animal and plant cells. The Rab6-binding domain appears to be the same region as this C-terminal family.


Pssm-ID: 432481 [Multi-domain]  Cd Length: 115  Bit Score: 43.30  E-value: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  403 QVESENADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEvrrlqqaqa 482
Cdd:pfam12325   23 RLEGELASLKEELARLEAQRDEARQEIVKLMKENEELKELKKELEELEKELKELEQRYETTLELLGEKSEE--------- 93

                           90       100       110
                   ....*....|....*....|....*....|
gi 2024466778  483 eakrehegaVQLLEARVKDLEDQCRSQTEQ 512
Cdd:pfam12325   94 ---------VEELKADVEDLKEMYREQVQQ 114
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 1546-1607 1.16e-04

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. 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: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 41.48  E-value: 1.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1546 IFVALFDYDPvsmspnpdAAEEELPFKEGQILKVCgDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11766      1 PAVVKFNYEA--------QREDELSLRKGDRVLVL-EKSSDGWWRGECNGQVGWFPSNYVTE 53
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
337-529 1.41e-04

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 46.83  E-value: 1.41e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEenlQLNEKAGWAGQVESENADLKLQVV 416
Cdd:COG4913    682 ASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLARLELRALLEERFAAA 758

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  417 LVTKERDSVI----QRNQGLQTKLENLE-QVLKHMR---------------------DVAERRQLLEAEHkeallvLQEK 470
Cdd:COG4913    759 LGDAVERELRenleERIDALRARLNRAEeELERAMRafnrewpaetadldadleslpEYLALLDRLEEDG------LPEY 832

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778  471 QEEVRRLQQAQAEAKREHegavqLLEArvkdLEDQCRSQTEQFSLLSQELKQFRLQTGK 529
Cdd:COG4913    833 EERFKELLNENSIEFVAD-----LLSK----LRRAIREIKERIDPLNDSLKRIPFGPGR 882
SH3_VAV_2 cd11830
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ...
 1568-1607 1.45e-04

C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. 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: 212764 [Multi-domain]  Cd Length: 54  Bit Score: 41.08  E-value: 1.45e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024466778 1568 ELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11830     15 ELSLKEGDVVKIYNKKGQQGWWRGEINGRIGWFPSTYVEE 54
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
 1690-1742 1.73e-04

Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) proteins; The MPP/p55 subfamily of MAGUK (membrane-associated guanylate kinase) proteins includes at least eight vertebrate members (MPP1-7 and CASK), four Drosophila proteins (Stardust, Varicose, CASK and Skiff), and other similar proteins; they all contain one each of the core of three domains characteristic of MAGUK proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, most members except for MPP1 contain N-terminal L27 domains and some also contain a Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. CASK has an additional calmodulin-dependent kinase (CaMK)-like domain at the N-terminus. Members of this subfamily are scaffolding proteins that play important roles in regulating and establishing cell polarity, cell adhesion, and synaptic targeting and transmission, among others. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212796  Cd Length: 61  Bit Score: 41.03  E-value: 1.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSPNADAEAELTFSAGDIITVFgSMDDDGFY----YGELNQQRGLVPS 1742
Cdd:cd11862      4 ALFDYDPEEDPLIPCKEAGLSFKKGDILQIV-NQDDPNWWqarkVGDPNGRAGLIPS 59
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
 1687-1745 1.74e-04

Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called Jouberin, is expressed in high levels in the brain, gonad tissues, and skeletal muscle. It is an adaptor protein that interacts with the small GTPase Rab8a and regulates it distribution and function, affecting cilium formation and vesicle transport. Mutations in the AHI-1 gene can cause Joubert syndrome, a disorder characterized by brainstem malformations, cerebellar aplasia/hypoplasia, and retinal dystrophy. AHI-1 variation is also associated with susceptibility to schizophrenia and type 2 diabetes mellitus progression. AHI-1 contains WD40 and SH3 domains. 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: 212746 [Multi-domain]  Cd Length: 52  Bit Score: 40.96  E-value: 1.74e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1687 SMVAVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGEL-NQQRGLVPSNFL 1745
Cdd:cd11812      1 TVVALYDYTANRSD-------ELTIHRGDIIRVL-YKDNDNWWFGSLvNGQQGYFPANYV 52
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
 1686-1751 1.84e-04

Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST (Epidermal growth factor receptor-associated protein with SH3 and TAM domain) or Hbp (Hrs binding protein), is part of the endosomal sorting complex required for transport (ESCRT-0). It plays a role in sorting mono-ubiquinated endosomal cargo for trafficking to the lysosome for degradation. It is also involved in the regulation of exocytosis. STAMs were discovered as proteins that are highly phosphorylated following cytokine and growth factor stimulation. They function in cytokine signaling and surface receptor degradation, as well as regulate Golgi morphology. They associate with many proteins including Jak2 and Jak3 tyrosine kinases, Hrs, AMSH, and UBPY. STAM adaptor proteins contain VHS (Vps27, Hrs, STAM homology), ubiquitin interacting (UIM), and SH3 domains. 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: 212896 [Multi-domain]  Cd Length: 57  Bit Score: 41.16  E-value: 1.84e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1686 RSMVAVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFleaVTSD 1751
Cdd:cd11963      2 RKVRALYDFEAVEDN-------ELTFKHGEIIIVLDDSDAN-WWKGENHRGVGLFPSNF---VTTD 56
SH3_Irsp53_BAIAP2L cd11779
Src Homology 3 domain of Insulin Receptor tyrosine kinase Substrate p53, Brain-specific ...
 1703-1747 1.85e-04

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: 41.15  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2024466778 1703 ADAEAELTFSAGDIITVFGSMDDDGFYYGEL--NQQRGLVPSNFLEA 1747
Cdd:cd11779     11 AGGETQLSFEEGDVITLLGPEPRDGWHYGENerSGRRGWFPIAYTEP 57
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 336-526 1.90e-04

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 46.27  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEF---ELKKKRKKCENLEHEVRKKH------KRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVES 406
Cdd:pfam05557  149 SEAEQLRQNLEKqqsSLAEAEQRIKELEFEIQSQEqdseivKNSKSELARIPELEKELERLREHNKHLNENIENKLLLKE 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  407 ENADLKLQVVLVTKERDSVIQrnqgLQTKLENLEQVLKHMRDVAErrqlleaEHKEALLVLQEKQEEVRRLQQAQAEAKR 486
Cdd:pfam05557  229 EVEDLKRKLEREEKYREEAAT----LELEKEKLEQELQSWVKLAQ-------DTGLNLRSPEDLSRRIEQLQQREIVLKE 297

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 2024466778  487 EH---EGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQF-----RLQ 526
Cdd:pfam05557  298 ENsslTSSARQLEKARRELEQELAQYLKKIEDLNKKLKRHkalvrRLQ 345
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
 1549-1604 2.25e-04

Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. 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: 212741 [Multi-domain]  Cd Length: 57  Bit Score: 40.83  E-value: 2.25e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1549 ALFDYDPvsmsPNPDaaeeELPFKEGQILKVC--GDKDADGFYRGECAGREGYIPCNM 1604
Cdd:cd11807      5 ALFDYEA----ENGD----ELSFREGDELTVLrkGDDDETEWWWARLNDKEGYVPRNL 54
SH3_DNMBP_N3 cd11796
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
 1566-1605 2.39e-04

Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or Tuba is a cdc42-specific guanine nucleotide exchange factor (GEF) that contains four N-terminal SH3 domains, a central RhoGEF [or Dbl homology (DH)] domain followed by a Bin/Amphiphysin/Rvs (BAR) domain, and two C-terminal SH3 domains. It provides a functional link between dynamin and key regulatory proteins of the actin cytoskeleton. It plays an important role in regulating cell junction configuration. The four N-terminal SH3 domains of DNMBP binds the GTPase dynamin, which plays an important role in the fission of endocytic vesicles. 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: 212730  Cd Length: 51  Bit Score: 40.42  E-value: 2.39e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024466778 1566 EEELPFKEGQILKVCGDKDaDGFYRGECAGREGYIPCNMV 1605
Cdd:cd11796     13 DEELDLREGDVVTITGILD-KGWFRGELNGRRGIFPEGFV 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 372-526 2.72e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 2.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  372 ELEIQLQ--EVQSENAR----LAEEnLQLNEKAGWAGQVESENADLKLQvvlvTKERDSVIQRNQGLQTKLENLEqvlkh 445
Cdd:COG1196    197 ELERQLEplERQAEKAEryreLKEE-LKELEAELLLLKLRELEAELEEL----EAELEELEAELEELEAELAELE----- 266

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  446 mrdvAERRQLlEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQL---LEARVKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG1196    267 ----AELEEL-RLELEELELELEEAQAEEYELLAELARLEQDIARLEERrreLEERLEELEEELAELEEELEELEEELEE 341


                   ....
gi 2024466778  523 FRLQ 526
Cdd:COG1196    342 LEEE 345
SH3_CSK cd11769
Src Homology 3 domain of C-terminal Src kinase; CSK is a cytoplasmic (or nonreceptor) tyr ...
 1548-1607 2.77e-04

Src Homology 3 domain of C-terminal Src kinase; CSK is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, CSK is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. CSK catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. It is expressed in a wide variety of tissues and plays a role, as a regulator of Src, in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. In addition, CSK also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. 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: 212703 [Multi-domain]  Cd Length: 57  Bit Score: 40.36  E-value: 2.77e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1548 VALFDYdpvsmspnPDAAEEELPFKEGQILKVCGD-KDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11769      5 IAKYNF--------NGASEEDLPFKKGDILTIVAVtKDPNWYKAKNKDGREGMIPANYVQK 57
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 1690-1746 2.85e-04

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). 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: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 40.48  E-value: 2.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11827      4 ALYAYDAQDTD-------ELSFNEGDIIEIL-KEDPSGWWTGRLRGKEGLFPGNYVE 52
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 340-422 3.17e-04

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 44.72  E-value: 3.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  340 QQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKagwAGQVESENADLKLQVVLVT 419
Cdd:COG4026    128 PEYNELREELLELKEKIDEIAKEKEKLTKENEELESELEELREEYKKLREENSILEEE---FDNIKSEYSDLKSRFEELL 204


                   ...
gi 2024466778  420 KER 422
Cdd:COG4026    205 KKR 207
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
 324-501 3.22e-04

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 45.40  E-value: 3.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  324 HENFPPKNAVADQESSQQIQQLEFELKKKRKKCENLEH---EVRKKHKRC----KELEIQLQEVQSENARLaEENLQLNE 396
Cdd:pfam05667  312 APAATSSPPTKVETEEELQQQREEELEELQEQLEDLESsiqELEKEIKKLessiKQVEEELEELKEQNEEL-EKQYKVKK 390

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  397 KAgwAGQVES-ENADLKLQVVLvtkerDSVIQRNQGLQTKLEnleqvlKHMR-DVAERRQLLEA---EHKEALLVLQEKQ 471
Cdd:pfam05667  391 KT--LDLLPDaEENIAKLQALV-----DASAQRLVELAGQWE------KHRVpLIEEYRALKEAksnKEDESQRKLEEIK 457

