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Conserved domains on  [gi|1835591054|ref|XP_033812235|]
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RIMS-binding protein 2 isoform X4 [Geotrypetes seraphini]

Protein Classification

fibronectin type III domain-containing protein( domain architecture ID 10878974)

fibronectin type III (FN3) domain-containing protein may be involved in specific interactions with other molecules through its FN3 domain

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 ...
 1222-1283 1.25e-40

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: 143.59  E-value: 1.25e-40
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1222 IFVALFDYDPLTMSPNPDAADEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd12012      1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1348-1408 1.04e-38

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: 138.28  E-value: 1.04e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12013      1 RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 483-543 4.79e-36

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: 130.55  E-value: 4.79e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054  483 LCIARYSYNPF-DGPNENPEAELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVEF 543
Cdd:cd12014      1 VFVARYSYNPLrDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER 62
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-378 1.23e-11

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  221 QWKDLEYELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMRE 300
Cdd:COG1196    233 KLRELEAELEELEAELEELE---AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  301 ----AAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFR 376
Cdd:COG1196    310 rrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389


                   ..
gi 1835591054  377 QQ 378
Cdd:COG1196    390 EA 391
SMC_prok_B super family cl37069
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 65-384 3.51e-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]


The actual alignment was detected with superfamily member TIGR02168:

Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.53  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   65 AVRLRKEIKPESRI-SPAAALKKPSAkqrmrSVNGGPGQfqGINKDLATEKDME-----IKLLQVECEELKNRLCCLKEG 138
Cdd:TIGR02168  634 ALELAKKLRPGYRIvTLDGDLVRPGG-----VITGGSAK--TNSSILERRREIEeleekIEELEEKIAELEKALAELRKE 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  139 LmgqrpSDVEQLLKQSQKELLWLQRQLSFISTGGPTCILPSSKLRNDLPYLHPVLSQ-------------KTFDRIPFLE 205
Cdd:TIGR02168  707 L-----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerleEAEEELAEAE 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  206 EKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKalqydqvksdYDQLRETISKVIKERDLALKGKHQLQ 285
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER----------LESLERRIAATERRLEDLEEQIEELS 851

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  286 AKLENLEQVLKHMREAAErrqQLELEHEQALAVLTAKQQEIELLQKAQveakkehegavQLLETKVQELEEKCRIQSEQF 365
Cdd:TIGR02168  852 EDIESLAAEIEELEELIE---ELESELEALLNERASLEEALALLRSEL-----------EELSEELRELESKRSELRREL 917

                          330
                   ....*....|....*....
gi 1835591054  366 NLLSKELERFRQQTGKIDL 384
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEV 936
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 799-893 2.94e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  799 PAPPQDIRIQAGpTPTAILVTWKPPtltptgTSNGANITGY-VAY--AKGQKVAEVVFPTAESTVVdllRIQNLEAK--- 872
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPP------EDDGGPITGYvVEYreKGSGDWKEVEVTPGSETSY---TLTGLKPGtey 70

                           90       100
                   ....*....|....*....|.
gi 1835591054  873 EITIRSLSAQGESEDSAPTAI 893
Cdd:cd00063     71 EFRVRAVNGGGESPPSESVTV 91
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 766-1005 6.07e-05

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  766 LLAKPHQMPWQLPLEQREKKEAFAEFSTLPAGPPAPPQDIRIQAGPTPTAILVTW-------KPPTLTPTGTSNGANITG 838
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadpppppPTPEPAPHALVSATPLPP 2723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  839 YVAYAKGQKVAEVVFP----TAESTVVDllriqnleAKEITIRSLSAQGESEDSAPTAIPPELLMPPTPHPRTSPKLKPL 914
Cdd:PHA03247  2724 GPAAARQASPALPAAPappaVPAGPATP--------GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  915 ASAGAPDTKDEHLGP--PRKIDESWEQTPvhGHTLEPPTANFHSPAHGRRSPSPQRILPQPQGTPVSNTVAKAMAREAAQ 992
Cdd:PHA03247  2796 ESLPSPWDPADPPAAvlAPAAALPPAASP--AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAA 2873

                          250
                   ....*....|...
gi 1835591054  993 RVAESNRMEKRSI 1005
Cdd:PHA03247  2874 KPAAPARPPVRRL 2886
fn3 pfam00041
Fibronectin type III domain;
705-768 1.67e-04

Fibronectin type III domain;


:

Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 1.67e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  705 APSQLKVDNITQTSAGLSWLPTNSNYSHVIF-------LNEEEFD---IVKAAIYKYQFFNLKPNMAYKVKLLA 768
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGyeveyrpKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 612-693 5.67e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


:

Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 5.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  612 PRKITLIKQLAKSVIVGWEPPvvPPGWGNINSYNVLV-----DKDIRLSVNFGSRTKALIEKLNLATcTYRISIQSVTNR 686
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYrekgsGDWKEVEVTPGSETSYTLTGLKPGT-EYEFRVRAVNGG 80


                   ....*..
gi 1835591054  687 GNSDELQ 693
Cdd:cd00063     81 GESPPSE 87
 
Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1222-1283 1.25e-40

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: 143.59  E-value: 1.25e-40
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1222 IFVALFDYDPLTMSPNPDAADEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd12012      1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1348-1408 1.04e-38

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: 138.28  E-value: 1.04e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12013      1 RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 483-543 4.79e-36

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: 130.55  E-value: 4.79e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054  483 LCIARYSYNPF-DGPNENPEAELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVEF 543
Cdd:cd12014      1 VFVARYSYNPLrDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER 62
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1347-1407 2.46e-13

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: 65.64  E-value: 2.46e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054  1347 RRMVALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELN-GQKGLVPSNFLE 1407
Cdd:smart00326    3 PQVRALYDYTAQDPD-------ELSFKKGDIITVL-EKSDDGWWKGRLGrGKEGLFPSNYVE 56
SH3_9 pfam14604
Variant SH3 domain;
1351-1407 9.41e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 63.79  E-value: 9.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:pfam14604    1 ALYPYEPKD-------DDELSLQRGDVITVIEE-SEDGWWEGINTGRTGLVPANYVE 49
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-378 1.23e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  221 QWKDLEYELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMRE 300
Cdd:COG1196    233 KLRELEAELEELEAELEELE---AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  301 ----AAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFR 376
Cdd:COG1196    310 rrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389


                   ..
gi 1835591054  377 QQ 378
Cdd:COG1196    390 EA 391
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 480-542 2.06e-09

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: 54.85  E-value: 2.06e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054   480 KVHLCIARYSYNPfdgpnENPEaELPLTMGKYLYVYgDMDEDGFYEGELLDGQRGLVPSNFVE 542
Cdd:smart00326    1 EGPQVRALYDYTA-----QDPD-ELSFKKGDIITVL-EKSDDGWWKGRLGRGKEGLFPSNYVE 56
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1223-1284 6.91e-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: 52.98  E-value: 6.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1223 FVALFDYDPltmsPNPdaadEELPFKEGQIIKVYgDKDTDGFYRGATCARRGLIPCNMVSEI 1284
Cdd:pfam07653    2 GRVIFDYVG----TDK----NGLTLKKGDVVKVL-GKDNDGWWEGETGGRVGLVPSTAVEEI 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 65-384 3.51e-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: 58.53  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   65 AVRLRKEIKPESRI-SPAAALKKPSAkqrmrSVNGGPGQfqGINKDLATEKDME-----IKLLQVECEELKNRLCCLKEG 138
Cdd:TIGR02168  634 ALELAKKLRPGYRIvTLDGDLVRPGG-----VITGGSAK--TNSSILERRREIEeleekIEELEEKIAELEKALAELRKE 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  139 LmgqrpSDVEQLLKQSQKELLWLQRQLSFISTGGPTCILPSSKLRNDLPYLHPVLSQ-------------KTFDRIPFLE 205
Cdd:TIGR02168  707 L-----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerleEAEEELAEAE 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  206 EKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKalqydqvksdYDQLRETISKVIKERDLALKGKHQLQ 285
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER----------LESLERRIAATERRLEDLEEQIEELS 851

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  286 AKLENLEQVLKHMREAAErrqQLELEHEQALAVLTAKQQEIELLQKAQveakkehegavQLLETKVQELEEKCRIQSEQF 365
Cdd:TIGR02168  852 EDIESLAAEIEELEELIE---ELESELEALLNERASLEEALALLRSEL-----------EELSEELRELESKRSELRREL 917

                          330
                   ....*....|....*....
gi 1835591054  366 NLLSKELERFRQQTGKIDL 384
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEV 936
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-378 2.41e-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: 55.83  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  199 DRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKalqYDQVKSDYDQLRETISKVIKErdlal 278
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE---IEELQKELYALANEISRLEQQ----- 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  279 kgKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKC 358
Cdd:TIGR02168  304 --KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          170       180
                   ....*....|....*....|....*..
gi 1835591054  359 RIQS-------EQFNLLSKELERFRQQ 378
Cdd:TIGR02168  382 ETLRskvaqleLQIASLNNEIERLEAR 408
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1219-1281 2.43e-07

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


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 48.69  E-value: 2.43e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  1219 SVRIFVALFDYDPltmsPNPDaadeELPFKEGQIIKVYgDKDTDGFYRGATCA-RRGLIPCNMV 1281
Cdd:smart00326    1 EGPQVRALYDYTA----QDPD----ELSFKKGDIITVL-EKSDDGWWKGRLGRgKEGLFPSNYV 55
SH3_9 pfam14604
Variant SH3 domain;
486-542 4.05e-07

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 48.00  E-value: 4.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  486 ARYSYNPFDgpnenpEAELPLTMGKYLYVYGDmDEDGFYEGELlDGQRGLVPSNFVE 542
Cdd:pfam14604    1 ALYPYEPKD------DDELSLQRGDVITVIEE-SEDGWWEGIN-TGRTGLVPANYVE 49
mukB PRK04863
chromosome partition protein MukB;
224-378 1.09e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.81  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  224 DLEYELKDAVQEK----THLNLHYASLSQKALQYDQVKSDYDQLR-----------ETISKVIKE----RDLALKGK--- 281
Cdd:PRK04863   834 DPEAELRQLNRRRveleRALADHESQEQQQRSQLEQAKEGLSALNrllprlnlladETLADRVEEireqLDEAEEAKrfv 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  282 HQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLqkAQVEAKKEH---EGAVQLLEtKVQELEEKC 358
Cdd:PRK04863   914 QQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL--TEVVQRRAHfsyEDAAEMLA-KNSDLNEKL 990

                          170       180
                   ....*....|....*....|
gi 1835591054  359 RIQSEQfnlLSKELERFRQQ 378
Cdd:PRK04863   991 RQRLEQ---AEQERTRAREQ 1007
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 799-893 2.94e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  799 PAPPQDIRIQAGpTPTAILVTWKPPtltptgTSNGANITGY-VAY--AKGQKVAEVVFPTAESTVVdllRIQNLEAK--- 872
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPP------EDDGGPITGYvVEYreKGSGDWKEVEVTPGSETSY---TLTGLKPGtey 70

                           90       100
                   ....*....|....*....|.
gi 1835591054  873 EITIRSLSAQGESEDSAPTAI 893
Cdd:cd00063     71 EFRVRAVNGGGESPPSESVTV 91
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 250-379 5.29e-05

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 47.06  E-value: 5.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  250 ALQYDQVKSDYDQLRETISKvikerdlaLKGK-HQLQAKLENLEQvlKHMREAAERRQQLELEHEQALAVLTAKQ---QE 325
Cdd:pfam09787   46 TLELEELRQERDLLREEIQK--------LRGQiQQLRTELQELEA--QQQEEAESSREQLQELEEQLATERSARReaeAE 115

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054  326 IELLQKAQVEAKKEHEGAVQLLETKVQELE---EKCRIQ---SEQFNLLSKELE-RFRQQT 379
Cdd:pfam09787  116 LERLQEELRYLEEELRRSKATLQSRIKDREaeiEKLRNQltsKSQSSSSQSELEnRLHQLT 176
PHA03247 PHA03247
large tegument protein UL36; Provisional
 766-1005 6.07e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  766 LLAKPHQMPWQLPLEQREKKEAFAEFSTLPAGPPAPPQDIRIQAGPTPTAILVTW-------KPPTLTPTGTSNGANITG 838
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadpppppPTPEPAPHALVSATPLPP 2723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  839 YVAYAKGQKVAEVVFP----TAESTVVDllriqnleAKEITIRSLSAQGESEDSAPTAIPPELLMPPTPHPRTSPKLKPL 914
Cdd:PHA03247  2724 GPAAARQASPALPAAPappaVPAGPATP--------GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  915 ASAGAPDTKDEHLGP--PRKIDESWEQTPvhGHTLEPPTANFHSPAHGRRSPSPQRILPQPQGTPVSNTVAKAMAREAAQ 992
Cdd:PHA03247  2796 ESLPSPWDPADPPAAvlAPAAALPPAASP--AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAA 2873

                          250
                   ....*....|...
gi 1835591054  993 RVAESNRMEKRSI 1005
Cdd:PHA03247  2874 KPAAPARPPVRRL 2886
fn3 pfam00041
Fibronectin type III domain;
705-768 1.67e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 1.67e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  705 APSQLKVDNITQTSAGLSWLPTNSNYSHVIF-------LNEEEFD---IVKAAIYKYQFFNLKPNMAYKVKLLA 768
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGyeveyrpKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQA 75
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 799-885 1.71e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 1.71e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   799 PAPPQDIRIQAgPTPTAILVTWKPptltPTGTSNGANITGY-VAYAKGQKVAEVVFPTAESTVVdllRIQNLEAK---EI 874
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEP----PPDDGITGYIVGYrVEYREEGSEWKEVNVTPSSTSY---TLTGLKPGteyEF 72

                            90
                    ....*....|.
gi 1835591054   875 TIRSLSAQGES 885
Cdd:smart00060   73 RVRAVNGAGEG 83
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 222-378 4.87e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  222 WKDLEYELKDAV-----------QEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIkerdlaLKGKHQLQAKlEN 290
Cdd:cd16269    126 SAPLEEKISQGSysvpggyqlylEDREKLVEKYRQVPRKGVKAEEVLQEFLQSKEAEAEAI------LQADQALTEK-EK 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  291 LEQVLKHMREAAERRQQLEleheqalavltaKQQEIELLQKAQvEAKKEHEGAVQLLETKVQelEEKCRIQSEQFNLLS- 369
Cdd:cd16269    199 EIEAERAKAEAAEQERKLL------------EEQQRELEQKLE-DQERSYEEHLRQLKEKME--EERENLLKEQERALEs 263

                          170
                   ....*....|.
gi 1835591054  370 --KELERFRQQ 378
Cdd:cd16269    264 klKEQEALLEE 274
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 612-693 5.67e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 5.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  612 PRKITLIKQLAKSVIVGWEPPvvPPGWGNINSYNVLV-----DKDIRLSVNFGSRTKALIEKLNLATcTYRISIQSVTNR 686
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYrekgsGDWKEVEVTPGSETSYTLTGLKPGT-EYEFRVRAVNGG 80


                   ....*..
gi 1835591054  687 GNSDELQ 693
Cdd:cd00063     81 GESPPSE 87
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 34-384 7.25e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   34 EEGKLHKKERTDFT---KKERNHRSEAKIPQKPhaVRLrKEIK---PESRISP-------------AAALKKPSAKQRMR 94
Cdd:pfam02463   83 NEDHELPIDKEEVSirrRVYRGGDSEYYINGKN--VTK-KEVAellESQGISPeaynflvqggkieIIAMMKPERRLEIE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   95 SVNGGPGQFQGI---NKDLATEKDMEIKLLQVECEELKNRLcclKEGLMGQRPSDVEQLLKQSQKELLWLqrqlsfistg 171
Cdd:pfam02463  160 EEAAGSRLKRKKkeaLKKLIEETENLAELIIDLEELKLQEL---KLKEQAKKALEYYQLKEKLELEEEYL---------- 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  172 gptcilpssklrndlpylhpvlsqkTFDRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKThlnlhyaslsqkal 251
Cdd:pfam02463  227 -------------------------LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL-------------- 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  252 qyDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMREAAERrqqLELEHEQALAVLTAKQQEIELLQK 331
Cdd:pfam02463  268 --AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE---SEKEKKKAEKELKKEKEEIEELEK 342

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  332 AqveaKKEHEGAVQLLETKVQELEEKCR--IQSEQFNLLSKELERFRQQTGKIDL 384
Cdd:pfam02463  343 E----LKELEIKREAEEEEEEELEKLQEklEQLEEELLAKKKLESERLSSAAKLK 393
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
40-359 1.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   40 KKERTDFTKKERNHRSEAKipqkphavRLRKEIKPESRISPaaaLKKpSAKQrMRSVNGgpgQFQGINKDLATEKDMEIK 119
Cdd:PRK03918   465 EKELKEIEEKERKLRKELR--------ELEKVLKKESELIK---LKE-LAEQ-LKELEE---KLKKYNLEELEKKAEEYE 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  120 LLQVECEELKNRLCCLKEglmgqrpsDVEQLlKQSQKELLWLQRQLSfistggptcilpssKLRNDLPYLHPVLSQKTFD 199
Cdd:PRK03918   529 KLKEKLIKLKGEIKSLKK--------ELEKL-EELKKKLAELEKKLD--------------ELEEELAELLKELEELGFE 585

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  200 RIPFLEEKTQVFKSDVNqekqqwkdlEY-ELKDAVQEKTHLnlhyaslsQKALqydqvksdyDQLRETISKVIKERDLAL 278
Cdd:PRK03918   586 SVEELEERLKELEPFYN---------EYlELKDAEKELERE--------EKEL---------KKLEEELDKAFEELAETE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  279 KGKHQLQAKLENLEQvlKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQ----------KAQVEAKKEHEGAVQLLE 348
Cdd:PRK03918   640 KRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRReeikktleklKEELEEREKAKKELEKLE 717

                          330
                   ....*....|....
gi 1835591054  349 ---TKVQELEEKCR 359
Cdd:PRK03918   718 kalERVEELREKVK 731
fn3 pfam00041
Fibronectin type III domain;
801-888 2.02e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  801 PPQDIRIQaGPTPTAILVTWKPPtltptgTSNGANITGY-VAYAK---GQKVAEVVFPTAESTVVdllrIQNLEAK---E 873
Cdd:pfam00041    2 APSNLTVT-DVTSTSLTVSWTPP------PDGNGPITGYeVEYRPknsGEPWNEITVPGTTTSVT----LTGLKPGteyE 70

                           90
                   ....*....|....*
gi 1835591054  874 ITIRSLSAQGESEDS 888
Cdd:pfam00041   71 VRVQAVNGGGEGPPS 85
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 705-769 2.20e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 2.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  705 APSQLKVDNITQTSAGLSWLPTNSNYSHV----IFLNE------EEFDIVKAAIYKYQFFNLKPNMAYKVKLLAK 769
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPItgyvVEYREkgsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 612-689 3.50e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.98  E-value: 3.50e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   612 PRKITLIKQLAKSVIVGWEPPVVPPGWGNINSYNVLVDKDIRLSVNF---GSRTKALIEKLNLATcTYRISIQSVTNRGN 688
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVnvtPSSTSYTLTGLKPGT-EYEFRVRAVNGAGE 82


                    .
gi 1835591054   689 S 689
Cdd:smart00060   83 G 83
fn3 pfam00041
Fibronectin type III domain;
610-691 4.98e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 4.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  610 PYPRKITLIKQLAKSVIVGWEPPvvPPGWGNINSYNVLV------DKDIRLSVnFGSRTKALIEKLNLATcTYRISIQSV 683
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYrpknsgEPWNEITV-PGTTTSVTLTGLKPGT-EYEVRVQAV 76


                   ....*...
gi 1835591054  684 TNRGNSDE 691
Cdd:pfam00041   77 NGGGEGPP 84
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 705-769 9.50e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.82  E-value: 9.50e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054   705 APSQLKVDNITQTSAGLSWLP--TNSNYSHVIFL--------NEEEFDIVKAAIYKYQFFNLKPNMAYKVKLLAK 769
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYrveyreegSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
 
Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1222-1283 1.25e-40

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: 143.59  E-value: 1.25e-40
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1222 IFVALFDYDPLTMSPNPDAADEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd12012      1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1348-1408 1.04e-38

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: 138.28  E-value: 1.04e-38
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12013      1 RMVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 483-543 4.79e-36

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: 130.55  E-value: 4.79e-36
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054  483 LCIARYSYNPF-DGPNENPEAELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVEF 543
Cdd:cd12014      1 VFVARYSYNPLrDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER 62
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 1348-1408 4.23e-29

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: 110.87  E-value: 4.23e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1348 RMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNG-QKGLVPSNFLEE 1408
Cdd:cd11851      1 LMVALYDYNPETMSPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGgRKGLVPSNFVQE 62
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 483-543 2.19e-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: 108.94  E-value: 2.19e-28
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054  483 LCIARYSYNPFDG-PNENPEAELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVEF 543
Cdd:cd11851      1 LMVALYDYNPETMsPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGGRKGLVPSNFVQE 62
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
 1222-1283 1.25e-24

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: 98.16  E-value: 1.25e-24
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054 1222 IFVALFDYDPLTMSPNPDAaDEELPFKEGQIIKVYGDKDTDGFYRGATCA-RRGLIPCNMVSE 1283
Cdd:cd11851      1 LMVALYDYNPETMSPNDDP-EEELSFHAGDVVRVYGPMDEDGFYYGELEGgRKGLVPSNFVQE 62
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1350-1408 9.44e-23

