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Conserved domains on  [gi|157909774|ref|NP_766037|]
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Protein Classification

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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 ...
1620-1681 2.94e-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: 142.82  E-value: 2.94e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774 1620 VFVALFDYDPVSMSPNPDAGEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1681
Cdd:cd12012     1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1760-1819 4.81e-37

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


:

Pssm-ID: 212946  Cd Length: 61  Bit Score: 133.66  E-value: 4.81e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1760 MVAAFDYNPRENSPNMDVEAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLEG 1819
Cdd:cd12013     2 MVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
653-713 8.26e-37

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: 133.25  E-value: 8.26e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774  653 VFLARYSYNPFE-GPNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVER 713
Cdd:cd12014     1 VFVARYSYNPLRdSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER 62
Smc super family cl34174
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
158-501 6.11e-14

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 77.83  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  158 RRLKRKNAELAVIAKRLEERAQKLQETNMRVvsapvprpgSSLELCRKALaRQRARDLSETASALlakDKQIAALQRECR 237
Cdd:COG1196   667 RELKELEEELAELEAQLEKLEEELKSLKNEL---------RSLEDLLEEL-RRQLEELERQLEEL---KRELAALEEELE 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  238 ELQARLSLVGKEgpqwlhMRDFDRLLRESQREVLRLQRQIALRNQREplrparspgptapsrvgapapgapgeAVLQDDV 317
Cdd:COG1196   734 QLQSRLEELEEE------LEELEEELEELQERLEELEEELESLEEAL--------------------------AKLKEEI 781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  318 ESPQVVLREpeKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEEnsrLSGRATEKEQVEW 397
Cdd:COG1196   782 EELEEKRQA--LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEK---LDELEEELEELEK 856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  398 ENSELKGQLlgvtqerdsallksQGLQSKLESLEQVLK-----------HMREVAQRRQQLEVEHEQARLSLQEKQEEVR 466
Cdd:COG1196   857 ELEELKEEL--------------EELEAEKEELEDELKeleeekeeleeELRELESELAELKEEIEKLRERLEELEAKLE 922
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 157909774  467 RLQQ----AQAEAKREHE-GAVQLLESTLDSMQARVRELE 501
Cdd:COG1196   923 RLEVelpeLEEELEEEYEdTLETELEREIERLEEEIEALG 962
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
881-943 3.35e-05

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: 44.02  E-value: 3.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157909774  881 PSQLRIHRLTATSAEIAWVPGNSNLAHAI-YL---------NGEECPPARPSTYWATFCNLRPGTLYQARVEA 943
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVveyrekgsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
PHA03247 super family cl33720
large tegument protein UL36; Provisional
1339-1730 7.14e-04

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1339 PGPSRTSqdPSQPELALLGPGCDSSQPQGPGLCPLSPELSGVrehledvlgvVGGNGRRRGGGSPEKLPNRKRPQDPREH 1418
Cdd:PHA03247 2656 PAPGRVS--RPRRARRLGRAAQASSPPQRPRRRAARPTVGSL----------TSLADPPPPPPTPEPAPHALVSATPLPP 2723
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1419 CSRLLGNGGPQASARPVPPR--ERGSLPVIEGTRVG-QEPGGRGRPGLSRRCPRGPAPESS--LVSCLSPKCLEISIEYD 1493
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAvpAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTrpAVASLSESRESLPSPWD 2803
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1494 SEDEQEAGSGGVS-INSSCYPTDGEAWGTAAVgrPRGPPKVNPGPNAYLRLPAW-EKGEPERRgrsaigrtkEPPSRATE 1571
Cdd:PHA03247 2804 PADPPAAVLAPAAaLPPAASPAGPLPPPTSAQ--PTAPPPPPGPPPPSLPLGGSvAPGGDVRR---------RPPSRSPA 2872
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1572 TGESrgqdnSGRRGPQRRGARVPRSGTTE-LAPPRSPQEAPPHQDLPVRvfvalfdydpvsmsPNPDAGEEELPFKEGQL 1650
Cdd:PHA03247 2873 AKPA-----APARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPPP--------------PQPQPQPPPPPQPQPPP 2933
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1651 lkvfgdkdadgfyrgESGGRTGYIPCNMVAEVAVDSPAGRQQLLQRGFLPPNVLTEASGNGPSVYSSAHTPGPPPKPRRS 1730
Cdd:PHA03247 2934 ---------------PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
ATG16 super family cl25514
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
123-183 2.29e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


The actual alignment was detected with superfamily member pfam08614:

Pssm-ID: 400781 [Multi-domain]  Cd Length: 176  Bit Score: 40.68  E-value: 2.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774   123 ELLRALGELQQRCTILKEENQMLRKssfpETEEKVRRLKRKNAELAVIAKRLEERAQKLQE 183
Cdd:pfam08614   68 ELYRSRGELAQQLVDLNEELQELES----ELREDERRLAELEAERAQLEEKLRDREEELRE 124
 
Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1620-1681 2.94e-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: 142.82  E-value: 2.94e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774 1620 VFVALFDYDPVSMSPNPDAGEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1681
Cdd:cd12012     1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1760-1819 4.81e-37

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212946  Cd Length: 61  Bit Score: 133.66  E-value: 4.81e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1760 MVAAFDYNPRENSPNMDVEAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLEG 1819
Cdd:cd12013     2 MVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
653-713 8.26e-37

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: 133.25  E-value: 8.26e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774  653 VFLARYSYNPFE-GPNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVER 713
Cdd:cd12014     1 VFVARYSYNPLRdSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER 62
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
158-501 6.11e-14

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 77.83  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  158 RRLKRKNAELAVIAKRLEERAQKLQETNMRVvsapvprpgSSLELCRKALaRQRARDLSETASALlakDKQIAALQRECR 237
Cdd:COG1196   667 RELKELEEELAELEAQLEKLEEELKSLKNEL---------RSLEDLLEEL-RRQLEELERQLEEL---KRELAALEEELE 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  238 ELQARLSLVGKEgpqwlhMRDFDRLLRESQREVLRLQRQIALRNQREplrparspgptapsrvgapapgapgeAVLQDDV 317
Cdd:COG1196   734 QLQSRLEELEEE------LEELEEELEELQERLEELEEELESLEEAL--------------------------AKLKEEI 781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  318 ESPQVVLREpeKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEEnsrLSGRATEKEQVEW 397
Cdd:COG1196   782 EELEEKRQA--LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEK---LDELEEELEELEK 856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  398 ENSELKGQLlgvtqerdsallksQGLQSKLESLEQVLK-----------HMREVAQRRQQLEVEHEQARLSLQEKQEEVR 466
Cdd:COG1196   857 ELEELKEEL--------------EELEAEKEELEDELKeleeekeeleeELRELESELAELKEEIEKLRERLEELEAKLE 922
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 157909774  467 RLQQ----AQAEAKREHE-GAVQLLESTLDSMQARVRELE 501
Cdd:COG1196   923 RLEVelpeLEEELEEEYEdTLETELEREIERLEEEIEALG 962
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-531 1.28e-13

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: 76.63  E-value: 1.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   194 PRPGSSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLSLVGKEGPqwlhmrDFDRLLRESQREVLRL 273
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------ELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   274 QRQIALRNQREPLRPARSPGPTAPSRVGAPAPGAPGEAVLQDDVESPQVVLREPEKQQRVQQLESELCKKRKKCESLEQE 353
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   354 ARKKQRRCEELELQLRAAQNENARLVEENSRLSGRAT----EKEQVEWENSELKGQLLGVTQERDSALLKSQGLQSKLES 429
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   430 LEQVLkhmREVAQRRQQLevehEQARLSLQEKQEEVR-RLQQAQAEAKREHEGAVQLLESTLDSMQARVRELEGQCRSQT 508
Cdd:TIGR02168  899 LSEEL---RELESKRSEL----RRELEELREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
                          330       340
                   ....*....|....*....|...
gi 157909774   509 ERFSLLAQELQAFrlhpGPLDLL 531
Cdd:TIGR02168  972 RRLKRLENKIKEL----GPVNLA 990
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1760-1818 1.01e-11

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


Pssm-ID: 214620  Cd Length: 56  Bit Score: 61.40  E-value: 1.01e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   1760 MVAAFDYNPREnspnmdvEAELPFRAGDVITVFgNMDDDGFYYGELN-GQRGLVPSNFLE 1818
Cdd:smart00326    5 VRALYDYTAQD-------PDELSFKKGDIITVL-EKSDDGWWKGRLGrGKEGLFPSNYVE 56
SH3_9 pfam14604
Variant SH3 domain;
1762-1818 1.07e-11

Variant SH3 domain;


Pssm-ID: 405311 [Multi-domain]  Cd Length: 49  Bit Score: 61.07  E-value: 1.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774  1762 AAFDYNPREnspnmdvEAELPFRAGDVITVfGNMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:pfam14604    1 ALYPYEPRD-------DDELSLRRGDVITV-IEESEDGWWYGINTGRTGLVPANYVE 49
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
1620-1680 1.33e-10

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


Pssm-ID: 400139  Cd Length: 52  Bit Score: 58.24  E-value: 1.33e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774  1620 VFVALFDYDPvsmspnpdAGEEELPFKEGQLLKVFgDKDADGFYRGESGGRTGYIPCNMVA 1680
Cdd:pfam07653    1 YGRVIFDYVG--------TDKNGLSLKKGDVVKVL-SKDNDGWWEGETGGRVGLVPNTAVE 52
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
100-502 2.04e-10

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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 65.97  E-value: 2.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   100 LEEEEAQaykakfnigfgdRPNLELLRA-----LGELQQRCTILKEENQMLRK-------------SSFPETEEKVRRL- 160
Cdd:pfam01576  112 LEEEEAA------------RQKLQLEKVtteakIKKLEEDILLLEDQNSKLSKerklleeriseftSNLAEEEEKVKSLn 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   161 KRKNAELAVIAKrLEERAQKLQETNMRVVSAPVPRPGSSLELcRKALARQRARdLSETASALLAKDKQIAALQRECRELQ 240
Cdd:pfam01576  180 KLKNKHEAMISD-LEDRLKKEEKGRQELEKAKRKLDGESTDL-QEQIAELQAQ-IEELRAQLAKKEEELQAALARLEEEG 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   241 ARLSLVGKEgpqwlhmrdfdrlLRESQREVLRLQRQIalrnqrEPLRPARSPGPTAPSRVGAPAPGAPGEavLQD--DVE 318
Cdd:pfam01576  257 AQKNNALKK-------------LRELQAQIAELQEDL------ESERAARAKAEKQRRDLGEELEALKTE--LEDtlDST 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   319 SPQVVLREpEKQQRVQQLESELCKKRKKCESLEQEARKKQRRC-EELELQLRAA--------------QNENARLVEENS 383
Cdd:pfam01576  316 AAQQELRS-KREQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELSEQLEQAkrnkanlekakqalESENNELQAELK 394
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   384 RLSGRATEKEQ----VEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVL--------KHMREVAQ--------- 442
Cdd:pfam01576  395 TLQQAKQDSEHkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLseaegksiKLSKDVSSlesqlqdtq 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   443 ------RRQQLEVEH-----EQARLSLQEKQEE-----------VRRLQQAQAEAKREHE---GAVQLLESTLDSMQarv 497
Cdd:pfam01576  475 ellqeeTRQKLNLSSrlrqlEDERNSLQEQLEEeeeakrnverqLSTLQAQLSEMKKKLEedaGAVEALEEAKKRLQ--- 551