                          170       180       190
                   ....*....|....*....|....*....|...
gi 2024466778  472 EEVRRLQQAQAEAKREHEGAVQL---LEARVKD 501
Cdd:pfam05667  458 ELREKIKEVAEEAKQKEELYKQLvaeYERLPKD 490
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 341-585 3.66e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 45.48  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  341 QIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENlqlNEKAGWAGQVESENADLKLQVVLVTK 420
Cdd:pfam05483  100 ELKQKENKLQENRKIIEAQRKAIQELQFENEKVSLKLEEEIQENKDLIKEN---NATRHLCNLLKETCARSAEKTKKYEY 176

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  421 ERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLleaehkEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQLL----- 495
Cdd:pfam05483  177 EREETRQVYMDLNNNIEKMILAFEELRVQAENARL------EMHFKLKEDHEKIQHLEEEYKKEINDKEKQVSLLliqit 250

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  496 --EARVKDL-------EDQCRSQTEQFSLLSQELKQFrlqTGKIDLLTSTLVTSELPLALCSSTpQPHWEKDSPGPALLA 566
Cdd:pfam05483  251 ekENKMKDLtflleesRDKANQLEEKTKLQDENLKEL---IEKKDHLTKELEDIKMSLQRSMST-QKALEEDLQIATKTI 326

                          250       260
                   ....*....|....*....|.
gi 2024466778  567 HQST--KKVHNEETNESESSQ 585
Cdd:pfam05483  327 CQLTeeKEAQMEELNKAKAAH 347
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 343-530 3.82e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 45.73  E-value: 3.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  343 QQLEfELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESENADLKLQVVLVTKER 422
Cdd:TIGR00618  373 QQHT-LTQHIHTLQQQKTTLTQKLQSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTA 451

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  423 DSVIQRN---QGLQTKLENLEQVLKHMRDVAERRqllEAEHKEALLVLQEKQEEVRRL--QQAQAEAKREH--------- 488
Cdd:TIGR00618  452 QCEKLEKihlQESAQSLKEREQQLQTKEQIHLQE---TRKKAVVLARLLELQEEPCPLcgSCIHPNPARQDidnpgpltr 528

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 2024466778  489 -----EGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQFRLQTGKI 530
Cdd:TIGR00618  529 rmqrgEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSIL 575
SH3_srGAP cd11809
Src homology 3 domain of Slit-Robo GTPase Activating Proteins; Slit-Robo GTPase Activating ...
 1689-1745 3.86e-04

Src homology 3 domain of Slit-Robo GTPase Activating Proteins; Slit-Robo GTPase Activating Proteins (srGAPs) are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. Vertebrates contain three isoforms of srGAPs (srGAP1-3), all of which are expressed during embryonic and early development in the nervous system but with different localization and timing. A fourth member has also been reported (srGAP4, also called ARHGAP4). srGAPs contain an N-terminal F-BAR domain, a Rho GAP 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: 212743 [Multi-domain]  Cd Length: 53  Bit Score: 40.08  E-value: 3.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFL 1745
Cdd:cd11809      3 TAQFDYT-------GRSERELSFKKGDSLTLYRQVSDD-WWRGQLNGQDGLVPHKYI 51
SH3_MPP3 cd12039
Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); ...
 1688-1742 3.90e-04

Src Homology 3 domain of Membrane Protein, Palmitoylated 3 (or MAGUK p55 subfamily member 3); MPP3 is a scaffolding protein that colocalizes with MPP5 and CRB1 at the subdpical region adjacent to adherens junctions and may function in photoreceptor polarity. It interacts with some nectins and regulates their trafficking and processing. Nectins are cell-cell adhesion proteins involved in the establishment apical-basal polarity at cell adhesion sites. It is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains two L27 domains followed by the core of three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212972  Cd Length: 62  Bit Score: 40.33  E-value: 3.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNPKESSPNADAEAELTFSAGDIITVFgSMDDDGFY----YGELNQQRGLVPS 1742
Cdd:cd12039      2 MRALFDYNPYEDRAIPCQEAGLPFKRRDILEVV-SQDDPTWWqakrVGDTNLRAGLIPS 59
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 1687-1746 4.16e-04

Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This family is composed of the tandem SH3 domains of p47phox subunit of NADPH oxidase and Nox Organizing protein 1 (NoxO1), the four SH3 domains of Tks4 (Tyr kinase substrate with four SH3 domains), the five SH3 domains of Tks5, the SH3 domain of obscurin, Myosin-I, and similar domains. Most members of this group also contain Phox homology (PX) domains, except for obscurin and Myosin-I. p47phox and NoxO1 are regulators of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) and nonphagocytic NADPH oxidase Nox1, respectively. They play roles in the activation of their respective NADPH oxidase, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Tks proteins are Src substrates and scaffolding proteins that play important roles in the formation of podosomes and invadopodia, the dynamic actin-rich structures that are related to cell migration and cancer cell invasion. Obscurin is a giant muscle protein that plays important roles in the organization and assembly of the myofibril and the sarcoplasmic reticulum. Type I myosins (Myosin-I) are actin-dependent motors in endocytic actin structures and actin patches. They play roles in membrane traffic in endocytic and secretory pathways, cell motility, and mechanosensing. Myosin-I contains an N-terminal actin-activated ATPase, a phospholipid-binding TH1 (tail homology 1) domain, and a C-terminal extension which includes an F-actin-binding TH2 domain, an SH3 domain, and an acidic peptide that participates in activating the Arp2/3complex. The SH3 domain of myosin-I is required for myosin-I-induced actin polymerization. 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: 212790 [Multi-domain]  Cd Length: 53  Bit Score: 39.93  E-value: 4.16e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1687 SMVAVFDYNPKESSpnadaeaELTFSAGDIITVFGSmDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11856      1 SYVAIADYEAQGDD-------EISLQEGEVVEVLEK-NDSGWWYVRKGDKEGWVPASYLE 52
SH3_Endophilin_B cd11802
Src homology 3 domain of Endophilin-B; Endophilins play roles in synaptic vesicle formation, ...
 1690-1744 4.24e-04

Src homology 3 domain of Endophilin-B; Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They are classified into two types, A and B. Vertebrates contain two endophilin-B isoforms. Endophilin-B proteins are cytoplasmic proteins expressed mainly in the heart, placenta, and skeletal muscle. Endophilins contain an N-terminal N-BAR domain (BAR domain with an additional N-terminal amphipathic helix), followed by a variable region containing proline clusters, 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: 212736 [Multi-domain]  Cd Length: 52  Bit Score: 39.96  E-value: 4.24e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFG--SMDDDgFYYGELNQQRGLVPSNF 1744
Cdd:cd11802      4 VLYDYDAEDST-------ELSLLADEVITVYElpGMDED-YMMGERGSQRGKVPVAY 52
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
 1690-1747 4.30e-04

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) and PACSIN 2; PACSIN 1 or Syndapin I (Synaptic dynamin-associated protein I) is expressed specifically in the brain and is localized in neurites and synaptic boutons. It binds the brain-specific proteins dynamin I, synaptojanin, synapsin I, and neural Wiskott-Aldrich syndrome protein (nWASP), and functions as a link between the cytoskeletal machinery and synaptic vesicle endocytosis. PACSIN 1 interacts with huntingtin and may be implicated in the neuropathology of Huntington's disease. PACSIN 2 or Syndapin II is expressed ubiquitously and is involved in the regulation of tubulin polymerization. It associates with Golgi membranes and forms a complex with dynamin II which is crucial in promoting vesicle formation from the trans-Golgi network. PACSINs act as regulators of cytoskeletal and membrane dynamics. Vetebrates harbor three isoforms with distinct expression patterns and specific functions. PACSINs contain 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: 212931 [Multi-domain]  Cd Length: 56  Bit Score: 39.93  E-value: 4.30e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1690 AVFDYNPKEsspnadaEAELTFSAGDIITVFGSMDDDGFYYGELNQ-QRGLVPSNFLEA 1747
Cdd:cd11998      5 ALYDYDGQE-------QDELSFKAGDELTKLEDEDEQGWCKGRLDSgQVGLYPANYVEP 56
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
432-522 4.31e-04

Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 41.80  E-value: 4.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  432 LQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQE-----EVRR------LQQAQAEAKREHEGAVQLLEARVK 500
Cdd:COG1382      9 VQNQLAQLQQLQQQLQAVAAQKQQVESELKEAEKALEELEKlpddaEVYKsvgnllVKTDKEEVIKELEEKKETLELRLK 88

                           90       100
                   ....*....|....*....|..
gi 2024466778  501 DLEDQCRSQTEQFSLLSQELKQ 522
Cdd:COG1382     89 TLEKQEERLQKQLEELQEKLQE 110
gimC_beta TIGR02338
prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular ...
 430-522 4.51e-04

prefoldin, beta subunit, archaeal; Chaperonins are cytosolic, ATP-dependent molecular chaperones, with a conserved toroidal architecture, that assist in the folding of nascent and/or denatured polypeptide chains. The group I chaperonin system consists of GroEL and GroES, and is found (usually) in bacteria and organelles of bacterial origin. The group II chaperonin system, called the thermosome in Archaea and TRiC or CCT in the Eukaryota, is structurally similar but only distantly related. Prefoldin, also called GimC, is a complex in Archaea and Eukaryota, that works with group II chaperonins. Members of this protein family are the archaeal clade of the beta class of prefoldin subunit. Closely related, but outside the scope of this family are the eukaryotic beta-class prefoldin subunits, Gim-1,3,4 and 6. The alpha class prefoldin subunits are more distantly related.


Pssm-ID: 131391 [Multi-domain]  Cd Length: 110  Bit Score: 41.57  E-value: 4.51e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  430 QGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQE-----EVRR------LQQAQAEAKREHEGAVQLLEAR 498
Cdd:TIGR02338    3 PQVQNQLAQLQQLQQQLQAVATQKQQVEAQLKEAEKALEELERlpddtPVYKsvgnllVKTDKEEAIQELKEKKETLELR 82

                           90       100
                   ....*....|....*....|....
gi 2024466778  499 VKDLEDQCRSQTEQFSLLSQELKQ 522
Cdd:TIGR02338   83 VKTLQRQEERLREQLKELQEKIQE 106
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 341-526 4.64e-04

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 45.33  E-value: 4.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  341 QIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVqSENARLAEENLQLNEKAgwAGQVEsenADLKLqVVLVTK 420
Cdd:COG3096    414 QYQQAVQALEKARALCGLPDLTPENAEDYLAAFRAKEQQA-TEEVLELEQKLSVADAA--RRQFE---KAYEL-VCKIAG 486

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  421 ErdsvIQRNQGLQTKLENLEQVLKHmRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAVQL------ 494
Cdd:COG3096    487 E----VERSQAWQTARELLRRYRSQ-QALAQRLQQLRAQLAELEQRLRQQQNAERLLEEFCQRIGQQLDAAEELeellae 561

                          170       180       190
                   ....*....|....*....|....*....|..
gi 2024466778  495 LEARVKDLEDQCRSQTEQFSLLSQELKQFRLQ 526
Cdd:COG3096    562 LEAQLEELEEQAAEAVEQRSELRQQLEQLRAR 593
SH3_SGSM3 cd11813
Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called ...
 1706-1746 4.76e-04

Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called Merlin-associated protein (MAP), RUN and SH3 domain-containing protein (RUSC3), RUN and TBC1 domain-containing protein 3 (RUTBC3), Rab GTPase-activating protein 5 (RabGAP5), or Rab GAP-like protein (RabGAPLP). It is expressed ubiquitously and functions as a regulator of small G protein RAP- and RAB-mediated neuronal signaling. It is involved in modulating NGF-mediated neurite outgrowth and differentiation. It also interacts with the tumor suppressor merlin and may play a role in the merlin-associated suppression of cell growth. SGSM3 contains TBC, SH3, and RUN domains. 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: 212747  Cd Length: 53  Bit Score: 39.79  E-value: 4.76e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2024466778 1706 EAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11813     13 DDELGFRKNDIITII-SQKDEHCWVGELNGLRGWFPAKFVE 52
SH3_CIN85_3 cd12057
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 1703-1746 4.91e-04

Third Src Homology 3 domain (SH3C) 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 third SH3 domain (SH3C) of CIN85. SH3C has been shown to bind 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: 212990 [Multi-domain]  Cd Length: 56  Bit Score: 39.88  E-value: 4.91e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 2024466778 1703 ADAEAELTFSAGDIITVFgSMD--DDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12057     10 AQNEDELTIKEGDIVTLI-SKDciDAGWWEGELNGRRGVFPDNFVK 54
SH3_Intersectin1_5 cd11995
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
 1688-1746 5.10e-04

Fifth Src homology 3 domain (or SH3E) 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 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: 212928 [Multi-domain]  Cd Length: 54  Bit Score: 39.55  E-value: 5.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11995      3 VIGMYDYT-------AQNDDELAFSKGQIINVLNKEDPD-WWKGELNGQVGLFPSNYVK 53
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 320-539 5.27e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.96  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  320 ALEGHENFPPKN-AVADQESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEKA 398
Cdd:TIGR00618  611 ACEQHALLRKLQpEQDLQDVRLHLQQCSQELALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKE 690

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  399 GWAGQVESENADLKLQVVLVTKERDSVIQRNQ----------GLQTKLENLEQVLKHMRdvAERRQLLEAEHKEALLVLQ 468
Cdd:TIGR00618  691 QLTYWKEMLAQCQTLLRELETHIEEYDREFNEienassslgsDLAAREDALNQSLKELM--HQARTVLKARTEAHFNNNE 768

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778  469 EKQEEVRRLQQAQaEAKREHEGAVQLLEARV---KDLEDQCRSQT---EQFSLLSQELKQFRLQT--GKIDLLTSTLVT 539
Cdd:TIGR00618  769 EVTAALQTGAELS-HLAAEIQFFNRLREEDThllKTLEAEIGQEIpsdEDILNLQCETLVQEEEQflSRLEEKSATLGE 846
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 87-513 5.39e-04

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 45.17  E-value: 5.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   87 ADYSFLVSQNMKLLSALEDLRHRCSSLTeensllrrSCFPETEEKVKHL-KRKNAELAVIAKrLEERARKLQEANLKVVT 165
Cdd:pfam01576  138 EDILLLEDQNSKLSKERKLLEERISEFT--------SNLAEEEEKAKSLsKLKNKHEAMISD-LEERLKKEEKGRQELEK 208

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  166 APVPLKGSSLELckkafaRQRAKDLTEQASALLAKdkqieaLQQECRELQAKLiaGKGDPRCLNVVEFDRLLRESQKEVL 245
Cdd:pfam01576  209 AKRKLEGESTDL------QEQIAELQAQIAELRAQ------LAKKEEELQAAL--ARLEEETAQKNNALKKIRELEAQIS 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  246 RLQRQIALknfkECLRPSKGSSggslpsAASCPGPALNAC------SKDSPAAKEvcsggpalggAAHGKVEPGVLPLGP 319
Cdd:pfam01576  275 ELQEDLES----ERAARNKAEK------QRRDLGEELEALkteledTLDTTAAQQ----------ELRSKREQEVTELKK 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  320 ALE----GHE----NFPPKNAVADQESSQQIQQLE---FELKKKRKKCE----NLEHEVR--------KKHKRcKELEIQ 376
Cdd:pfam01576  335 ALEeetrSHEaqlqEMRQKHTQALEELTEQLEQAKrnkANLEKAKQALEsenaELQAELRtlqqakqdSEHKR-KKLEGQ 413

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  377 LQEVQSENARLAEENLQLNEKAGwAGQVESENA-----DLKLQVVLVTKERDSViqrNQGLQTKLENLEQVLKHMRDVAE 451
Cdd:pfam01576  414 LQELQARLSESERQRAELAEKLS-KLQSELESVssllnEAEGKNIKLSKDVSSL---ESQLQDTQELLQEETRQKLNLST 489

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778  452 RRQLLEAEhKEALLVLQEKQEEVRR--------LQQAQAEAKREHE---GAVQLLEARVKDLEDQCRSQTEQF 513
Cdd:pfam01576  490 RLRQLEDE-RNSLQEQLEEEEEAKRnverqlstLQAQLSDMKKKLEedaGTLEALEEGKKRLQRELEALTQQL 561
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 1690-1746 5.77e-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: 39.59  E-value: 5.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKEsspnadaEAELTFSAGDIITVFGSMDDdGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12055      4 VAFSYLPQN-------EDELELKVGDIIEVVGEVEE-GWWEGVLNGKTGMFPSNFIK 52
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1690-1747 5.80e-04

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: 39.65  E-value: 5.80e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1690 AVFDYNPKesspNADaeaELTFSAGDIITVFGSMD-DDGFYYGELNQQRGLVPSNFLEA 1747
Cdd:cd11836      4 ALYAFEAR----NPD---EISFQPGDIIQVDESQVaEPGWLAGELKGKTGWFPANYVEK 55
SH3_p67phox_C cd12046
C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, ...
 1688-1746 6.28e-04

C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, also called Neutrophil cytosol factor 2 (NCF-2), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox plays a regulatory role and contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. It binds, via its C-terminal SH3 domain, to a proline-rich region of p47phox and upon activation, this complex assembles with flavocytochrome b558, the Nox2-p22phox heterodimer. Concurrently, RacGTP translocates to the membrane and interacts with the TPR domain of p67phox, which leads to the activation of NADPH oxidase. The PB1 domain of p67phox binds to its partner PB1 domain in p40phox, and this facilitates the assembly of p47phox-p67phox at the membrane. 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: 212979 [Multi-domain]  Cd Length: 53  Bit Score: 39.40  E-value: 6.28e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYnpkESSPNADaeaeLTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12046      2 VVALFSY---EASQPED----LEFQKGDVILVLSKVNED-WLEGQCKGKIGIFPSAFVE 52
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 336-503 6.36e-04

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 44.72  E-value: 6.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRckeLEIQLQEVQseNARLAEENLQlnekagwagQVESENADLKLQV 415
Cdd:pfam15921  492 ESSERTVSDLTASLQEKERAIEATNAEITKLRSR---VDLKLQELQ--HLKNEGDHLR---------NVQTECEALKLQM 557

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VlvtkERDSVIQRnqgLQTKLENLEQVLKHMRDVAERRQLLEAEhkeallvlQEKQEEVRRLQQAQAEA-KREHEGAVQL 494
Cdd:pfam15921  558 A----EKDKVIEI---LRQQIENMTQLVGQHGRTAGAMQVEKAQ--------LEKEINDRRLELQEFKIlKDKKDAKIRE 622


                   ....*....
gi 2024466778  495 LEARVKDLE 503
Cdd:pfam15921  623 LEARVSDLE 631
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
 1549-1606 6.43e-04

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. It is ubiquitously expressed in all tissues throughout development and is important in cell cycle progression, motility, morphogenesis, and angiogenesis. In lymphocytes, GRB2 is associated with antigen receptor signaling components. GRB2 contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The C-terminal SH3 domain of GRB2 binds to Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, as well as to the proline-rich C-terminus of FGRF2. SH3 domains are protein interaction domains that typically 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: 212882 [Multi-domain]  Cd Length: 53  Bit Score: 39.44  E-value: 6.43e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1549 ALFDYDPvsmspnpdAAEEELPFKEGQILKVCGDKDADgFYRGECAGREGYIPCNMVS 1606
Cdd:cd11949      4 ALFDFDP--------QEDGELGFRRGDFIEVMDNSDPN-WWKGACHGQTGMFPRNYVT 52
SH3_Sdc25 cd11883
Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is ...
 1689-1744 6.75e-04

Src Homology 3 domain of Sdc25/Cdc25 guanine nucleotide exchange factors; This subfamily is composed of the Saccharomyces cerevisiae guanine nucleotide exchange factors (GEFs) Sdc25 and Cdc25, and similar proteins. These GEFs regulate Ras by stimulating the GDP/GTP exchange on Ras. Cdc25 is involved in the Ras/PKA pathway that plays an important role in the regulation of metabolism, stress responses, and proliferation, depending on available nutrients and conditions. Proteins in this subfamily contain an N-terminal SH3 domain as well as REM (Ras exchanger motif) and RasGEF domains at the C-terminus. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212816  Cd Length: 55  Bit Score: 39.19  E-value: 6.75e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1689 VAVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDD---DGFYYGELNQ-QRGLVPSNF 1744
Cdd:cd11883      3 VALYDFTPKSKN-------QLSFKAGDIIYVLNKDPSgwwDGVIISSSGKvKRGWFPSNY 55
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 116-524 7.08e-04

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 44.57  E-value: 7.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  116 ENSLLRRSCFPETEEKVKHLKRKNAELAV------IAKRLEERARKLQEANLKVVTAPVPLKGSSLELCKKAFARQRAKD 189
Cdd:TIGR00618  362 EVATSIREISCQQHTLTQHIHTLQQQKTTltqklqSLCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQQELQQRYAE 441

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  190 LTEQASALLAK-DKQIEALQQECRELQAKLIAGKGDPRCLnvvefdrLLRESQKEVLRLQRqiaLKNFKECLRPSKGSSg 268
Cdd:TIGR00618  442 LCAAAITCTAQcEKLEKIHLQESAQSLKEREQQLQTKEQI-------HLQETRKKAVVLAR---LLELQEEPCPLCGSC- 510

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  269 gslpsaaSCPGPALNACSKDSPAAKEVCSGgpALGGAAHGKVEPGVLPLGPALEGH-ENFPPKNAVADQESS---QQIQQ 344
Cdd:TIGR00618  511 -------IHPNPARQDIDNPGPLTRRMQRG--EQTYAQLETSEEDVYHQLTSERKQrASLKEQMQEIQQSFSiltQCDNR 581

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  345 LEFELKKKRKKCENLEHEVRK-------------KHKRCKELEIQLQEVQSENARLAEEnLQLNEKAGWAGQVESENADL 411
Cdd:TIGR00618  582 SKEDIPNLQNITVRLQDLTEKlseaedmlaceqhALLRKLQPEQDLQDVRLHLQQCSQE-LALKLTALHALQLTLTQERV 660

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  412 KLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEallVLQEKQEEVRRLQQAQAEAKREHEGA 491
Cdd:TIGR00618  661 REHALSIRVLPKELLASRQLALQKMQSEKEQLTYWKEMLAQCQTLLRELET---HIEEYDREFNEIENASSSLGSDLAAR 737