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: 92.74  E-value: 9.44e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1350 VALYDYDPRESSPNVD-VEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12012      3 VALFDYDPLTMSPNPDaAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1350-1407 7.52e-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: 87.41  E-value: 7.52e-21
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1350 VALYDYDPRESSPNVDVEAELTFCTGDIITVFGEIDEDGFYYGEL-NGQKGLVPSNFLE 1407
Cdd:cd12014      3 VARYSYNPLRDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELlDGRRGLVPSNFVE 61
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 485-542 3.10e-20

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: 85.51  E-value: 3.10e-20
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054  485 IARYSYNPFD-GPNENPEAELPLTMGKYLYVYGDMDEDGFYEGElLDGQRGLVPSNFVE 542
Cdd:cd12013      3 VALFDYDPREsSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGE-LNGQRGLVPSNFLE 60
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1222-1283 3.79e-19

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: 82.43  E-value: 3.79e-19
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1222 IFVALFDYDPLTMSPNPDAaDEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd12013      1 RMVALFDYDPRESSPNVDA-EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 1222-1281 3.61e-16

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: 73.93  E-value: 3.61e-16
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054 1222 IFVALFDYDPLTMSPN--PDAadeELPFKEGQIIKVYGDKDTDGFYRGATC-ARRGLIPCNMV 1281
Cdd:cd12014      1 VFVARYSYNPLRDSPNenPEA---ELPLNAGDYVYVYGDMDEDGFYEGELLdGRRGLVPSNFV 60
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
 485-542 9.32e-14

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: 67.32  E-value: 9.32e-14
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  485 IARYSYNPFD-GPNENP-EAELPLTMGKYLYVYGDMDEDGFYEGElLDGQRGLVPSNFVE 542
Cdd:cd12012      3 VALFDYDPLTmSPNPDAaEEELPFKEGQLIKVYGDKDADGFYLGE-INGRRGLVPCNMVS 61
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1347-1407 2.46e-13

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: 65.64  E-value: 2.46e-13
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054  1347 RRMVALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELN-GQKGLVPSNFLE 1407
Cdd:smart00326    3 PQVRALYDYTAQDPD-------ELSFKKGDIITVL-EKSDDGWWKGRLGrGKEGLFPSNYVE 56
SH3_9 pfam14604
Variant SH3 domain;
1351-1407 9.41e-13

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 63.79  E-value: 9.41e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:pfam14604    1 ALYPYEPKD-------DDELSLQRGDVITVIEE-SEDGWWEGINTGRTGLVPANYVE 49
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1348-1405 4.90e-12

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: 62.10  E-value: 4.90e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELN-GQKGLVPSNF 1405
Cdd:cd00174      1 YARALYDYEAQDDD-------ELSFKKGDIITVL-EKDDDGWWEGELNgGREGLFPANY 51
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 221-378 1.23e-11

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 69.58  E-value: 1.23e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  221 QWKDLEYELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMRE 300
Cdd:COG1196    233 KLRELEAELEELEAELEELE---AELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEE 309

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  301 ----AAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFR 376
Cdd:COG1196    310 rrreLEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL 389


                   ..
gi 1835591054  377 QQ 378
Cdd:COG1196    390 EA 391
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 1348-1408 2.69e-11

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: 60.05  E-value: 2.69e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFgEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11823      1 RCKALYSYTANR-------EDELSLQPGDIIEVH-EKQDDGWWLGELNGKKGIFPATYVEE 53
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1348-1409 3.54e-11

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: 59.53  E-value: 3.54e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1348 RMVALYDYDPRESSPnvdveaeLTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:pfam07653    1 YGRVIFDYVGTDKNG-------LTLKKGDVVKVLGK-DNDGWWEGETGGRVGLVPSTAVEEI 54
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 1351-1409 8.39e-11

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: 58.42  E-value: 8.39e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd11803      5 ALYDFEPEN-------EGELGFKEGDIITLTNQIDEN-WYEGMVNGQSGFFPVNYVEVL 55
SH3_PACSIN cd11843
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ...
 1348-1407 1.91e-10

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: 57.43  E-value: 1.91e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11843      1 PVRALYDYEGQESD-------ELSFKAGDILTKLEEEDEQGWCKGRLDGRVGLYPANYVE 53
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 480-542 2.06e-09

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: 54.85  E-value: 2.06e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054   480 KVHLCIARYSYNPfdgpnENPEaELPLTMGKYLYVYgDMDEDGFYEGELLDGQRGLVPSNFVE 542
Cdd:smart00326    1 EGPQVRALYDYTA-----QDPD-ELSFKKGDIITVL-EKSDDGWWKGRLGRGKEGLFPSNYVE 56
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1348-1408 3.21e-09

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: 53.96  E-value: 3.21e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYdpresspNVDVEAELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11840      1 QVIALFPY-------TAQNEDELSFQKGDIINVLSK-DDPDWWRGELNGQTGLFPSNYVEP 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
220-382 3.50e-09

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 61.32  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  220 QQWKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIKERDL--ALKGKHQLQAKLENLEQVLKH 297
Cdd:COG4717     71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLEE 150

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  298 MREAAERRQQLELEHEQALAVLTAKQQEIELLQKaqvEAKKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFRQ 377
Cdd:COG4717    151 LEERLEELRELEEELEELEAELAELQEELEELLE---QLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEE 227


                   ....*
gi 1835591054  378 QTGKI 382
Cdd:COG4717    228 ELEQL 232
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
 1349-1405 5.14e-09

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: 53.27  E-value: 5.14e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1349 MVALYDYDPresspnvDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNF 1405
Cdd:cd11778      2 VEALYDYEA-------QGDDEISIRVGDRIAVIRGDDGSGWTYGEINGVKGLFPTSY 51
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 1223-1284 6.91e-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: 52.98  E-value: 6.91e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1223 FVALFDYDPltmsPNPdaadEELPFKEGQIIKVYgDKDTDGFYRGATCARRGLIPCNMVSEI 1284
Cdd:pfam07653    2 GRVIFDYVG----TDK----NGLTLKKGDVVKVL-GKDNDGWWEGETGGRVGLVPSTAVEEI 54
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1350-1403 7.02e-09

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: 52.98  E-value: 7.02e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELN-GQKGLVPS 1403
Cdd:pfam00018    1 VALYDYTAQEPD-------ELSFKKGDIIIVL-EKSEDGWWKGRNKgGKEGLIPS 47
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 1348-1407 7.90e-09

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: 53.09  E-value: 7.90e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEdGFYYGELN-GQKGLVPSNFLE 1407
Cdd:cd11819      1 RAKALYDYQAAE-------DNEISFVEGDIITQIEQIDE-GWWLGVNAkGQKGLFPANYVE 53
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
 1348-1407 9.28e-09

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: 52.68  E-value: 9.28e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11882      1 RARALYACKAEDES-------ELSFEPGQIITNVQPSDEPGWLEGTLNGRTGLIPENYVE 53
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 1351-1408 9.99e-09

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: 52.74  E-value: 9.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDED-GFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11875      4 VLFDYEAEN-------EDELTLREGDIVTILSKDCEDkGWWKGELNGKRGVFPDNFVEP 55
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1351-1408 1.97e-08

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: 51.86  E-value: 1.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11805      4 ALYDFNPQEPG-------ELEFRRGDIITVLDSSDPD-WWKGELRGRVGIFPANYVQP 53
SH3_MyoIe_If_like cd11827
Src homology 3 domain of Myosins Ie, If, and similar proteins; Myosins Ie (MyoIe) and If ...
 1351-1408 2.24e-08

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: 51.65  E-value: 2.24e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11827      4 ALYAYDAQDTD-------ELSFNEGDIIEILKE-DPSGWWTGRLRGKEGLFPGNYVEK 53
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1351-1408 3.06e-08

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: 51.15  E-value: 3.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11772      4 ALYDYEAQHPD-------ELSFEEGDLLYIS-DKSDPNWWKATCGGKTGLIPSNYVEE 53
SH3_SH3RF_1 cd11786
First Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ...
 1351-1407 3.17e-08

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: 51.21  E-value: 3.17e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11786      4 ALYNYEGKEPG-------DLSFKKGDIILLRKRIDEN-WYHGECNGKQGFFPASYVQ 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 65-384 3.51e-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: 58.53  E-value: 3.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   65 AVRLRKEIKPESRI-SPAAALKKPSAkqrmrSVNGGPGQfqGINKDLATEKDME-----IKLLQVECEELKNRLCCLKEG 138
Cdd:TIGR02168  634 ALELAKKLRPGYRIvTLDGDLVRPGG-----VITGGSAK--TNSSILERRREIEeleekIEELEEKIAELEKALAELRKE 706

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  139 LmgqrpSDVEQLLKQSQKELLWLQRQLSFISTGGPTCILPSSKLRNDLPYLHPVLSQ-------------KTFDRIPFLE 205
Cdd:TIGR02168  707 L-----EELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEleaeieeleerleEAEEELAEAE 781

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  206 EKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKalqydqvksdYDQLRETISKVIKERDLALKGKHQLQ 285
Cdd:TIGR02168  782 AEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRER----------LESLERRIAATERRLEDLEEQIEELS 851

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  286 AKLENLEQVLKHMREAAErrqQLELEHEQALAVLTAKQQEIELLQKAQveakkehegavQLLETKVQELEEKCRIQSEQF 365
Cdd:TIGR02168  852 EDIESLAAEIEELEELIE---ELESELEALLNERASLEEALALLRSEL-----------EELSEELRELESKRSELRREL 917

                          330
                   ....*....|....*....
gi 1835591054  366 NLLSKELERFRQQTGKIDL 384
Cdd:TIGR02168  918 EELREKLAQLELRLEGLEV 936
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
 1351-1408 3.90e-08

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: 51.18  E-value: 3.90e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPResspNVDveaELTFCTGDIITVFGEIdEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11874      4 VLFSYTPQ----NED---ELELKVGDTIEVLGEV-EEGWWEGKLNGKVGVFPSNFVKE 53
SH3_FCHSD_2 cd11762
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 1351-1408 5.66e-08

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: 50.86  E-value: 5.66e-08
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEID---EDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11762      4 ALYDYEAQS-------DEELSFPEGAIIRILRKDDngvDDGWWEGEFNGRVGVFPSLVVEE 57
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-378 6.55e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 57.64  E-value: 6.55e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQ 283
Cdd:COG1196    321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAE---AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 LQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSE 363
Cdd:COG1196    398 LAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEA 477

                          170
                   ....*....|....*
gi 1835591054  364 QFNLLSKELERFRQQ 378
Cdd:COG1196    478 ALAELLEELAEAAAR 492
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
 1348-1407 1.16e-07

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: 49.95  E-value: 1.16e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDGFYYGEL-NGQKGLVPSNFLE 1407
Cdd:cd11998      2 RVRALYDYDGQE-------QDELSFKAGDELTKLEDEDEQGWCKGRLdSGQVGLYPANYVE 55
SH3_Abi cd11826
Src homology 3 domain of Abl Interactor proteins; Abl interactor (Abi) proteins are adaptor ...
 1348-1407 1.22e-07

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: 49.63  E-value: 1.22e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYDpresspnVDVEAELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11826      1 KVVALYDYT-------ADKDDELSFQEGDIIYVTKK-NDDGWYEGVLNGVTGLFPGNYVE 52
SH3_PSTPIP1 cd11824
Src homology 3 domain of Proline-Serine-Threonine Phosphatase-Interacting Protein 1; PSTPIP1, ...
 1350-1407 1.27e-07

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: 49.68  E-value: 1.27e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11824      3 SVLYDYTAQEDD-------ELSISKGDVVAVI-EKGEDGWWTVERNGQKGLVPGTYLE 52
SH3_CD2AP_1 cd12053
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1353-1409 1.77e-07

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: 49.07  E-value: 1.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1353 YDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd12053      6 YDYDAVH-------EDELTIRVGEIIRNVKKLEEEGWLEGELNGRRGMFPDNFVKEI 55
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 250-378 2.37e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.37e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  250 ALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAK------- 322
Cdd:COG1196    231 LLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDiarleer 310

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054  323 ----QQEIELLQKAQVEAKKEHEGAVQLLET---KVQELEEKCRIQSEQFNLLSKELERFRQQ 378
Cdd:COG1196    311 rrelEERLEELEEELAELEEELEELEEELEEleeELEEAEEELEEAEAELAEAEEALLEAEAE 373
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 199-378 2.41e-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: 55.83  E-value: 2.41e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  199 DRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKalqYDQVKSDYDQLRETISKVIKErdlal 278
Cdd:TIGR02168  232 LRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEE---IEELQKELYALANEISRLEQQ----- 303

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  279 kgKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKC 358
Cdd:TIGR02168  304 --KQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQL 381

                          170       180
                   ....*....|....*....|....*..
gi 1835591054  359 RIQS-------EQFNLLSKELERFRQQ 378
Cdd:TIGR02168  382 ETLRskvaqleLQIASLNNEIERLEAR 408
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
 1219-1281 2.43e-07

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


Pssm-ID: 214620 [Multi-domain]  Cd Length: 56  Bit Score: 48.69  E-value: 2.43e-07
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  1219 SVRIFVALFDYDPltmsPNPDaadeELPFKEGQIIKVYgDKDTDGFYRGATCA-RRGLIPCNMV 1281
Cdd:smart00326    1 EGPQVRALYDYTA----QDPD----ELSFKKGDIITVL-EKSDDGWWKGRLGRgKEGLFPSNYV 55
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 204-386 2.49e-07

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 55.71  E-value: 2.49e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLhyaSLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQ 283
Cdd:COG1196    237 LEAELEELEAELEELEAELEELEAELAELEAELEELRL---ELEELELELEEAQAEEYELLAELARLEQDIARLEERRRE 313

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 LQAKL-------ENLEQVLkhmREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEE 356
Cdd:COG1196    314 LEERLeeleeelAELEEEL---EELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLE 390

                          170       180       190
                   ....*....|....*....|....*....|
gi 1835591054  357 kcrIQSEQFNLLSKELERFRQQTGKIDLLS 386
Cdd:COG1196    391 ---ALRAAAELAAQLEELEEAEEALLERLE 417
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 1222-1283 2.64e-07

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: 48.45  E-value: 2.64e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1222 IFVALFDYDPltmspnpdAADEELPFKEGQIIKVYgDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11772      1 VFRALYDYEA--------QHPDELSFEEGDLLYIS-DKSDPNWWKATCGGKTGLIPSNYVEE 53
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 484-540 3.33e-07

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: 48.23  E-value: 3.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  484 CIARYSYNPfdgpneNPEAELPLTMGKYLYVYgDMDEDGFYEGELLDGQRGLVPSNF 540
Cdd:cd00174      2 ARALYDYEA------QDDDELSFKKGDIITVL-EKDDDGWWEGELNGGREGLFPANY 51
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
 1222-1279 3.46e-07

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: 48.23  E-value: 3.46e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1222 IFVALFDYDPltmspnpdAADEELPFKEGQIIKVYgDKDTDGFYRGATC-ARRGLIPCN 1279
Cdd:cd00174      1 YARALYDYEA--------QDDDELSFKKGDIITVL-EKDDDGWWEGELNgGREGLFPAN 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 113-378 3.74e-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: 55.06  E-value: 3.74e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  113 EKDMEIKLLQVECEELKNRLcclkeglmgqrpSDVEQLLKQSQKELLWLQRQLSFISTggptcilpssklrndlpYLHPV 192
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEI------------SRLEQQKQILRERLANLERQLEELEA-----------------QLEEL 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  193 LSQKTFDRipflEEKTQVfKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQkalQYDQVKSDYDQLRETISKVIK 272
Cdd:TIGR02168  329 ESKLDELA----EELAEL-EEKLEELKEELESLEAELEELEAELEELESRLEELEE---QLETLRSKVAQLELQIASLNN 400

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  273 ERDLALKGKHQLQAKLENLEQvlkhmreaaerrQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQ 352
Cdd:TIGR02168  401 EIERLEARLERLEDRRERLQQ------------EIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELRE 468

                          250       260
                   ....*....|....*....|....*.
gi 1835591054  353 ELEEKcriqSEQFNLLSKELERFRQQ 378
Cdd:TIGR02168  469 ELEEA----EQALDAAERELAQLQAR 490
SH3_CD2AP_2 cd12054
Second Src Homology 3 domain (SH3B) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1347-1409 4.02e-07

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


Pssm-ID: 212987 [Multi-domain]  Cd Length: 55  Bit Score: 48.42  E-value: 4.02e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054 1347 RRMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEdGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd12054      1 RQCKVLFEYVPQN-------EDELELKVGDIIDINEEVEE-GWWSGTLNGKSGLFPSNFVKEL 55
SH3_9 pfam14604
Variant SH3 domain;
486-542 4.05e-07

Variant SH3 domain;


Pssm-ID: 434066 [Multi-domain]  Cd Length: 49  Bit Score: 48.00  E-value: 4.05e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  486 ARYSYNPFDgpnenpEAELPLTMGKYLYVYGDmDEDGFYEGELlDGQRGLVPSNFVE 542
Cdd:pfam14604    1 ALYPYEPKD------DDELSLQRGDVITVIEE-SEDGWWEGIN-TGRTGLVPANYVE 49
SH3_CD2AP-like_1 cd11873
First Src Homology 3 domain (SH3A) of CD2-associated protein and similar proteins; This ...
 1349-1408 4.92e-07

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: 48.03  E-value: 4.92e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1349 MVALYDYDPRESSpnvdveaELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11873      2 VIVEFDYDAEEPD-------ELTLKVGDIITNVKK-MEEGWWEGTLNGKRGMFPDNFVKV 53
SH3_Eve1_5 cd11818
Fifth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1351-1405 5.81e-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: 47.48  E-value: 5.81e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054 1351 ALYDYdpresspNVDVEAELTFCTGDIITVFGEIDEDGFyYGELNGQKGLVPSNF 1405
Cdd:cd11818      4 ALYDF-------TGENEDELSFKAGDIITELESIDEEWM-SGELRGKSGIFPKNF 50
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 1367-1408 6.49e-07

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: 47.68  E-value: 6.49e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835591054 1367 EAELTFCTGDIITVFGEIDEdGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12055     13 EDELELKVGDIIEVVGEVEE-GWWEGVLNGKTGMFPSNFIKE 53
SH3_AHI-1 cd11812
Src Homology 3 domain of Abelson helper integration site-1 (AHI-1); AHI-1, also called ...
 1348-1406 7.74e-07

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: 47.51  E-value: 7.74e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEiDEDGFYYGEL-NGQKGLVPSNFL 1406
Cdd:cd11812      1 TVVALYDYTANRSD-------ELTIHRGDIIRVLYK-DNDNWWFGSLvNGQQGYFPANYV 52
SH3_Nck_2 cd11766
Second Src Homology 3 domain of Nck adaptor proteins; Nck adaptor proteins regulate actin ...
 1350-1408 7.96e-07

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: 47.26  E-value: 7.96e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1350 VALYDYDPREsspnvdvEAELTFCTGDIITVFgEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11766      3 VVKFNYEAQR-------EDELSLRKGDRVLVL-EKSSDGWWRGECNGQVGWFPSNYVTE 53
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
 1347-1406 8.10e-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: 47.25  E-value: 8.10e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1347 RRMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFL 1406
Cdd:cd11964      1 RKVRAIYDFEAAEDN-------ELTFKAGDIITILDDSDPN-WWKGETPQGTGLFPSNFV 52
mukB PRK04863
chromosome partition protein MukB;
224-378 1.09e-06

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 53.81  E-value: 1.09e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  224 DLEYELKDAVQEK----THLNLHYASLSQKALQYDQVKSDYDQLR-----------ETISKVIKE----RDLALKGK--- 281
Cdd:PRK04863   834 DPEAELRQLNRRRveleRALADHESQEQQQRSQLEQAKEGLSALNrllprlnlladETLADRVEEireqLDEAEEAKrfv 913

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  282 HQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLqkAQVEAKKEH---EGAVQLLEtKVQELEEKC 358
Cdd:PRK04863   914 QQHGNALAQLEPIVSVLQSDPEQFEQLKQDYQQAQQTQRDAKQQAFAL--TEVVQRRAHfsyEDAAEMLA-KNSDLNEKL 990

                          170       180
                   ....*....|....*....|
gi 1835591054  359 RIQSEQfnlLSKELERFRQQ 378
Cdd:PRK04863   991 RQRLEQ---AEQERTRAREQ 1007
SH3_Sla1p_2 cd11774
Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1349-1406 1.21e-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: 46.69  E-value: 1.21e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1349 MVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFL 1406
Cdd:cd11774      2 AKALYDYDKQT-------EEELSFNEGDTLDVYDDSDSDWILVGFNGTQFGFVPANYI 52
SH3_alphaPIX cd12060
Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho ...
 1367-1409 1.21e-06

Src Homology 3 domain of alpha-Pak Interactive eXchange factor; Alpha-PIX, also called Rho guanine nucleotide exchange factor 6 (ARHGEF6) or Cool (Cloned out of Library)-2, activates small GTPases by exchanging bound GDP for free GTP. It acts as a GEF for both Cdc42 and Rac 1, and is localized in dendritic spines where it regulates spine morphogenesis. It controls dendritic length and spine density in the hippocampus. Mutations in the ARHGEF6 gene cause X-linked intellectual disability in humans. 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: 212993  Cd Length: 58  Bit Score: 46.92  E-value: 1.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1835591054 1367 EAELTFCTGDIITVfGEIDEDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd12060     15 EDELSVCKGDIIYV-TRVEEGGWWEGTLNGKTGWFPSNYVREI 56
SH3_Nebulin_family_C cd11789
C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins ...
 1348-1407 1.59e-06