                   ....*
gi 157909774   498 RELEG 502
Cdd:pfam01576  552 RELEA 556
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
662-712 4.39e-10

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


Pssm-ID: 214620  Cd Length: 56  Bit Score: 56.78  E-value: 4.39e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 157909774    662 PFEGPNENpeaELPLTAGEYIYIYgNMDEDGFFEGELMDGRRGLVPSNFVE 712
Cdd:smart00326   10 DYTAQDPD---ELSFKKGDIITVL-EKSDDGWWKGRLGRGKEGLFPSNYVE 56
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1617-1680 5.81e-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  Cd Length: 56  Bit Score: 53.70  E-value: 5.81e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157909774   1617 PVRVFVALFDYDPVSmspnpdagEEELPFKEGQLLKVFGDKDaDGFYRGESG-GRTGYIPCNMVA 1680
Cdd:smart00326    1 EGPQVRALYDYTAQD--------PDELSFKKGDIITVLEKSD-DGWWKGRLGrGKEGLFPSNYVE 56
SH3_9 pfam14604
Variant SH3 domain;
656-712 1.33e-08

Variant SH3 domain;


Pssm-ID: 405311 [Multi-domain]  Cd Length: 49  Bit Score: 52.21  E-value: 1.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774   656 ARYSYNPFEgpnenpEAELPLTAGEYIYIyGNMDEDGFFEGELmDGRRGLVPSNFVE 712
Cdd:pfam14604    1 ALYPYEPRD------DDELSLRRGDVITV-IEESEDGWWYGIN-TGRTGLVPANYVE 49
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
146-520 2.32e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 59.28  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  146 RKSSFPETEEKVR---RLKRKNAE-LAVIAKRLEERAQKLQETnmrvvsapvprpgsslelcrkalARQRARDLSETASA 221
Cdd:PRK02224  322 RDEELRDRLEECRvaaQAHNEEAEsLREDADDLEERAEELREE-----------------------AAELESELEEAREA 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  222 LLAKDKQIAALQRECRELQARLSLVGKegpqwlhmrDFDRLlrESQREVLRLQRQiALRNQREPLRPARSpgpTAPSRVg 301
Cdd:PRK02224  379 VEDRREEIEELEEEIEELRERFGDAPV---------DLGNA--EDFLEELREERD-ELREREAELEATLR---TARERV- 442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  302 apapgAPGEAVL---------QDDVESPQVVLREpEKQQRVQQLESELCKKRKKCESLEQ------EARKKQRRCEELE- 365
Cdd:PRK02224  443 -----EEAEALLeagkcpecgQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEe 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  366 ----LQLRAAQNEnARLVEENSRLSGRATEKEQVEWENSE---------------------LKGQLLGVTQERDSaLLKS 420
Cdd:PRK02224  517 rredLEELIAERR-ETIEEKRERAEELRERAAELEAEAEEkreaaaeaeeeaeeareevaeLNSKLAELKERIES-LERI 594
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  421 QGLQSKLESLEQVLKHMREvaqRRQQLEVEHEQARLSLQEKQEEVR---------RLQQAQAEAKR------EHEGAVQL 485
Cdd:PRK02224  595 RTLLAAIADAEDEIERLRE---KREALAELNDERRERLAEKRERKReleaefdeaRIEEAREDKERaeeyleQVEEKLDE 671
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 157909774  486 LESTLDSMQARVreleGQCRSQTERFSLLAQELQA 520
Cdd:PRK02224  672 LREERDDLQAEI----GAVENELEELEELRERREA 702
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
330-518 4.58e-06

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: 49.37  E-value: 4.58e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  330 QQRVQQLESELCKKRKKCESLE-----QEARKKQRRCEELELQLRAAQ------NENA-RLVEENSRLSGRATEKEQV-- 395
Cdd:cd00176     6 LRDADELEAWLSEKEELLSSTDygddlESVEALLKKHEALEAELAAHEervealNELGeQLIEEGHPDAEEIQERLEEln 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  396 -EWEnselkgQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQRRQQLEV------------EHEQARLSLQEKQ 462
Cdd:cd00176    86 qRWE------ELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLgkdlesveellkKHKELEEELEAHE 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774  463 EEVRRLQQAQAE-AKREHEGAVQLLESTLDSMQARVRELEGQCRsqtERFSLLAQEL 518
Cdd:cd00176   160 PRLKSLNELAEElLEEGHPDADEEIEEKLEELNERWEELLELAE---ERQKKLEEAL 213
FN3 cd00063
Fibronectin type 3 domain; One of three types of internal repeats found in the plasma protein ...
881-943 3.35e-05

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: 44.02  E-value: 3.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157909774  881 PSQLRIHRLTATSAEIAWVPGNSNLAHAI-YL---------NGEECPPARPSTYWATFCNLRPGTLYQARVEA 943
Cdd:cd00063     4 PTNLRVTDVTSTSVTLSWTPPEDDGGPITgYVveyrekgsgDWKEVEVTPGSETSYTLTGLKPGTEYEFRVRA 76
PHA03247 PHA03247
large tegument protein UL36; Provisional
1339-1730 7.14e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.93  E-value: 7.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1339 PGPSRTSqdPSQPELALLGPGCDSSQPQGPGLCPLSPELSGVrehledvlgvVGGNGRRRGGGSPEKLPNRKRPQDPREH 1418
Cdd:PHA03247 2656 PAPGRVS--RPRRARRLGRAAQASSPPQRPRRRAARPTVGSL----------TSLADPPPPPPTPEPAPHALVSATPLPP 2723
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1419 CSRLLGNGGPQASARPVPPR--ERGSLPVIEGTRVG-QEPGGRGRPGLSRRCPRGPAPESS--LVSCLSPKCLEISIEYD 1493
Cdd:PHA03247 2724 GPAAARQASPALPAAPAPPAvpAGPATPGGPARPARpPTTAGPPAPAPPAAPAAGPPRRLTrpAVASLSESRESLPSPWD 2803
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1494 SEDEQEAGSGGVS-INSSCYPTDGEAWGTAAVgrPRGPPKVNPGPNAYLRLPAW-EKGEPERRgrsaigrtkEPPSRATE 1571
Cdd:PHA03247 2804 PADPPAAVLAPAAaLPPAASPAGPLPPPTSAQ--PTAPPPPPGPPPPSLPLGGSvAPGGDVRR---------RPPSRSPA 2872
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1572 TGESrgqdnSGRRGPQRRGARVPRSGTTE-LAPPRSPQEAPPHQDLPVRvfvalfdydpvsmsPNPDAGEEELPFKEGQL 1650
Cdd:PHA03247 2873 AKPA-----APARPPVRRLARPAVSRSTEsFALPPDQPERPPQPQAPPP--------------PQPQPQPPPPPQPQPPP 2933
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1651 lkvfgdkdadgfyrgESGGRTGYIPCNMVAEVAVDSPAGRQQLLQRGFLPPNVLTEASGNGPSVYSSAHTPGPPPKPRRS 1730
Cdd:PHA03247 2934 ---------------PPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPLTG 2998
FN3 smart00060
Fibronectin type 3 domain; One of three types of internal repeat within the plasma protein, ...
881-943 1.20e-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: 39.52  E-value: 1.20e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157909774    881 PSQLRIHRLTATSAEIAWVPGNSNLAHAIYLN----------GEECPPARPSTYWATFCNLRPGTLYQARVEA 943
Cdd:smart00060    4 PSNLRVTDVTSTSVTLSWEPPPDDGITGYIVGyrveyreegsEWKEVNVTPSSTSYTLTGLKPGTEYEFRVRA 76
ATG16 pfam08614
Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for ...
123-183 2.29e-03

Autophagy protein 16 (ATG16); Autophagy is a ubiquitous intracellular degradation system for eukaryotic cells. During autophagy, cytoplasmic components are enclosed in autophagosomes and delivered to lysosomes/vacuoles. ATG16 (also known as Apg16) has been shown to be bind to Apg5 and is required for the function of the Apg12p-Apg5p conjugate in the yeast autophagy pathway.


Pssm-ID: 400781 [Multi-domain]  Cd Length: 176  Bit Score: 40.68  E-value: 2.29e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774   123 ELLRALGELQQRCTILKEENQMLRKssfpETEEKVRRLKRKNAELAVIAKRLEERAQKLQE 183
Cdd:pfam08614   68 ELYRSRGELAQQLVDLNEELQELES----ELREDERRLAELEAERAQLEEKLRDREEELRE 124
fn3 pfam00041
Fibronectin type III domain;
881-944 4.14e-03

Fibronectin type III domain;


Pssm-ID: 394996  Cd Length: 85  Bit Score: 38.16  E-value: 4.14e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157909774   881 PSQLRIHRLTATSAEIAWVP---GNSNLAHaiY------LNGEECPP---ARPSTYWATFCNLRPGTLYQARVEAQ 944
Cdd:pfam00041    3 PSNLTVTDVTSTSLTVSWTPppdGNGPITG--YeveyrpKNSGEPWNeitVPGTTTSVTLTGLKPGTEYEVRVQAV 76
 
Name Accession Description Interval E-value
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1620-1681 2.94e-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: 142.82  E-value: 2.94e-40
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774 1620 VFVALFDYDPVSMSPNPDAGEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1681
Cdd:cd12012     1 LFVALFDYDPLTMSPNPDAAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVSE 62
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1760-1819 4.81e-37

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212946  Cd Length: 61  Bit Score: 133.66  E-value: 4.81e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1760 MVAAFDYNPRENSPNMDVEAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLEG 1819
Cdd:cd12013     2 MVALFDYDPRESSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
653-713 8.26e-37

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: 133.25  E-value: 8.26e-37
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774  653 VFLARYSYNPFE-GPNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVER 713
Cdd:cd12014     1 VFVARYSYNPLRdSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELLDGRRGLVPSNFVER 62
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
1760-1818 1.18e-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: 109.71  E-value: 1.18e-28
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1760 MVAAFDYNPRENSPNMDVEAELPFRAGDVITVFGNMDDDGFYYGELNG-QRGLVPSNFLE 1818
Cdd:cd11851     2 MVALYDYNPETMSPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGgRKGLVPSNFVQ 61
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
653-712 9.09e-26

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: 101.62  E-value: 9.09e-26
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774  653 VFLARYSYNPFEG-PNENPEAELPLTAGEYIYIYGNMDEDGFFEGELMDGRRGLVPSNFVE 712
Cdd:cd11851     1 LMVALYDYNPETMsPNDDPEEELSFHAGDVVRVYGPMDEDGFYYGELEGGRKGLVPSNFVQ 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1761-1818 5.54e-24