                          410       420       430
                   ....*....|....*....|....*....|...
gi 2024466778  492 VQLLEARVKDLEDQCRSQteqfsLLSQELKQFR 524
Cdd:TIGR00618  738 EDALNQSLKELMHQARTV-----LKARTEAHFN 765
SH3_MPP1 cd12080
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); ...
 1688-1742 7.64e-04

Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); MPP1, also called 55 kDa erythrocyte membrane protein (p55), is a ubiquitously-expressed scaffolding protein that plays roles in regulating neutrophil polarity, cell shape, hair cell development, and neural development and patterning of the retina. It was originally identified as an erythrocyte protein that stabilizes the actin cytoskeleton to the plasma membrane by forming a complex with 4.1R protein and glycophorin C. MPP1 is one of seven vertebrate homologs of the Drosophila Stardust protein, which is required in establishing cell polarity, and it contains the three domains characteristic of MAGUK (membrane-associated guanylate kinase) proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, it also contains the Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 213013  Cd Length: 62  Bit Score: 39.55  E-value: 7.64e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1688 MVAVFDYNPKESSPNADAEAELTFSAGDIITVFGSmDDDGFYYGELN----QQRGLVPS 1742
Cdd:cd12080      2 MRAQFDYDPKKDNLIPCKEAGLKFQTGDIIQIINK-DDSNWWQGRVEgsgeESAGLIPS 59
SH3_SH3RF3_1 cd11928
First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ...
 1690-1746 8.37e-04

First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ligase; SH3RF3 is also called POSH2 (Plenty of SH3s 2) or SH3MD4 (SH3 multiple domains protein 4). It is a scaffold protein with E3 ubiquitin-protein ligase activity. It was identified in the screen for interacting partners of p21-activated kinase 2 (PAK2). It may play a role in regulating JNK mediated apoptosis in certain conditions. It also interacts with GTP-loaded Rac1. SH3RF3 is highly homologous to SH3RF1; it also contains an N-terminal RING finger domain and four SH3 domains. This model represents the first SH3 domain, located at the N-terminal half, of SH3RF3. 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: 212861  Cd Length: 54  Bit Score: 39.14  E-value: 8.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESspnadaeAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11928      5 ALYSYEGKEP-------GDLKFNKGDIIILRRKVDEN-WYHGELNGCHGFLPASYIQ 53
SH3_HS1 cd12073
Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 ...
 1687-1746 8.54e-04

Src homology 3 domain of Hematopoietic lineage cell-specific protein 1; HS1, also called HCLS1 (hematopoietic cell-specific Lyn substrate 1), is a cortactin homolog expressed specifically in hematopoietic cells. It is an actin regulatory protein that binds the Arp2/3 complex and stabilizes branched actin filaments. It is required for cell spreading and signaling in lymphocytes. It regulates cytoskeletal remodeling that controls lymphocyte trafficking, and it also affects tissue invasion and infiltration of leukemic B cells. Like cortactin, HS1 contains an N-terminal acidic domain, several copies of a repeat domain found in cortactin and HS1, a proline-rich region, and a C-terminal SH3 domain. The N-terminal region binds the Arp2/3 complex and F-actin, while the C-terminal region acts as an adaptor or scaffold that can connect varied proteins that bind the SH3 domain within the actin network. 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: 213006 [Multi-domain]  Cd Length: 55  Bit Score: 39.04  E-value: 8.54e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1687 SMVAVFDYNpkesspnADAEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd12073      2 CAVALYDYQ-------GEGDDEISFDPQETITDI-EMVDEGWWKGTCHGHRGLFPANYVE 53
SH3_Ysc84p_like cd11842
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the ...
 1689-1747 8.80e-04

Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the Saccharomyces cerevisiae proteins, Ysc84p (also called LAS17-binding protein 4, Lsb4p) and Lsb3p, and similar fungal proteins. They contain an N-terminal SYLF domain (also called DUF500) and a C-terminal SH3 domain. Ysc84p localizes to actin patches and plays an important in actin polymerization during endocytosis. The N-terminal domain of both Ysc84p and Lsb3p can bind and bundle actin filaments. A study of the yeast SH3 domain interactome predicts that the SH3 domains of Lsb3p and Lsb4p may function as molecular hubs for the assembly of endocytic complexes. 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: 212776 [Multi-domain]  Cd Length: 55  Bit Score: 38.94  E-value: 8.80e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1689 VAVFDYNPKEsspnadaEAELTFSAGDIITVF---GSMDDdgFYYGELNQQRGLVPSNFLEA 1747
Cdd:cd11842      3 VALYDFAGEQ-------PGDLAFQKGDIITILkksDSQND--WWTGRIGGREGIFPANYVEL 55
SH3_Abp1_fungi_C2 cd11961
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ...
 1690-1746 9.13e-04

Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. 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: 212894 [Multi-domain]  Cd Length: 53  Bit Score: 39.04  E-value: 9.13e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11961      4 ALYDYDAAEDN-------ELSFFENDKIINIEFVDDD-WWLGECHGSRGLFPSNYVE 52
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
 1688-1747 9.95e-04

Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to Myosin XVa. Myosin XVa is an unconventional myosin that is critical for the normal growth of mechanosensory stereocilia of inner ear hair cells. Mutations in the myosin XVa gene are associated with nonsyndromic hearing loss. Myosin XVa contains a unique N-terminal extension followed by a motor domain, light chain-binding IQ motifs, and a tail consisting of a pair of MyTH4-FERM tandems separated by a SH3 domain, and a PDZ domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212817 [Multi-domain]  Cd Length: 56  Bit Score: 38.85  E-value: 9.95e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1688 MVAVFDYNPKESSpnadaeaELTFSAGDIITVFG--SMDDDGFYYGELNQQRGLVPSNFLEA 1747
Cdd:cd11884      2 VVAVRAYITRDQT-------LLSFHKGDVIKLLPkeGPLDPGWLFGTLDGRSGAFPKEYVQP 56
SH3_ASAP cd11821
Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing ...
 1703-1744 1.14e-03

Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing proteins; ASAPs are Arf GTPase activating proteins (GAPs) and they function in regulating cell growth, migration, and invasion. They contain an N-terminal BAR domain, followed by a Pleckstrin homology (PH) domain, an Arf GAP domain, ankyrin (ANK) repeats, and a C-terminal SH3 domain. Vertebrates contain at least three members, ASAP1, ASAP2, and ASAP3, but some ASAP3 proteins do not seem to harbor a C-terminal SH3 domain. ASAP1 and ASAP2 show GTPase activating protein (GAP) activity towards Arf1 and Arf5. They do not show GAP activity towards Arf6, but are able to mediate Arf6 signaling by binding stably to GTP-Arf6. ASAP3 is an Arf6-specific GAP. 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: 212755 [Multi-domain]  Cd Length: 53  Bit Score: 38.45  E-value: 1.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2024466778 1703 ADAEAELTFSAGDIITVFGSMDDDgFYYGELN---QQRGLVPSNF 1744
Cdd:cd11821     10 ADNDDELTFSEGEIIVVTGEEDDE-WWEGHIEgdpSRRGVFPVSF 53
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
 1690-1746 1.19e-03

Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in endocytosis and other membrane remodeling events. They exist in several isoforms and mammals possess two amphiphysin proteins from distinct genes. Amphiphysin I proteins, enriched in the brain and nervous system, contain domains that bind clathrin, Adaptor Protein complex 2 (AP2), dynamin, and synaptojanin. They function in synaptic vesicle endocytosis. Human autoantibodies to amphiphysin I hinder GABAergic signaling and contribute to the pathogenesis of paraneoplastic stiff-person syndrome. Some amphiphysin II isoforms, also called Bridging integrator 1 (Bin1), are localized in many different tissues and may function in intracellular vesicle trafficking. In skeletal muscle, Bin1 plays a role in the organization and maintenance of the T-tubule network. Mutations in Bin1 are associated with autosomal recessive centronuclear myopathy. Amphiphysins contain an N-terminal BAR domain with an additional N-terminal amphipathic helix (an N-BAR), a variable central domain, and a C-terminal SH3 domain. The SH3 domain of amphiphysins bind proline-rich motifs present in binding partners such as dynamin, synaptojanin, and nsP3. It also belongs to a subset of SH3 domains that bind ubiquitin in a site that overlaps with the peptide 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: 212724 [Multi-domain]  Cd Length: 64  Bit Score: 38.85  E-value: 1.19e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMD----DDGFYYG--ELNQQRGLVPSNFLE 1746
Cdd:cd11790      7 ATHDYTAEDTD-------ELTFEKGDVILVIPFDDpeeqDEGWLMGvkESTGCRGVFPENFTE 62
SH3_SH3RF1_1 cd11927
First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ...
 1690-1746 1.25e-03

First Src Homology 3 domain of SH3 domain containing ring finger protein 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 first SH3 domain, located at the N-terminal half, 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: 212860  Cd Length: 54  Bit Score: 38.78  E-value: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESspnadaeAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11927      5 ALYNYEGKEP-------GDLKFSKGDIIILRRQVDEN-WYHGEVNGIHGFFPTNFVQ 53
SH3_VAV_2 cd11830
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ...
 1708-1746 1.27e-03

C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as cytoplasmic guanine nucleotide exchange factors (GEFs) for Rho GTPases and scaffold proteins and they play important roles in cell signaling by coupling cell surface receptors to various effector functions. They play key roles in processes that require cytoskeletal reorganization including immune synapse formation, phagocytosis, cell spreading, and platelet aggregation, among others. Vertebrates have three VAV proteins (VAV1, VAV2, and VAV3). VAV proteins contain several domains that enable their function: N-terminal calponin homology (CH), acidic, RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), C1 (zinc finger), SH2, and two SH3 domains. The SH3 domain of VAV is involved in the localization of proteins to specific sites within the cell, by interacting with proline-rich sequences within target proteins. 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: 212764 [Multi-domain]  Cd Length: 54  Bit Score: 38.76  E-value: 1.27e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2024466778 1708 ELTFSAGDIITVFGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11830     15 ELSLKEGDVVKIYNKKGQQGWWRGEINGRIGWFPSTYVE 53
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1561-1606 1.27e-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: 38.49  E-value: 1.27e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 2024466778 1561 NPDaaeeELPFKEGQILKVCGDKDAD-GFYRGECAGREGYIPCNMVS 1606
Cdd:cd11836     12 NPD----EISFQPGDIIQVDESQVAEpGWLAGELKGKTGWFPANYVE 54
SH3_MLK cd11876
Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), ...
 1689-1745 1.30e-03

Src Homology 3 domain of Mixed Lineage Kinases; MLKs are Serine/Threonine Kinases (STKs), catalyzing the transfer of the gamma-phosphoryl group from ATP to S/T residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. 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: 212809 [Multi-domain]  Cd Length: 58  Bit Score: 38.65  E-value: 1.30e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFgSMD-----DDGFYYGELNQQRGLVPSNFL 1745
Cdd:cd11876      3 TALFDYD-------ARGEDELTLRRGQPVEVL-SKDaavsgDEGWWTGKIGDKVGIFPSNYV 56
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 336-512 1.34e-03

Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins in this family are typically between 427 and 674 amino acids in length. There are two completely conserved residues (D and I) that may be functionally important.