C-terminal Src Homology 3 domain of the Nebulin family of proteins; Nebulin family proteins contain multiple nebulin repeats, and may contain an N-terminal LIM domain and/or a C-terminal SH3 domain. They have molecular weights ranging from 34 to 900 kD, depending on the number of nebulin repeats, and they all bind actin. They are involved in the regulation of actin filament architecture and function as stabilizers and scaffolds for cytoskeletal structures with which they associate, such as long actin filaments or focal adhesions. Nebulin family proteins that contain a C-terminal SH3 domain include the giant filamentous protein nebulin, nebulette, Lasp1, and Lasp2. Lasp2, also called LIM-nebulette, is an alternatively spliced variant of nebulette. 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: 212723 [Multi-domain]  Cd Length: 55  Bit Score: 46.54  E-value: 1.59e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDeDGFYYG--ELNGQKGLVPSNFLE 1407
Cdd:cd11789      1 RYRAMYDYAAADDD-------EVSFQEGDVIINVEIID-DGWMEGtvQRTGQSGMLPANYVE 54
SH3_SH3RF1_1 cd11927
First Src Homology 3 domain of SH3 domain containing ring finger protein 1, an E3 ...
 1351-1407 1.74e-06

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: 46.48  E-value: 1.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPRESspnvdveAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11927      5 ALYNYEGKEP-------GDLKFSKGDIIILRRQVDEN-WYHGEVNGIHGFFPTNFVQ 53
SH3_STAM cd11820
Src homology 3 domain of Signal Transducing Adaptor Molecules; STAMs were discovered as ...
 1347-1405 1.79e-06

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: 46.30  E-value: 1.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1347 RRMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNF 1405
Cdd:cd11820      1 RKVRALYDFEAAE-------DNELTFKAGEIITVLDDSDPN-WWKGSNHRGEGLFPANF 51
SH3_Abp1_fungi_C2 cd11961
Second C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ...
 1351-1408 1.92e-06

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: 46.36  E-value: 1.92e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11961      4 ALYDYDAAEDN-------ELSFFENDKIINIEFVDDD-WWLGECHGSRGLFPSNYVEL 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
217-341 1.97e-06

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 52.46  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  217 QEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKviKERDLALKGKHQLQAKLENLEQVLK 296
Cdd:COG4717    122 EKLLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAE--LQEELEELLEQLSLATEEELQDLAE 199

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1835591054  297 HMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHE 341
Cdd:COG4717    200 ELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALEER 244
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 247-378 2.02e-06

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 52.63  E-value: 2.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  247 SQKALQYDQVKSDYDQLretiskvikERDLALKGKHQLQAKLENLEQVLKH----MREAAERRQQLELEHEQALAVLTAK 322
Cdd:COG1196    209 AEKAERYRELKEELKEL---------EAELLLLKLRELEAELEELEAELEEleaeLEELEAELAELEAELEELRLELEEL 279

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054  323 QQEIELLQKAQVEAKKE---HEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFRQQ 378
Cdd:COG1196    280 ELELEEAQAEEYELLAElarLEQDIARLEERRRELEERLEELEEELAELEEELEELEEE 338
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 206-377 2.32e-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: 52.37  E-value: 2.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  206 EKTQVFKSDVNQEKQ-QWKDLEYELKDAVQEKTHLNLHYASLSQK----ALQYDQVKSDYDQLRETISKVIKERDLALKG 280
Cdd:TIGR02168  210 EKAERYKELKAELRElELALLVLRLEELREELEELQEELKEAEEEleelTAELQELEEKLEELRLEVSELEEEIEELQKE 289

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  281 KHQLQAKLENLEQvlkHMREAAERRQQLELEHEQALAVLTAKQQEIELLQK--AQVEAKKEH-EGAVQLLETKVQELEEK 357
Cdd:TIGR02168  290 LYALANEISRLEQ---QKQILRERLANLERQLEELEAQLEELESKLDELAEelAELEEKLEElKEELESLEAELEELEAE 366

                          170       180
                   ....*....|....*....|
gi 1835591054  358 CRIQSEQFNLLSKELERFRQ 377
Cdd:TIGR02168  367 LEELESRLEELEEQLETLRS 386
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 1351-1408 2.34e-06

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: 46.17  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGE-LNGQKGLVPSNFLEE 1408
Cdd:cd11763      4 ALYDFDSQPSG-------ELSLRAGEVLTITRQDVGDGWLEGRnSRGEVGLFPSSYVEI 55
SH3_FCHSD2_2 cd11894
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain ...
 1351-1408 2.41e-06

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: 46.08  E-value: 2.41e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1351 ALYDYDPResspnvdVEAELTFCTGDIITVFGE--IDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11894      4 ALYDYEGQ-------TDDELSFPEGAIIRILNKenQDDDGFWEGEFNGRIGVFPSVLVEE 56
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 204-370 2.78e-06

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: 51.94  E-value: 2.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKalqYDQVKSDYDQLRETISKV---IKERDLALKg 280
Cdd:TIGR04523  466 LETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKKELEEK---VKDLTKKISSLKEKIEKLeseKKEKESKIS- 541

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  281 khQLQAKLENLEQVLKHM---REAAERRQQLE-LEHEQALavLTAKQQEIELL----QKAQVEAKKEHEGAVQLLETKVQ 352
Cdd:TIGR04523  542 --DLEDELNKDDFELKKEnleKEIDEKNKEIEeLKQTQKS--LKKKQEEKQELidqkEKEKKDLIKEIEEKEKKISSLEK 617

                          170       180
                   ....*....|....*....|..
gi 1835591054  353 ELE----EKCRIQSEQFNLLSK 370
Cdd:TIGR04523  618 ELEkakkENEKLSSIIKNIKSK 639
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 799-893 2.94e-06

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 47.11  E-value: 2.94e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  799 PAPPQDIRIQAGpTPTAILVTWKPPtltptgTSNGANITGY-VAY--AKGQKVAEVVFPTAESTVVdllRIQNLEAK--- 872
Cdd:cd00063      1 PSPPTNLRVTDV-TSTSVTLSWTPP------EDDGGPITGYvVEYreKGSGDWKEVEVTPGSETSY---TLTGLKPGtey 70

                           90       100
                   ....*....|....*....|.
gi 1835591054  873 EITIRSLSAQGESEDSAPTAI 893
Cdd:cd00063     71 EFRVRAVNGGGESPPSESVTV 91
SH3_Intersectin_1 cd11836
First Src homology 3 domain (or SH3A) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1351-1407 3.42e-06

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: 45.43  E-value: 3.42e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPResspNVDveaELTFCTGDIITVFGEID-EDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11836      4 ALYAFEAR----NPD---EISFQPGDIIQVDESQVaEPGWLAGELKGKTGWFPANYVE 54
SH3_Abi2 cd11972
Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It ...
 1348-1409 3.51e-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: 45.77  E-value: 3.51e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1348 RMVALYDYDPresspnvDVEAELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd11972      4 KVVAIYDYTK-------DKEDELSFQEGAIIYVIKK-NDDGWYEGVMNGVTGLFPGNYVESI 57
SH3_VAV_2 cd11830
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ...
 1350-1408 3.57e-06

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: 45.70  E-value: 3.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11830      3 KARYDFCARDMR-------ELSLKEGDVVKIYNKKGQQGWWRGEINGRIGWFPSTYVEE 54
SH3_Lasp1_C cd11934
C-terminal Src Homology 3 domain of LIM and SH3 domain protein 1; Lasp1 is a cytoplasmic ...
 1345-1409 3.67e-06

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: 45.76  E-value: 3.67e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1345 STRRMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDeDGFYYG--ELNGQKGLVPSNFLEEV 1409
Cdd:cd11934      1 GGKRYRAVYDYNAAD-------EDEVSFQDGDTIVNVQQID-DGWMYGtvERTGDTGMLPANYVEAI 59
SH3_Cortactin cd11959
Src homology 3 domain of Cortactin; Cortactin was originally identified as a substrate of Src ...
 1350-1407 3.95e-06

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: 45.49  E-value: 3.95e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1350 VALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEdGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11959      3 VALYDYQAAD-------DDEISFDPDDIITNIEMIDE-GWWRGVCRGKYGLFPANYVE 52
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 204-423 4.26e-06

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


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 50.98  E-value: 4.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEkthlnlhyasLSQKALQYDQVKSDYDQLRETISKVIkeRDLALKGKHQ 283
Cdd:COG3883     35 AQAELDALQAELEELNEEYNELQAELEALQAE----------IDKLQAEIAEAEAEIEERREELGERA--RALYRSGGSV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 ------LQAK--------LENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLET 349
Cdd:COG3883    103 syldvlLGSEsfsdfldrLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEA 182

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  350 KVQELEEKCRIQSEQFNLLSKELERFRQQTGKIDLLSGASVASSDIIGSPSKSLSQFMNGIATAIGHESSPGSR 423
Cdd:COG3883    183 LLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
204-382 4.53e-06

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 50.29  E-value: 4.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKAlqyDQVKSDYDQLRETISKVIKERDLALKGKHQ 283
Cdd:COG1340     13 LEEKIEELREEIEELKEKRDELNEELKELAEKRDELNAQVKELREEA---QELREKRDELNEKVKELKEERDELNEKLNE 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 LQAKLENLEQVLKHMREA----AERRQQLE-LEHEQALAVLTaKQQEIELLQKAQV------EAKKEHEGAVQLLETKvQ 352
Cdd:COG1340     90 LREELDELRKELAELNKAggsiDKLRKEIErLEWRQQTEVLS-PEEEKELVEKIKElekeleKAKKALEKNEKLKELR-A 167

                          170       180       190
                   ....*....|....*....|....*....|
gi 1835591054  353 ELEEKcRIQSEQFNllsKELERFRQQTGKI 382
Cdd:COG1340    168 ELKEL-RKEAEEIH---KKIKELAEEAQEL 193
SH3_GRB2_N cd11946
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
 1349-1407 4.65e-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: 45.40  E-value: 4.65e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1349 MVALYDYDPRESSpnvdvEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11946      1 MEAIAKYDFKATA-----DDELSFKRGDILKVLNEECDQNWYKAELNGKDGFIPKNYIE 54
SH3_DNMBP_N3 cd11796
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
 1367-1406 4.96e-06

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: 45.04  E-value: 4.96e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054 1367 EAELTFCTGDIITVFGEIDeDGFYYGELNGQKGLVPSNFL 1406
Cdd:cd11796     13 DEELDLREGDVVTITGILD-KGWFRGELNGRRGIFPEGFV 51
SH3_PIX cd11877
Src Homology 3 domain of Pak Interactive eXchange factors; PIX proteins are Rho guanine ...
 1367-1408 5.32e-06

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: 45.00  E-value: 5.32e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835591054 1367 EAELTFCTGDIITVFGEIdEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11877     13 EDELSFDKGDIITVTQVV-EGGWWEGTLNGKTGWFPSNYVKE 53
SH3_MYO15 cd11884
Src Homology 3 domain of Myosin XV; This subfamily is composed of proteins with similarity to ...
 1349-1407 5.70e-06

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: 45.01  E-value: 5.70e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1349 MVALYDYDPRESSpnvdveaELTFCTGDIITVF---GEIDEdGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11884      2 VVAVRAYITRDQT-------LLSFHKGDVIKLLpkeGPLDP-GWLFGTLDGRSGAFPKEYVQ 55
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
 1352-1407 6.38e-06

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: 44.76  E-value: 6.38e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1352 LYDYDPREsspnvdvEAELTFCTGDIITVFGEIDED-GFYYGELNGQKGLVPSNFLE 1407
Cdd:cd12142      5 LFDYNPVA-------PDELALKKGDVIEVISKETEDeGWWEGELNGRRGFFPDNFVM 54
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 221-373 6.44e-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: 6.44e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  221 QWKDLEYELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGK-HQLQAKLENLEQVLK--- 296
Cdd:TIGR02169  238 QKEAIERQLASLEEELEKLT---EEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKEKiGELEAEIASLERSIAeke 314

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  297 -HMREAAERRQQLELEHEQALAVLTAKQQEIELLQ--KAQVEAK-KEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKEL 372
Cdd:TIGR02169  315 rELEDAEERLAKLEAEIDKLLAEIEELEREIEEERkrRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKL 394


                   .
gi 1835591054  373 E 373
Cdd:TIGR02169  395 E 395
SH3_CD2AP-like_2 cd11874
Second Src Homology 3 domain (SH3B) of CD2-associated protein and similar proteins; This ...
 484-542 6.91e-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: 44.63  E-value: 6.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054  484 CIARYSYNPfdgpnENpEAELPLTMGKYLYVYGDmDEDGFYEGELlDGQRGLVPSNFVE 542
Cdd:cd11874      2 CKVLFSYTP-----QN-EDELELKVGDTIEVLGE-VEEGWWEGKL-NGKVGVFPSNFVK 52
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
191-378 6.93e-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: 6.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  191 PVLSQKTFDRIPFLEEKTQVFKSDVNQEKQQWKDLEyELKDAVQEKthlnlhyASLSQKALQYDQVKSDYDQLRETISKV 270
Cdd:COG4913    602 YVLGFDNRAKLAALEAELAELEEELAEAEERLEALE-AELDALQER-------REALQRLAEYSWDEIDVASAEREIAEL 673

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  271 IKERDLALKGKH---QLQAKLENLEQVLKHMREA-----------AERRQQLELEHEQALAVLTAKQQEIELLQKAQVEA 336
Cdd:COG4913    674 EAELERLDASSDdlaALEEQLEELEAELEELEEEldelkgeigrlEKELEQAEEELDELQDRLEAAEDLARLELRALLEE 753

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1835591054  337 KKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFRQQ 378
Cdd:COG4913    754 RFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRA 795
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 228-385 7.83e-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: 50.83  E-value: 7.83e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  228 ELKDAVQEKTHLNLHYASLSQKAlqyDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQvlkHMREAAERRQQ 307
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAELEKAL---AELRKELEELEEELEQLRKELEELSRQISALRKDLARLEA---EVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  308 LELEHEQALAVLTAKQQEIELLQkaqvEAKKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKEL----ERFRQQTGKID 383
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEAE----EELAEAEAEIEELEAQIEQLKEELKALREALDELRAELtllnEEAANLRERLE 827


                   ..
gi 1835591054  384 LL 385
Cdd:TIGR02168  828 SL 829
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 1350-1407 8.94e-06

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: 44.42  E-value: 8.94e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11948      3 VALYSFQATESD-------ELPFQKGDILKILNMEDDQNWYKAELQGREGYIPKNYIK 53
SH3_Ysc84p_like cd11842
Src homology 3 domain of Ysc84p and similar fungal proteins; This family is composed of the ...
 1348-1408 8.99e-06

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: 44.34  E-value: 8.99e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEID-EDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11842      1 KAVALYDFAGEQ-------PGDLAFQKGDIITILKKSDsQNDWWTGRIGGREGIFPANYVEL 55
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
216-380 1.13e-05

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 50.30  E-value: 1.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  216 NQEKQqwKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIkerDLAlkgkhQLQAKLENLEQVL 295
Cdd:COG4913    608 NRAKL--AALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEI---DVA-----SAEREIAELEAEL 677

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  296 KHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQfnlLSKELE-R 374
Cdd:COG4913    678 ERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE---LRALLEeR 754


                   ....*.
gi 1835591054  375 FRQQTG 380
Cdd:COG4913    755 FAAALG 760
SH3_Sla1p_2 cd11774
Second Src Homology 3 domain of the fungal endocytic adaptor protein Sla1p; Sla1p facilitates ...
 1225-1281 1.20e-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: 43.99  E-value: 1.20e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1225 ALFDYDPLTmspnpdaaDEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMV 1281
Cdd:cd11774      4 ALYDYDKQT--------EEELSFNEGDTLDVYDDSDSDWILVGFNGTQFGFVPANYI 52
SH3_p67phox_C cd12046
C-terminal (or second) Src Homology 3 domain of the p67phox subunit of NADPH oxidase; p67phox, ...
 1349-1408 1.23e-05

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: 44.02  E-value: 1.23e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1349 MVALYDYdprESSPNVDveaeLTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12046      2 VVALFSY---EASQPED----LEFQKGDVILVLSKVNED-WLEGQCKGKIGIFPSAFVED 53
SH3_SH3RF3_1 cd11928
First Src Homology 3 domain of SH3 domain containing ring finger 3, an E3 ubiquitin-protein ...
 1351-1407 1.54e-05

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: 43.76  E-value: 1.54e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPRESspnvdveAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11928      5 ALYSYEGKEP-------GDLKFNKGDIIILRRKVDEN-WYHGELNGCHGFLPASYIQ 53
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
214-378 1.55e-05

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 49.38  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  214 DVNQEKQQWKDLEYELK--DAVQEKTHLnLHYA------SLSQKALQYDQvksdYDQLRETIsKVIKERDLALKGKHQLQ 285
Cdd:COG4717    348 ELQELLREAEELEEELQleELEQEIAAL-LAEAgvedeeELRAALEQAEE----YQELKEEL-EELEEQLEELLGELEEL 421

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  286 AKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEgaVQLLETKVQELEEKCRIQSEQF 365
Cdd:COG4717    422 LEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEEDGELAELLQE--LEELKAELRELAEEWAALKLAL 499

                          170
                   ....*....|...
gi 1835591054  366 NLLSKELERFRQQ 378
Cdd:COG4717    500 ELLEEAREEYREE 512
SH3_CIN85_1 cd12052
First Src Homology 3 domain (SH3A) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 1367-1408 1.63e-05

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: 43.73  E-value: 1.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835591054 1367 EAELTFCTGDIITVFGEiDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd12052     13 EDELTITVGDIITKIKK-DDGGWWEGEIKGRRGLFPDNFVRE 53
SH3_PACSIN3 cd11997
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); ...
 1348-1407 1.81e-05

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. 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: 212930 [Multi-domain]  Cd Length: 56  Bit Score: 43.41  E-value: 1.81e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGEL-NGQKGLVPSNFLE 1407
Cdd:cd11997      3 RVRALYDYTGQEAD-------ELSFKAGEELLKIGEEDEQGWCKGRLlSGRIGLYPANYVE 56
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
 1347-1406 1.86e-05

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: 43.47  E-value: 1.86e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1347 RRMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFL 1406
Cdd:cd11963      2 RKVRALYDFEAVEDN-------ELTFKHGEIIIVLDDSDAN-WWKGENHRGVGLFPSNFV 53
SH3_ASAP cd11821
Src homology 3 domain of ArfGAP with SH3 domain, ankyrin repeat and PH domain containing ...
 1348-1405 1.96e-05

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: 43.46  E-value: 1.96e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDpresspnVDVEAELTFCTGDIITVFGEIDEDgFYYGELNGQ---KGLVPSNF 1405
Cdd:cd11821      1 RVRALYDCQ-------ADNDDELTFSEGEIIVVTGEEDDE-WWEGHIEGDpsrRGVFPVSF 53
SH3_Intersectin2_5 cd11996
Fifth Src homology 3 domain (or SH3E) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 1348-1407 1.99e-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: 43.43  E-value: 1.99e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYdpreSSPNVDveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11996      2 QVIAMYDY----TANNED---ELSFSKGQLINVLNKDDPD-WWQGEINGVTGLFPSNYVK 53
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1350-1406 2.18e-05

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: 43.11  E-value: 2.18e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1350 VALYDYdpresspNVDVEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFL 1406
Cdd:cd11804      3 VAKHDF-------KATAEDELSFKKGSILKVLNMEDDPNWYKAELDGKEGLIPKNYI 52
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 204-357 2.31e-05

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: 47.61  E-value: 2.31e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKAlqydqvksdyDQLRETISKVIKERDLalkgkHQ 283
Cdd:COG1579     29 LPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEARI----------KKYEEQLGNVRNNKEY-----EA 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  284 LQAKLENLEqvlKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEK 357
Cdd:COG1579     94 LQKEIESLK---RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAE 164
SH3_Abi1 cd11971
Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of ...
 1348-1409 2.73e-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: 43.09  E-value: 2.73e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1348 RMVALYDYDPresspnvDVEAELTFCTGDIITVFGEIDeDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd11971      1 KVVAIYDYSK-------DKDDELSFMEGAIIYVIKKND-DGWYEGVCNGVTGLFPGNYVESI 54
SH3_Sorbs_1 cd11781
First Src Homology 3 domain of Sorbin and SH3 domain containing (Sorbs) proteins and similar ...
 1349-1408 2.83e-05

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


Pssm-ID: 212715 [Multi-domain]  Cd Length: 53  Bit Score: 43.10  E-value: 2.83e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1349 MVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11781      2 ARALYPFKAQSAK-------ELSLKKGDIIYIRRQIDKN-WYEGEHNGRVGIFPASYVEI 53
SH3_FCHSD2_2 cd11894
Second Src Homology 3 domain of FCH and double SH3 domains protein 2; FCHSD2 has a domain ...
 1225-1283 3.26e-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: 3.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1225 ALFDYDpltmspnpDAADEELPFKEGQIIKVYG--DKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11894      4 ALYDYE--------GQTDDELSFPEGAIIRILNkeNQDDDGFWEGEFNGRIGVFPSVLVEE 56
SH3_Intersectin1_5 cd11995
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
 1348-1407 3.34e-05

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: 42.63  E-value: 3.34e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYdpreSSPNVDveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11995      2 QVIGMYDY----TAQNDD---ELAFSKGQIINVLNKEDPD-WWKGELNGQVGLFPSNYVK 53
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 218-378 3.44e-05