First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212947  Cd Length: 62  Bit Score: 96.65  E-value: 5.54e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157909774 1761 VAAFDYNPRENSPNMDVEAELPFRAGDVITVFGNMDDDGFYYGEL-NGQRGLVPSNFLE 1818
Cdd:cd12014     3 VARYSYNPLRDSPNENPEAELPLNAGDYVYVYGDMDEDGFYEGELlDGRRGLVPSNFVE 61
SH3_RIM-BP cd11851
Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding ...
1620-1681 1.64e-23

Src homology 3 domains of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212785  Cd Length: 62  Bit Score: 95.08  E-value: 1.64e-23
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157909774 1620 VFVALFDYDPVSMSPNPDaGEEELPFKEGQLLKVFGDKDADGFYRGE-SGGRTGYIPCNMVAE 1681
Cdd:cd11851     1 LMVALYDYNPETMSPNDD-PEEELSFHAGDVVRVYGPMDEDGFYYGElEGGRKGLVPSNFVQE 62
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1761-1818 5.04e-22

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: 90.81  E-value: 5.04e-22
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157909774 1761 VAAFDYNPRENSPNMD-VEAELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:cd12012     3 VALFDYDPLTMSPNPDaAEEELPFKEGQLIKVYGDKDADGFYLGEINGRRGLVPCNMVS 61
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
656-712 9.72e-21

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: 87.05  E-value: 9.72e-21
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157909774  656 ARYSYNPFE-GPNENPEAELPLTAGEYIYIYGNMDEDGFFEGELmDGRRGLVPSNFVE 712
Cdd:cd12013     4 ALFDYDPREsSPNVDAEVELSFRAGDIITVFGEMDEDGFYYGEL-NGQRGLVPSNFLE 60
SH3_RIM-BP_3 cd12013
Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1622-1681 1.48e-18

Third Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs binding proteins (RBPs, RIM-BPs) associate with calcium channels present in photoreceptors, neurons, and hair cells; they interact simultaneously with specific calcium channel subunits, and active zone proteins, RIM1 and RIM2. RIMs are part of the matrix at the presynaptic active zone and are associated with synaptic vesicles through their interaction with the small GTPase Rab3. RIM-BPs play a role in regulating synaptic transmission by serving as adaptors and linking calcium channels with the synaptic vesicle release machinery. RIM-BPs contain three SH3 domains and two to three fibronectin III repeats. Invertebrates contain one, while vertebrates contain at least two RIM-BPs, RIM-BP1 and RIM-BP2. RIM-BP1 is also called peripheral-type benzodiazapine receptor associated protein 1 (PRAX-1). Mammals contain a third protein, RIM-BP3. RIM-BP1 and RIM-BP2 are predominantly expressed in the brain where they display overlapping but distinct expression patterns, while RIM-BP3 is almost exclusively expressed in the testis and is essential in spermiogenesis. The SH3 domains of RIM-BPs bind to the PxxP motifs of RIM1, RIM2, and L-type (alpha1D) and N-type (alpha1B) calcium channel subunits. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212946  Cd Length: 61  Bit Score: 80.89  E-value: 1.48e-18
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1622 VALFDYDPVSMSPNPDAgEEELPFKEGQLLKVFGDKDADGFYRGESGGRTGYIPCNMVAE 1681
Cdd:cd12013     3 VALFDYDPRESSPNVDA-EVELSFRAGDIITVFGEMDEDGFYYGELNGQRGLVPSNFLEE 61
SH3_RIM-BP_2 cd12012
Second Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
653-712 4.80e-15

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: 71.17  E-value: 4.80e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774  653 VFLARYSYNPFE-GPNENP-EAELPLTAGEYIYIYGNMDEDGFFEGElMDGRRGLVPSNFVE 712
Cdd:cd12012     1 LFVALFDYDPLTmSPNPDAaEEELPFKEGQLIKVYGDKDADGFYLGE-INGRRGLVPCNMVS 61
SH3_RIM-BP_1 cd12014
First Src homology 3 domain of Rab3-interacting molecules (RIMs) binding proteins; RIMs ...
1620-1679 1.29e-14

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: 69.69  E-value: 1.29e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774 1620 VFVALFDYDPVSMSPNpDAGEEELPFKEGQLLKVFGDKDADGFYRGES-GGRTGYIPCNMV 1679
Cdd:cd12014     1 VFVARYSYNPLRDSPN-ENPEAELPLNAGDYVYVYGDMDEDGFYEGELlDGRRGLVPSNFV 60
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
158-501 6.11e-14

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 77.83  E-value: 6.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  158 RRLKRKNAELAVIAKRLEERAQKLQETNMRVvsapvprpgSSLELCRKALaRQRARDLSETASALlakDKQIAALQRECR 237
Cdd:COG1196   667 RELKELEEELAELEAQLEKLEEELKSLKNEL---------RSLEDLLEEL-RRQLEELERQLEEL---KRELAALEEELE 733
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  238 ELQARLSLVGKEgpqwlhMRDFDRLLRESQREVLRLQRQIALRNQREplrparspgptapsrvgapapgapgeAVLQDDV 317
Cdd:COG1196   734 QLQSRLEELEEE------LEELEEELEELQERLEELEEELESLEEAL--------------------------AKLKEEI 781
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  318 ESPQVVLREpeKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEEnsrLSGRATEKEQVEW 397
Cdd:COG1196   782 EELEEKRQA--LQEELEELEEELEEAERRLDALERELESLEQRRERLEQEIEELEEEIEELEEK---LDELEEELEELEK 856
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  398 ENSELKGQLlgvtqerdsallksQGLQSKLESLEQVLK-----------HMREVAQRRQQLEVEHEQARLSLQEKQEEVR 466
Cdd:COG1196   857 ELEELKEEL--------------EELEAEKEELEDELKeleeekeeleeELRELESELAELKEEIEKLRERLEELEAKLE 922
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 157909774  467 RLQQ----AQAEAKREHE-GAVQLLESTLDSMQARVRELE 501
Cdd:COG1196   923 RLEVelpeLEEELEEEYEdTLETELEREIERLEEEIEALG 962
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
194-531 1.28e-13

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: 76.63  E-value: 1.28e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   194 PRPGSSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLSLVGKEGPqwlhmrDFDRLLRESQREVLRL 273
Cdd:TIGR02168  665 SAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELE------ELSRQISALRKDLARL 738
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   274 QRQIALRNQREPLRPARSPGPTAPSRVGAPAPGAPGEAVLQDDVESPQVVLREPEKQQRVQQLESELCKKRKKCESLEQE 353
Cdd:TIGR02168  739 EAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE 818
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   354 ARKKQRRCEELELQLRAAQNENARLVEENSRLSGRAT----EKEQVEWENSELKGQLLGVTQERDSALLKSQGLQSKLES 429
Cdd:TIGR02168  819 AANLRERLESLERRIAATERRLEDLEEQIEELSEDIEslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEE 898
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   430 LEQVLkhmREVAQRRQQLevehEQARLSLQEKQEEVR-RLQQAQAEAKREHEGAVQLLESTLDSMQARVRELEGQCRSQT 508
Cdd:TIGR02168  899 LSEEL---RELESKRSEL----RRELEELREKLAQLElRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDEEEAR 971
                          330       340
                   ....*....|....*....|...
gi 157909774   509 ERFSLLAQELQAFrlhpGPLDLL 531
Cdd:TIGR02168  972 RRLKRLENKIKEL----GPVNLA 990
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
152-500 1.38e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 73.21  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  152 ETEEKVRRLKRKNAELAVIAKRLEERAQKLQetnmrvvsapvpRPGSSLELCRKALARQRARDLSETASALLAKDKQIAA 231
Cdd:COG1196   176 EAERKLERTEENLERLEDLLEELEKQLEKLE------------RQAEKAERYQELKAELRELELALLLAKLKELRKELEE 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  232 -------LQRECRELQARLSLVGKEGPQWLHMR-DFDRLLRESQREVLRLQRQIA-----LRNQREPLRPARSpgptaps 298
Cdd:COG1196   244 leeelsrLEEELEELQEELEEAEKEIEELKSELeELREELEELQEELLELKEEIEelegeISLLRERLEELEN------- 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  299 rvgapapgapGEAVLQDDVESPQVVLREPEKQ-QRVQQLESELCKKRKKCESLEQEARKKQRRC-EELELQLRAAQNENA 376
Cdd:COG1196   317 ----------ELEELEERLEELKEKIEALKEElEERETLLEELEQLLAELEEAKEELEEKLSALlEELEELFEALREELA 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  377 RLVEENSRLSGR----ATEKEQVEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKH----MREVAQRRQQLE 448
Cdd:COG1196   387 ELEAELAEIRNEleelKREIESLEERLERLSERLEDLKEELKELEAELEELQTELEELNEELEEleeqLEELRDRLKELE 466
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157909774  449 VEHEQARLSLQEKQEEVRRLQQ------AQAEAKREHEGAVQLLESTLDSMQARVREL 500
Cdd:COG1196   467 RELAELQEELQRLEKELSSLEArldrleAEQRASQGVRAVLEALESGLPGVYGPVAEL 524
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
204-522 2.35e-12