Pssm-ID: 464768 [Multi-domain]  Cd Length: 374  Bit Score: 43.10  E-value: 1.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKC-----ENLEHEVRKKHKRCKELEiqlQEVQSENarLAEENLQLNEKAGWAGQVESENAD 410
Cdd:pfam15558  123 QCQEQRLKEKEEELQALREQNslqlqERLEEACHKRQLKEREEQ---KKVQENN--LSELLNHQARKVLVDCQAKAEELL 197

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  411 LKL---QVVLVTKER--DSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQE-------------KQE 472
Cdd:pfam15558  198 RRLsleQSLQRSQENyeQLVEERHRELREKAQKEEEQFQRAKWRAEEKEEERQEHKEALAELADrkiqqarqvahktVQD 277

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 2024466778  473 EVRRLQQAQAEAKREHegavQLLEARVKDLEDQCRSQTEQ 512
Cdd:pfam15558  278 KAQRARELNLEREKNH----HILKLKVEKEEKCHREGIKE 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 85-255 1.38e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 43.89  E-value: 1.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   85 SGADYSFLVSQNMKLLSALEDLRHRCSSLTEENSLLR------RSCFPETEEKVKHLKRKNAELAVIAKRLEERARKLQE 158
Cdd:TIGR02168  230 LVLRLEELREELEELQEELKEAEEELEELTAELQELEekleelRLEVSELEEEIEELQKELYALANEISRLEQQKQILRE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  159 ANLKVVTAPVPLKGSSLELCKKafarqrakdLTEQASALLAKDKQIEALQQECRELQAKLIAGKGDPRCLN--VVEFDRL 236
Cdd:TIGR02168  310 RLANLERQLEELEAQLEELESK---------LDELAEELAELEEKLEELKEELESLEAELEELEAELEELEsrLEELEEQ 380

                          170
                   ....*....|....*....
gi 2024466778  237 LRESQKEVLRLQRQIALKN 255
Cdd:TIGR02168  381 LETLRSKVAQLELQIASLN 399
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 190-511 1.44e-03

RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part of the CAZ (cytomatrix at the active zone) complex which is involved in determining the site of synaptic vesicle fusion. The C-terminus is a PDZ-binding motif that binds directly to RIM (a small G protein Rab-3A effector). The family also contains four coiled-coil domains.


Pssm-ID: 431111 [Multi-domain]  Cd Length: 766  Bit Score: 43.66  E-value: 1.44e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  190 LTEQASALLAKDKQIEALQQecrelqakliagkgdprclnvvEFDRLLRESQKEVLRLQRQiaLKNFKE---CLRP---S 263
Cdd:pfam10174  438 LTTLEEALSEKERIIERLKE----------------------QREREDRERLEELESLKKE--NKDLKEkvsALQPeltE 493

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  264 KGSSGGSLPSAAScpgpalnacSKDSPAAKEVcSGGPALGGAAHGKVEPGVLPLGPALEGHENfpPKNAVADQESSQQIQ 343
Cdd:pfam10174  494 KESSLIDLKEHAS---------SLASSGLKKD-SKLKSLEIAVEQKKEECSKLENQLKKAHNA--EEAVRTNPEINDRIR 561

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  344 QLEFELKKKR----------------------------KKCENLEHEVRKKHKRCKELEIQLQEVQSENARlaeENLQLN 395
Cdd:pfam10174  562 LLEQEVARYKeesgkaqaeverllgilrevenekndkdKKIAELESLTLRQMKEQNKKVANIKHGQQEMKK---KGAQLL 638

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  396 EKAGWAGQVESEN-ADLKLQVVLVTKER-----DSVIQRNQGLQTKLENLEQVLKHMRdvAERRQLLEA--EHK-EALL- 465
Cdd:pfam10174  639 EEARRREDNLADNsQQLQLEELMGALEKtrqelDATKARLSSTQQSLAEKDGHLTNLR--AERRKQLEEilEMKqEALLa 716

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 2024466778  466 VLQEKQEEVRRLQQAQAEAKREHEGAVQLleARVKD-LEDQCRSQTE 511
Cdd:pfam10174  717 AISEKDANIALLELSSSKKKKTQEEVMAL--KREKDrLVHQLKQQTQ 761
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 346-524 1.46e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 1.46e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  346 EFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSE-----------NARLAEENLQLNEKAgwagqvESENADLKLQ 414
Cdd:TIGR02169  222 EYEGYELLKEKEALERQKEAIERQLASLEEELEKLTEEiselekrleeiEQLLEELNKKIKDLG------EEEQLRVKEK 295

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  415 VVLVTKERDSviqrnqgLQTKLENLEQvlkHMRDVAERRQLLEAEHKEallvLQEKQEEVRRLQQAQAEAKREHEGAVQL 494
Cdd:TIGR02169  296 IGELEAEIAS-------LERSIAEKER---ELEDAEERLAKLEAEIDK----LLAEIEELEREIEEERKRRDKLTEEYAE 361

                          170       180       190
                   ....*....|....*....|....*....|
gi 2024466778  495 LEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:TIGR02169  362 LKEELEDLRAELEEVDKEFAETRDELKDYR 391
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
 343-475 1.55e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 43.28  E-value: 1.55e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  343 QQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEvqsenaRLAEENLQLNEKAgwagQVESENAdlklqvvlvTKER 422
Cdd:PRK00409   526 EELERELEQKAEEAEALLKEAEKLKEELEEKKEKLQE------EEDKLLEEAEKEA----QQAIKEA---------KKEA 586

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 2024466778  423 DSVIQRNQGLQtKLENLEQVLKHMRDvaERRQLLEA--EHKEALLVLQEKQEEVR 475
Cdd:PRK00409   587 DEIIKELRQLQ-KGGYASVKAHELIE--ARKRLNKAneKKEKKKKKQKEKQEELK 638
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
 1690-1746 1.60e-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: 38.06  E-value: 1.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNpkesspnADAEAELTFSAGDIITVfGSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11877      4 AKFNFE-------GTNEDELSFDKGDIITV-TQVVEGGWWEGTLNGKTGWFPSNYVK 52
Spc7 smart00787
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ...
 404-549 1.63e-03

Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.


Pssm-ID: 197874 [Multi-domain]  Cd Length: 312  Bit Score: 42.70  E-value: 1.63e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   404 VESENADLKLQVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRD--------VAERRQLLEAEHKEALLVLQEKQEEVR 475
Cdd:smart00787  156 LKEDYKLLMKELELLNSIKPKLRDRKDALEEELRQLKQLEDELEDcdpteldrAKEKLKKLLQEIMIKVKKLEELEEELQ 235

                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2024466778   476 RLQQAQAEAKREhegaVQLLEARVKDLEDQcRSQTEQFSLLsqELKQFRLQTGKIDLLTSTLVTSELPLALCSS 549
Cdd:smart00787  236 ELESKIEDLTNK----KSELNTEIAEAEKK-LEQCRGFTFK--EIEKLKEQLKLLQSLTGWKITKLSGNTLSMT 302
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 1549-1607 1.63e-03

Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If (MyoIf) are nonmuscle, unconventional, long tailed, class I myosins containing an N-terminal motor domain and a myosin tail with TH1, TH2, and SH3 domains. MyoIe interacts with the endocytic proteins, dynamin and synaptojanin-1, through its SH3 domain; it may play a role in clathrin-dependent endocytosis. In the kidney, MyoIe is critical for podocyte function and normal glomerular filtration. Mutations in MyoIe is associated with focal segmental glomerulosclerosis, a disease characterized by massive proteinuria and progression to end-stage kidney disease. MyoIf is predominantly expressed in the immune system; it plays a role in immune cell motility and innate immunity. Mutations in MyoIf may be associated with the loss of hearing. The MyoIf gene has also been found to be fused to the MLL (Mixed lineage leukemia) gene in infant acute myeloid leukemias (AML). 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: 212761 [Multi-domain]  Cd Length: 53  Bit Score: 38.16  E-value: 1.63e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1549 ALFDYDPVSMspnpdaaeEELPFKEGQILKVCgDKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11827      4 ALYAYDAQDT--------DELSFNEGDIIEIL-KEDPSGWWTGRLRGKEGLFPGNYVEK 53
SH3_Bbc1 cd11887
Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces ...
 1685-1746 1.66e-03

Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces cerevisiae Bbc1p, also called Mti1p (Myosin tail region-interacting protein), and similar proteins. Bbc1p interacts with and regulates type I myosins in yeast, Myo3p and Myo5p, which are involved in actin cytoskeletal reorganization. It also binds and inhibits Las17, a WASp family protein that functions as an activator of the Arp2/3 complex. Bbc1p contains an N-terminal SH3 domain. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212820 [Multi-domain]  Cd Length: 60  Bit Score: 38.48  E-value: 1.66e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1685 PRSMVAVFDYNPkesspnaDAEAELTFSAGDIITVFGSMDDDgFYYGEL-----NQQRGLVPSNFLE 1746
Cdd:cd11887      1 PFKVKALYPYES-------DHEDDLNFDVGQLITVTEEEDAD-WYFGEYvdsngNTKEGIFPKNFVE 59
CCCAP pfam15964
Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in ...
 334-530 1.82e-03

Centrosomal colon cancer autoantigen protein family; CCCAP is a family of proteins found in eukaryotes. CCCAP is also known as SDCCAG8, serologically defined colon cancer antigen 8. It is associated with the centrosome.


Pssm-ID: 435040 [Multi-domain]  Cd Length: 703  Bit Score: 43.36  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  334 ADQESSQQIQQLE---FELKKKRKKCENLEHEV-RKKHKRCKELEIQLQEVQSENARLAEENLQLNEKAGWAGQVESEN- 408
Cdd:pfam15964  333 AYEQVKQAVQMTEeanFEKTKALIQCEQLKSELeRQKERLEKELASQQEKRAQEKEALRKEMKKEREELGATMLALSQNv 412

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  409 ADLKLQVVLVTKERDSVIQRNQGLQTKLENLE----QVLKHMRDVAERRQL----LEAEHKE----ALLVLQEKQEEVRR 476
Cdd:pfam15964  413 AQLEAQVEKVTREKNSLVSQLEEAQKQLASQEmdvtKVCGEMRYQLNQTKMkkdeAEKEHREyrtkTGRQLEIKDQEIEK 492

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024466778  477 LQQAQAEAKREHEGAvQLLEARVKdleDQCRSQTEQFSLLSQELKQFRLQTGKI 530
Cdd:pfam15964  493 LGLELSESKQRLEQA-QQDAARAR---EECLKLTELLGESEHQLHLTRLEKESI 542
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
 1549-1604 1.86e-03

Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) proteins; The MPP/p55 subfamily of MAGUK (membrane-associated guanylate kinase) proteins includes at least eight vertebrate members (MPP1-7 and CASK), four Drosophila proteins (Stardust, Varicose, CASK and Skiff), and other similar proteins; they all contain one each of the core of three domains characteristic of MAGUK proteins: PDZ, SH3, and guanylate kinase (GuK). In addition, most members except for MPP1 contain N-terminal L27 domains and some also contain a Hook (Protein 4.1 Binding) motif in between the SH3 and GuK domains. CASK has an additional calmodulin-dependent kinase (CaMK)-like domain at the N-terminus. Members of this subfamily are scaffolding proteins that play important roles in regulating and establishing cell polarity, cell adhesion, and synaptic targeting and transmission, among others. The GuK domain in MAGUK proteins is enzymatically inactive; instead, the domain mediates protein-protein interactions and associates intramolecularly with the 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: 212796  Cd Length: 61  Bit Score: 38.33  E-value: 1.86e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2024466778 1549 ALFDYDPV--SMSPNPDAAeeeLPFKEGQILKVCGDKDAD---GFYRGECAGREGYIPCNM 1604
Cdd:cd11862      4 ALFDYDPEedPLIPCKEAG---LSFKKGDILQIVNQDDPNwwqARKVGDPNGRAGLIPSQD 61
PRK12704 PRK12704
phosphodiesterase; Provisional
 334-512 1.88e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.84  E-value: 1.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  334 ADQESSQQIQQLEFELKKKRKKCENLEHEVRKKhkrckeleiqlqevqsenarlaEENLQlnekagwagqvesenadlkl 413
Cdd:PRK12704    62 AKEEIHKLRNEFEKELRERRNELQKLEKRLLQK----------------------EENLD-------------------- 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  414 qvvlvtKERDSVIQRNQGLQTKLENLEQVLKhmrDVAERRQLLEAEHKEALLVLQE----KQEEVRRLQQAQAEAKREHE 489
Cdd:PRK12704   100 ------RKLELLEKREEELEKKEKELEQKQQ---ELEKKEEELEELIEEQLQELERisglTAEEAKEILLEKVEEEARHE 170

                          170       180
                   ....*....|....*....|...
gi 2024466778  490 GAvqlleARVKDLEDQCRSQTEQ 512
Cdd:PRK12704   171 AA-----VLIKEIEEEAKEEADK 188
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
 335-476 1.89e-03

Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 43.19  E-value: 1.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  335 DQESSQQIQQLEFELKKKRKKCENLEHEVRKKhkrckeleiqlQEVQSENARLAEENLQLNEKAgwagQVESENADLKL- 413
Cdd:pfam17380  455 EQERQQQVERLRQQEEERKRKKLELEKEKRDR-----------KRAEEQRRKILEKELEERKQA----MIEEERKRKLLe 519

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778  414 ------QVVLVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVRR 476
Cdd:pfam17380  520 kemeerQKAIYEEERRREAEEERRKQQEMEERRRIQEQMRKATEERSRLEAMEREREMMRQIVESEKAR 588
PRK09039 PRK09039
peptidoglycan -binding protein;
378-520 2.04e-03

peptidoglycan -binding protein;


Pssm-ID: 181619 [Multi-domain]  Cd Length: 343  Bit Score: 42.65  E-value: 2.04e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  378 QEVQSENARLAEENLQLNEKAGWAGQVESENADLKLQVVLVTKERDSViqrnQGLQTKLENLEQVLKHMRDVAERR-QLL 456
Cdd:PRK09039    46 REISGKDSALDRLNSQIAELADLLSLERQGNQDLQDSVANLRASLSAA----EAERSRLQALLAELAGAGAAAEGRaGEL 121

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2024466778  457 EAEHKEALLVLQEKQEEVRRLQQaQAEAKREHEGAVQ-LLEARvkdlEDQCRSQTEQFSLLSQEL 520
Cdd:PRK09039   122 AQELDSEKQVSARALAQVELLNQ-QIAALRRQLAALEaALDAS----EKRDRESQAKIADLGRRL 181
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 1690-1746 2.09e-03

Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox homology (PX) domain containing proteins that are involved in regulating membrane traffic and protein sorting in the endosomal system. SNXs differ from each other in their lipid-binding specificity, subcellular localization and specific function in the endocytic pathway. This subfamily consists of SH3 domain containing SNXs including SNX9, SNX18, SNX33, and similar proteins. SNX9 is localized to plasma membrane endocytic sites and acts primarily in clathrin-mediated endocytosis, while SNX18 is localized to peripheral endosomal structures, and acts in a trafficking pathway that is clathrin-independent but relies on AP-1 and PACS1. 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: 212697 [Multi-domain]  Cd Length: 55  Bit Score: 38.08  E-value: 2.09e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDGFYYGE-LNQQRGLVPSNFLE 1746
Cdd:cd11763      4 ALYDFDSQPSG-------ELSLRAGEVLTITRQDVGDGWLEGRnSRGEVGLFPSSYVE 54
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 1564-1605 2.24e-03

N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS (GRB2-related adapter downstream of Shc), GrpL, GRB2L, Mona, or GRID (Grb2-related protein with insert domain). It is expressed specifically in the hematopoietic system. It plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. It also have roles in antigen-receptor and tyrosine kinase mediated signaling. GRAP2 is unique from other GRB2-like adaptor proteins in that it can be regulated by caspase cleavage. It contains an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. The N-terminal SH3 domain of the related protein GRB2 binds to Sos and Sos-derived proline-rich peptides. 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: 212880 [Multi-domain]  Cd Length: 52  Bit Score: 37.85  E-value: 2.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2024466778 1564 AAEEELPFKEGQILKVCGDKDAdgFYRGECAGREGYIPCNMV 1605
Cdd:cd11947     11 SGEDELSFKKGDVLKILSSDDI--WFKAELNGEEGYVPKNFV 50
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1689-1744 2.25e-03

Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, Yes, and Brk. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). However, Brk lacks the N-terminal myristoylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells, and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, Lyn, and Brk show a limited expression pattern. This subfamily also includes Drosophila Src42A, Src oncogene at 42A (also known as Dsrc41) which accumulates at sites of cell-cell or cell-matrix adhesion, and participates in Drosphila development and wound healing. It has been shown to promote tube elongation in the tracheal system, is essential for proper cell-cell matching during dorsal closure, and regulates cell-cell contacts in developing Drosophila eyes. The SH3 domain of Src kinases contributes to substrate recruitment by binding adaptor proteins/substrates, and regulation of kinase activity through an intramolecular interaction. 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: 212779 [Multi-domain]  Cd Length: 52  Bit Score: 37.95  E-value: 2.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDGFYYGELN-QQRGLVPSNF 1744
Cdd:cd11845      3 VALYDYE-------ARTDDDLSFKKGDRLQILDDSDGDWWLARHLStGKEGYIPSNY 52
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
436-524 2.45e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  436 LENLEQVLKHMRDVAE-RRQLLEAEHK-EALLVLQEKQEEVRRLQQAQAEAKR--------EHEGAVQLLEARVKDLEDQ 505
Cdd:COG4913    224 FEAADALVEHFDDLERaHEALEDAREQiELLEPIRELAERYAAARERLAELEYlraalrlwFAQRRLELLEAELEELRAE 303

                           90
                   ....*....|....*....
gi 2024466778  506 CRSQTEQFSLLSQELKQFR 524
Cdd:COG4913    304 LARLEAELERLEARLDALR 322
SH3_p67phox_C cd12046
C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, ...
 1548-1607 2.52e-03

C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, also called Neutrophil cytosol factor 2 (NCF-2), is a cytosolic subunit of the phagocytic NADPH oxidase complex (also called Nox2 or gp91phox) which plays a crucial role in the cellular response to bacterial infection. NADPH oxidase catalyzes the transfer of electrons from NADPH to oxygen during phagocytosis forming superoxide and reactive oxygen species. p67phox plays a regulatory role and contains N-terminal TPR, first SH3 (or N-terminal or central SH3), PB1, and C-terminal SH3 domains. It binds, via its C-terminal SH3 domain, to a proline-rich region of p47phox and upon activation, this complex assembles with flavocytochrome b558, the Nox2-p22phox heterodimer. Concurrently, RacGTP translocates to the membrane and interacts with the TPR domain of p67phox, which leads to the activation of NADPH oxidase. The PB1 domain of p67phox binds to its partner PB1 domain in p40phox, and this facilitates the assembly of p47phox-p67phox at the membrane. 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: 212979 [Multi-domain]  Cd Length: 53  Bit Score: 37.86  E-value: 2.52e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778 1548 VALFDYDpvsmSPNPdaaeEELPFKEGQILKVCGdKDADGFYRGECAGREGYIPCNMVSE 1607
Cdd:cd12046      3 VALFSYE----ASQP----EDLEFQKGDVILVLS-KVNEDWLEGQCKGKIGIFPSAFVED 53
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
89-505 2.59e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 2.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778   89 YSFLVSQNMKLLSALEDLRHRCSSLTEENSLLRR--SCFPETEEKVKHLKRKNAELAVIAKRLEERARKLQEANLKVVTA 166
Cdd:PRK03918   295 YIKLSEFYEEYLDELREIEKRLSRLEEEINGIEEriKELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEEL 374

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  167 ---PVPLKGSSLELCKKAF--ARQRAKDLTEQASALLAKDKQIEALQQECRELQAKLIAGKGD-PRC---LNVVEFDRLL 237
Cdd:PRK03918   375 erlKKRLTGLTPEKLEKELeeLEKAKEEIEEEISKITARIGELKKEIKELKKAIEELKKAKGKcPVCgreLTEEHRKELL 454

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  238 RESQKEVLRLQRQiaLKNFKECLRPSKgssggslpsaascpgpalnacskdspaAKEVcsggpalggaahgKVEPgvlpl 317
Cdd:PRK03918   455 EEYTAELKRIEKE--LKEIEEKERKLR---------------------------KELR-------------ELEK----- 487

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  318 gpALEGHENFPPKNAVADQ----ESSQQIQQLEfELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQ 393
Cdd:PRK03918   488 --VLKKESELIKLKELAEQlkelEEKLKKYNLE-ELEKKAEEYEKLKEKLIKLKGEIKSLKKELEKLEELKKKLAELEKK 564

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  394 LNEkagwagqVESENADLKLQVVLV----TKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQE 469
Cdd:PRK03918   565 LDE-------LEEELAELLKELEELgfesVEELEERLKELEPFYNEYLELKDAEKELEREEKELKKLEEELDKAFEELAE 637

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|.
gi 2024466778  470 KQEEVRRLQQAQAEAKR-----EHEGAVQL----------LEARVKDLEDQ 505
Cdd:PRK03918   638 TEKRLEELRKELEELEKkyseeEYEELREEylelsrelagLRAELEELEKR 688
SH3_betaPIX cd12061
Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho ...
 1706-1748 2.64e-03

Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho guanine nucleotide exchange factor 7 (ARHGEF7) or Cool (Cloned out of Library)-1, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and plays important 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: 212994 [Multi-domain]  Cd Length: 54  Bit Score: 37.74  E-value: 2.64e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 2024466778 1706 EAELTFSAGDIITVfGSMDDDGFYYGELNQQRGLVPSNFLEAV 1748
Cdd:cd12061     13 EDELSFSKGDVIHV-TRVEEGGWWEGTHNGRTGWFPSNYVREI 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 341-476 2.75e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 42.75  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  341 QIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARL------AEENLQLNEKAGWAGQVESENaDLKLQ 414
Cdd:TIGR02169  876 ALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKRKRLSELkakleaLEEELSEIEDPKGEDEEIPEE-ELSLE 954

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778  415 VvlVTKERDSVIQRNQGLQT----KLENLEQVLKHMRDVAERRQLLEAEhKEALLVLQEKQEEVRR 476
Cdd:TIGR02169  955 D--VQAELQRVEEEIRALEPvnmlAIQEYEEVLKRLDELKEKRAKLEEE-RKAILERIEEYEKKKR 1017
SH3_Eve1_3 cd11816
Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1689-1744 2.78e-03

Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. 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: 212750 [Multi-domain]  Cd Length: 51  Bit Score: 37.39  E-value: 2.78e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNF 1744
Cdd:cd11816      3 VARFDFE-------GEQEDELSFSEGDVITLKEYVGEE-WAKGELNGKIGIFPLNF 50
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
 1690-1745 2.95e-03

Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac 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: 212762 [Multi-domain]  Cd Length: 53  Bit Score: 37.36  E-value: 2.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFL 1745
Cdd:cd11828      4 ALWDHVTMDPE-------ELGFKAGDVIEVL-DMSDKDWWWGSIRDEEGWFPASFV 51
Lebercilin pfam15619
Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of ...
 371-522 2.98e-03

Ciliary protein causing Leber congenital amaurosis disease; Lebercilin is a family of eukaryotic ciliary proteins. Mutations in the gene, LCA5, are implicated in the disease Leber congenital amaurosis. In photoreceptors, lebercilin is uniquely localized at the cilium that bridges the inner and outer segments. Lebercilin functions as an integral element of selective protein transport through photoreceptor cilia. Lebercilin specifically interacts with the intraflagellar transport (IFT), and disruption of IFT can lead to Leber congenital amaurosis.