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: 48.51  E-value: 3.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  218 EKQQWKDLEY-ELKDavqEKTHLNLHYAslsqkALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLK 296
Cdd:TIGR02168  206 ERQAEKAERYkELKA---ELRELELALL-----VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVS 277

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  297 HMREAAERRQQLELEHEQALAvltAKQQEIELLQK--AQVEAK-KEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELE 373
Cdd:TIGR02168  278 ELEEEIEELQKELYALANEIS---RLEQQKQILRErlANLERQlEELEAQLEELESKLDELAEELAELEEKLEELKEELE 354


                   ....*
gi 1835591054  374 RFRQQ 378
Cdd:TIGR02168  355 SLEAE 359
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
 484-542 4.53e-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: 42.33  E-value: 4.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054  484 CIARYSYNPfdgpneNPEAELPLTMGKYLYVYgDMDEDGFYEGELlDGQRGLVPSNFVE 542
Cdd:cd11823      2 CKALYSYTA------NREDELSLQPGDIIEVH-EKQDDGWWLGEL-NGKKGIFPATYVE 52
SH3_Endophilin_B cd11802
Src homology 3 domain of Endophilin-B; Endophilins play roles in synaptic vesicle formation, ...
 1351-1405 4.77e-05

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: 42.27  E-value: 4.77e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDG-FYYGELNGQKGLVPSNF 1405
Cdd:cd11802      4 VLYDYDAEDST-------ELSLLADEVITVYELPGMDEdYMMGERGSQRGKVPVAY 52
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 224-378 5.28e-05

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: 48.02  E-value: 5.28e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  224 DLEYELKDAVQEKT----HLNLHYASLSQKALQYDQVKSDYDQLR---------------ETISKVIKERDLALKGKHQL 284
Cdd:COG3096    833 DPEAELAALRQRRSelerELAQHRAQEQQLRQQLDQLKEQLQLLNkllpqanlladetlaDRLEELREELDAAQEAQAFI 912

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  285 Q---AKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLqkAQVEAKKEH---EGAVQLLeTKVQELEEKC 358
Cdd:COG3096    913 QqhgKALAQLEPLVAVLQSDPEQFEQLQADYLQAKEQQRRLKQQIFAL--SEVVQRRPHfsyEDAVGLL-GENSDLNEKL 989

                          170       180
                   ....*....|....*....|
gi 1835591054  359 RIQSEQfnlLSKELERFRQQ 378
Cdd:COG3096    990 RARLEQ---AEEARREAREQ 1006
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 250-379 5.29e-05

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 47.06  E-value: 5.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  250 ALQYDQVKSDYDQLRETISKvikerdlaLKGK-HQLQAKLENLEQvlKHMREAAERRQQLELEHEQALAVLTAKQ---QE 325
Cdd:pfam09787   46 TLELEELRQERDLLREEIQK--------LRGQiQQLRTELQELEA--QQQEEAESSREQLQELEEQLATERSARReaeAE 115

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054  326 IELLQKAQVEAKKEHEGAVQLLETKVQELE---EKCRIQ---SEQFNLLSKELE-RFRQQT 379
Cdd:pfam09787  116 LERLQEELRYLEEELRRSKATLQSRIKDREaeiEKLRNQltsKSQSSSSQSELEnRLHQLT 176
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 108-383 5.71e-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: 5.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  108 KDLATEKDMEIKLLQVECEELKNRLCCLKEGLmgqrpSDVEQLLKQSQKELLWLQRQLSfistggptcILPSSKLRNDLp 187
Cdd:TIGR04523  151 EKELEKLNNKYNDLKKQKEELENELNLLEKEK-----LNIQKNIDKIKNKLLKLELLLS---------NLKKKIQKNKS- 215

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  188 ylhpvLSQKTFDripfLEEKTQVFKSDVNQEKQQWKDLEYE-------LKDAVQEKTHLNlhyASLSQKALQYDQVKSDY 260
Cdd:TIGR04523  216 -----LESQISE----LKKQNNQLKDNIEKKQQEINEKTTEisntqtqLNQLKDEQNKIK---KQLSEKQKELEQNNKKI 283

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  261 DQLRETISKV---------IKERDLALKGKHQLQAKLENLEQVLKHMREAAER--------------RQQLELEHEQALA 317
Cdd:TIGR04523  284 KELEKQLNQLkseisdlnnQKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIisqlneqisqlkkeLTNSESENSEKQR 363

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054  318 VLTAKQQEIELLQKAQVEAKKEhegaVQLLETKVQELEEKCRIQSEQFNLLSKELERFRQQTGKID 383
Cdd:TIGR04523  364 ELEEKQNEIEKLKKENQSYKQE----IKNLESQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLE 425
SH3_betaPIX cd12061
Src Homology 3 domain of beta-Pak Interactive eXchange factor; Beta-PIX, also called Rho ...
 1367-1409 5.78e-05

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: 41.98  E-value: 5.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1835591054 1367 EAELTFCTGDIITVfGEIDEDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd12061     13 EDELSFSKGDVIHV-TRVEEGGWWEGTHNGRTGWFPSNYVREI 54
PHA03247 PHA03247
large tegument protein UL36; Provisional
 766-1005 6.07e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 6.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  766 LLAKPHQMPWQLPLEQREKKEAFAEFSTLPAGPPAPPQDIRIQAGPTPTAILVTW-------KPPTLTPTGTSNGANITG 838
Cdd:PHA03247  2644 PTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRAARPTVGSLTSLadpppppPTPEPAPHALVSATPLPP 2723

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  839 YVAYAKGQKVAEVVFP----TAESTVVDllriqnleAKEITIRSLSAQGESEDSAPTAIPPELLMPPTPHPRTSPKLKPL 914
Cdd:PHA03247  2724 GPAAARQASPALPAAPappaVPAGPATP--------GGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESR 2795

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  915 ASAGAPDTKDEHLGP--PRKIDESWEQTPvhGHTLEPPTANFHSPAHGRRSPSPQRILPQPQGTPVSNTVAKAMAREAAQ 992
Cdd:PHA03247  2796 ESLPSPWDPADPPAAvlAPAAALPPAASP--AGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDVRRRPPSRSPAA 2873

                          250
                   ....*....|...
gi 1835591054  993 RVAESNRMEKRSI 1005
Cdd:PHA03247  2874 KPAAPARPPVRRL 2886
SH3_ASPP cd11807
Src homology 3 domain of Apoptosis Stimulating of p53 proteins (ASPP); The ASPP family of ...
 1351-1406 6.70e-05

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: 41.98  E-value: 6.70e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVF--GEIDEDGFYYGELNGQKGLVPSNFL 1406
Cdd:cd11807      5 ALFDYEAENGD-------ELSFREGDELTVLrkGDDDETEWWWARLNDKEGYVPRNLL 55
DUF4659 pfam15558
Domain of unknown function (DUF4659); This family of proteins is found in eukaryotes. Proteins ...
 217-377 6.99e-05

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: 46.95  E-value: 6.99e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  217 QEKQQWKDLEYELKD---AVQEKTHLNLHYASLSQKALQYDQVksdYDQLretiskvIKERDLALKGKhqlqAKLEnlEQ 293
Cdd:pfam15558  170 QENNLSELLNHQARKvlvDCQAKAEELLRRLSLEQSLQRSQEN---YEQL-------VEERHRELREK----AQKE--EE 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  294 VLKHMREAAERRQQLELEHEQALAVLT------AKQQEIELLQ-KAQ--VEAKKEHEGAVQLLETKVQElEEKCRIQ--- 361
Cdd:pfam15558  234 QFQRAKWRAEEKEEERQEHKEALAELAdrkiqqARQVAHKTVQdKAQraRELNLEREKNHHILKLKVEK-EEKCHREgik 312

                          170       180
                   ....*....|....*....|....*....
gi 1835591054  362 ---------SEQfnlLSKE----LERFRQ 377
Cdd:pfam15558  313 eaikkkeqrSEQ---ISREkeatLEEARK 338
SH3_FCHSD_2 cd11762
Second Src Homology 3 domain of FCH and double SH3 domains proteins; This group is composed of ...
 1225-1283 7.37e-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: 42.00  E-value: 7.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1835591054 1225 ALFDYDPLTmspnpdaaDEELPFKEGQIIKVYGDKDT---DGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11762      4 ALYDYEAQS--------DEELSFPEGAIIRILRKDDNgvdDGWWEGEFNGRVGVFPSLVVEE 57
SH3_GRB2_C cd11949
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2; GRB2 is a critical ...
 1351-1407 7.45e-05

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: 41.75  E-value: 7.45e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11949      4 ALFDFDPQE-------DGELGFRRGDFIEVMDNSDPN-WWKGACHGQTGMFPRNYVT 52
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
204-374 9.73e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 46.43  E-value: 9.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQ 283
Cdd:COG4372     43 LQEELEQLREELEQAREELEQLEEELEQARSELEQLE---EELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEE 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 LQAKLENLEQvlkhmreaaeRRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEhegaVQLLETKVQELEEKCRIQse 363
Cdd:COG4372    120 LQKERQDLEQ----------QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEE----LAALEQELQALSEAEAEQ-- 183

                          170
                   ....*....|.
gi 1835591054  364 QFNLLSKELER 374
Cdd:COG4372    184 ALDELLKEANR 194
SH3_p47phox_like cd11856
Src homology 3 domains of the p47phox subunit of NADPH oxidase and similar domains; This ...
 1349-1408 1.02e-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: 41.47  E-value: 1.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1349 MVALYDYDPRESSpnvdveaELTFCTGDIITVFgEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11856      2 YVAIADYEAQGDD-------EISLQEGEVVEVL-EKNDSGWWYVRKGDKEGWVPASYLEP 53
V-ATPase_G_2 pfam16999
Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from ...
 272-353 1.09e-04

Vacuolar (H+)-ATPase G subunit; This family represents vacuolar (H+)-ATPase G subunit from several bacterial and archaeal species. Subunit G is a component of the peripheral stalk of the ATPase complex


Pssm-ID: 339878 [Multi-domain]  Cd Length: 104  Bit Score: 42.81  E-value: 1.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  272 KERDLALK---GKHQLQAKLENLEQVLKH-MREAAERRQQLELEHEQALAVLTAKQQEiELLQKAQVEAKKEHEGAVQLL 347
Cdd:pfam16999   13 REAALDQQieaARKEAEREVEAAEAEAARiLREAEAKAKALQAEYRQELAAETARIRE-EARARAEAEAQAVRTRAEGRL 91


                   ....*.
gi 1835591054  348 ETKVQE 353
Cdd:pfam16999   92 QQAVEL 97
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1350-1405 1.11e-04

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: 41.03  E-value: 1.11e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1350 VALYDYDPResspnvdVEAELTFCTGDIITVFGEIDEDGFYYGELN-GQKGLVPSNF 1405
Cdd:cd11845      3 VALYDYEAR-------TDDDLSFKKGDRLQILDDSDGDWWLARHLStGKEGYIPSNY 52
SH3_Src_like cd11845
Src homology 3 domain of Src kinase-like Protein Tyrosine Kinases; Src subfamily members ...
 1222-1279 1.14e-04

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: 41.03  E-value: 1.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1222 IFVALFDYDPLTmspnpdaaDEELPFKEGQIIKVygDKDTDG---FYRGATCARRGLIPCN 1279
Cdd:cd11845      1 IYVALYDYEART--------DDDLSFKKGDRLQI--LDDSDGdwwLARHLSTGKEGYIPSN 51
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
203-378 1.14e-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: 1.14e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  203 FLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQkalQYDQvkSDYDQLrETISKVIKERDLALKgkh 282
Cdd:COG4913    285 FAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEA---QIRG--NGGDRL-EQLEREIERLERELE--- 355

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  283 QLQAKLENLEQVLKHMREAAER-RQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEekcRIQ 361
Cdd:COG4913    356 ERERRRARLEALLAALGLPLPAsAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIA---SLE 432

                          170
                   ....*....|....*..
gi 1835591054  362 SEQFNlLSKELERFRQQ 378
Cdd:COG4913    433 RRKSN-IPARLLALRDA 448
SH3_Eve1_3 cd11816
Third Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1348-1405 1.17e-04

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: 41.24  E-value: 1.17e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNF 1405
Cdd:cd11816      1 RCVARFDFEGEQ-------EDELSFSEGDVITLKEYVGEE-WAKGELNGKIGIFPLNF 50
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 204-385 1.18e-04

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: 46.30  E-value: 1.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  204 LEEKTQVFKSDVNQEKQQWKDLEYELKDAVQE----KTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIkeRDLALK 279
Cdd:COG4942     39 LEKELAALKKEEKALLKQLAALERRIAALARRiralEQELAALEAELAELEKEIAELRAELEAQKEELAELL--RALYRL 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  280 GKH---QLQAKLENLEQVLKH---MREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQE 353
Cdd:COG4942    117 GRQpplALLLSPEDFLDAVRRlqyLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAE 196

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1835591054  354 LEEKCRIQSEQFNLLSKELERFRQQTGKIDLL 385
Cdd:COG4942    197 RQKLLARLEKELAELAAELAELQQEAEELEAL 228
SH3_MPP cd11862
Src Homology 3 domain of Membrane Protein, Palmitoylated (or MAGUK p55 subfamily member) ...
 1348-1403 1.23e-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: 41.41  E-value: 1.23e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEidEDGFYY-----GELNGQKGLVPS 1403
Cdd:cd11862      1 FVRALFDYDPEEDPLIPCKEAGLSFKKGDILQIVNQ--DDPNWWqarkvGDPNGRAGLIPS 59
SH3_1 pfam00018
SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in signal ...
 1224-1278 1.23e-04

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: 41.04  E-value: 1.23e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054 1224 VALFDYDPltmspnpdAADEELPFKEGQIIKVYgDKDTDGFYRGA-TCARRGLIPC 1278
Cdd:pfam00018    1 VALYDYTA--------QEPDELSFKKGDIIIVL-EKSEDGWWKGRnKGGKEGLIPS 47
SH3_PLCgamma cd11825
Src homology 3 domain of Phospholipase C (PLC) gamma; PLC catalyzes the hydrolysis of ...
 1351-1408 1.34e-04

Src homology 3 domain of Phospholipase C (PLC) gamma; PLC catalyzes the hydrolysis of phosphatidylinositol (4,5)-bisphosphate [PtdIns(4,5)P2] to produce Ins(1,4,5)P3 and diacylglycerol (DAG) in response to various receptors. Ins(1,4,5)P3 initiates the calcium signaling cascade while DAG functions as an activator of PKC. PLCgamma catalyzes this reaction in tyrosine kinase-dependent signaling pathways. It is activated and recruited to its substrate at the membrane. Vertebrates contain two forms of PLCgamma, PLCgamma1, which is widely expressed, and PLCgamma2, which is primarily found in haematopoietic cells. PLCgamma contains a Pleckstrin homology (PH) domain followed by an elongation factor (EF) domain, two catalytic regions of PLC domains that flank two tandem SH2 domains, followed by a SH3 domain and C2 domain. The SH3 domain of PLCgamma1 directly interacts with dynamin-1 and can serve as a guanine nucleotide exchange factor (GEF). It also interacts with Cbl, inhibiting its phosphorylation and activity. 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: 212759 [Multi-domain]  Cd Length: 54  Bit Score: 41.16  E-value: 1.34e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFgEIDEDGFYYGELNGQK-GLVPSNFLEE 1408
Cdd:cd11825      4 ALYDYRAQR-------PDELSFCKHAIITNV-EKEDGGWWRGDYGGKKqKWFPANYVEE 54
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
222-366 1.37e-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: 1.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  222 WKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIKERDlalkgkhQLQAKLENLEQVLKHMREA 301
Cdd:COG4913    663 VASAEREIAELEAELERLDASSDDLAALEEQLEELEAELEELEEELDELKGEIG-------RLEKELEQAEEELDELQDR 735

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  302 AERRQQLELEHEQALAvltAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQFN 366
Cdd:COG4913    736 LEAAEDLARLELRALL---EERFAAALGDAVERELRENLEERIDALRARLNRAEEELERAMRAFN 797
SH3_VAV1_2 cd11976
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ...
 1351-1408 1.40e-04

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: 41.08  E-value: 1.40e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11976      4 ARYDFCARDRS-------ELSLKEGDIIKILNKKGQQGWWRGEIYGRVGWFPANYVEE 54
SH3_Abp1_eu cd11960
Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like ...
 1348-1407 1.47e-04

Src homology 3 domain of eumetazoan Actin-binding protein 1; Abp1, also called drebrin-like protein, 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 helical domain, and a C-terminal SH3 domain. Mammalian Abp1, unlike yeast Abp1, does not contain an acidic domain that interacts with the Arp2/3 complex. It regulates actin dynamics indirectly by interacting with dynamin and WASP family proteins. Abp1 deficiency causes abnormal organ structure and function of the spleen, heart, and lung of mice. 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: 212893 [Multi-domain]  Cd Length: 54  Bit Score: 40.85  E-value: 1.47e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEdGFYYG-ELNGQKGLVPSNFLE 1407
Cdd:cd11960      1 RARALYDYQAAD-------DTEISFDPGDIITDIEQIDE-GWWRGtGPDGTYGLFPANYVE 53
SH3_VAV3_2 cd11978
C-terminal (or second) Src homology 3 domain of VAV3 protein; VAV3 is ubiquitously expressed ...
 1350-1408 1.54e-04

C-terminal (or second) Src homology 3 domain of VAV3 protein; VAV3 is ubiquitously expressed and functions as a phosphorylation-dependent guanine nucleotide exchange factor (GEF) for RhoA, RhoG, and Rac1. It has been implicated to function in the hematopoietic, bone, cerebellar, and cardiovascular systems. VAV3 is essential in axon guidance in neurons that control blood pressure and respiration. It is overexpressed in prostate cancer cells and it plays a role in regulating androgen receptor transcriptional activity. 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: 212911 [Multi-domain]  Cd Length: 56  Bit Score: 41.16  E-value: 1.54e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11978      4 IARYDFCARDMR-------ELSLLKGDVVKIYTKMSTNGWWRGEVNGRVGWFPSTYVEE 55
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 282-373 1.62e-04

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: 44.92  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  282 HQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKE---HEGAVQLLETKVQELEEKc 358
Cdd:COG1579      3 PEDLRALLDLQELDSELDRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEikrLELEIEEVEARIKKYEEQ- 81

                           90       100
                   ....*....|....*....|
gi 1835591054  359 riQSE-----QFNLLSKELE 373
Cdd:COG1579     82 --LGNvrnnkEYEALQKEIE 99
fn3 pfam00041
Fibronectin type III domain;
705-768 1.67e-04

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 41.63  E-value: 1.67e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  705 APSQLKVDNITQTSAGLSWLPTNSNYSHVIF-------LNEEEFD---IVKAAIYKYQFFNLKPNMAYKVKLLA 768
Cdd:pfam00041    2 APSNLTVTDVTSTSLTVSWTPPPDGNGPITGyeveyrpKNSGEPWneiTVPGTTTSVTLTGLKPGTEYEVRVQA 75
SH3_GRAP2_N cd11947
N-terminal Src homology 3 domain of GRB2-related adaptor protein 2; GRAP2 is also called GADS ...
 1367-1407 1.69e-04

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: 40.55  E-value: 1.69e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1835591054 1367 EAELTFCTGDIITVFGeiDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11947     13 EDELSFKKGDVLKILS--SDDIWFKAELNGEEGYVPKNFVD 51
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 799-885 1.71e-04

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 41.83  E-value: 1.71e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   799 PAPPQDIRIQAgPTPTAILVTWKPptltPTGTSNGANITGY-VAYAKGQKVAEVVFPTAESTVVdllRIQNLEAK---EI 874
Cdd:smart00060    1 PSPPSNLRVTD-VTSTSVTLSWEP----PPDDGITGYIVGYrVEYREEGSEWKEVNVTPSSTSY---TLTGLKPGteyEF 72

                            90
                    ....*....|.
gi 1835591054   875 TIRSLSAQGES 885
Cdd:smart00060   73 RVRAVNGAGEG 83
SH3_GRAP_N cd11948
N-terminal Src homology 3 domain of GRB2-related adaptor protein; GRAP is a GRB-2 like adaptor ...
 1224-1282 1.74e-04

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: 40.57  E-value: 1.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1224 VALFDYdpltmspnPDAADEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVS 1282
Cdd:cd11948      3 VALYSF--------QATESDELPFQKGDILKILNMEDDQNWYKAELQGREGYIPKNYIK 53
SH3_CASS4 cd12000
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member 4; ...
 1351-1407 1.78e-04

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding protein family member 4; CASS4, also called HEPL (HEF1-EFS-p130Cas-like), localizes to focal adhesions and plays a role in regulating FAK activity, focal adhesion integrity, and cell spreading. It is most abundant in blood cells and lung tissue, and is also found in high levels in leukemia and ovarian cell lines. CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, 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: 212933  Cd Length: 57  Bit Score: 40.63  E-value: 1.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPresspnvDVEAELTFCTGDIITVFGE--IDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd12000      5 ALYDNKA-------DCSDELAFRRGDILTVLEQnvPGSEGWWKCLLHGRQGLAPANRLQ 56
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 217-383 1.80e-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: 46.12  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  217 QEKQQWKDLEYELKDAVQEKTHLnLHYASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKgkhQLQAKLENLEQVLK 296
Cdd:TIGR00618  253 EEQLKKQQLLKQLRARIEELRAQ-EAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHT---ELQSKMRSRAKLLM 328

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  297 HMREAAERRQQLElehEQALAVLTAKQQEIELLQKAQVEAK-KEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERF 375
Cdd:TIGR00618  329 KRAAHVKQQSSIE---EQRRLLQTLHSQEIHIRDAHEVATSiREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDIL 405


                   ....*...
gi 1835591054  376 RQQTGKID 383
Cdd:TIGR00618  406 QREQATID 413
SH3_Eve1_4 cd11817
Fourth Src homology 3 domain of ADAM-binding protein Eve-1; Eve-1, also called SH3 ...
 1350-1405 1.86e-04

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: 40.54  E-value: 1.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054 1350 VALYDYDPResspnvdVEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNF 1405
Cdd:cd11817      3 VALYDFTGE-------TEEDLSFQRGDRILVTEHLDAE-WSRGRLNGREGIFPRAF 50
SH3_CIN85_3 cd12057
Third Src Homology 3 domain (SH3C) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 1367-1407 1.93e-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: 40.65  E-value: 1.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835591054 1367 EAELTFCTGDIITVFG-EIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd12057     13 EDELTIKEGDIVTLISkDCIDAGWWEGELNGRRGVFPDNFVK 54
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
200-378 1.93e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  200 RIPFLEEKTQVFKSDVNQEKQQWKDleyELKDAVQEKTHLNlhyASLSQKALQYDQVKSDYDQLRETISKVIKERDlalk 279
Cdd:COG4372     14 SLFGLRPKTGILIAALSEQLRKALF---ELDKLQEELEQLR---EELEQAREELEQLEEELEQARSELEQLEEELE---- 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  280 gkhQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCR 359
Cdd:COG4372     84 ---ELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLE 160

                          170
                   ....*....|....*....
gi 1835591054  360 IQSEQFNLLSKELERFRQQ 378
Cdd:COG4372    161 SLQEELAALEQELQALSEA 179
DUF745 pfam05335
Protein of unknown function (DUF745); This family consists of several uncharacterized ...
 277-377 1.98e-04

Protein of unknown function (DUF745); This family consists of several uncharacterized Drosophila melanogaster proteins of unknown function.