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: 72.41  E-value: 2.35e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   204 RKALAR-QRARDLSETASALLA-KDKQIAALQRE------CRELQARLslvgKEGPQWLHM---RDFDRLLRESQREVLR 272
Cdd:TIGR02169  173 EKALEElEEVEENIERLDLIIDeKRQQLERLRRErekaerYQALLKEK----REYEGYELLkekEALERQKEAIERQLAS 248
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   273 LQRQIAlrnQREPLRPARspgptapsrvgapapgapgeavlQDDVESPQVVLREPEKqqRVQQL-ESELCKKRKKCESLE 351
Cdd:TIGR02169  249 LEEELE---KLTEEISEL-----------------------EKRLEEIEQLLEELNK--KIKDLgEEEQLRVKEKIGELE 300
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   352 QEARKKQRRCEELELQLRAAQNENARLVEENSRLSGratEKEQVEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLE 431
Cdd:TIGR02169  301 AEIASLERSIAEKERELEDAEERLAKLEAEIDKLLA---EIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVD 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   432 QVLKHMR-EVAQRRQQLEV---EHEQARLSLQEKQEEVRRLQQAQAEAKREHEGAVQ---LLESTLDSMQARVRELEGQC 504
Cdd:TIGR02169  378 KEFAETRdELKDYREKLEKlkrEINELKRELDRLQEELQRLSEELADLNAAIAGIEAkinELEEEKEDKALEIKKQEWKL 457
                          330
                   ....*....|....*...
gi 157909774   505 RSQTERFSLLAQELQAFR 522
Cdd:TIGR02169  458 EQLAADLSKYEQELYDLK 475
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
62-499 3.56e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 71.67  E-value: 3.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   62 PEGAHSPGPVGNTDPEATETGLPKLGQQAESPGYSCSGLEEEEAQAYKAKFnigfgdrpnlELLRALGELQQRCTILKEE 141
Cdd:COG1196   648 PSGSITGGSRNKRSSLAQKRELKELEEELAELEAQLEKLEEELKSLKNELR----------SLEDLLEELRRQLEELERQ 717
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  142 NQMLRKssfpETEEKVRRLKRKNAELaviaKRLEERAQKLQEtnmrvvsapvprpgsSLELCRKALARQRaRDLSETASA 221
Cdd:COG1196   718 LEELKR----ELAALEEELEQLQSRL----EELEEELEELEE---------------ELEELQERLEELE-EELESLEEA 773
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  222 LLAKDKQIAALQRECRELQ-ARLSLVGKEGPQWLHMRDFDRLLRESQREVLRLQRQIA-LRNQREPLrparspgptapsr 299
Cdd:COG1196   774 LAKLKEEIEELEEKRQALQeELEELEEELEEAERRLDALERELESLEQRRERLEQEIEeLEEEIEEL------------- 840
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  300 vgapapgapgEAVLQDDVESPQVVlrepekQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLV 379
Cdd:COG1196   841 ----------EEKLDELEEELEEL------EKELEELKEELEELEAEKEELEDELKELEEEKEELEEELRELESELAELK 904
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  380 EENSRLSGRATEKEQVEWEnSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVaqrrqQLEVEHEqarlsLQ 459
Cdd:COG1196   905 EEIEKLRERLEELEAKLER-LEVELPELEEELEEEYEDTLETELEREIERLEEEIEALGPV-----NLRAIEE-----YE 973
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 157909774  460 EKQEEVRRLqqaqaEAKRE-HEGAVQLLESTLDSMQARVRE 499
Cdd:COG1196   974 EVEERYEEL-----KSQREdLEEAKEKLLEVIEELDKEKRE 1009
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
172-519 4.55e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 71.67  E-value: 4.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  172 KRLEERAQKLQETNMRVvsapvprpgSSLELCRKALARQRARdlsetasalLAKDKQIA----ALQRECRELQARLSLVg 247
Cdd:COG1196   172 ERKEEAERKLERTEENL---------ERLEDLLEELEKQLEK---------LERQAEKAeryqELKAELRELELALLLA- 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  248 kegpQWLHMRdfdRLLRESQREVLRLQRQIALRNQReplrparspgptapsrvgapapgapgeavlQDDVESPQVVLRE- 326
Cdd:COG1196   233 ----KLKELR---KELEELEEELSRLEEELEELQEE------------------------------LEEAEKEIEELKSe 275
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  327 -PEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSGRATEKEQVEWENSELKGQ 405
Cdd:COG1196   276 lEELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEELEQLLAE 355
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  406 LLGVTQERDSAL-LKSQGLQSKLESLEQ----VLKHMREVAQRRQQLEVEHEQARLSLQEKQEEVRRLQQAQAEAKREHE 480
Cdd:COG1196   356 LEEAKEELEEKLsALLEELEELFEALREelaeLEAELAEIRNELEELKREIESLEERLERLSERLEDLKEELKELEAELE 435
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 157909774  481 G----------AVQLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQ 519
Cdd:COG1196   436 ElqteleelneELEELEEQLEELRDRLKELERELAELQEELQRLEKELS 484
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
152-517 5.26e-12

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: 71.24  E-value: 5.26e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   152 ETEEKVRRLKRKnAELAVIAKRLEERAQKLQetnmrvvsapvprpgsslelcrKALARQRARDLSEtasALLAKDKQIAA 231
Cdd:TIGR02168  197 ELERQLKSLERQ-AEKAERYKELKAELRELE----------------------LALLVLRLEELRE---ELEELQEELKE 250
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   232 LQRECRELQARLSLVGKegpQWLHMRDFDRLLRES----QREVLRLQRQIA-LRNQREPLRPARSPGPTAPSRVgapapg 306
Cdd:TIGR02168  251 AEEELEELTAELQELEE---KLEELRLEVSELEEEieelQKELYALANEISrLEQQKQILRERLANLERQLEEL------ 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   307 apgEAVLQDDVESPQvvlrepEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEE----- 381
Cdd:TIGR02168  322 ---EAQLEELESKLD------ELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKvaqle 392
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   382 ------NSRLSGRATEKEQVEWENSELKGQLLGVTQERDSALLKSqgLQSKLESLEQVLKhmrevaqrrqQLEVEHEQAR 455
Cdd:TIGR02168  393 lqiaslNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAELKE--LQAELEELEEELE----------ELQEELERLE 460
                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774   456 LSLQEKQEEVRRLQQAQAEAKREHegavQLLESTLDSMQARVRELEGqcRSQTERFSLLAQE 517
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAEREL----AQLQARLDSLERLQENLEG--FSEGVKALLKNQS 516
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
169-520 5.77e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 71.28  E-value: 5.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  169 VIAKRLE--ERAQKLQETNMRVVSapvpRPGsslELCRKALARQRArdlSETASALLAKDKQIAALQRECRELQARLSLV 246
Cdd:COG1196   617 LVVDDLEqaRRLARKLRIKYRIVT----LDG---DLVEPSGSITGG---SRNKRSSLAQKRELKELEEELAELEAQLEKL 686
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  247 GKEgpqwlhmrdfdrlLRESQREVLRLQRQIA-LRNQREPLRparspgptapsrvgapapgapgeavlqddvespqvvLR 325
Cdd:COG1196   687 EEE-------------LKSLKNELRSLEDLLEeLRRQLEELE------------------------------------RQ 717
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  326 EPEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSgraTEKEQVEWENSELKGQ 405
Cdd:COG1196   718 LEELKRELAALEEELEQLQSRLEELEEELEELEEELEELQERLEELEEELESLEEALAKLK---EEIEELEEKRQALQEE 794
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  406 LLGVTQERDSALLKSQGLQSKLESLEQVL----KHMREVAQRRQQLEVEHEQARLSLQEKQEEVRRLQ---QAQAEAKRE 478
Cdd:COG1196   795 LEELEEELEEAERRLDALERELESLEQRRerleQEIEELEEEIEELEEKLDELEEELEELEKELEELKeelEELEAEKEE 874
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 157909774  479 HEGAVQLLESTLDSMQARVRELE---GQCRSQTERFSLLAQELQA 520
Cdd:COG1196   875 LEDELKELEEEKEELEEELRELEselAELKEEIEKLRERLEELEA 919
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
123-520 7.69e-12

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 70.90  E-value: 7.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  123 ELLRALGELQQRCTILKEENQML---RKSSFPETEEKVRRLKRKNAELAVIAKRLEERAQKLQETNMRVVSA-----PVP 194
Cdd:COG1196   401 ELKREIESLEERLERLSERLEDLkeeLKELEAELEELQTELEELNEELEELEEQLEELRDRLKELERELAELqeelqRLE 480
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  195 RPGSSLELcRKALARQRARDLSETASALLAKDK-------QIAALQRECRELQARLSLVGKEGPQWLHMRDfdrllRESQ 267
Cdd:COG1196   481 KELSSLEA-RLDRLEAEQRASQGVRAVLEALESglpgvygPVAELIKVKEKYETALEAALGNRLQAVVVEN-----EEVA 554
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  268 REVLRLQRQIALRnqREPLRPARSPGPTAPSRvGAPAPGAPG------------EAVLQ---------DDVESPQVVLRE 326
Cdd:COG1196   555 KKAIEFLKENKAG--RATFLPLDRIKPLRSLK-SDAAPGFLGlasdlidfdpkyEPAVRfvlgdtlvvDDLEQARRLARK 631
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  327 PEKQQRVQQLESELCKK--------RKKCESLEQEARKK--QRRCEELELQLRAAQNENARLVEENSRLSGRATEKEQve 396
Cdd:COG1196   632 LRIKYRIVTLDGDLVEPsgsitggsRNKRSSLAQKRELKelEEELAELEAQLEKLEEELKSLKNELRSLEDLLEELRR-- 709
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  397 wENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVL--------KHMREVAQRRQQLEvEHEQARLSLQEKQEEVRRL 468
Cdd:COG1196   710 -QLEELERQLEELKRELAALEEELEQLQSRLEELEEELeeleeeleELQERLEELEEELE-SLEEALAKLKEEIEELEEK 787
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|..
gi 157909774  469 QQAQAEAKREHEGAVQLLEstldsmqARVRELEGQCRSQTERFSLLAQELQA 520
Cdd:COG1196   788 RQALQEELEELEEELEEAE-------RRLDALERELESLEQRRERLEQEIEE 832
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
137-531 7.76e-12

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: 70.86  E-value: 7.76e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   137 ILKE-ENQM--LRKSSfpETEEKVRRLKR--KNAELAVIAKRLEERAQKLQETNMRVvsapvprpgSSLELCRKALARQr 211
Cdd:TIGR02168  194 ILNElERQLksLERQA--EKAERYKELKAelRELELALLVLRLEELREELEELQEEL---------KEAEEELEELTAE- 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   212 ardLSETASALLAKDKQIAALQRECRELQARLSLVGKEgpqwlhMRDFDRLLRESQREVLRLQRQIALRNQReplrpars 291
Cdd:TIGR02168  262 ---LQELEEKLEELRLEVSELEEEIEELQKELYALANE------ISRLEQQKQILRERLANLERQLEELEAQ-------- 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   292 pgptapsrvgapapgapgeavlQDDVESpqvvlREPEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAA 371
Cdd:TIGR02168  325 ----------------------LEELES-----KLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEEL 377
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   372 QNENARLVEEnsrlsgRATEKEQVEWENSELkgQLLGVTQERdsallksqgLQSKLESLEQVLKHMREVAQRRQQLEV-- 449
Cdd:TIGR02168  378 EEQLETLRSK------VAQLELQIASLNNEI--ERLEARLER---------LEDRRERLQQEIEELLKKLEEAELKELqa 440
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   450 ---EHEQARLSLQEKQEEVRRLQQAQAEAKREHEGAVQLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQAFRLHPG 526
Cdd:TIGR02168  441 eleELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLEGFSEGVKALLKNQSGLSG 520

                   ....*
gi 157909774   527 PLDLL 531
Cdd:TIGR02168  521 ILGVL 525
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1760-1818 1.01e-11

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


Pssm-ID: 214620  Cd Length: 56  Bit Score: 61.40  E-value: 1.01e-11
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   1760 MVAAFDYNPREnspnmdvEAELPFRAGDVITVFgNMDDDGFYYGELN-GQRGLVPSNFLE 1818
Cdd:smart00326    5 VRALYDYTAQD-------PDELSFKKGDIITVL-EKSDDGWWKGRLGrGKEGLFPSNYVE 56
SH3_9 pfam14604
Variant SH3 domain;
1762-1818 1.07e-11

Variant SH3 domain;


Pssm-ID: 405311 [Multi-domain]  Cd Length: 49  Bit Score: 61.07  E-value: 1.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774  1762 AAFDYNPREnspnmdvEAELPFRAGDVITVfGNMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:pfam14604    1 ALYPYEPRD-------DDELSLRRGDVITV-IEESEDGWWYGINTGRTGLVPANYVE 49
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
1759-1818 3.89e-11