Pssm-ID: 464776 [Multi-domain]  Cd Length: 193  Bit Score: 40.66  E-value: 2.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  371 KELEIQLQEVQSENARLAEENLQLN------EKAgwAGQVESENADLKLQV------VLVTKER-----DSVIQRNQGLQ 433
Cdd:pfam15619   14 KELQNELAELQSKLEELRKENRLLKrlqkrqEKA--LGKYEGTESELPQLIarhneeVRVLRERlrrlqEKERDLERKLK 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  434 TK---LENLEQVLKHMRDVAERRQLLEAE---HKEALL--VLQEKQEEVRRLQQ--AQAEAKREHEGAVQLleARVKDLE 503
Cdd:pfam15619   92 EKeaeLLRLRDQLKRLEKLSEDKNLAEREelqKKLEQLeaKLEDKDEKIQDLERklELENKSFRRQLAAEK--KKHKEAQ 169

                          170
                   ....*....|....*....
gi 2024466778  504 DQCRSQTEQFSLLSQELKQ 522
Cdd:pfam15619  170 EEVKILQEEIERLQQKLKE 188
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
 1690-1745 3.02e-03

Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of proteins bind to important regulators of apoptosis (p53, Bcl-2, and RelA) and cell growth (APCL, PP1). They share similarity at their C-termini, where they harbor a proline-rich region, four ankyrin (ANK) repeats, and an SH3 domain. Vertebrates contain three members of the family: ASPP1, ASPP2, and iASPP. ASPP1 and ASPP2 activate the apoptotic function of the p53 family of tumor suppressors (p53, p63, and p73), while iASPP is an oncoprotein that specifically inhibits p53-induced apoptosis. The expression of ASPP proteins is altered in tumors; ASPP1 and ASPP2 are downregulated whereas iASPP is upregulated is some cancer types. ASPP proteins also bind and regulate protein phosphatase 1 (PP1), and this binding is competitive with p53 binding. The SH3 domain and the ANK repeats of ASPP contribute to the p53 binding site; they bind to the DNA binding domain of p53. 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: 212741 [Multi-domain]  Cd Length: 57  Bit Score: 37.74  E-value: 3.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDD--GFYYGELNQQRGLVPSNFL 1745
Cdd:cd11807      5 ALFDYEAENGD-------ELSFREGDELTVLRKGDDDetEWWWARLNDKEGYVPRNLL 55
SH3_CD2AP_3 cd12056
Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1549-1606 3.06e-03

Third Src Homology 3 domain (SH3C) 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 third SH3 domain (SH3C) of CD2AP. SH3C has been shown to bind 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: 212989 [Multi-domain]  Cd Length: 57  Bit Score: 37.50  E-value: 3.06e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 2024466778 1549 ALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDAD-GFYRGECAGREGYIPCNMVS 1606
Cdd:cd12056      6 ALFHYEGTN--------EDELDFKEGEIILIISKDTGEpGWWKGELNGKEGVFPDNFVS 56
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 342-524 3.42e-03

Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.


Pssm-ID: 460256 [Multi-domain]  Cd Length: 1081  Bit Score: 42.47  E-value: 3.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  342 IQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQsenARLAEENLQLNEKagwagqvESENADLKLQVVLVTKE 421
Cdd:pfam01576  189 ISDLEERLKKEEKGRQELEKAKRKLEGESTDLQEQIAELQ---AQIAELRAQLAKK-------EEELQAALARLEEETAQ 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  422 RDSVIQRNQGLQTKLENLEQVL-----------KHMRDVAERRQLLEAEHKEALLVLQEKQE-------EVRRLQQAQAE 483
Cdd:pfam01576  259 KNNALKKIRELEAQISELQEDLeseraarnkaeKQRRDLGEELEALKTELEDTLDTTAAQQElrskreqEVTELKKALEE 338

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 2024466778  484 AKREHEgaVQLLEARVKdledqcrsQTEQFSLLSQELKQFR 524
Cdd:pfam01576  339 ETRSHE--AQLQEMRQK--------HTQALEELTEQLEQAK 369
SH3_Eve1_4 cd11817
Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1689-1744 3.54e-03

Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. 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: 212751 [Multi-domain]  Cd Length: 50  Bit Score: 37.07  E-value: 3.54e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778 1689 VAVFDYNpkesspnADAEAELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNF 1744
Cdd:cd11817      3 VALYDFT-------GETEEDLSFQRGDRILVTEHLDAE-WSRGRLNGREGIFPRAF 50
Crescentin pfam19220
Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament ...
 336-505 3.54e-03

Crescentin protein; This entry represents a bacterial equivalent to Intermediate Filament proteins, named crescentin, whose cytoskeletal function is required for the vibrioid and helical shapes of Caulobacter crescentus. Without crescentin, the cells adopt a straight-rod morphology. Crescentin has characteriztic features of IF proteins including the ability to assemble into filaments in vitro without energy or cofactor requirements. In vivo, crescentin forms a helical structure that colocalizes with the inner cell curvatures beneath the cytoplasmic membrane.


Pssm-ID: 437057 [Multi-domain]  Cd Length: 401  Bit Score: 41.98  E-value: 3.54e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  336 QESSQQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAeenLQLNEKagwagqvESENADLKLQV 415
Cdd:pfam19220   58 AQERAAYGKLRRELAGLTRRLSAAEGELEELVARLAKLEAALREAEAAKEELR---IELRDK-------TAQAEALERQL 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  416 VLVTKERDSVIQRNQGLQTKLENLEQVL----KHMRDVAERRQLLEAEhKEALLVLQEKQEevrrLQQAQAEAK-REHEG 490
Cdd:pfam19220  128 AAETEQNRALEEENKALREEAQAAEKALqraeGELATARERLALLEQE-NRRLQALSEEQA----AELAELTRRlAELET 202

                          170
                   ....*....|....*
gi 2024466778  491 AVQLLEARVKDLEDQ 505
Cdd:pfam19220  203 QLDATRARLRALEGQ 217
DUF4670 pfam15709
Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins ...
 335-507 3.56e-03

Domain of unknown function (DUF4670); This family of proteins is found in eukaryotes. Proteins in this family are typically between 373 and 763 amino acids in length.


Pssm-ID: 464815 [Multi-domain]  Cd Length: 522  Bit Score: 42.25  E-value: 3.56e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  335 DQESSQQIQQLEFELKKKRKkcENLEHEVRKKHKrckelEIQLQEVQSENARLAEENLQLNEKAGWagQVESENADLKlQ 414
Cdd:pfam15709  356 EQEEQRRLQQEQLERAEKMR--EELELEQQRRFE-----EIRLRKQRLEEERQRQEEEERKQRLQL--QAAQERARQQ-Q 425

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  415 VVLVTKERDSVIQRNQGLQTKLENLEQVLKH--MRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAV 492
Cdd:pfam15709  426 EEFRRKLQELQRKKQQEEAERAEAEKQRQKEleMQLAEEQKRLMEMAEEERLEYQRQKQEAEEKARLEAEERRQKEEEAA 505

                          170
                   ....*....|....*.
gi 2024466778  493 QL-LEARVKDLEDQCR 507
Cdd:pfam15709  506 RLaLEEAMKQAQEQAR 521
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 1689-1746 3.60e-03

Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin cytoskeleton dynamics by linking proline-rich effector molecules to protein tyrosine kinases and phosphorylated signaling intermediates. They contain three SH3 domains and a C-terminal SH2 domain. They function downstream of the PDGFbeta receptor and are involved in Rho GTPase signaling and actin dynamics. Vertebrates contain two Nck adaptor proteins: Nck1 (also called Nckalpha) and Nck2 (also called Nckbeta or Growth factor receptor-bound protein 4, Grb4), which show partly overlapping functions but also bind distinct targets. Their SH3 domains are involved in recruiting downstream effector molecules, such as the N-WASP/Arp2/3 complex, which when activated induces actin polymerization that results in the production of pedestals, or protrusions of the plasma membrane. The second SH3 domain of Nck appears to prefer ligands containing the APxxPxR motif. SH3 domains are protein interaction domains that usually bind to proline-rich ligands with moderate affinity and selectivity, preferentially a PxxP motif. 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: 212700 [Multi-domain]  Cd Length: 53  Bit Score: 37.24  E-value: 3.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 2024466778 1689 VAVFDYNPKEsspnadaEAELTFSAGDIITVFgSMDDDGFYYGELNQQRGLVPSNFLE 1746
Cdd:cd11766      3 VVKFNYEAQR-------EDELSLRKGDRVLVL-EKSSDGWWRGECNGQVGWFPSNYVT 52
SH3_srGAP4 cd11956
Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, ...
 1689-1745 3.91e-03

Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, is highly expressed in hematopoietic cells and may play a role in lymphocyte differentiation. It is able to stimulate the GTPase activity of Rac1, Cdc42, and RhoA. In the nervous system, srGAP4 has been detected in differentiating neurites and may be involved in axon and dendritic growth. srGAPs are Rho GAPs that interact with Robo1, the transmembrane receptor of Slit proteins. Slit proteins are secreted proteins that control axon guidance and the migration of neurons and leukocytes. srGAPs contain an N-terminal F-BAR domain, a Rho GAP 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: 212889 [Multi-domain]  Cd Length: 55  Bit Score: 37.13  E-value: 3.91e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1689 VAVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDgFYYGELNQQRGLVPSNFL 1745
Cdd:cd11956      5 VACFDYTGRTAQ-------ELSFKRGDVLLLHSKASSD-WWRGEHNGMRGLIPHKYI 53
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 377-530 4.17e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 42.26  E-value: 4.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  377 LQEVQSENARLAEENLQLNEKAGWAGQVESENADLKLQVVLVTKE----RDSVIQRNQGLQTKLENLEQVLKHMRDVAER 452
Cdd:TIGR00618  158 LKAKSKEKKELLMNLFPLDQYTQLALMEFAKKKSLHGKAELLTLRsqllTLCTPCMPDTYHERKQVLEKELKHLREALQQ 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  453 RQlleaEHKEALLVLQEKQEEVRRLQQAQAEAKREHEGAvQLLEARVKDLEDQC--RSQTEQFSLLSQELKQFRLQTGKI 530
Cdd:TIGR00618  238 TQ----QSHAYLTQKREAQEEQLKKQQLLKQLRARIEEL-RAQEAVLEETQERInrARKAAPLAAHIKAVTQIEQQAQRI 312
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 325-497 4.32e-03