Pssm-ID: 398808 [Multi-domain]  Cd Length: 180  Bit Score: 43.71  E-value: 1.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  277 ALKGKHQLqakLENLEQvlkHMREAAERRQQL--ELEHEQA---LAVLTAKQ--QEIELLQKAQVEAKKEHE-------G 342
Cdd:pfam05335   53 ALAGKQQI---VEQLEQ---ELREAEAVVQEEsaSLQQSQAnanAAQRAAQQaqQQLEALTAALKAAQANLEnaeqvaaG 126

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1835591054  343 AVQLLETKVQELEE-KCRIQS--EQFNLLSKELERFRQ 377
Cdd:pfam05335  127 AQQELAEKTQLLEAaKKRVERlqRQLAEARADLEKTKK 164
SH3_SGSM3 cd11813
Src Homology 3 domain of Small G protein Signaling Modulator 3; SGSM3 is also called ...
 1348-1407 2.02e-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: 40.56  E-value: 2.02e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11813      1 RAKALLDFERHD-------DDELGFRKNDIITIISQKDEH-CWVGELNGLRGWFPAKFVE 52
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 23-383 2.03e-04

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: 46.20  E-value: 2.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   23 KVENHSSKQQEEEGKLH--KKERTDFTKKERNHRSEakipqkphaVRLRKEIKPESRISPAAALKkpSAKQRMRSVNGGP 100
Cdd:TIGR02168  678 EIEELEEKIEELEEKIAelEKALAELRKELEELEEE---------LEQLRKELEELSRQISALRK--DLARLEAEVEQLE 746

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  101 GQFQGINKDLaTEKDMEIKLLQVECEELKNRLCCLKEGLmgqrpSDVEQLLKQSQKELLWLQRQLSfistggptcilpss 180
Cdd:TIGR02168  747 ERIAQLSKEL-TELEAEIEELEERLEEAEEELAEAEAEI-----EELEAQIEQLKEELKALREALD-------------- 806

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  181 KLRNDLPYLHPVLSQKTFdRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTH-----------LNLHYASLSQK 249
Cdd:TIGR02168  807 ELRAELTLLNEEAANLRE-RLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEEleelieeleseLEALLNERASL 885

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  250 ALQYDQVKSDYDQLRETI-------SKVIKERDLALKGKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAK 322
Cdd:TIGR02168  886 EEALALLRSELEELSEELreleskrSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  323 qqEIELLQK--AQVEAKKEHEGAVQLL-ETKVQELEEKCRIQSEQFNLLSKELERFRQQTGKID 383
Cdd:TIGR02168  966 --DEEEARRrlKRLENKIKELGPVNLAaIEEYEELKERYDFLTAQKEDLTEAKETLEEAIEEID 1027
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 1225-1283 2.24e-04

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: 40.41  E-value: 2.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1225 ALFDYDPLtmspNPDaadeELPFKEGQIIKVYgDKDTD--GFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11875      4 VLFDYEAE----NED----ELTLREGDIVTIL-SKDCEdkGWWKGELNGKRGVFPDNFVEP 55
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
 497-544 2.45e-04

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: 40.27  E-value: 2.45e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1835591054  497 NENPEAELPLTMGKYLYVYgDMDEDGFYEGELLdGQRGLVPSNFVEFV 544
Cdd:pfam07653    9 VGTDKNGLTLKKGDVVKVL-GKDNDGWWEGETG-GRVGLVPSTAVEEI 54
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 117-347 2.50e-04

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: 45.82  E-value: 2.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  117 EIKLLQVECEELKNRLCCLKEGLmgqrpSDVEQLLKQSQKELLWLQRQLSfistggptcilpssKLRNDLPYLHpvlsqk 196
Cdd:TIGR02168  317 QLEELEAQLEELESKLDELAEEL-----AELEEKLEELKEELESLEAELE--------------ELEAELEELE------ 371

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  197 tfDRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQ--KALQYDQVKSDYDQLRETISKVIKER 274
Cdd:TIGR02168  372 --SRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQeiEELLKKLEEAELKELQAELEELEEEL 449

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  275 dlalkgkHQLQAKLENLEqvlkhmrEAAERRQQLELEHEQAL----AVLTAKQQEIELLQKAQVEAKKEHEGAVQLL 347
Cdd:TIGR02168  450 -------EELQEELERLE-------EALEELREELEEAEQALdaaeRELAQLQARLDSLERLQENLEGFSEGVKALL 512
SH3_CAS cd11844
Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins ...
 1351-1407 2.70e-04

Src homology 3 domain of CAS (Crk-Associated Substrate) scaffolding proteins; CAS proteins function as molecular scaffolds to regulate protein complexes that are involved in many cellular processes including migration, chemotaxis, apoptosis, differentiation, and progenitor cell function. They mediate the signaling of integrins at focal adhesions where they localize, and thus, regulate cell invasion and survival. Over-expression of these proteins is implicated in poor prognosis, increased metastasis, and resistance to chemotherapeutics in many cancers such as breast, lung, melanoma, and glioblastoma. CAS proteins have also been linked to the pathogenesis of inflammatory disorders, Alzheimer's, Parkinson's, and developmental defects. They share a common domain structure that includes an N-terminal SH3 domain, an unstructured substrate domain that contains many YxxP motifs, a serine-rich four-helix bundle, and a FAT-like C-terminal domain. Vertebrates contain four CAS proteins: BCAR1 (or p130Cas), NEDD9 (or HEF1), EFS (or SIN), and CASS4 (or HEPL). The SH3 domain of CAS proteins binds to diverse partners including FAK, FRNK, Pyk2, PTP-PEST, DOCK180, 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: 212778  Cd Length: 56  Bit Score: 40.41  E-value: 2.70e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1351 ALYDydpresspNV-DVEAELTFCTGDIITVFGEIDE--DGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11844      4 ALYD--------NVaESPDELAFRRGDILTVLEQNTAglEGWWLCSLRGRQGIAPGNRLK 55
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
220-403 2.91e-04

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


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 45.39  E-value: 2.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  220 QQWKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSD------YDQLRETISKVIKERDLALKG---KH----QLQA 286
Cdd:COG3206    219 QQLSELESQLAEARAELAEAEARLAALRAQLGSGPDALPEllqspvIQQLRAQLAELEAELAELSARytpNHpdviALRA 298

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  287 KLENLEQVLKhmREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKehegavqlLETKVQELEEKCRIQSEQFN 366
Cdd:COG3206    299 QIAALRAQLQ--QEAQRILASLEAELEALQAREASLQAQLAQLEARLAELPE--------LEAELRRLEREVEVARELYE 368

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1835591054  367 LLSKELERFR----QQTGKIDLLSGASVASSDIigSPSKSL 403
Cdd:COG3206    369 SLLQRLEEARlaeaLTVGNVRVIDPAVVPLKPV--SPKKLL 407
COG1340 COG1340
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
215-382 3.10e-04

Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];


Pssm-ID: 440951 [Multi-domain]  Cd Length: 297  Bit Score: 44.52  E-value: 3.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  215 VNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETI-SKVI---KERDLALKGKhQLQAKLEN 290
Cdd:COG1340     73 VKELKEERDELNEKLNELREELDELRKELAELNKAGGSIDKLRKEIERLEWRQqTEVLspeEEKELVEKIK-ELEKELEK 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  291 LEQVLKHMREAAERRQQLELEHEQA------LAVLTAKQQE-----IELLQKAQvEAKKEHEGAVQlletKVQELEEKCR 359
Cdd:COG1340    152 AKKALEKNEKLKELRAELKELRKEAeeihkkIKELAEEAQElheemIELYKEAD-ELRKEADELHK----EIVEAQEKAD 226

                          170       180
                   ....*....|....*....|...
gi 1835591054  360 IQSEQFNLLSKELERFRQQTGKI 382
Cdd:COG1340    227 ELHEEIIELQKELRELRKELKKL 249
SH3_Bbc1 cd11887
Src Homology 3 domain of Bbc1 and similar domains; This subfamily is composed of Saccharomyces ...
 1348-1408 3.24e-04

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: 40.02  E-value: 3.24e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054 1348 RMVALYDYDPresspnvDVEAELTFCTGDIITVFGEIDEDgFYYGEL-----NGQKGLVPSNFLEE 1408
Cdd:cd11887      3 KVKALYPYES-------DHEDDLNFDVGQLITVTEEEDAD-WYFGEYvdsngNTKEGIFPKNFVEV 60
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
215-380 3.31e-04

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 45.42  E-value: 3.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  215 VNQEKQQWKDLEYELKD-------AVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAK 287
Cdd:PRK02224   208 LNGLESELAELDEEIERyeeqreqARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDLRER 287

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  288 LENLEQVLKHMREAAE------------------RRQQLELEHEQALAVLTAKQQEIELLQKA----QVEAKKEHEGAVQ 345
Cdd:PRK02224   288 LEELEEERDDLLAEAGlddadaeavearreeledRDEELRDRLEECRVAAQAHNEEAESLREDaddlEERAEELREEAAE 367

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1835591054  346 lLETKVQELEEKCRIQSEQFNLLSKELERFRQQTG 380
Cdd:PRK02224   368 -LESELEEAREAVEDRREEIEELEEEIEELRERFG 401
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
252-378 3.33e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 45.29  E-value: 3.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  252 QYDQVKSDYDQLRETISKVIKERDlalkgkhqlqaKLENLEQVLKHMREAAERRQQLE-LEHEQALAVLTAKQQEIELLQ 330
Cdd:COG4913    226 AADALVEHFDDLERAHEALEDARE-----------QIELLEPIRELAERYAAARERLAeLEYLRAALRLWFAQRRLELLE 294

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1835591054  331 KAQVEAKKEHegavqlletkvQELEEKCRIQSEQFNLLSKELERFRQQ 378
Cdd:COG4913    295 AELEELRAEL-----------ARLEAELERLEARLDALREELDELEAQ 331
tolA_full TIGR02794
TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the ...
 214-357 3.81e-04

TolA protein; TolA couples the inner membrane complex of itself with TolQ and TolR to the outer membrane complex of TolB and OprL (also called Pal). Most of the length of the protein consists of low-complexity sequence that may differ in both length and composition from one species to another, complicating efforts to discriminate TolA (the most divergent gene in the tol-pal system) from paralogs such as TonB. Selection of members of the seed alignment and criteria for setting scoring cutoffs are based largely conserved operon struction. //The Tol-Pal complex is required for maintaining outer membrane integrity. Also involved in transport (uptake) of colicins and filamentous DNA, and implicated in pathogenesis. Transport is energized by the proton motive force. TolA is an inner membrane protein that interacts with periplasmic TolB and with outer membrane porins ompC, phoE and lamB. [Transport and binding proteins, Other, Cellular processes, Pathogenesis]


Pssm-ID: 274303 [Multi-domain]  Cd Length: 346  Bit Score: 44.45  E-value: 3.81e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  214 DVNQEKQQWKDLEYELKDAvqEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQ 293
Cdd:TIGR02794   44 DPGAVAQQANRIQQQKKPA--AKKEQERQKKLEQQAEEAEKQRAAEQARQKELEQRAAAEKAAKQAEQAAKQAEEKQKQA 121

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  294 VLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLET---KVQELEEK 357
Cdd:TIGR02794  122 EEAKAKQAAEAKAKAEAEAERKAKEEAAKQAEEEAKAKAAAEAKKKAEEAKKKAEAeakAKAEAEAK 188
SH3_srGAP4 cd11956
Src homology 3 domain of Slit-Robo GTPase Activating Protein 4; srGAP4, also called ARHGAP4, ...
 1350-1406 3.97e-04

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: 39.82  E-value: 3.97e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFL 1406
Cdd:cd11956      5 VACFDYTGRTAQ-------ELSFKRGDVLLLHSKASSD-WWRGEHNGMRGLIPHKYI 53
SH3_CIN85_2 cd12055
Second Src Homology 3 domain (SH3B) of Cbl-interacting protein of 85 kDa; CIN85, also called ...
 484-542 4.00e-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: 4.00e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054  484 CIARYSYNPfdgpneNPEAELPLTMGKYLYVYGDMDEdGFYEGeLLDGQRGLVPSNFVE 542
Cdd:cd12055      2 CQVAFSYLP------QNEDELELKVGDIIEVVGEVEE-GWWEG-VLNGKTGMFPSNFIK 52
PRK12704 PRK12704
phosphodiesterase; Provisional
 219-364 4.17e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.77  E-value: 4.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  219 KQQWKDLEYELKDAVQEKthlNLHYASLSQKALQydQVKSDYDQLRETISKVIKERDLALKgkhQLQAKLENLEQVLKHM 298
Cdd:PRK12704    30 EAKIKEAEEEAKRILEEA---KKEAEAIKKEALL--EAKEEIHKLRNEFEKELRERRNELQ---KLEKRLLQKEENLDRK 101

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054  299 REAAERRQQlELEHEQAlaVLTAKQQEIELLQKaqvEAKKehegavqLLETKVQELEEKCRIQSEQ 364
Cdd:PRK12704   102 LELLEKREE-ELEKKEK--ELEQKQQELEKKEE---ELEE-------LIEEQLQELERISGLTAEE 154
SH3_PACSIN3 cd11997
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); ...
 503-542 4.56e-04

Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 3 (PACSIN3); PACSIN 3 or Syndapin III (Synaptic dynamin-associated protein III) is expressed ubiquitously and regulates glucose uptake in adipocytes through its role in GLUT1 trafficking. It also modulates the subcellular localization and stimulus-specific function of the cation channel TRPV4. 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: 212930 [Multi-domain]  Cd Length: 56  Bit Score: 39.56  E-value: 4.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054  503 ELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVE 542
Cdd:cd11997     17 ELSFKAGEELLKIGEEDEQGWCKGRLLSGRIGLYPANYVE 56
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 102-374 4.63e-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: 4.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  102 QFQGINKDLATEKDMEIKLLQVECEELKNrlccLKEGLMGQRPSD--VEQLLK------QSQKELLWLQRQLSfistggp 173
Cdd:TIGR00618  202 RSQLLTLCTPCMPDTYHERKQVLEKELKH----LREALQQTQQSHayLTQKREaqeeqlKKQQLLKQLRARIE------- 270

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  174 tcilpssKLRNDLPYLHpvLSQKTFDRIPFLEEKTQVFKSdVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKALQY 253
Cdd:TIGR00618  271 -------ELRAQEAVLE--ETQERINRARKAAPLAAHIKA-VTQIEQQAQRIHTELQSKMRSRAKLLMKRAAHVKQQSSI 340

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  254 DQVKSDYDQL------------RETISKVIKERDLALKGK-HQLQAKLENLEQVLK-------------------HMRE- 300
Cdd:TIGR00618  341 EEQRRLLQTLhsqeihirdaheVATSIREISCQQHTLTQHiHTLQQQKTTLTQKLQslckeldilqreqatidtrTSAFr 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  301 -------AAERRQQLELEHEQALAVLTAKQQEIELLQKA-QVEAKKEHEGAVQLLETKVQELEEKCRIQS--EQFNLLSK 370
Cdd:TIGR00618  421 dlqgqlaHAKKQQELQQRYAELCAAAITCTAQCEKLEKIhLQESAQSLKEREQQLQTKEQIHLQETRKKAvvLARLLELQ 500


                   ....
gi 1835591054  371 ELER 374
Cdd:TIGR00618  501 EEPC 504
SH3_FCHSD1_2 cd11895
Second Src Homology 3 domain of FCH and double SH3 domains protein 1; FCHSD1 has a domain ...
 1351-1409 4.69e-04

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: 39.56  E-value: 4.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054 1351 ALYDYDPResSPNvdveaELTFCTGDIITVF----GEIDeDGFYYGELNGQKGLVPSNFLEEV 1409
Cdd:cd11895      4 ALYSYTGQ--SPE-----ELSFPEGALIRLLpraqDGVD-DGFWRGEFGGRVGVFPSLLVEEL 58
SH3_Amphiphysin cd11790
Src Homology 3 domain of Amphiphysin and related domains; Amphiphysins function primarily in ...
 1348-1409 4.69e-04

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: 40.00  E-value: 4.69e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFG----EIDEDGFYYG--ELNGQKGLVPSNFLEEV 1409
Cdd:cd11790      4 KVRATHDYTAEDTD-------ELTFEKGDVILVIPfddpEEQDEGWLMGvkESTGCRGVFPENFTERI 64
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 222-378 4.87e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.72  E-value: 4.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  222 WKDLEYELKDAV-----------QEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIkerdlaLKGKHQLQAKlEN 290
Cdd:cd16269    126 SAPLEEKISQGSysvpggyqlylEDREKLVEKYRQVPRKGVKAEEVLQEFLQSKEAEAEAI------LQADQALTEK-EK 198

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  291 LEQVLKHMREAAERRQQLEleheqalavltaKQQEIELLQKAQvEAKKEHEGAVQLLETKVQelEEKCRIQSEQFNLLS- 369
Cdd:cd16269    199 EIEAERAKAEAAEQERKLL------------EEQQRELEQKLE-DQERSYEEHLRQLKEKME--EERENLLKEQERALEs 263

                          170
                   ....*....|.
gi 1835591054  370 --KELERFRQQ 378
Cdd:cd16269    264 klKEQEALLEE 274
SH3_Noxa1_C cd12047
C-terminal Src Homology 3 domain of NADPH oxidase activator 1; Noxa1 is a homolog of p67phox ...
 1348-1405 4.90e-04

C-terminal Src Homology 3 domain of NADPH oxidase activator 1; Noxa1 is a homolog of p67phox and is a cytosolic subunit of the nonphagocytic NADPH oxidase complex Nox1, which catalyzes the transfer of electrons from NADPH to molecular oxygen to form superoxide. Noxa1 is co-expressed with Nox1 in colon, stomach, uterus, prostate, and vascular smooth muscle cells, consistent with its regulatory role. It does not interact with p40phox, unlike p67phox, making Nox1 activity independent of p40phox, unlike Nox2. Noxa1 contains TPR, PB1, and C-terminal SH3 domains, but lacks the central SH3 domain that is present in p67phox. The TPR domain binds activated GTP-bound Rac. The C-terminal SH3 domain binds the polyproline motif found at the C-terminus of Noxo1, a homolog of p47phox. 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: 212980  Cd Length: 53  Bit Score: 39.42  E-value: 4.90e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1348 RMVALYDYDPResSPnvdveAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNF 1405
Cdd:cd12047      1 RMVAQHDYSAQ--GP-----EDLEFSQGDTIDILSEVNQE-WLEGHCDGRIGIFPKCF 50
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
228-383 5.53e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 44.52  E-value: 5.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  228 ELKDAVQEKTHLN--LHYASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKL---------------EN 290
Cdd:COG4913    263 RYAAARERLAELEylRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELdeleaqirgnggdrlEQ 342

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  291 LEQVLKHMREAAERRQQLELEHEQALAVLTAK----QQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQFN 366
Cdd:COG4913    343 LEREIERLERELEERERRRARLEALLAALGLPlpasAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELR 422

                          170
                   ....*....|....*..
gi 1835591054  367 LLSKELERFRQQTGKID 383
Cdd:COG4913    423 ELEAEIASLERRKSNIP 439
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
 484-542 5.59e-04

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: 39.37  E-value: 5.59e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  484 CIARYSYNPFdgpneNPEaELPLTMGKYLYVYGDMDED-GFYEGELlDGQRGLVPSNFVE 542
Cdd:cd12142      2 CRVLFDYNPV-----APD-ELALKKGDVIEVISKETEDeGWWEGEL-NGRRGFFPDNFVM 54
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 612-693 5.67e-04