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


Pssm-ID: 400139  Cd Length: 52  Bit Score: 59.78  E-value: 3.89e-11
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  1759 PMVAAFDYNPRENSPnmdveaeLPFRAGDVITVFGnMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:pfam07653    1 YGRVIFDYVGTDKNG-------LSLKKGDVVKVLS-KDNDGWWEGETGGRVGLVPNTAVE 52
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
100-487 3.95e-11

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 68.25  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  100 LEEEEAQAYKAKfnigfgdRPNLELLRALGELQQRC-TILKEENQMLRKSsFPETEEKVRRLKRKNAELAVIAKRLEERA 178
Cdd:COG0419   366 LEERLEELEKEL-------EKALERLKQLEEAIQELkEELAELSAALEEI-QEELEELEKELEELERELEELEEEIKKLE 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  179 QKLQETNMRVVSAPVPR-PGSSLELCRKALARQRARDLSETASA-------LLAKDKQIAALQRECRELQARLSLVGKEg 250
Cdd:COG0419   438 EQINQLESKELMIAELAgAGEKCPVCGQELPEEHEKELLELYELeleeleeELSREKEEAELREEIEELEKELRELEEE- 516
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  251 pqwlhmrdFDRLLRESQREVLRLQRQI-ALRNQREPLRPARspgptapsrvgapapgapGEAVLQD------DVESPQVV 323
Cdd:COG0419   517 --------LIELLELEEALKEELEEKLeKLENLLEELEELK------------------EKLQLQQlkeelrQLEDRLQE 570
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  324 LREPEKQQRVQQLESELCKKRKKCEsleQEARKKQRRCEELELQLR-------------AAQNENARLVEENSRLSGRAT 390
Cdd:COG0419   571 LKELLEELRLLRTRKEELEELRERL---KELKKKLKELEERLSQLEellqslelseaenELEEAEEELESELEKLNLQAE 647
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  391 EKEQVEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHEQaRLSLQEKQEEVRRLQQ 470
Cdd:COG0419   648 LEELLQAALEELEEKVEELEAEIRRELQRIENEEQLEEKLEELEQLEEELEQLREELEELLKK-LGEIEQLIEELESRKA 726
                         410
                  ....*....|....*..
gi 157909774  471 AQAEAKREHEGAVQLLE 487
Cdd:COG0419   727 ELEELKKELEKLEKALE 743
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
126-463 4.56e-11

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: 68.17  E-value: 4.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   126 RALGELQQRCTILKEENQMLrKSSFPETEEKVRRLKRKNAELAVIAKRLEERAQKLQETnmrvvsapvprpgssLELCRK 205
Cdd:TIGR02169  716 RKIGEIEKEIEQLEQEEEKL-KERLEELEEDLSSLEQEIENVKSELKELEARIEELEED---------------LHKLEE 779
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   206 ALARQRARDLSEtasallaKDKQIAALQRECRELQARLSLVGKEGPQWLHMRDFDRLLRESQREVLrLQRQIALRNQREP 285
Cdd:TIGR02169  780 ALNDLEARLSHS-------RIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQEL-QEQRIDLKEQIKS 851
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   286 LRPArspgptapsrvgapapgapgEAVLQDDVESPQVVLREpeKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELE 365
Cdd:TIGR02169  852 IEKE--------------------IENLNGKKEELEEELEE--LEAALRDLESRLGDLKKERDELEAQLRELERKIEELE 909
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   366 LQLRaaqnenarlvEENSRLSGRATEKEQVEWENSELkGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQRRQ 445
Cdd:TIGR02169  910 AQIE----------KKRKRLSELKAKLEALEEELSEI-EDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNMLAI 978
                          330
                   ....*....|....*....
gi 157909774   446 QlEVEHEQARL-SLQEKQE 463
Cdd:TIGR02169  979 Q-EYEEVLKRLdELKEKRA 996
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
96-524 6.89e-11

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


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 67.69  E-value: 6.89e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774    96 SCSGLEEEEAQAYKAKFNIGFGDRPNLELLRALGE--LQQRCTILKEEnqmlrkssfpETEEKVRRLKRKNAELAVIAKR 173
Cdd:TIGR00618  398 LCKELDILQREQATIDTRTSAFRDLQGQLAHAKKQqeLQQRYAELCAA----------AITCTAQCEKLEKIHLQESAQS 467
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   174 LEERAQKLQetNMRVVSAPVPRPGSsLELCRKALARQRARDLSETASALLAKDKQI---AALQRECRELQARLSLVGKEG 250
Cdd:TIGR00618  468 LKEREQQLQ--TKEQIHLQETRKKA-VVLARLLELQEEPCPLCGSCIHPNPARQDIdnpGPLTRRMQRGEQTYAQLETSE 544
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   251 PQWLHmrdfdrllresQREVLRLQRQIaLRNQREPLRPARSPGPTAPSRVGAPAPGapgeavLQDDVESPQVVLREPEKQ 330
Cdd:TIGR00618  545 EDVYH-----------QLTSERKQRAS-LKEQMQEIQQSFSILTQCDNRSKEDIPN------LQNITVRLQDLTEKLSEA 606
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   331 QRVQQLESELCKKRKKCESLEQEARKKQRRC-EELELQLRAAQNENARLVEENSRLSGRATEK------EQVEWENSELK 403
Cdd:TIGR00618  607 EDMLACEQHALLRKLQPEQDLQDVRLHLQQCsQELALKLTALHALQLTLTQERVREHALSIRVlpkellASRQLALQKMQ 686
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   404 GQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQ----RRQQLEVEHEQARLSLQEKQEEVRRLQQAQAEAKREH 479
Cdd:TIGR00618  687 SEKEQLTYWKEMLAQCQTLLRELETHIEEYDREFNEIENasssLGSDLAAREDALNQSLKELMHQARTVLKARTEAHFNN 766
                          410       420       430       440
                   ....*....|....*....|....*....|....*....|....*
gi 157909774   480 EGAVQLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQAFRLH 524
Cdd:TIGR00618  767 NEEVTAALQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQE 811
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
123-520 8.84e-11

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 67.09  E-value: 8.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  123 ELLRALGELQQRctilKEENQMLRKSSFPETEEKVRRLKRKNAELAVIAKRLEERAQKLQETNMRVVSAPVPRpgsslel 202
Cdd:COG0419   204 LLEALEEELKEL----KKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKIR------- 272
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  203 crKALARQRARDLSETASALlakdKQIAALQRECRELQARLSLVGKEGPQWLHMRDFDRLLREsqrEVLRLQRQI-ALRN 281
Cdd:COG0419   273 --EEELRELERLLEELEEKI----ERLEELEREIEELEEELEGLRALLEELEELLEKLKSLEE---RLEKLEEKLeKLES 343
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  282 QREPLRPARSPGPTAPSRVGAPAPG----------APGEAVLQDDVESPQVVLREPEKQQRVQQLESELCKKRKKCESLE 351
Cdd:COG0419   344 ELEELAEEKNELAKLLEERLKELEErleelekeleKALERLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELE 423
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  352 QEARKKQRRCEELELQLRAAQNENARLVEENSR----------LSGRATEK--EQVEWENSELKGQLLgVTQERDSALLK 419
Cdd:COG0419   424 RELEELEEEIKKLEEQINQLESKELMIAELAGAgekcpvcgqeLPEEHEKEllELYELELEELEEELS-REKEEAELREE 502
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  420 SQGLQSKLESLEQVLKH---------------MREVAQRRQQLEVEHEqaRLSLQEKQEEVRRLQQAQAEAKREHEGAVQ 484
Cdd:COG0419   503 IEELEKELRELEEELIElleleealkeeleekLEKLENLLEELEELKE--KLQLQQLKEELRQLEDRLQELKELLEELRL 580
                         410       420       430       440
                  ....*....|....*....|....*....|....*....|....*...
gi 157909774  485 LL------------ESTLDSMQARVRELEGQCRSQTERFSLLAQELQA 520
Cdd:COG0419   581 LRtrkeeleelrerLKELKKKLKELEERLSQLEELLQSLELSEAENEL 628
SH3_2 pfam07653
Variant SH3 domain; SH3 (Src homology 3) domains are often indicative of a protein involved in ...
1620-1680 1.33e-10

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


Pssm-ID: 400139  Cd Length: 52  Bit Score: 58.24  E-value: 1.33e-10
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774  1620 VFVALFDYDPvsmspnpdAGEEELPFKEGQLLKVFgDKDADGFYRGESGGRTGYIPCNMVA 1680
Cdd:pfam07653    1 YGRVIFDYVG--------TDKNGLSLKKGDVVKVL-SKDNDGWWEGETGGRVGLVPNTAVE 52
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1760-1816 1.56e-10

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


Pssm-ID: 212690  Cd Length: 51  Bit Score: 57.86  E-value: 1.56e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157909774 1760 MVAAFDYNPREnspnmdvEAELPFRAGDVITVFgNMDDDGFYYGELN-GQRGLVPSNF 1816
Cdd:cd00174     2 ARALYDYEAQD-------DDELSFKKGDIITVL-EKDDDGWWEGELNgGREGLFPANY 51
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
100-502 2.04e-10

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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 65.97  E-value: 2.04e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   100 LEEEEAQaykakfnigfgdRPNLELLRA-----LGELQQRCTILKEENQMLRK-------------SSFPETEEKVRRL- 160
Cdd:pfam01576  112 LEEEEAA------------RQKLQLEKVtteakIKKLEEDILLLEDQNSKLSKerklleeriseftSNLAEEEEKVKSLn 179
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   161 KRKNAELAVIAKrLEERAQKLQETNMRVVSAPVPRPGSSLELcRKALARQRARdLSETASALLAKDKQIAALQRECRELQ 240
Cdd:pfam01576  180 KLKNKHEAMISD-LEDRLKKEEKGRQELEKAKRKLDGESTDL-QEQIAELQAQ-IEELRAQLAKKEEELQAALARLEEEG 256
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   241 ARLSLVGKEgpqwlhmrdfdrlLRESQREVLRLQRQIalrnqrEPLRPARSPGPTAPSRVGAPAPGAPGEavLQD--DVE 318
Cdd:pfam01576  257 AQKNNALKK-------------LRELQAQIAELQEDL------ESERAARAKAEKQRRDLGEELEALKTE--LEDtlDST 315
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   319 SPQVVLREpEKQQRVQQLESELCKKRKKCESLEQEARKKQRRC-EELELQLRAA--------------QNENARLVEENS 383
Cdd:pfam01576  316 AAQQELRS-KREQEVTELKKALEEETRSHEAQLQEMRQKHTQAlEELSEQLEQAkrnkanlekakqalESENNELQAELK 394
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   384 RLSGRATEKEQ----VEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVL--------KHMREVAQ--------- 442
Cdd:pfam01576  395 TLQQAKQDSEHkrkkLEGQLQELQARLSESERQRAELAEKLSKLQSELESVSGLLseaegksiKLSKDVSSlesqlqdtq 474
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   443 ------RRQQLEVEH-----EQARLSLQEKQEE-----------VRRLQQAQAEAKREHE---GAVQLLESTLDSMQarv 497
Cdd:pfam01576  475 ellqeeTRQKLNLSSrlrqlEDERNSLQEQLEEeeeakrnverqLSTLQAQLSEMKKKLEedaGAVEALEEAKKRLQ--- 551