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442330 [Multi-domain]  Cd Length: 1470  Bit Score: 42.25  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  325 ENFPPKNAVADQESSQQIQQLEFE-LKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSE-NARLAEENLQLNEKAGWAG 402
Cdd:COG3096    502 RRYRSQQALAQRLQQLRAQLAELEqRLRQQQNAERLLEEFCQRIGQQLDAAEELEELLAElEAQLEELEEQAAEAVEQRS 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  403 QVESENADLKLQVVLVTKERDSVIQRNQGLQT-------KLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVR 475
Cdd:COG3096    582 ELRQQLEQLRARIKELAARAPAWLAAQDALERlreqsgeALADSQEVTAAMQQLLEREREATVERDELAARKQALESQIE 661

                          170       180
                   ....*....|....*....|....*...
gi 2024466778  476 RLQQAQ-AEAKR-----EHEGAVQLLEA 497
Cdd:COG3096    662 RLSQPGgAEDPRllalaERLGGVLLSEI 689
SH3_ARHGEF9_like cd11828
Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this ...
 1549-1605 4.37e-03

Src homology 3 domain of ARHGEF9-like Rho guanine nucleotide exchange factors; Members of this family contain a SH3 domain followed by RhoGEF (also called Dbl-homologous or DH) and Pleckstrin Homology (PH) domains. They include the Rho guanine nucleotide exchange factors ARHGEF9, ASEF (also called ARHGEF4), ASEF2, and similar proteins. GEFs activate small GTPases by exchanging bound GDP for free GTP. ARHGEF9 specifically activates Cdc42, while both ASEF and ASEF2 can activate Rac1 and Cdc42. ARHGEF9 is highly expressed in the brain and it interacts with gephyrin, a postsynaptic protein associated with GABA and glycine receptors. ASEF plays a role in angiogenesis and cell migration. ASEF2 is important in cell migration and adhesion dynamics. ASEF exists in an autoinhibited form and is activated upon binding of the tumor suppressor APC (adenomatous polyposis coli), leading to the activation of Rac1 or Cdc42. In its autoinhibited form, the SH3 domain of ASEF forms an extensive interface with the DH and PH domains, blocking the Rac 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: 212762 [Multi-domain]  Cd Length: 53  Bit Score: 36.98  E-value: 4.37e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1549 ALFDYdpVSMSPnpdaaeEELPFKEGQILKVCGDKDADGFYrGECAGREGYIPCNMV 1605
Cdd:cd11828      4 ALWDH--VTMDP------EELGFKAGDVIEVLDMSDKDWWW-GSIRDEEGWFPASFV 51
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
 335-411 4.83e-03

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 37.93  E-value: 4.83e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778  335 DQESSQQIQQLEFELKKKRKKCENLEHEVrkkhkrcKELEIQLQEVQSENARLAEENLQLNEKagwAGQVESENADL 411
Cdd:cd22887      6 LQELEKRLAELEAELASLEEEIKDLEEEL-------KEKNKANEILNDELIALQIENNLLEEK---LRKLQEENDEL 72
SH3_Intersectin1_5 cd11995
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
 1566-1605 5.17e-03

Fifth Src homology 3 domain (or SH3E) 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 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: 212928 [Multi-domain]  Cd Length: 54  Bit Score: 36.86  E-value: 5.17e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 2024466778 1566 EEELPFKEGQILKVCGDKDADgFYRGECAGREGYIPCNMV 1605
Cdd:cd11995     14 DDELAFSKGQIINVLNKEDPD-WWKGELNGQVGLFPSNYV 52
SH3_Eve1_4 cd11817
Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1548-1601 5.35e-03

Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 domain-containing protein 19 (SH3D19) or EEN-binding protein (EBP), exists in multiple alternatively spliced isoforms. The longest isoform contains five SH3 domain in the C-terminal region and seven proline-rich motifs in the N-terminal region. It is abundantly expressed in skeletal muscle and heart, and may be involved in regulating the activity of ADAMs (A disintegrin and metalloproteases). Eve-1 interacts with EEN, an endophilin involved in endocytosis and may be the target of the MLL-EEN fusion protein that is implicated in leukemogenesis. 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: 212751 [Multi-domain]  Cd Length: 50  Bit Score: 36.69  E-value: 5.35e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2024466778 1548 VALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDADgFYRGECAGREGYIP 1601
Cdd:cd11817      3 VALYDFTGET--------EEDLSFQRGDRILVTEHLDAE-WSRGRLNGREGIFP 47
SH3_Abp1_fungi_C2 cd11961
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ...
 1549-1607 6.48e-03

Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor protein that functions in receptor-mediated endocytosis and vesicle trafficking. It contains an N-terminal actin-binding module, the actin-depolymerizing factor (ADF) homology domain, a central proline-rich region, and a C-terminal SH3 domain (many yeast Abp1 proteins contain two C-terminal SH3 domains). Yeast Abp1 also contains two acidic domains that bind directly to the Arp2/3 complex, which is required to initiate actin polymerization. The SH3 domain of yeast Abp1 binds and localizes the kinases, Ark1p and Prk1p, which facilitate actin patch disassembly following vesicle internalization. It also mediates the localization to the actin patch of the synaptojanin-like protein, Sjl2p, which plays a key role in endocytosis. 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: 212894 [Multi-domain]  Cd Length: 53  Bit Score: 36.73  E-value: 6.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2024466778 1549 ALFDYDpvsmspnpdAAEE-ELPFKEGQILKV--CGDKDadgFYRGECAGREGYIPCNMVSE 1607
Cdd:cd11961      4 ALYDYD---------AAEDnELSFFENDKIINieFVDDD---WWLGECHGSRGLFPSNYVEL 53
SH3_CD2AP_1 cd12053
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1547-1609 7.09e-03

First Src Homology 3 domain (SH3A) 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 first SH3 domain (SH3A) of CD2AP. SH3A binds to the PXXXPR motif present in c-Cbl and the cytoplasmic domain of cell adhesion protein CD2. Its interaction with CD2 anchors CD2 at sites of cell contact. 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: 212986  Cd Length: 56  Bit Score: 36.36  E-value: 7.09e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2024466778 1547 FVALFDYDPVSmspnpdaaEEELPFKEGQILKVCGDKDADGFYRGECAGREGYIPCNMVSEVQ 1609
Cdd:cd12053      2 YIVEYDYDAVH--------EDELTIRVGEIIRNVKKLEEEGWLEGELNGRRGMFPDNFVKEIK 56
SH3_Bem1p_1 cd11878
First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this ...
 1690-1744 7.60e-03

First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this subfamily bear similarity to Saccharomyces cerevisiae Bem1p, containing two Src Homology 3 (SH3) domains at the N-terminus, a central PX domain, and a C-terminal PB1 domain. Bem1p is a scaffolding protein that is critical for proper Cdc42p activation during bud formation in yeast. During budding and mating, Bem1p migrates to the plasma membrane where it can serve as an adaptor for Cdc42p and some other proteins. Bem1p also functions as an effector of the G1 cyclin Cln3p and the cyclin-dependent kinase Cdc28p in promoting vacuolar fusion. SH3 domains bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs; they play a role in the regulation of enzymes by intramolecular interactions, changing the subcellular localization of signal pathway components and mediate multiprotein complex assemblies.


Pssm-ID: 212811 [Multi-domain]  Cd Length: 54  Bit Score: 36.50  E-value: 7.60e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 2024466778 1690 AVFDYNPKESSpnadaeaELTFSAGDIITVFGSMDDDGFY--YGELNQQRGLVPSNF 1744
Cdd:cd11878      4 ALYDYRAQTPG-------ELSFSKGDFFHVIGEEDQGEWYeaTNPVTGKRGLVPKSY 53
Laminin_I pfam06008
Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from ...
 340-524 8.27e-03

Laminin Domain I; coiled-coil structure. It has been suggested that the domains I and II from laminin A, B1 and B2 may come together to form a triple helical coiled-coil structure.


Pssm-ID: 310534 [Multi-domain]  Cd Length: 258  Bit Score: 40.09  E-value: 8.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  340 QQIQQLEFELKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQsenaRLAEEnlqLNEKAGWAGQVESENADLKLQVVLVT 419
Cdd:pfam06008   54 QETEELQKKATQTLAKAQQVNAESERTLGHAKELAEAIKNLI----DNIKE---INEKVATLGENDFALPSSDLSRMLAE 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  420 KERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQE-----------KQEEVR-RLQQAQAEAkRE 487
Cdd:pfam06008  127 AQRMLGEIRSRDFGTQLQNAEAELKAAQDLLSRIQTWFQSPQEENKALANalrdslaeyeaKLSDLReLLREAAAKT-RD 205

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 2024466778  488 HEGAVQLLEARVKDLEDQCRSQTEQFSLLSQELKQFR 524
Cdd:pfam06008  206 ANRLNLANQANLREFQRKKEEVSEQKNQLEETLKTAR 242
AtpF COG0711
FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ...
 432-502 9.79e-03

FoF1-type ATP synthase, membrane subunit b or b' [Energy production and conversion]; FoF1-type ATP synthase, membrane subunit b or b' is part of the Pathway/BioSystem: FoF1-type ATP synthase


Pssm-ID: 440475 [Multi-domain]  Cd Length: 152  Bit Score: 38.62  E-value: 9.79e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2024466778  432 LQTKLENLEQVLKHMRdvAERRQLLEAEHKEALLVLQEKQEEV-----RRLQQAQAEAKREHEGAVQLLEARVKDL 502
Cdd:COG0711     50 AEAALAEYEEKLAEAR--AEAAEIIAEARKEAEAIAEEAKAEAeaeaeRIIAQAEAEIEQERAKALAELRAEVADL 123
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
337-504 9.88e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 9.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  337 ESSQQIQQLefeLKKKRKKCENLEHEVRKKHKRCKELEIQLQEVQSENARLAEENLQLNEkagwagqvesenadLKLQVV 416
Cdd:PRK03918   186 KRTENIEEL---IKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEEIEE--------------LEKELE 248

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2024466778  417 LVTKERDSVIQRNQGLQTKLENLEQVLKHMRDVAERRQLLEAEHKEALLVLQEKQEEVRRLQQAQAEAKReHEGAVQLLE 496
Cdd:PRK03918   249 SLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKELKEKAEEYIKLSEFYEEYLDELREIEKRLSR-LEEEINGIE 327


                   ....*...
gi 2024466778  497 ARVKDLED 504
Cdd:PRK03918   328 ERIKELEE 335
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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