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 40.56  E-value: 5.67e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  612 PRKITLIKQLAKSVIVGWEPPvvPPGWGNINSYNVLV-----DKDIRLSVNFGSRTKALIEKLNLATcTYRISIQSVTNR 686
Cdd:cd00063      4 PTNLRVTDVTSTSVTLSWTPP--EDDGGPITGYVVEYrekgsGDWKEVEVTPGSETSYTLTGLKPGT-EYEFRVRAVNGG 80


                   ....*..
gi 1835591054  687 GNSDELQ 693
Cdd:cd00063     81 GESPPSE 87
SH3_SH3RF_2 cd11787
Second Src Homology 3 domain of SH3 domain containing ring finger proteins; This model ...
 1351-1405 5.82e-04

Second Src Homology 3 domain of SH3 domain containing ring finger proteins; This model represents the second 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: 212721 [Multi-domain]  Cd Length: 53  Bit Score: 39.24  E-value: 5.82e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054 1351 ALYDYDPRESspnvDVEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNF 1405
Cdd:cd11787      4 ALYDFEMKDE----DEKDCLTFKKGDVITVIRRVDEN-WAEGRLGDKIGIFPISF 53
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
 108-381 5.89e-04

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: 44.43  E-value: 5.89e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  108 KDLATEKDMEIKLLQVECEELKNRLcclkeglmgqrpSDVEQLLKQSQKELLWLQRQlsfistggptcilpSSKLRNDLP 187
Cdd:pfam10174  330 KESLTAKEQRAAILQTEVDALRLRL------------EEKESFLNKKTKQLQDLTEE--------------KSTLAGEIR 383

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  188 YLHPVLSQKtfdripflEEKTQVFKSDVNQEKQQWKDLEY---ELKDAVqekthlnlhyaslsqKALQYDQVKSD--YDQ 262
Cdd:pfam10174  384 DLKDMLDVK--------ERKINVLQKKIENLQEQLRDKDKqlaGLKERV---------------KSLQTDSSNTDtaLTT 440

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  263 LRETISKviKERDL-ALKGKHQL--QAKLENLEQVLKHMREAAE-----RRQQLE--------LEHEQALAVLTAKQQEI 326
Cdd:pfam10174  441 LEEALSE--KERIIeRLKEQRERedRERLEELESLKKENKDLKEkvsalQPELTEkesslidlKEHASSLASSGLKKDSK 518

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054  327 ELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSE---QFNLLSKELERFRQQTGK 381
Cdd:pfam10174  519 LKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRTNPEindRIRLLEQEVARYKEESGK 576
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 203-378 6.17e-04

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 43.75  E-value: 6.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  203 FLEEKTQVfksDVNQEKQQWKDL-EYELKDAVQEKTHLNLHYA---SLSQKALQYDQVKSDYDQLRETISKviKERDLAL 278
Cdd:pfam13868   96 KLQEREQM---DEIVERIQEEDQaEAEEKLEKQRQLREEIDEFneeQAEWKELEKEEEREEDERILEYLKE--KAEREEE 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  279 KGKHQLQAKLEnLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKC 358
Cdd:pfam13868  171 REAEREEIEEE-KEREIARLRAQQEKAQDEKAERDELRAKLYQEEQERKERQKEREEAEKKARQRQELQQAREEQIELKE 249

                          170       180
                   ....*....|....*....|.
gi 1835591054  359 RIQSEQfnllsKELER-FRQQ 378
Cdd:pfam13868  250 RRLAEE-----AEREEeEFER 265
SH3_SNX9_like cd11763
Src Homology 3 domain of Sorting Nexin 9 and similar proteins; Sorting nexins (SNXs) are Phox ...
 500-542 6.40e-04

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: 39.23  E-value: 6.40e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1835591054  500 PEAELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVE 542
Cdd:cd11763     12 PSGELSLRAGEVLTITRQDVGDGWLEGRNSRGEVGLFPSSYVE 54
SH3_MPP1 cd12080
Src Homology 3 domain of Membrane Protein, Palmitoylated 1 (or MAGUK p55 subfamily member 1); ...
 1349-1403 6.71e-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: 6.71e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1349 MVALYDYDPRESSPNVDVEAELTFCTGDIITVFGEiDEDGFYYGELNGQ----KGLVPS 1403
Cdd:cd12080      2 MRAQFDYDPKKDNLIPCKEAGLKFQTGDIIQIINK-DDSNWWQGRVEGSgeesAGLIPS 59
SH3_Nebulette_C cd11935
C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a ...
 1351-1409 6.71e-04

C-terminal Src Homology 3 domain of Nebulette and LIM-nebulette (or Lasp2); Nebulette is a cardiac-specific protein that localizes to the Z-disc. It interacts with tropomyosin and is important in stabilizing actin thin filaments in cardiac muscles. Polymorphisms in the nebulette gene are associated with dilated cardiomyopathy, with some mutations resulting in severe heart failure. Nebulette is a 107kD protein that contains an N-terminal acidic region, multiple nebulin repeats, and a C-terminal SH3 domain. LIM-nebulette, also called Lasp2 (LIM and SH3 domain protein 2), is an alternatively spliced variant of nebulette. Although it shares a gene with nebulette, Lasp2 is not transcribed from a muscle-specific promoter, giving rise to its multiple tissue expression pattern with highest amounts in the brain. It can crosslink actin filaments and it affects cell spreading. Lasp2 is a 34kD protein containing an N-terminal LIM domain, three 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: 212868 [Multi-domain]  Cd Length: 58  Bit Score: 39.22  E-value: 6.71e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1351 ALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEdGFYYGEL--NGQKGLVPSNFLEEV 1409
Cdd:cd11935      5 AMYDYSAQD-------EDEVSFRDGDYIVNVQPIDE-GWMYGTVqrTGRTGMLPANYIEFV 57
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
 1224-1281 6.73e-04

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: 38.88  E-value: 6.73e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1224 VALFDYDPltmspnpdAADEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMV 1281
Cdd:cd11804      3 VAKHDFKA--------TAEDELSFKKGSILKVLNMEDDPNWYKAELDGKEGLIPKNYI 52
SH3_STAM1 cd11964
Src homology 3 domain of Signal Transducing Adaptor Molecule 1; STAM1 is part of the endosomal ...
 1225-1282 6.78e-04

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: 39.16  E-value: 6.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1225 ALFDYDPltmspnpdAADEELPFKEGQIIKVYGDKDTDgFYRGATCARRGLIPCNMVS 1282
Cdd:cd11964      5 AIYDFEA--------AEDNELTFKAGDIITILDDSDPN-WWKGETPQGTGLFPSNFVT 53
SH3_SH3RF2_1 cd11929
First Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ...
 1348-1407 6.85e-04

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


Pssm-ID: 212862  Cd Length: 54  Bit Score: 39.15  E-value: 6.85e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYdpRESSPnvdveAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11929      2 RAKALCNY--RGHNP-----GDLKFNKGDVILLRRQLDEN-WYLGEINGVSGIFPASSVE 53
SH3_VAV_2 cd11830
C-terminal (or second) Src homology 3 domain of VAV proteins; VAV proteins function both as ...
 1244-1283 6.93e-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: 39.15  E-value: 6.93e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054 1244 ELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11830     15 ELSLKEGDVVKIYNKKGQQGWWRGEINGRIGWFPSTYVEE 54
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 12-382 7.25e-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: 44.19  E-value: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   12 QESSKISQPITKVENHSSKQQEEeGKLHKKERTDFTKKERNHRSEAKIPQKPHAVRLRKEIKPESRISPAAALKKPSAKQ 91
Cdd:TIGR00618  240 QSHAYLTQKREAQEEQLKKQQLL-KQLRARIEELRAQEAVLEETQERINRARKAAPLAAHIKAVTQIEQQAQRIHTELQS 318

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   92 RMRSVNGGPGQFQGINKDLATEKDMEIKLLQVECEELKNRLCCLKEGL----MGQRPSDVEQLLK-QSQKELLWLQRQLS 166
Cdd:TIGR00618  319 KMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSireiSCQQHTLTQHIHTlQQQKTTLTQKLQSL 398

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  167 FISTggptcilpsSKLRNDLPYLHPVLSQKTFDRIPFLEEKTQVfKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASL 246
Cdd:TIGR00618  399 CKEL---------DILQREQATIDTRTSAFRDLQGQLAHAKKQQ-ELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSL 468

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  247 SQKALQYDQVksdydqlrETISKVIKErdlalkgKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEI 326
Cdd:TIGR00618  469 KEREQQLQTK--------EQIHLQETR-------KKAVVLARLLELQEEPCPLCGSCIHPNPARQDIDNPGPLTRRMQRG 533

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054  327 E--LLQKAQVEAKKEHEGA-----VQLLETKVQELEEKCRIQSEQFNLLSKELERFRQQTGKI 382
Cdd:TIGR00618  534 EqtYAQLETSEEDVYHQLTserkqRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITVRL 596
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 34-384 7.25e-04

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 44.19  E-value: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   34 EEGKLHKKERTDFT---KKERNHRSEAKIPQKPhaVRLrKEIK---PESRISP-------------AAALKKPSAKQRMR 94
Cdd:pfam02463   83 NEDHELPIDKEEVSirrRVYRGGDSEYYINGKN--VTK-KEVAellESQGISPeaynflvqggkieIIAMMKPERRLEIE 159

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   95 SVNGGPGQFQGI---NKDLATEKDMEIKLLQVECEELKNRLcclKEGLMGQRPSDVEQLLKQSQKELLWLqrqlsfistg 171
Cdd:pfam02463  160 EEAAGSRLKRKKkeaLKKLIEETENLAELIIDLEELKLQEL---KLKEQAKKALEYYQLKEKLELEEEYL---------- 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  172 gptcilpssklrndlpylhpvlsqkTFDRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKThlnlhyaslsqkal 251
Cdd:pfam02463  227 -------------------------LYLDYLKLNEERIDLLQELLRDEQEEIESSKQEIEKEEEKL-------------- 267

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  252 qyDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMREAAERrqqLELEHEQALAVLTAKQQEIELLQK 331
Cdd:pfam02463  268 --AQVLKENKEEEKEKKLQEEELKLLAKEEEELKSELLKLERRKVDDEEKLKE---SEKEKKKAEKELKKEKEEIEELEK 342

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  332 AqveaKKEHEGAVQLLETKVQELEEKCR--IQSEQFNLLSKELERFRQQTGKIDL 384
Cdd:pfam02463  343 E----LKELEIKREAEEEEEEELEKLQEklEQLEEELLAKKKLESERLSSAAKLK 393
EmrA COG1566
Multidrug resistance efflux pump EmrA [Defense mechanisms];
244-357 7.31e-04

Multidrug resistance efflux pump EmrA [Defense mechanisms];


Pssm-ID: 441174 [Multi-domain]  Cd Length: 331  Bit Score: 43.50  E-value: 7.31e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  244 ASLSQKALQYDQVKSDYDQLRETISKvikERDLAlkgkhQLQAKLENLEQVLKHMREAAERRQQL-------ELEHEQAL 316
Cdd:COG1566     83 AALAQAEAQLAAAEAQLARLEAELGA---EAEIA-----AAEAQLAAAQAQLDLAQRELERYQALykkgavsQQELDEAR 154

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1835591054  317 AVLTAKQQEIELLQKAQVEAKKEHEGAVQL--LETKVQELEEK 357
Cdd:COG1566    155 AALDAAQAQLEAAQAQLAQAQAGLREEEELaaAQAQVAQAEAA 197
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
 209-378 8.63e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 42.43  E-value: 8.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  209 QVFKSDVNQEKQqW-KDLEYELKDAVQEKTHLNLHyaSLSQKalqYDQVKSDYDQLRETISKVIKE-RDLALKGKH---Q 283
Cdd:cd00176      3 QQFLRDADELEA-WlSEKEELLSSTDYGDDLESVE--ALLKK---HEALEAELAAHEERVEALNELgEQLIEEGHPdaeE 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 LQAKLENLEQVLKHMRE-AAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEG---AVQLLETKVQELEEKCR 359
Cdd:cd00176     77 IQERLEELNQRWEELRElAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKdleSVEELLKKHKELEEELE 156

                          170
                   ....*....|....*....
gi 1835591054  360 IQSEQFNLLSKELERFRQQ 378
Cdd:cd00176    157 AHEPRLKSLNELAEELLEE 175
SH3_Sho1p cd11855
Src homology 3 domain of High osmolarity signaling protein Sho1p; Sho1p (or Sho1), also called ...
 1351-1407 8.72e-04

Src homology 3 domain of High osmolarity signaling protein Sho1p; Sho1p (or Sho1), also called SSU81 (Suppressor of SUA8-1 mutation), is a yeast membrane protein that regulates adaptation to high salt conditions by activating the HOG (high-osmolarity glycerol) pathway. High salt concentrations lead to the localization to the membrane of the MAPKK Pbs2, which is then activated by the MAPKK Ste11 and in turn, activates the MAPK Hog1. Pbs2 is localized to the membrane though the interaction of its PxxP motif with the SH3 domain of Sho1p. 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: 212789 [Multi-domain]  Cd Length: 55  Bit Score: 38.94  E-value: 8.72e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPRESSPNvdveaELTFCTGDIITVfgeIDEDGFYYG--ELNGQKGLVPSNFLE 1407
Cdd:cd11855      4 ALYPYDASPDDPN-----ELSFEKGEILEV---SDTSGKWWQarKSNGETGICPSNYLQ 54
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 30-380 8.88e-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: 44.19  E-value: 8.88e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   30 KQQEEEGK-LHKKERTdfTKKERNHRSEakipqkphavRLRKEIKP--ESRISPAAAlkkpsakqRMRSVNGGPGQ---F 103
Cdd:TIGR00618  472 EQQLQTKEqIHLQETR--KKAVVLARLL----------ELQEEPCPlcGSCIHPNPA--------RQDIDNPGPLTrrmQ 531

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  104 QGINKDLATEKdmEIKLLQVECEELKNRLCCLKEGLmgQRPSDVEQLLKQSQKELlwlqrqlsfistggpTCILPssKLR 183
Cdd:TIGR00618  532 RGEQTYAQLET--SEEDVYHQLTSERKQRASLKEQM--QEIQQSFSILTQCDNRS---------------KEDIP--NLQ 590

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  184 NDLPYLHPVLSQKTFDRIPFLEE--------KTQVFKSDVNQEKQQwKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQ 255
Cdd:TIGR00618  591 NITVRLQDLTEKLSEAEDMLACEqhallrklQPEQDLQDVRLHLQQ-CSQELALKLTALHALQLTLTQERVREHALSIRV 669

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  256 VKSDYDQLRETISKVIKERdlalkgKHQLQAKLENLEQVLKHMREAAERRQQLELE-HEQALAVLTAK---QQEIELLQK 331
Cdd:TIGR00618  670 LPKELLASRQLALQKMQSE------KEQLTYWKEMLAQCQTLLRELETHIEEYDREfNEIENASSSLGsdlAAREDALNQ 743

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054  332 AQVEAKKEHEGAVQLLE-----------------TKVQELEEKCRIQSEQFNLLSKELERFRQQTG 380
Cdd:TIGR00618  744 SLKELMHQARTVLKARTeahfnnneevtaalqtgAELSHLAAEIQFFNRLREEDTHLLKTLEAEIG 809
SH3_Bem1p_1 cd11878
First Src Homology 3 domain of Bud emergence protein 1 and similar domains; Members of this ...
 1351-1405 9.22e-04

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: 38.81  E-value: 9.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFY--YGELNGQKGLVPSNF 1405
Cdd:cd11878      4 ALYDYRAQTPG-------ELSFSKGDFFHVIGEEDQGEWYeaTNPVTGKRGLVPKSY 53
SH3_VAV1_2 cd11976
C-terminal (or second) Src homology 3 domain of VAV1 protein; VAV1 is expressed predominantly ...
 1244-1283 9.54e-04

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: 38.77  E-value: 9.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054 1244 ELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11976     15 ELSLKEGDIIKILNKKGQQGWWRGEIYGRVGWFPANYVEE 54
SH3_STAM2 cd11963
Src homology 3 domain of Signal Transducing Adaptor Molecule 2; STAM2, also called EAST ...
 1225-1282 1.11e-03

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: 38.46  E-value: 1.11e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054 1225 ALFDYDPLTmspnpdaaDEELPFKEGQIIKVYGDKDTDgFYRGATCARRGLIPCNMVS 1282
Cdd:cd11963      6 ALYDFEAVE--------DNELTFKHGEIIIVLDDSDAN-WWKGENHRGVGLFPSNFVT 54
SH3_ephexin1_like cd11793
Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange ...
 503-543 1.11e-03

Src homology 3 domain of ephexin-1-like SH3 domain containing Rho guanine nucleotide exchange factors; Members of this family contain RhoGEF (also called Dbl-homologous or DH), Pleckstrin Homology (PH), and C-terminal SH3 domains. They include the Rho guanine nucleotide exchange factors ARHGEF5, ARHGEF16, ARHGEF19, ARHGEF26, ARHGEF27 (also called ephexin-1), and similar proteins, and are also called ephexins because they interact directly with ephrin A receptors. GEFs interact with Rho GTPases via their DH domains to catalyze nucleotide exchange by stabilizing the nucleotide-free GTPase intermediate. They play important roles in neuronal development. The SH3 domains of ARHGEFs play an autoinhibitory role through intramolecular interactions with a proline-rich region N-terminal to the DH 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: 212727 [Multi-domain]  Cd Length: 55  Bit Score: 38.47  E-value: 1.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1835591054  503 ELPLTMGKYLYVYGDMDeDGFYEGE-LLDGQRGLVPSNFVEF 543
Cdd:cd11793     15 ELTLEEGDVVNVLRKMP-DGWYEGErLRDGERGWFPSSYTEE 55
SH3_Nebulin_C cd11933
C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 ...
 1351-1409 1.12e-03

C-terminal Src Homology 3 domain of Nebulin; Nebulin is a giant filamentous protein (600-900 kD) that is expressed abundantly in skeletal muscle. It binds to actin thin filaments and regulates its assembly and function. Nebulin was thought to be part of a molecular ruler complex that is critical in determining the lengths of actin thin filaments in skeletal muscle since its length, which varies due to alternative splicing, correlates with the length of thin filaments in various muscle types. Recent studies indicate that nebulin regulates thin filament length by stabilizing the filaments and preventing depolymerization. Mutations in nebulin can cause nemaline myopathy, characterized by muscle weakness which can be severe and can lead to neonatal lethality. Nebulin contains an N-terminal LIM domain, many nebulin repeats/super 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: 212866 [Multi-domain]  Cd Length: 58  Bit Score: 38.45  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEdGFYYGELN--GQKGLVPSNFLEEV 1409
Cdd:cd11933      6 AMYDYRAADDD-------EVSFKDGDTIVNVQTIDE-GWMYGTVQrtGKTGMLPANYVEAI 58
SH3_Pex13p_fungal cd11771
Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the ...
 484-542 1.12e-03

Src Homology 3 domain of fungal peroxisomal membrane protein Pex13p; Pex13p, located in the peroxisomal membrane, contains two transmembrane regions and a C-terminal SH3 domain. It binds to the peroxisomal targeting type I (PTS1) receptor Pex5p and the docking factor Pex14p through its SH3 domain. It is essential for both PTS1 and PTS2 protein import pathways into the peroxisomal matrix. Pex13p binds Pex14p, which contains a PxxP motif, in a classical fashion to the proline-rich ligand binding site of its SH3 domain. It binds the WxxxF/Y motif of Pex5p in a novel site that does not compete with Pex14p binding. 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: 212705 [Multi-domain]  Cd Length: 60  Bit Score: 38.80  E-value: 1.12e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054  484 CIARYSYNPfdgpnENPEAELPLTMGKYLYVYGDMD----EDGFYEGELLDGQRGLVPSNFVE 542
Cdd:cd11771      2 CRALYDFTP-----ENPEMELSLKKGDIVAVLSKTDplgrDSEWWKGRTRDGRIGWFPSNYVE 59
SH3_Abp1_fungi_C1 cd11962
First C-terminal Src homology 3 domain of Fungal Actin-binding protein 1; Abp1 is an adaptor ...
 1348-1407 1.26e-03

First 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: 212895 [Multi-domain]  Cd Length: 54  Bit Score: 38.24  E-value: 1.26e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1348 RMVALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDGFYYGELNGQKGLVPSNFLE 1407
Cdd:cd11962      1 RAVVLYDYEKDE-------DNEIELVEGEIVTNIEMVDEDWWMGTNSKGESGLFPSNYVE 53
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
40-359 1.28e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 1.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   40 KKERTDFTKKERNHRSEAKipqkphavRLRKEIKPESRISPaaaLKKpSAKQrMRSVNGgpgQFQGINKDLATEKDMEIK 119
Cdd:PRK03918   465 EKELKEIEEKERKLRKELR--------ELEKVLKKESELIK---LKE-LAEQ-LKELEE---KLKKYNLEELEKKAEEYE 528

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  120 LLQVECEELKNRLCCLKEglmgqrpsDVEQLlKQSQKELLWLQRQLSfistggptcilpssKLRNDLPYLHPVLSQKTFD 199
Cdd:PRK03918   529 KLKEKLIKLKGEIKSLKK--------ELEKL-EELKKKLAELEKKLD--------------ELEEELAELLKELEELGFE 585