                   ....*
gi 157909774   498 RELEG 502
Cdd:pfam01576  552 RELEA 556
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
328-503 2.10e-10

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: 65.86  E-value: 2.10e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   328 EKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSGRATEKEQvewENSELKGQLL 407
Cdd:TIGR02169  706 ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEE---DLHKLEEALN 782
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   408 GVtqERDSALLKSQGLQSKLESLEQVLKH----MREVAQRRQQLEVEHEQARLSLQEKQEEVRRLQ-QAQAEAKREHEGA 482
Cdd:TIGR02169  783 DL--EARLSHSRIPEIQAELSKLEEEVSRiearLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKeQIKSIEKEIENLN 860
                          170       180
                   ....*....|....*....|...
gi 157909774   483 VQL--LESTLDSMQARVRELEGQ 503
Cdd:TIGR02169  861 GKKeeLEEELEELEAALRDLESR 883
SH3_OSTF1 cd11772
Src Homology 3 domain of metazoan osteoclast stimulating factor 1; OSTF1, also named OSF or ...
1620-1681 2.20e-10

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: 57.69  E-value: 2.20e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774 1620 VFVALFDYDPVsmspNPDageeELPFKEGQLLKVFgDKDADGFYRGESGGRTGYIPCNMVAE 1681
Cdd:cd11772     1 VFRALYDYEAQ----HPD----ELSFEEGDLLYIS-DKSDPNWWKATCGGKTGLIPSNYVEE 53
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
123-387 2.45e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.89  E-value: 2.45e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  123 ELLRALGELQQRCTILKEENQMLRKSS---FPETEEKVRRLKRKNAELAVIAKRLEERAQKLQETNMRVVSAPVPRPG-- 197
Cdd:COG1196   271 ELKSELEELREELEELQEELLELKEEIeelEGEISLLRERLEELENELEELEERLEELKEKIEALKEELEERETLLEEle 350
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  198 ---SSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLSLVGKEgpqwlhmrdfdrlLRESQREVLRLQ 274
Cdd:COG1196   351 qllAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNELEELKRE-------------IESLEERLERLS 417
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  275 RQIA-LRNQREPLRPARSPGPTAPsrvgapapgapgeAVLQDDVESPQVVLREpeKQQRVQQLESELCKKRKKCESLEQE 353
Cdd:COG1196   418 ERLEdLKEELKELEAELEELQTEL-------------EELNEELEELEEQLEE--LRDRLKELERELAELQEELQRLEKE 482
                         250       260       270
                  ....*....|....*....|....*....|....
gi 157909774  354 ARKKQRRCEELELQLRAAQNENARLVEENSRLSG 387
Cdd:COG1196   483 LSSLEARLDRLEAEQRASQGVRAVLEALESGLPG 516
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
265-520 3.27e-10

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 65.51  E-value: 3.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  265 ESQREVLRLQRQIALR--NQREPLRPARspgptapsrvgapapgapgEAVLQDDVEspqvvlrepEKQQRVQQLESELCK 342
Cdd:COG1196   199 EKQLEKLERQAEKAERyqELKAELRELE-------------------LALLLAKLK---------ELRKELEELEEELSR 250
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  343 KRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSgraTEKEQVEWENSELKGQLLGVTQERDSALLKSQG 422
Cdd:COG1196   251 LEEELEELQEELEEAEKEIEELKSELEELREELEELQEELLELK---EEIEELEGEISLLRERLEELENELEELEERLEE 327
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  423 LQSKLESLEQVLKHMREVAQRRQQLEVEHEQARLSLQEKQEEVRRLQQAQAEAKRE----HEGAVQLLESTLDSMQARVR 498
Cdd:COG1196   328 LKEKIEALKEELEERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREelaeLEAELAEIRNELEELKREIE 407
                         250       260
                  ....*....|....*....|..
gi 157909774  499 ELEGQCRSQTERFSLLAQELQA 520
Cdd:COG1196   408 SLEERLERLSERLEDLKEELKE 429
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
662-712 4.39e-10

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


Pssm-ID: 214620  Cd Length: 56  Bit Score: 56.78  E-value: 4.39e-10
                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|.
gi 157909774    662 PFEGPNENpeaELPLTAGEYIYIYgNMDEDGFFEGELMDGRRGLVPSNFVE 712
Cdd:smart00326   10 DYTAQDPD---ELSFKKGDIITVL-EKSDDGWWKGRLGRGKEGLFPSNYVE 56
Cast pfam10174
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ...
221-501 1.29e-09

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: 401982 [Multi-domain]  Cd Length: 765  Bit Score: 63.30  E-value: 1.29e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   221 ALLAKDKQIAALQRECRELqaRLSLVGKEgpqwlhmrdfdRLLRESQREVLRLQRQI-----ALRNQREPLRparspgpT 295
Cdd:pfam10174  331 SLTAKEQRAAILQTEVDAL--RLRLEEKE-----------SFLNKKTKQLQDLTEEKstlagEIRDLKDMLD-------V 390
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   296 APSRVGapapgapgeaVLQDDVESPQVVLREPEKQ-----QRVQQLESE--------------LCKKRKKCESL-EQEAR 355
Cdd:pfam10174  391 KERKIN----------VLQKKIENLQEQLRDKDKQlaglkERVKSLQTDssntdtalttleeaLSEKERIIERLkEQRER 460
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   356 KKQRRCEELElQLRaaqNENARLVEENSRLSGRATEKEQvewENSELKGQllgvTQERDSALLKSqglQSKLESLEQVLK 435
Cdd:pfam10174  461 EDRERLEELE-SLK---KENKDLKEKVSALQPELTEKES---SLIDLKEH----ASSLASSGLKK---DSKLKSLEIAIE 526
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774   436 HMREVAQRRQ-QLEVEHEQArLSLQEKQEEVRRLQQAQAEAKREHEGAVQlLESTLDSMQARVRELE 501
Cdd:pfam10174  527 QKKEECSKLEnQLKKAHNAE-EAVRTNPEINDRIRLLEQEVARYKEESGK-AQAEVERLLGILREVE 591
MukB COG3096
Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 ...
154-470 1.70e-09

Chromosome condensin MukBEF, ATPase and DNA-binding subunit MukB [Escherichia coli str. K-12 substr. MG1655 [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 225638 [Multi-domain]  Cd Length: 1480  Bit Score: 62.98  E-value: 1.70e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  154 EEKVRRLKrknAELAVIAKRLEERAQKLQETNMRVVSAPVPRPGSSLEL--CRKALAR-QRARDLSETASalLAKDKQIA 230
Cdd:COG3096   347 QEKIERYQ---ADLEELTIRLEEQNEVVEEANERQEENEARAEAAELEVdeLKSQLADyQQALDVQQTRA--IQYQQAIA 421
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  231 ALQReCRELQARLSLVGKEGPQWLhmRDFDRLLRESQREVLRLQRQIALRNQreplrpARSPGPTAPSRVGAPApgapGE 310
Cdd:COG3096   422 ALER-AKELCHLPDLTADSAEEWL--ETFQAKEEEATEKLLSLEQKMSMAQA------AHSQFEQAYQLVVAIA----GE 488
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  311 AVLQDDVESPQVVLRE-PEKQ---QRVQQLESEL------CKKRKKCESLEQEARKKQRRCEELElQLRAAQNENARLVE 380
Cdd:COG3096   489 LARSEAWDVARELLREgPDQRhlaEQVQPLRMRLseleqrLRQQQSAERLLADFCKRQGKNLDAE-ELEALHQELEALIE 567
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  381 ENS-RLSGRATEKEQVEWENSELKGQLLGVTQeRDSALLKSQGLQSKL--------ESLEQVLKHMREVAQRRQQLEVEH 451
Cdd:COG3096   568 SLSdSVSNAREQRMALRQEQEQLQSRIQSLMQ-RAPVWLAAQNALEQLseqsgeefTDSQDVTEYMQQLLEREREATVER 646
                         330
                  ....*....|....*....
gi 157909774  452 EQARLSLQEKQEEVRRLQQ 470
Cdd:COG3096   647 DELGARKNALDEEIERLSQ 665
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
102-522 2.05e-09

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 62.81  E-value: 2.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  102 EEEAQAYKAKFnigfgdrpnLELLRALGELQQRCTILKEENQMLRKSSFPETEEKVRRLKRKNAELAVIAKRLEERAQKL 181
Cdd:COG1196   329 KEKIEALKEEL---------EERETLLEELEQLLAELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRNEL 399
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  182 Q--ETNMRVVSAPVPRPGSSLELCRKALARQRArDLSETASALLAKDKQIAALQRECRELQARLSLVGKEgPQWLH--MR 257
Cdd:COG1196   400 EelKREIESLEERLERLSERLEDLKEELKELEA-ELEELQTELEELNEELEELEEQLEELRDRLKELERE-LAELQeeLQ 477
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  258 DFDRLLRESQREVLRLQ-RQIALRNQREPLRPARSPGPTAPSRVG-------------APAPGAPGEAVLQDDVESpQVV 323
Cdd:COG1196   478 RLEKELSSLEARLDRLEaEQRASQGVRAVLEALESGLPGVYGPVAelikvkekyetalEAALGNRLQAVVVENEEV-AKK 556
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  324 LREPEKQQR-------------------------VQQLESELCKKRKK--------------CESLEQeARkkqRRCEEL 364
Cdd:COG1196   557 AIEFLKENKagratflpldrikplrslksdaapgFLGLASDLIDFDPKyepavrfvlgdtlvVDDLEQ-AR---RLARKL 632
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  365 ELQLRAAQNENARLVEENSRLSGRATEKEQV--EWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQvlkHMREVAQ 442
Cdd:COG1196   633 RIKYRIVTLDGDLVEPSGSITGGSRNKRSSLaqKRELKELEEELAELEAQLEKLEEELKSLKNELRSLED---LLEELRR 709
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  443 RRQQLEVEHEQARLSLQEKQEEVRRLQQAQAEAKREHEgavqLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQAFR 522
Cdd:COG1196   710 QLEELERQLEELKRELAALEEELEQLQSRLEELEEELE----ELEEELEELQERLEELEEELESLEEALAKLKEEIEELE 785
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
321-521 3.90e-09

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 61.70  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  321 QVVLREPEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVE-ENSRLSGRATEKEQVEWEN 399
Cdd:COG0419   211 ELKELKKLEEIQEEQEEEELEQEIEALEERLAELEEEKERLEELKARLLEIESLELEALKiREEELRELERLLEELEEKI 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  400 SELKGQLLGVTQERdsalLKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHEQAR---LSLQEKQEEVRRLQQAQAEAK 476
Cdd:COG0419   291 ERLEELEREIEELE----EELEGLRALLEELEELLEKLKSLEERLEKLEEKLEKLEselEELAEEKNELAKLLEERLKEL 366
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 157909774  477 REHEGAVQLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQAF 521
Cdd:COG0419   367 EERLEELEKELEKALERLKQLEEAIQELKEELAELSAALEEIQEE 411
SH3 smart00326
Src homology 3 domains; Src homology 3 (SH3) domains bind to target proteins through sequences ...
1617-1680 5.81e-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  Cd Length: 56  Bit Score: 53.70  E-value: 5.81e-09
                            10        20        30        40        50        60
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157909774   1617 PVRVFVALFDYDPVSmspnpdagEEELPFKEGQLLKVFGDKDaDGFYRGESG-GRTGYIPCNMVA 1680
Cdd:smart00326    1 EGPQVRALYDYTAQD--------PDELSFKKGDIITVLEKSD-DGWWKGRLGrGKEGLFPSNYVE 56
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
314-522 6.50e-09

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 61.23  E-value: 6.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   314 QDDVESPQVVLREPEKQQRVQQLESELCKKRKKcesLEQEARKKQR-----RCEELELQLRAAQNENARLVEENSRLSGR 388
Cdd:TIGR02168  185 RENLDRLEDILNELERQLKSLERQAEKAERYKE---LKAELRELELallvlRLEELREELEELQEELKEAEEELEELTAE 261
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   389 ATEKEQvewENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMRE----VAQRRQQLEVEHEQARLSLQEKQEE 464
Cdd:TIGR02168  262 LQELEE---KLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRErlanLERQLEELEAQLEELESKLDELAEE 338
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774   465 VRRLQQAQAEAKREHEGAVQLLE---STLDSMQARVRELEGQCRSQTERFSLLAQELQAFR 522
Cdd:TIGR02168  339 LAELEEKLEELKEELESLEAELEeleAELEELESRLEELEEQLETLRSKVAQLELQIASLN 399
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
328-519 7.34e-09

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: 60.75  E-value: 7.34e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   328 EKQQRVQQLESELCKKRKKceslEQEARKKQRRCEELELQLRAAQNENARLVEENSRLSGR---------ATEKEQVEWE 398
Cdd:TIGR00618  233 EALQQTQQSHAYLTQKREA----QEEQLKKQQLLKQLRARIEELRAQEAVLEETQERINRArkaaplaahIKAVTQIEQQ 308
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   399 NSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHEQARLSLQEKQEE------VRRLQQaQ 472
Cdd:TIGR00618  309 AQRIHTELQSKMRSRAKLLMKRAAHVKQQSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQhtltqhIHTLQQ-Q 387
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 157909774   473 AEAKREHEGAVQLLESTLDSMQARVR--------------ELEGQCRSQTERFSLLAQELQ 519
Cdd:TIGR00618  388 KTTLTQKLQSLCKELDILQREQATIDtrtsafrdlqgqlaHAKKQQELQQRYAELCAAAIT 448
SH3_D21-like cd12142
Src Homology 3 domain of SH3 domain-containing protein 21 (SH3D21) and similar proteins; ...
1764-1818 1.31e-08

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  Cd Length: 55  Bit Score: 52.47  E-value: 1.31e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157909774 1764 FDYNPREnspnmdvEAELPFRAGDVITVFG-NMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:cd12142     6 FDYNPVA-------PDELALKKGDVIEVISkETEDEGWWEGELNGRRGFFPDNFVM 54
SH3_9 pfam14604
Variant SH3 domain;
656-712 1.33e-08

Variant SH3 domain;


Pssm-ID: 405311 [Multi-domain]  Cd Length: 49  Bit Score: 52.21  E-value: 1.33e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774   656 ARYSYNPFEgpnenpEAELPLTAGEYIYIyGNMDEDGFFEGELmDGRRGLVPSNFVE 712
Cdd:pfam14604    1 ALYPYEPRD------DDELSLRRGDVITV-IEESEDGWWYGIN-TGRTGLVPANYVE 49
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
1620-1677 1.34e-08

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


Pssm-ID: 212690  Cd Length: 51  Bit Score: 52.47  E-value: 1.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157909774 1620 VFVALFDYDPvsmspnpdAGEEELPFKEGQLLKVFgDKDADGFYRGES-GGRTGYIPCN 1677
Cdd:cd00174     1 YARALYDYEA--------QDDDELSFKKGDIITVL-EKDDDGWWEGELnGGREGLFPAN 50
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
123-468 1.48e-08

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 60.07  E-value: 1.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   123 ELLRALGELQQRCTILKEENQMLR------KSSFPETEEKVRRLKRKNAELAVIAKRLEERAQKLQETNMRVVSAPVPRP 196
Cdd:TIGR02168  243 ELQEELKEAEEELEELTAELQELEekleelRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELE 322
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   197 GSSLELcrkalarQRARDLSETASALLAkdKQIAALQRECRELQARLS-LVGKEGPQWLHMRDFDRLLRESQREVLRLQR 275
Cdd:TIGR02168  323 AQLEEL-------ESKLDELAEELAELE--EKLEELKEELESLEAELEeLEAELEELESRLEELEEQLETLRSKVAQLEL 393
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   276 QIA-LRNQREPLRPARSpgpTAPSRVgapapgapgeAVLQDDVESPQVVLREPEK---QQRVQQLESELCKKRKKCESLE 351
Cdd:TIGR02168  394 QIAsLNNEIERLEARLE---RLEDRR----------ERLQQEIEELLKKLEEAELkelQAELEELEEELEELQEELERLE 460
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   352 QEARKKQRRCEELELQLRAAQNENARLveeNSRLSGRATEKEQVE---------WENSELKGQLLGVTQErdsaLLKSqg 422
Cdd:TIGR02168  461 EALEELREELEEAEQALDAAERELAQL---QARLDSLERLQENLEgfsegvkalLKNQSGLSGILGVLSE----LISV-- 531
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*....
gi 157909774   423 lQSKLE-SLEQVLkhmrevAQRRQQLEVEHEQARLSLQE--KQEEVRRL 468
Cdd:TIGR02168  532 -DEGYEaAIEAAL------GGRLQAVVVENLNAAKKAIAflKQNELGRV 573
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
146-520 2.32e-08

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 59.28  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  146 RKSSFPETEEKVR---RLKRKNAE-LAVIAKRLEERAQKLQETnmrvvsapvprpgsslelcrkalARQRARDLSETASA 221
Cdd:PRK02224  322 RDEELRDRLEECRvaaQAHNEEAEsLREDADDLEERAEELREE-----------------------AAELESELEEAREA 378
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  222 LLAKDKQIAALQRECRELQARLSLVGKegpqwlhmrDFDRLlrESQREVLRLQRQiALRNQREPLRPARSpgpTAPSRVg 301
Cdd:PRK02224  379 VEDRREEIEELEEEIEELRERFGDAPV---------DLGNA--EDFLEELREERD-ELREREAELEATLR---TARERV- 442
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  302 apapgAPGEAVL---------QDDVESPQVVLREpEKQQRVQQLESELCKKRKKCESLEQ------EARKKQRRCEELE- 365
Cdd:PRK02224  443 -----EEAEALLeagkcpecgQPVEGSPHVETIE-EDRERVEELEAELEDLEEEVEEVEErleraeDLVEAEDRIERLEe 516
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  366 ----LQLRAAQNEnARLVEENSRLSGRATEKEQVEWENSE---------------------LKGQLLGVTQERDSaLLKS 420
Cdd:PRK02224  517 rredLEELIAERR-ETIEEKRERAEELRERAAELEAEAEEkreaaaeaeeeaeeareevaeLNSKLAELKERIES-LERI 594
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  421 QGLQSKLESLEQVLKHMREvaqRRQQLEVEHEQARLSLQEKQEEVR---------RLQQAQAEAKR------EHEGAVQL 485
Cdd:PRK02224  595 RTLLAAIADAEDEIERLRE---KREALAELNDERRERLAEKRERKReleaefdeaRIEEAREDKERaeeyleQVEEKLDE 671
                         410       420       430
                  ....*....|....*....|....*....|....*
gi 157909774  486 LESTLDSMQARVreleGQCRSQTERFSLLAQELQA 520
Cdd:PRK02224  672 LREERDDLQAEI----GAVENELEELEELRERREA 702
SH3_CD2AP-like_3 cd11875
Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This ...
1764-1818 2.71e-08

Third Src Homology 3 domain (SH3C) of CD2-associated protein and similar proteins; This subfamily is composed of the third SH3 domain (SH3C) of CD2AP, CIN85 (Cbl-interacting protein of 85 kDa), and similar domains. CD2AP and CIN85 are adaptor proteins that bind to protein partners and assemble complexes that have been implicated in T cell activation, kidney function, and apoptosis of neuronal cells. They also associate with endocytic proteins, actin cytoskeleton components, and other adaptor proteins involved in receptor tyrosine kinase (RTK) signaling. CD2AP and the main isoform of CIN85 contain three SH3 domains, a proline-rich region, and a C-terminal coiled-coil domain. All of these domains enable CD2AP and CIN85 to bind various protein partners and assemble complexes that have been implicated in many different functions. SH3C of both proteins have been shown to bind to ubiquitin. SH3 domains are protein interaction domains that bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212808  Cd Length: 55  Bit Score: 51.58  E-value: 2.71e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157909774 1764 FDYNPrENspnmdvEAELPFRAGDVITVFG-NMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:cd11875     6 FDYEA-EN------EDELTLREGDIVTILSkDCEDKGWWKGELNGKRGVFPDNFVE 54
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
332-522 2.73e-08

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 406229 [Multi-domain]  Cd Length: 384  Bit Score: 58.16  E-value: 2.73e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   332 RVQQLESELCKKRKKCESLEQEARKKQRRCEELELQ-LRAAQN--ENARLVEENSRLSGRATEKEQvewENSELKGQLLG 408
Cdd:pfam15742   63 ELKQAQQKLLDSTKMCSSLTAEWEHCQQKIRELELEvLKQAQSikSQNSLQEKLAQEKSKVAEAEK---KILELQQKLEH 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   409 VTQERdsaLLKSQGLQSKLesLEQVLKHMRE-VAQRRQQLEVEHEQARL---SLQEKQEEVRRLQQAQAEAKR---EHEG 481
Cdd:pfam15742  140 AHKVC---LTETCILEKKQ--LEEEIKEAQEnEAKLKQQYQEEQQKRKLldqNVNELQQQVRILQDKEAQLERtnsQQQL 214
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 157909774   482 AVQLLESTLDSMQARVRELEGQCRSQ---TERFSLLAQELQAFR 522
Cdd:pfam15742  215 RIQQQEAQLKQLENEKRKSDEHLKSNqelSEKLSSLQQEKEALQ 258
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
328-520 2.73e-08