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  200 RIPFLEEKTQVFKSDVNqekqqwkdlEY-ELKDAVQEKTHLnlhyaslsQKALqydqvksdyDQLRETISKVIKERDLAL 278
Cdd:PRK03918   586 SVEELEERLKELEPFYN---------EYlELKDAEKELERE--------EKEL---------KKLEEELDKAFEELAETE 639

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  279 KGKHQLQAKLENLEQvlKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQ----------KAQVEAKKEHEGAVQLLE 348
Cdd:PRK03918   640 KRLEELRKELEELEK--KYSEEEYEELREEYLELSRELAGLRAELEELEKRReeikktleklKEELEEREKAKKELEKLE 717

                          330
                   ....*....|....
gi 1835591054  349 ---TKVQELEEKCR 359
Cdd:PRK03918   718 kalERVEELREKVK 731
SH3_CD2AP_3 cd12056
Third Src Homology 3 domain (SH3C) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 1367-1405 1.35e-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: 38.27  E-value: 1.35e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054 1367 EAELTFCTGDIITVFG-EIDEDGFYYGELNGQKGLVPSNF 1405
Cdd:cd12056     15 EDELDFKEGEIILIISkDTGEPGWWKGELNGKEGVFPDNF 54
SH3_PACSIN1-2 cd11998
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons 1 (PACSIN1) ...
 486-542 1.47e-03

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: 38.39  E-value: 1.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  486 ARYSYnpfDGPNENpeaELPLTMGKYLYVYGDMDEDGFYEGELLDGQRGLVPSNFVE 542
Cdd:cd11998      5 ALYDY---DGQEQD---ELSFKAGDELTKLEDEDEQGWCKGRLDSGQVGLYPANYVE 55
SH3_Endophilin_B1 cd11945
Src homology 3 domain of Endophilin-B1; Endophilin-B1, also called Bax-interacting factor 1 ...
 1346-1407 1.49e-03

Src homology 3 domain of Endophilin-B1; Endophilin-B1, also called Bax-interacting factor 1 (Bif-1) or SH3GLB1 (SH3-domain GRB2-like endophilin B1), is localized mainly to the Golgi apparatus. It is involved in the regulation of many biological events including autophagy, tumorigenesis, nerve growth factor (NGF) trafficking, neurite outgrowth, mitochondrial outer membrane dynamics, and cell death. Endophilins play roles in synaptic vesicle formation, virus budding, mitochondrial morphology maintenance, receptor-mediated endocytosis inhibition, and endosomal sorting. They 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. Endophilin-B1 forms homo- and heterodimers (with endophilin-B2) through its BAR domain. It interacts with amphiphysin 1 and dynamin 1 through its 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: 212878  Cd Length: 61  Bit Score: 38.47  E-value: 1.49e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054 1346 TRRMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDG-FYYGELNGQKGLVPSNFLE 1407
Cdd:cd11945      3 SRKARVLYDYDAANST-------ELSLLADEVITVYSVPGMDSdWLMGERGNQKGKVPITYLE 58
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
 519-543 1.50e-03

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: 38.04  E-value: 1.50e-03
                           10        20
                   ....*....|....*....|....*
gi 1835591054  519 DEDGFYEGeLLDGQRGLVPSNFVEF 543
Cdd:cd11882     31 DEPGWLEG-TLNGRTGLIPENYVEF 54
SH3_srGAP cd11809
Src homology 3 domain of Slit-Robo GTPase Activating Proteins; Slit-Robo GTPase Activating ...
 1350-1406 1.77e-03

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: 37.77  E-value: 1.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1350 VALYDYDPREsspnvdvEAELTFCTGDIITVFGEIDEDgFYYGELNGQKGLVPSNFL 1406
Cdd:cd11809      3 TAQFDYTGRS-------ERELSFKKGDSLTLYRQVSDD-WWRGQLNGQDGLVPHKYI 51
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
251-357 1.80e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 41.35  E-value: 1.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  251 LQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLE-QVLKHM--------REAAERRQQLELEHEQAlavlta 321
Cdd:COG1842     30 QAIRDMEEDLVEARQALAQVIANQKRLERQLEELEAEAEKWEeKARLALekgredlaREALERKAELEAQAEAL------ 103

                           90       100       110
                   ....*....|....*....|....*....|....*.
gi 1835591054  322 kQQEIELLQKAQVEAKKehegAVQLLETKVQELEEK 357
Cdd:COG1842    104 -EAQLAQLEEQVEKLKE----ALRQLESKLEELKAK 134
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 205-379 1.82e-03

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 42.18  E-value: 1.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  205 EEKTQVFKS----DVNQEKQQwkdleyELKDAVQEKthlnlhYASLSQKALQ--YDQVKSDYDQLRETISKVIKERDLAL 278
Cdd:cd16269     73 KEALEVFMKrsfkDEDQKFQK------KLMEQLEEK------KEEFCKQNEEasSKRCQALLQELSAPLEEKISQGSYSV 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  279 KGKHQL-----QAKLENLEQVLKHMREAAERRQQ----LELEHE---QALAVLTAKQQEIELLQKAQVEAKKEHEGAVQL 346
Cdd:cd16269    141 PGGYQLyledrEKLVEKYRQVPRKGVKAEEVLQEflqsKEAEAEailQADQALTEKEKEIEAERAKAEAAEQERKLLEEQ 220

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1835591054  347 LETKVQELEEKCRIQSEQFNLLSKELERFRQQT 379
Cdd:cd16269    221 QRELEQKLEDQERSYEEHLRQLKEKMEEERENL 253
BAR_SNX cd07596
The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid ...
 218-379 1.84e-03

The Bin/Amphiphysin/Rvs (BAR) domain of Sorting Nexins; BAR domains are dimerization, lipid binding and curvature sensing modules found in many different proteins with diverse functions. 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. A subset of SNXs also contain BAR domains. The PX-BAR structural unit determines the specific membrane targeting of SNXs. BAR domains form dimers that bind to membranes, induce membrane bending and curvature, and may also be involved in protein-protein interactions.


Pssm-ID: 153280 [Multi-domain]  Cd Length: 218  Bit Score: 41.57  E-value: 1.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  218 EKQQWKDLEYELKDAVQEKTHLNLHYASLSQ-------KALQYDQVKSDYDQ-LRETISKVIK-ERDLALKGKHQLQAKL 288
Cdd:cd07596      9 AKDYILKLEEQLKKLSKQAQRLVKRRRELGSalgefgkALIKLAKCEEEVGGeLGEALSKLGKaAEELSSLSEAQANQEL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  289 ENLEQVLK---HM----REAAERRQQLELEHEQALAVLTAKQQEIELLQKA--QVEAKKEH-EGAVQLLETKVQELEEKC 358
Cdd:cd07596     89 VKLLEPLKeylRYcqavKETLDDRADALLTLQSLKKDLASKKAQLEKLKAApgIKPAKVEElEEELEEAESALEEARKRY 168

                          170       180
                   ....*....|....*....|.
gi 1835591054  359 RIQSEqfnLLSKELERFRQQT 379
Cdd:cd07596    169 EEISE---RLKEELKRFHEER 186
fn3 pfam00041
Fibronectin type III domain;
801-888 2.02e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 38.55  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  801 PPQDIRIQaGPTPTAILVTWKPPtltptgTSNGANITGY-VAYAK---GQKVAEVVFPTAESTVVdllrIQNLEAK---E 873
Cdd:pfam00041    2 APSNLTVT-DVTSTSLTVSWTPP------PDGNGPITGYeVEYRPknsGEPWNEITVPGTTTSVT----LTGLKPGteyE 70

                           90
                   ....*....|....*
gi 1835591054  874 ITIRSLSAQGESEDS 888
Cdd:pfam00041   71 VRVQAVNGGGEGPPS 85
SH3_SH3RF_C cd11785
C-terminal (Fourth) Src Homology 3 domain of SH3 domain containing ring finger 1 (SH3RF1), ...
 499-542 2.11e-03

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


Pssm-ID: 212719  Cd Length: 55  Bit Score: 37.83  E-value: 2.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1835591054  499 NPEAELPLTMGKYLYVYGDMdEDGFYEGELL-DGQRGLVPSNFVE 542
Cdd:cd11785     11 QSEAELELKEGDIVFVHKKR-EDGWFKGTLQrTGKTGLFPGSFVE 54
SH3_RUSC1_like cd11810
Src homology 3 domain of RUN and SH3 domain-containing proteins 1 and 2; RUSC1 and RUSC2, that ...
 1348-1402 2.12e-03

Src homology 3 domain of RUN and SH3 domain-containing proteins 1 and 2; RUSC1 and RUSC2, that were originally characterized in silico. They are adaptor proteins consisting of RUN, leucine zipper, and SH3 domains. RUSC1, also called NESCA (New molecule containing SH3 at the carboxy-terminus), is highly expressed in the brain and is translocated to the nuclear membrane from the cytoplasm upon stimulation with neurotrophin. It plays a role in facilitating neurotrophin-dependent neurite outgrowth. It also interacts with NEMO (or IKKgamma) and may function in NEMO-mediated activation of NF-kB. RUSC2, also called Iporin, is expressed ubiquitously with highest amounts in the brain and testis. It interacts with the small GTPase Rab1 and the Golgi matrix protein GM130, and may function in linking GTPases to certain intracellular signaling pathways. 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: 212744  Cd Length: 50  Bit Score: 37.42  E-value: 2.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054 1348 RMVALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDEDGFYYGeLNGQKGLVP 1402
Cdd:cd11810      1 VVRALCHHVATDSG-------QLSFRKGDILRVIARVDDDWLLCT-RGSTKGLVP 47
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
 705-769 2.20e-03

Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein fibronectin. Its tenth fibronectin type III repeat contains an RGD cell recognition sequence in a flexible loop between 2 strands. Approximately 2% of all animal proteins contain the FN3 repeat; including extracellular and intracellular proteins, membrane spanning cytokine receptors, growth hormone receptors, tyrosine phosphatase receptors, and adhesion molecules. FN3-like domains are also found in bacterial glycosyl hydrolases.


Pssm-ID: 238020 [Multi-domain]  Cd Length: 93  Bit Score: 39.02  E-value: 2.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  705 APSQLKVDNITQTSAGLSWLPTNSNYSHV----IFLNE------EEFDIVKAAIYKYQFFNLKPNMAYKVKLLAK 769
Cdd:cd00063      3 PPTNLRVTDVTSTSVTLSWTPPEDDGGPItgyvVEYREkgsgdwKEVEVTPGSETSYTLTGLKPGTEYEFRVRAV 77
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
272-378 2.25e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 42.45  E-value: 2.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  272 KERDLALKGKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQ-----VEAKKEHEGAVQL 346
Cdd:COG4717     64 RKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLqllplYQELEALEAELAE 143

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1835591054  347 LETKVQELEEK-CRIQSEQFNL--LSKELERFRQQ 378
Cdd:COG4717    144 LPERLEELEERlEELRELEEELeeLEAELAELQEE 178
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
 205-377 2.72e-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: 2.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  205 EEKTQvfksdvnQEKQQWK-DLEYELKDAVQEKTHLNLHYASLSQkalqydQVKSDYDQLRETISKVIKE---RDLALKG 280
Cdd:pfam01576  199 EEKGR-------QELEKAKrKLEGESTDLQEQIAELQAQIAELRA------QLAKKEEELQAALARLEEEtaqKNNALKK 265

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  281 KHQLQAKLENLEQVL-----------KHMREAAERRQQLELEHEQALAVLTAKQ-------QEIELLQKAQVEAKKEHeg 342
Cdd:pfam01576  266 IRELEAQISELQEDLeseraarnkaeKQRRDLGEELEALKTELEDTLDTTAAQQelrskreQEVTELKKALEEETRSH-- 343

                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1835591054  343 avqllETKVQELEEKcriQSEQFNLLSKELERFRQ 377
Cdd:pfam01576  344 -----EAQLQEMRQK---HTQALEELTEQLEQAKR 370
TPH pfam13868
Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of ...
 205-378 2.84e-03

Trichohyalin-plectin-homology domain; This family is a mixtrue of two different families of eukaryotic proteins. Trichoplein or mitostatin, was first defined as a meiosis-specific nuclear structural protein. It has since been linked with mitochondrial movement. It is associated with the mitochondrial outer membrane, and over-expression leads to reduction in mitochondrial motility whereas lack of it enhances mitochondrial movement. The activity appears to be mediated through binding the mitochondria to the actin intermediate filaments (IFs). The family is in the trichohyalin-plectin-homology domain.


Pssm-ID: 464007 [Multi-domain]  Cd Length: 341  Bit Score: 41.83  E-value: 2.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  205 EEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKThlnlhyASLSQKALQYDQVKSDYDQLR------ETISK-VIKERDLA 277
Cdd:pfam13868  154 DERILEYLKEKAEREEEREAEREEIEEEKEREI------ARLRAQQEKAQDEKAERDELRaklyqeEQERKeRQKEREEA 227

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  278 LKgKHQLQAKL--ENLEQVLKHMREAAERRQQLELEHEQALAVLtAKQQEIELLQKAQVEAK-KEHEGAVQLLETKVQEL 354
Cdd:pfam13868  228 EK-KARQRQELqqAREEQIELKERRLAEEAEREEEEFERMLRKQ-AEDEEIEQEEAEKRRMKrLEHRRELEKQIEEREEQ 305

                          170       180
                   ....*....|....*....|....
gi 1835591054  355 EEKCRIQSEQFNLLSKELERFRQQ 378
Cdd:pfam13868  306 RAAEREEELEEGERLREEEAERRE 329
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
127-374 2.85e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.36  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  127 ELKNRLCCLKEGLMgqRPSDVEQLLKQSQKELLWLQRQLSFISTGGPTCILPSSKLRNDLPYLhpvlsQKTFDRIPFLEE 206
Cdd:PRK03918   173 EIKRRIERLEKFIK--RTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKEL-----EELKEEIEELEK 245

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  207 KTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYA---SLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQ 283
Cdd:PRK03918   246 ELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEING 325

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  284 LQAKLENLEQVLKHMREAAERRQQLELEHE------QALAVLTAKQQEIELLQKAQVEAKKEH-EGAVQLLETKVQELEE 356
Cdd:PRK03918   326 IEERIKELEEKEERLEELKKKLKELEKRLEeleerhELYEEAKAKKEELERLKKRLTGLTPEKlEKELEELEKAKEEIEE 405

                          250
                   ....*....|....*....
gi 1835591054  357 KCR-IQSEQFNLLSKELER 374
Cdd:PRK03918   406 EISkITARIGELKKEIKEL 424
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 484-544 2.85e-03

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: 37.24  E-value: 2.85e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054  484 CIARYSYNPfdgpnENpEAELPLTMGKYLYVYGDMDEDgFYEGELlDGQRGLVPSNFVEFV 544
Cdd:cd11803      3 CRALYDFEP-----EN-EGELGFKEGDIITLTNQIDEN-WYEGMV-NGQSGFFPVNYVEVL 55
SH3_Intersectin2_1 cd11988
First Src homology 3 domain (or SH3A) of Intersectin-2; Intersectin-2 (ITSN2) is an adaptor ...
 1351-1408 2.87e-03

First Src homology 3 domain (or SH3A) 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 first SH3 domain (or SH3A) of ITSN2 is expected to bind many protein partners, similar to ITSN1 which has been shown to bind 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: 212921 [Multi-domain]  Cd Length: 57  Bit Score: 37.54  E-value: 2.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1835591054 1351 ALYDYDPRESSpnvdveaELTFCTGDIITV-FGEIDEDGFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11988      6 ALYPFEARNHD-------EMSFNAGDIIQVdEKTVGEPGWLYGSFQGNFGWFPCNYVEK 57
SH3_GRAF-like cd11882
Src Homology 3 domain of GTPase Regulator Associated with Focal adhesion kinase and similar ...
 1242-1282 3.15e-03

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: 37.27  E-value: 3.15e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1835591054 1242 DEELPFKEGQIIKVYGDKDTDGFYRGATCARRGLIPCNMVS 1282
Cdd:cd11882     13 ESELSFEPGQIITNVQPSDEPGWLEGTLNGRTGLIPENYVE 53
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
 493-542 3.23e-03

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: 37.33  E-value: 3.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1835591054  493 FDGPNENPEaELPLTMGKYLYVYG-DMDEDGFYEGELlDGQRGLVPSNFVE 542
Cdd:cd11875      6 FDYEAENED-ELTLREGDIVTILSkDCEDKGWWKGEL-NGKRGVFPDNFVE 54
GimC COG1382
Prefoldin, chaperonin cofactor [Posttranslational modification, protein turnover, chaperones];
283-372 3.23e-03

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


Pssm-ID: 440992 [Multi-domain]  Cd Length: 121  Bit Score: 39.10  E-value: 3.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  283 QLQAKLENLEQVLKHMREAAERRQQLELEH---EQALAVLTAKQQEIE--------LLQKAQVEAKKEHEGAVQLLETKV 351
Cdd:COG1382      8 EVQNQLAQLQQLQQQLQAVAAQKQQVESELkeaEKALEELEKLPDDAEvyksvgnlLVKTDKEEVIKELEEKKETLELRL 87

                           90       100
                   ....*....|....*....|...
gi 1835591054  352 QELE--EKcRIQsEQFNLLSKEL 372
Cdd:COG1382     88 KTLEkqEE-RLQ-KQLEELQEKL 108
ATP-synt_Fo_b cd06503
F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex ...
 267-354 3.32e-03

F-type ATP synthase, membrane subunit b; Membrane subunit b is a component of the Fo complex of FoF1-ATP synthase. The F-type ATP synthases (FoF1-ATPase) consist of two structural domains: the F1 (assembly factor one) complex containing the soluble catalytic core, and the Fo (oligomycin sensitive factor) complex containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. F1 is composed of alpha (or A), beta (B), gamma (C), delta (D) and epsilon (E) subunits with a stoichiometry of 3:3:1:1:1, while Fo consists of the three subunits a, b, and c (1:2:10-14). An oligomeric ring of 10-14 c subunits (c-ring) make up the Fo rotor. The flux of protons through the ATPase channel (Fo) drives the rotation of the c-ring, which in turn is coupled to the rotation of the F1 complex gamma subunit rotor due to the permanent binding between the gamma and epsilon subunits of F1 and the c-ring of Fo. The F-ATP synthases are primarily found in the inner membranes of eukaryotic mitochondria, in the thylakoid membranes of chloroplasts or in the plasma membranes of bacteria. The F-ATP synthases are the primary producers of ATP, using the proton gradient generated by oxidative phosphorylation (mitochondria) or photosynthesis (chloroplasts). Alternatively, under conditions of low driving force, ATP synthases function as ATPases, thus generating a transmembrane proton or Na(+) gradient at the expense of energy derived from ATP hydrolysis. This group also includes F-ATP synthase that has also been found in the archaea Candidatus Methanoperedens.


Pssm-ID: 349951 [Multi-domain]  Cd Length: 132  Bit Score: 39.34  E-value: 3.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  267 ISKVIKER--------DLALKGKHQLQAKLENLEQVLKHMR-EAAERRQQLELEHEQALAVLTAK-QQEIE-LLQKAQVE 335
Cdd:cd06503     24 ILKALDEReekiaeslEEAEKAKEEAEELLAEYEEKLAEARaEAQEIIEEARKEAEKIKEEILAEaKEEAErILEQAKAE 103

                           90
                   ....*....|....*....
gi 1835591054  336 AKKEHEGAVQLLETKVQEL 354
Cdd:cd06503    104 IEQEKEKALAELRKEVADL 122
SH3_Cortactin_like cd11819
Src homology 3 domain of Cortactin and related proteins; This subfamily includes cortactin, ...
 485-542 3.49e-03

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: 36.91  E-value: 3.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1835591054  485 IARYSYNPfdgpneNPEAELPLTMGKYLYVYGDMDEdGFYEGELLDGQRGLVPSNFVE 542
Cdd:cd11819      3 KALYDYQA------AEDNEISFVEGDIITQIEQIDE-GWWLGVNAKGQKGLFPANYVE 53
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 612-689 3.50e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 37.98  E-value: 3.50e-03
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054   612 PRKITLIKQLAKSVIVGWEPPVVPPGWGNINSYNVLVDKDIRLSVNF---GSRTKALIEKLNLATcTYRISIQSVTNRGN 688
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGYRVEYREEGSEWKEVnvtPSSTSYTLTGLKPGT-EYEFRVRAVNGAGE 82


                    .
gi 1835591054   689 S 689
Cdd:smart00060   83 G 83
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 283-414 3.57e-03

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: 41.67  E-value: 3.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  283 QLQAKLENLEQvlkHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKE---HEGAVQLLETKVQELEEKCR 359
Cdd:COG4942     24 EAEAELEQLQQ---EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQElaaLEAELAELEKEIAELRAELE 100

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  360 IQSEQFNLLSKELERFRQQTGKIDLLSGASVASSDIIGSPSKSLSQFMNGIATAI 414
Cdd:COG4942    101 AQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARREQAEEL 155
HMMR_N pfam15905
Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of ...
 232-375 3.79e-03

Hyaluronan mediated motility receptor N-terminal; HMMR_N is the N-terminal region of eukaryotic hyaluronan-mediated motility receptor proteins. The protein is functionally associated with BRCA1 and thus predicted to be a common, low-penetrance breast cancer candidate.


Pssm-ID: 464932 [Multi-domain]  Cd Length: 329  Bit Score: 41.34  E-value: 3.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  232 AVQEKTHLNLHYAslsQKALQydQVKSDYDQLRETISKVIKErdlalkgKHQLQAKLENLEQVLKHMREAAERRQQLELE 311
Cdd:pfam15905  177 AKQEGMEGKLQVT---QKNLE--HSKGKVAQLEEKLVSTEKE-------KIEEKSETEKLLEYITELSCVSEQVEKYKLD 244

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054  312 HEQALAVLTAKQQEIELLQKAqVEAKKEHegavqlLETKVQELEEKCR-IQSEQFNLLSKELERF 375
Cdd:pfam15905  245 IAQLEELLKEKNDEIESLKQS-LEEKEQE------LSKQIKDLNEKCKlLESEKEELLREYEEKE 302
SH3_SH3RF2_3 cd11784
Third Src Homology 3 domain of SH3 domain containing ring finger 2; SH3RF2 is also called ...
 483-541 3.91e-03

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


Pssm-ID: 212718  Cd Length: 55  Bit Score: 37.06  E-value: 3.91e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  483 LCIARYSYNPfdgpnENPEaELPLTMGKYLYVYGDMdEDGFYEG-ELLDGQRGLVPSNFV 541
Cdd:cd11784      1 MCVALHSYSA-----HRPE-ELELQKGEGVRVLGKF-QEGWLRGlSLVTGRVGIFPSNYV 53
mukB PRK04863
chromosome partition protein MukB;
220-390 3.96e-03

chromosome partition protein MukB;


Pssm-ID: 235316 [Multi-domain]  Cd Length: 1486  Bit Score: 41.87  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  220 QQWKDLEYELKDAVQE-KTHLNLHYASLSQKALQYDQVKS---------DYDQLRETISKVIKERDLALKGkHQLQAKLE 289
Cdd:PRK04863   445 EEFQAKEQEATEELLSlEQKLSVAQAAHSQFEQAYQLVRKiagevsrseAWDVARELLRRLREQRHLAEQL-QQLRMRLS 523

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  290 NLEQVLK------HMREAAERRQQLELEHEQALAVLTAKQ-QEIELL--QKAQV-EAKKEHEGAVQLLETKVQELEekcr 359
Cdd:PRK04863   524 ELEQRLRqqqraeRLLAEFCKRLGKNLDDEDELEQLQEELeARLESLseSVSEArERRMALRQQLEQLQARIQRLA---- 599

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1835591054  360 IQSEQFNLLSKELERFRQQTGKiDLLSGASV 390
Cdd:PRK04863   600 ARAPAWLAAQDALARLREQSGE-EFEDSQDV 629
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
221-378 3.96e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 3.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  221 QWKDLEYELKDAVQEKthlnlhyasLSQKALQYDQVKSDYDQLRETISKV----------IKERDLALKGKHQLQAKLEN 290
Cdd:PRK03918   504 QLKELEEKLKKYNLEE---------LEKKAEEYEKLKEKLIKLKGEIKSLkkelekleelKKKLAELEKKLDELEEELAE 574

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  291 LEQVL-----KHMREAAERRQQLELEHEQALAV------LTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCR 359
Cdd:PRK03918   575 LLKELeelgfESVEELEERLKELEPFYNEYLELkdaekeLEREEKELKKLEEELDKAFEELAETEKRLEELRKELEELEK 654

                          170       180
                   ....*....|....*....|....*..
gi 1835591054  360 IQSEQ--------FNLLSKELERFRQQ 378
Cdd:PRK03918   655 KYSEEeyeelreeYLELSRELAGLRAE 681
SH3_VAV2_2 cd11977
C-terminal (or second) Src homology 3 domain of VAV2 protein; VAV2 is widely expressed and ...
 1350-1408 4.00e-03

C-terminal (or second) Src homology 3 domain of VAV2 protein; VAV2 is widely expressed and functions as a guanine nucleotide exchange factor (GEF) for RhoA, RhoB and RhoG and also activates Rac1 and Cdc42. It is implicated in many cellular and physiological functions including blood pressure control, eye development, neurite outgrowth and branching, EGFR endocytosis and degradation, and cell cluster morphology, among others. It has been reported to associate with Nek3. 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: 212910 [Multi-domain]  Cd Length: 58  Bit Score: 36.91  E-value: 4.00e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1350 VALYDYDPRESSpnvdveaELTFCTGDIITVFGEIDED-GFYYGELNGQKGLVPSNFLEE 1408
Cdd:cd11977      4 VARYNFAARDMR-------ELSLREGDVVRIYSRIGGDqGWWKGETNGRIGWFPSTYVEE 56
SH3_DNMBP_N3 cd11796
Third N-terminal Src homology 3 domain of Dynamin Binding Protein, also called Tuba; DNMBP or ...
 1242-1281 4.02e-03

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: 36.95  E-value: 4.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054 1242 DEELPFKEGQIIKVYGDKDtDGFYRGATCARRGLIPCNMV 1281
Cdd:cd11796     13 DEELDLREGDVVTITGILD-KGWFRGELNGRRGIFPEGFV 51
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
 486-542 4.14e-03

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: 36.89  E-value: 4.14e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054  486 ARYSYNPfdgpnENPEaELPLTMGKYLYVYgDMDEDGFYEGELlDGQRGLVPSNFVE 542
Cdd:cd11772      4 ALYDYEA-----QHPD-ELSFEEGDLLYIS-DKSDPNWWKATC-GGKTGLIPSNYVE 52
ClpA COG0542
ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein ...
 254-351 4.45e-03

ATP-dependent Clp protease, ATP-binding subunit ClpA [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440308 [Multi-domain]  Cd Length: 836  Bit Score: 41.61  E-value: 4.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  254 DQVKSDYDQLRETISKVIKERDLALKGK-HQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKA 332
Cdd:COG0542    414 DELERRLEQLEIEKEALKKEQDEASFERlAELRDELAELEEELEALKARWEAEKELIEEIQELKEELEQRYGKIPELEKE 493

                           90
                   ....*....|....*....
gi 1835591054  333 QVEAKKEHEGAVQLLETKV 351
Cdd:COG0542    494 LAELEEELAELAPLLREEV 512
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
224-385 4.53e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 4.53e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  224 DLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMREAAE 303
Cdd:PRK03918   159 DYENAYKNLGEVIKEIKRRIERLEKFIKRTENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKE 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  304 RRQQLELEH---EQALAVLTAKQQEIEllqkAQVEAKKEHegaVQLLETKVQELEEkCRIQSEQFNLLSKELERFRQQTG 380
Cdd:PRK03918   239 EIEELEKELeslEGSKRKLEEKIRELE----ERIEELKKE---IEELEEKVKELKE-LKEKAEEYIKLSEFYEEYLDELR 310


                   ....*
gi 1835591054  381 KIDLL 385
Cdd:PRK03918   311 EIEKR 315
SH3_Intersectin1_5 cd11995
Fifth Src homology 3 domain (or SH3E) of Intersectin-1; Intersectin-1 (ITSN1) is an adaptor ...
 1242-1281 4.54e-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: 4.54e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 1835591054 1242 DEELPFKEGQIIKVYGDKDTDgFYRGATCARRGLIPCNMV 1281
Cdd:cd11995     14 DDELAFSKGQIINVLNKEDPD-WWKGELNGQVGLFPSNYV 52
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
117-371 4.62e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.04  E-value: 4.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  117 EIKLLQVECEELKNRLcclkeglmgqrpSDVEQLLKQSQKELLWLQRQLsfistggptcilpsSKLRNDLpylhpvlsQK 196
Cdd:COG4372     46 ELEQLREELEQAREEL------------EQLEEELEQARSELEQLEEEL--------------EELNEQL--------QA 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  197 TFDRIPFLEEKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKALQYDQVKSdydQLRETISKviKERDL 276
Cdd:COG4372     92 AQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELK---ELEEQLES--LQEEL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  277 ALKGKHQLQAKLENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLLETKVQELEE 356
Cdd:COG4372    167 AALEQELQALSEAEAEQALDELLKEANRNAEKEEELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEE 246

                          250
                   ....*....|....*
gi 1835591054  357 KCRIQSEQFNLLSKE 371
Cdd:COG4372    247 DKEELLEEVILKEIE 261
PRK12704 PRK12704
phosphodiesterase; Provisional
 281-378 4.69e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 41.30  E-value: 4.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  281 KHQLQAKLENLEQVLKHMREAAERrqqlELEHEQALAVLTAKQQEIELLQKAQVEaKKEHEGAVQLLETKVQELEEKCRI 360
Cdd:PRK12704    26 KKIAEAKIKEAEEEAKRILEEAKK----EAEAIKKEALLEAKEEIHKLRNEFEKE-LRERRNELQKLEKRLLQKEENLDR 100

                           90
                   ....*....|....*...
gi 1835591054  361 QSEQFNLLSKELERFRQQ 378
Cdd:PRK12704   101 KLELLEKREEELEKKEKE 118
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 274-376 4.70e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 38.75  E-value: 4.70e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  274 RDLALKGKHQLQAKLENLEQVLKHMREAAERRQQ--LELEH-----EQALAVLTAKQQEIE-LLQKAQVEAKKEHEGAVQ 345
Cdd:pfam20492    1 REEAEREKQELEERLKQYEEETKKAQEELEESEEtaEELEEerrqaEEEAERLEQKRQEAEeEKERLEESAEMEAEEKEQ 80

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1835591054  346 L------LETKVQELEEKCRIQSEQFNLLSKELERFR 376
Cdd:pfam20492   81 LeaelaeAQEEIARLEEEVERKEEEARRLQEELEEAR 117
SH3_Intersectin_5 cd11840
Fifth Src homology 3 domain (or SH3E) of Intersectin; Intersectins (ITSNs) are adaptor ...
 1224-1283 4.70e-03

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


Pssm-ID: 212774 [Multi-domain]  Cd Length: 53  Bit Score: 36.62  E-value: 4.70e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054 1224 VALFDYDPLTmspnpdaaDEELPFKEGQIIKVYgDKDTDGFYRGATCARRGLIPCNMVSE 1283
Cdd:cd11840      3 IALFPYTAQN--------EDELSFQKGDIINVL-SKDDPDWWRGELNGQTGLFPSNYVEP 53
PspA COG1842
Phage shock protein A [Transcription, Signal transduction mechanisms];
198-378 4.78e-03

Phage shock protein A [Transcription, Signal transduction mechanisms];


Pssm-ID: 441447 [Multi-domain]  Cd Length: 217  Bit Score: 40.19  E-value: 4.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  198 FDRIpfleekTQVFKSDVNQEKQQWKD----LEYELKDAvqEKTHLNLHYASLSQKALQyDQVKSDYDQLRETISK---- 269
Cdd:COG1842      3 FKRL------SDIIRANINALLDKAEDpekmLDQAIRDM--EEDLVEARQALAQVIANQ-KRLERQLEELEAEAEKweek 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  270 ----VIKERD----LALKGKHQLQAKLENLEQVLKHMREAAErrqQLELEHEQALAVLTAKQQEIELL------QKAQVE 335
Cdd:COG1842     74 arlaLEKGREdlarEALERKAELEAQAEALEAQLAQLEEQVE---KLKEALRQLESKLEELKAKKDTLkarakaAKAQEK 150

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1835591054  336 AKKEHEG--------AVQLLETKVQELEEKCRIQSE---------QFNLLSK------ELERFRQQ 378
Cdd:COG1842    151 VNEALSGidsddatsALERMEEKIEEMEARAEAAAElaagdslddELAELEAdsevedELAALKAK 216
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 244-377 4.88e-03

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: 40.90  E-value: 4.88e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  244 ASLSQKALQYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKhmrEAAERRQQLELEHEQALAVLTAKQ 323
Cdd:COG4942     13 LAAAAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIA---ALARRIRALEQELAALEAELAELE 89

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1835591054  324 QEIELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQFNLLSKELERFRQ 377
Cdd:COG4942     90 KEIAELRAELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKY 143
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 272-378 4.90e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 4.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  272 KERdlalkgKHQLQAKL----ENLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKAQVEAKKEHEGAVQLL 347
Cdd:COG1196    171 KER------KEEAERKLeateENLERLEDILGELERQLEPLERQAEKAERYRELKEELKELEAELLLLKLRELEAELEEL 244

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1835591054  348 ETKVQELEEKCRIQSEQFNLLSKELERFRQQ 378
Cdd:COG1196    245 EAELEELEAELEELEAELAELEAELEELRLE 275
fn3 pfam00041
Fibronectin type III domain;
610-691 4.98e-03

Fibronectin type III domain;


Pssm-ID: 394996 [Multi-domain]  Cd Length: 85  Bit Score: 37.39  E-value: 4.98e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  610 PYPRKITLIKQLAKSVIVGWEPPvvPPGWGNINSYNVLV------DKDIRLSVnFGSRTKALIEKLNLATcTYRISIQSV 683
Cdd:pfam00041    1 SAPSNLTVTDVTSTSLTVSWTPP--PDGNGPITGYEVEYrpknsgEPWNEITV-PGTTTSVTLTGLKPGT-EYEVRVQAV 76


                   ....*...
gi 1835591054  684 TNRGNSDE 691
Cdd:pfam00041   77 NGGGEGPP 84
MscS_porin pfam12795
Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part ...
 206-364 5.37e-03

Mechanosensitive ion channel porin domain; The small mechanosensitive channel, MscS, is a part of the turgor-driven solute efflux system that protects bacteria from lysis in the event of osmotic shock. The MscS protein alone is sufficient to form a functional mechanosensitive channel gated directly by tension in the lipid bilayer. The MscS proteins are heptamers of three transmembrane subunits with seven converging M3 domains, and this MscS_porin is towards the N-terminal of the molecules. The high concentration of negative charges at the extracellular entrance of the pore helps select the cations for efflux.


Pssm-ID: 432790 [Multi-domain]  Cd Length: 238  Bit Score: 40.36  E-value: 5.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  206 EKTQVFKSDVNQEKQQWKDLEYELKDAVQEKTHLNL--------HYASLSQKAL--QYDQVKSDYDQLRETI----SKVI 271
Cdd:pfam12795   30 DKIDASKQRAAAYQKALDDAPAELRELRQELAALQAkaeaapkeILASLSLEELeqRLLQTSAQLQELQNQLaqlnSQLI 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  272 KERDLALKGKHQL---QAKLENLEQVLKHMREAAER---RQQLELEHEQALAVLTAKQQEIEL--------LQKAQVEAK 337
Cdd:pfam12795  110 ELQTRPERAQQQLseaRQRLQQIRNRLNGPAPPGEPlseAQRWALQAELAALKAQIDMLEQELlsnnnrqdLLKARRDLL 189

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1835591054  338 KEHegaVQLLETKVQELEE----KCRIQSEQ 364
Cdd:pfam12795  190 TLR---IQRLEQQLQALQEllneKRLQEAEQ 217
SH3_SKAP1-like cd11866
Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This ...
 1369-1406 5.72e-03

Src Homology 3 domain of Src Kinase-Associated Phosphoprotein 1 and similar proteins; This subfamily is composed of SKAP1, SKAP2, and similar proteins. SKAP1 and SKAP2 are immune cell-specific adaptor proteins that play roles in T- and B-cell adhesion, respectively, and are thus important in the migration of T- and B-cells to sites of inflammation and for movement during T-cell conjugation with antigen-presenting cells. Both SKAP1 and SKAP2 bind to ADAP (adhesion and degranulation-promoting adaptor protein), among many other binding partners. They contain a pleckstrin homology (PH) domain, a C-terminal SH3 domain, and several tyrosine phosphorylation sites. The SH3 domain of SKAP1 is necessary for its ability to regulate T-cell conjugation with antigen-presenting cells and the formation of LFA-1 clusters. SKAP1 binds primarily to a proline-rich region of ADAP through its SH3 domain; its degradation is regulated by ADAP. A secondary interaction occurs via the ADAP SH3 domain and the RKxxYxxY motif in SKAP1. 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: 212800  Cd Length: 53  Bit Score: 36.26  E-value: 5.72e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1835591054 1369 ELTFCTGDIITVFG-EIDEDGFYYGELNGQKGLVPSNFL 1406
Cdd:cd11866     15 ELSFKRGDLIYIISkEYDSFGWWVGELNGKVGLVPKDYL 53
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
 1225-1281 5.97e-03

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: 36.47  E-value: 5.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1835591054 1225 ALFDYDPltmspnpdAADEELPFKEGQIIKVYGDKDtDGFYRGATCARRGLIPCNMV 1281
Cdd:cd11803      5 ALYDFEP--------ENEGELGFKEGDIITLTNQID-ENWYEGMVNGQSGFFPVNYV 52
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 220-374 6.06e-03

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: 41.26  E-value: 6.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  220 QQWKDLEYELKDAVQEKTHLNlhyaSLSQKALQYDQVKSDYDQLRETISKV--IKERDLALK-GKHQLQAKLENLEqvlK 296
Cdd:pfam05557  170 QRIKELEFEIQSQEQDSEIVK----NSKSELARIPELEKELERLREHNKHLneNIENKLLLKeEVEDLKRKLEREE---K 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  297 HMREAAErrQQLELEHEQA---------------LAVLTAKQQEIELLQ---KAQVEAKKEHEGAVQLLETKVQELEEKC 358
Cdd:pfam05557  243 YREEAAT--LELEKEKLEQelqswvklaqdtglnLRSPEDLSRRIEQLQqreIVLKEENSSLTSSARQLEKARRELEQEL 320

                          170
                   ....*....|....*.
gi 1835591054  359 RIQSEQFNLLSKELER 374
Cdd:pfam05557  321 AQYLKKIEDLNKKLKR 336
SH3_CD2AP_1 cd12053
First Src Homology 3 domain (SH3A) of CD2-associated protein; CD2AP, also called CMS (Cas ...
 501-545 6.29e-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: 6.29e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1835591054  501 EAELPLTMGKYLYVYGDMDEDGFYEGELlDGQRGLVPSNFVEFVQ 545
Cdd:cd12053     13 EDELTIRVGEIIRNVKKLEEEGWLEGEL-NGRRGMFPDNFVKEIK 56
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 290-372 6.39e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 38.71  E-value: 6.39e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  290 NLEQVLKHMREAAERRQQLELEHEQALAVLTAKQQEI----ELLQKAQVEAKKEHEGAVQLLETKVQELEEKCRIQSEQF 365
Cdd:pfam03938    6 DMQKILEESPEGKAAQAQLEKKFKKRQAELEAKQKELqklyEELQKDGALLEEEREEKEQELQKKEQELQQLQQKAQQEL 85


                   ....*..
gi 1835591054  366 NLLSKEL 372
Cdd:pfam03938   86 QKKQQEL 92
SH3_Abi1 cd11971
Src homology 3 domain of Abl Interactor 1; Abi1, also called e3B1, is a central regulator of ...
 1224-1284 6.95e-03

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: 36.54  E-value: 6.95e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1224 VALFDYDpltmspnpDAADEELPFKEGQIIKVYgDKDTDGFYRGATCARRGLIPCNMVSEI 1284
Cdd:cd11971      3 VAIYDYS--------KDKDDELSFMEGAIIYVI-KKNDDGWYEGVCNGVTGLFPGNYVESI 54
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Cell cycle control, cell ...
 216-348 7.10e-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: 41.09  E-value: 7.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  216 NQEKQQWKDLEYELKDAVQEKTHLNLHYASLSQKAL----QYDQVKSDYDQLRETISKVIKERDLALKGKHQLQAKLENL 291
Cdd:COG3096    546 GQQLDAAEELEELLAELEAQLEELEEQAAEAVEQRSelrqQLEQLRARIKELAARAPAWLAAQDALERLREQSGEALADS 625

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1835591054  292 EQVLKHMREAAERRQQLELEHEQALAVLTAKQQEIELLQKA------QVEAKKEHEGAVQLLE 348
Cdd:COG3096    626 QEVTAAMQQLLEREREATVERDELAARKQALESQIERLSQPggaedpRLLALAERLGGVLLSE 688
PRK12704 PRK12704
phosphodiesterase; Provisional
 258-378 7.32e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.92  E-value: 7.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1835591054  258 SDYDQLRETISKVIKERDLALKGKHQLQAKLENLEQVLKHMREAAERRQQLElEHEQALavltaKQQEIELLQKAQVEAK 337
Cdd:PRK12704    34 KEAEEEAKRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRERRNELQ-KLEKRL-----LQKEENLDRKLELLEK 107

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1835591054  338 KEHEgavqlLETKVQELEEKcriqSEQFNLLSKELERFRQQ 378
Cdd:PRK12704   108 REEE-----LEKKEKELEQK----QQELEKKEEELEELIEE 139
SH3_Abi2 cd11972
Src homology 3 domain of Abl Interactor 2; Abi2 is highly expressed in the brain and eye. It ...
 1224-1284 7.74e-03

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: 36.53  E-value: 7.74e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1835591054 1224 VALFDYdpltmspnPDAADEELPFKEGQIIKVYgDKDTDGFYRGATCARRGLIPCNMVSEI 1284
Cdd:cd11972      6 VAIYDY--------TKDKEDELSFQEGAIIYVI-KKNDDGWYEGVMNGVTGLFPGNYVESI 57
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
 705-769 9.50e-03

Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, fibronectin. The tenth fibronectin type III repeat contains a RGD cell recognition sequence in a flexible loop between 2 strands. Type III modules are present in both extracellular and intracellular proteins.


Pssm-ID: 214495 [Multi-domain]  Cd Length: 83  Bit Score: 36.82  E-value: 9.50e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1835591054   705 APSQLKVDNITQTSAGLSWLP--TNSNYSHVIFL--------NEEEFDIVKAAIYKYQFFNLKPNMAYKVKLLAK 769
Cdd:smart00060    3 PPSNLRVTDVTSTSVTLSWEPppDDGITGYIVGYrveyreegSEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRAV 77
 
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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