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 58.96  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  328 EKQQRVQQLESELCKKRKKCESLEQEARKKQR------RCEELEL-----QLRAAQNENARLVEE-----------NSRL 385
Cdd:COG1196   183 RTEENLERLEDLLEELEKQLEKLERQAEKAERyqelkaELRELELalllaKLKELRKELEELEEElsrleeeleelQEEL 262
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  386 SGRATEKEQVEWENSELKGQLLGVTQERDSALLKSQGLQSKLESLEQVLKHMREvAQRRQQLEVEHEQARLSLQEKQEEV 465
Cdd:COG1196   263 EEAEKEIEELKSELEELREELEELQEELLELKEEIEELEGEISLLRERLEELEN-ELEELEERLEELKEKIEALKEELEE 341
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 157909774  466 RRLQQAQAEAKR-EHEGAVQLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQA 520
Cdd:COG1196   342 RETLLEELEQLLaELEEAKEELEEKLSALLEELEELFEALREELAELEAELAEIRN 397
SH3 cd00174
Src Homology 3 domain superfamily; Src Homology 3 (SH3) domains are protein interaction ...
656-710 3.23e-08

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


Pssm-ID: 212690  Cd Length: 51  Bit Score: 51.31  E-value: 3.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 157909774  656 ARYSYNPfegpneNPEAELPLTAGEYIYIYgNMDEDGFFEGELMDGRRGLVPSNF 710
Cdd:cd00174     4 ALYDYEA------QDDDELSFKKGDIITVL-EKDDDGWWEGELNGGREGLFPANY 51
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
118-522 3.26e-08

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: 368498 [Multi-domain]  Cd Length: 660  Bit Score: 58.60  E-value: 3.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   118 DRPNLELLRALGELQQRCTILKEENQML--RKSSFPETEEKVRRLKRKNAELA-VIAKRLEERAQKLQETNMRVVSApvp 194
Cdd:pfam05557   26 KRARIELEKKASALKRQLDRESDRNQELqkRIRLLEKREAEAEEALREQAELNrLKKKYLEALNKKLNEKESQLADA--- 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   195 rpgSSLELCRKALARQRARDLSETASALLAKDKQIAALQRECRELQARLSLVGKEGPQwLHMRDfdRLLRESQREVLRLQ 274
Cdd:pfam05557  103 ---REVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQN-LEKQQ--SSLAEAEQRIKELE 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   275 RQIALRNQreplrparspgptapsrvgapapgapGEAVLQDdveSPQVVLREPEKQQRVQQLESE---LCKKRKKCESLE 351
Cdd:pfam05557  177 FEIQSQEQ--------------------------DSEIVKN---SKSELARIPELEKELERLREHnkhLNENIENKLLLK 227
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   352 QEARKKQRRCEELElqlrAAQNENARLVEENSRLsgratEKEQVEWENSELKGQLLGVTQERDSALLKS--QG---LQSK 426
Cdd:pfam05557  228 EEVEDLKRKLEREE----KYREEAATLELEKEKL-----EQELQSWVKLAQDTGLNLRSPEDLSRRIEQlqQReivLKEE 298
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   427 LESLEQVLKHMREVaqrRQQLEVEHEQARLSLQEKQ-------EEVRRLQQAQAEAKREHEGAVQLLES----------- 488
Cdd:pfam05557  299 NSSLTSSARQLEKA---RRELEQELAQYLKKIEDLNkklkrhkALVRRLQRRVLLLTKERDGYRAILESydkeltmsnys 375
                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157909774   489 -------------------TLDSMQARVRELEGQCRSQTERFSLLAQELQAFR 522
Cdd:pfam05557  376 pqllerieeaedmtqkmqaHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR 428
SH3_Bzz1_2 cd11778
Second Src Homology 3 domain of Bzz1 and similar domains; Bzz1 (or Bzz1p) is a WASP ...
1760-1816 3.75e-08

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  Cd Length: 51  Bit Score: 51.34  E-value: 3.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774 1760 MVAAFDYNPRENSpnmdveaELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNF 1816
Cdd:cd11778     2 VEALYDYEAQGDD-------EISIRVGDRIAVIRGDDGSGWTYGEINGVKGLFPTSY 51
SbcC COG0419
DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];
324-522 5.48e-08

DNA repair exonuclease SbcCD ATPase subunit [Replication, recombination and repair];


Pssm-ID: 223496 [Multi-domain]  Cd Length: 908  Bit Score: 57.85  E-value: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  324 LREPEKQQRVQQLESE---LCKKRKKCESLEQEARKKQRRCEE-----------LELQLRAAQNENARLVEENSRLSGRA 389
Cdd:COG0419   218 LEEIQEEQEEEELEQEieaLEERLAELEEEKERLEELKARLLEieslelealkiREEELRELERLLEELEEKIERLEELE 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  390 TEKEqvewensELKGQLlgvtQERDSALLKSQGLQSKLESLEQVLKHMRE----VAQRRQQLEVEHEQARLSLQEKQEEV 465
Cdd:COG0419   298 REIE-------ELEEEL----EGLRALLEELEELLEKLKSLEERLEKLEEklekLESELEELAEEKNELAKLLEERLKEL 366
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157909774  466 R-RLQQAQAEA------KREHEGAVQLLESTLDSMQARVRELEGQCRSQTERFSLLAQELQAFR 522
Cdd:COG0419   367 EeRLEELEKELekalerLKQLEEAIQELKEELAELSAALEEIQEELEELEKELEELERELEELE 430
SH3_Nostrin cd11823
Src homology 3 domain of Nitric Oxide Synthase TRaffic INducer; Nostrin is expressed in ...
1761-1818 5.89e-08

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


Pssm-ID: 212757  Cd Length: 53  Bit Score: 50.80  E-value: 5.89e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 157909774 1761 VAAFDYNPRENSpnmdveaELPFRAGDVITVFgNMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:cd11823     3 KALYSYTANRED-------ELSLQPGDIIEVH-EKQDDGWWLGELNGKKGIFPATYVE 52
GOLGA2L5 pfam15070
Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...
261-499 7.11e-08

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes. Proteins in this family are typically between and 840 amino acids in length.


Pssm-ID: 405716 [Multi-domain]  Cd Length: 523  Bit Score: 57.38  E-value: 7.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   261 RLLRE----SQREVLRLQRQIA-LRNQREPLRPARSPGPTA-PSRVgapapgapgEAVLQDDVESPQVVLRE-------- 326
Cdd:pfam15070   39 RTLREekerSVSQVQELETSLAeLKNQAAVPPAEEEAQPPAgPSEE---------EQRLQEEAEQLQKELEAlagqlqaq 109
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   327 -----------PEKQQRVQQLESELckkrkKCESLEQEARKK-----------------QRRceELELQLRAAQNENARL 378
Cdd:pfam15070  110 vrdneqlsrlnQEQEQRLLELERAA-----ERWGEQAEDRKQiledmqsdratisralsQNR--ELKEQLAELQNGFVKL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   379 VEENSRLSGrATEKEQ-VEWENSELKGQLlgvtQERDSAL-----LKSQGLQSKLESLEQVLKHMREVAQRRQQLEVEHE 452
Cdd:pfam15070  183 TNENMELTS-ALQSEQhVKKELAKKLGQL----QEELGELketleLKSQEAQSLQEQRDQYLAHLQQYVAAYQQLASEKE 257
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 157909774   453 QARLSLQEKQEEVRRLQQAQAEAKREHEGAVQLLESTLDSMQARVRE 499
Cdd:pfam15070  258 ELHKQYLLQTQLMDRLQHEEVQGKVAAEMARQELQETQERLEAAAQQ 304
SH3_PACSIN cd11843
Src homology 3 domain of Protein kinase C and Casein kinase Substrate in Neurons (PACSIN) ...
1759-1818 8.03e-08

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  Cd Length: 53  Bit Score: 50.50  E-value: 8.03e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774 1759 PMVAAFDYNPRENSpnmdveaELPFRAGDVITVFGNMDDDGFYYGELNGQRGLVPSNFLE 1818
Cdd:cd11843     1 PVRALYDYEGQESD-------ELSFKAGDILTKLEEEDEQGWCKGRLDGRVGLYPANYVE 53
Myosin_tail_1 pfam01576
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ...
154-500 8.30e-08

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: 396244 [Multi-domain]  Cd Length: 1081  Bit Score: 57.49  E-value: 8.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   154 EEKVRRLKRKNAELAviAKRLEERAQKLQetnmrVVSAPVPRPGSSLELCRKALARQRARDlsETASALLAKDKQIAALQ 233
Cdd:pfam01576  741 EEKRRQLVKQVRELE--AELEDERKQRAQ-----AVAAKKKLELDLKELEAQIDAANKGRD--EAVKQLKKLQAQMKELQ 811
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   234 RECREL-QARLSLVGKEgpqwlhmRDFDRLLRESQREVLRLQRQIA----LRNQREPLRPARSPgptapsrvgAPAPGAP 308
Cdd:pfam01576  812 RELEETrASRDEILAQS-------KESEKKLKSLEAELLQLQEDLAaserAKRQAQQERDELAD---------EIANGAS 875
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   309 GEAVLQDdvespqvvlrepEKQQ---RVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRA-----AQNENAR--L 378
Cdd:pfam01576  876 GKSALLD------------EKRRleaRIAQLEEELEEEQSNTELLNDRYRKLTLQVEQLTTELSAersfsQKSESARqqL 943
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   379 VEENSRLSGRATEKEQ------------VEWENSELKGQLLGVTQERDSALLKSQGLQSKL-ESLEQVLKHMREVAQRRQ 445
Cdd:pfam01576  944 ERQNKELKAKLQEMEGtvkskykssiaaLEAKIAQLEEQLEQESRERQAANKLVRRTEKKLkEVLLQVEDERRNADQYKD 1023
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 157909774   446 QLEVEH---EQARLSLQEKQEEVRRLQQAQAEAKREhegavqlLESTLDSMQARVREL 500
Cdd:pfam01576 1024 QAEKANsrmKQLKRQLEEAEEEASRANAARRKLQRE-------LDDATESAESMNREV 1074
DUF5401 pfam17380
Family of unknown function (DUF5401); This is a family of unknown function found in ...
126-485 8.40e-08

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


Pssm-ID: 375164 [Multi-domain]  Cd Length: 722  Bit Score: 57.44  E-value: 8.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   126 RALGELQQRCTILKEENQMLRKssfpETEEKVRRLkrknaelaviakrleERAQKLQETnmrvvsapvprpgsslELCRK 205
Cdd:pfam17380  282 KAVSERQQQEKFEKMEQERLRQ----EKEEKAREV---------------ERRRKLEEA----------------EKARQ 326
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   206 ALARQRARDLSETASALLAKDKQIAALQRECRELQARLSLVGKEGPQWLHMRDFDRLLRESQREVLRLQRQIALRNQREP 285
Cdd:pfam17380  327 AEMDRQAAIYAEQERMAMERERELERIRQEERKRELERIRQEEIAMEISRMRELERLQMERQQKNERVRQELEAARKVKI 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   286 LRPARSPGPTAPSRVGAPAPGAPGEA------VLQDDV--ESPQVVLREPEKQQRVQQLESELCKKRKKCESLEQEARKK 357
Cdd:pfam17380  407 LEEERQRKIQQQKVEMEQIRAEQEEArqrevrRLEEERarEMERVRLEEQERQQQVERLRQQEEERKRKKLELEKEKRDR 486
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   358 QRRCEE----LELQLRAaqNENARLVEENSRlsgRATEKEQvewenselkgqllgvtQERDSALLKSQGlQSKLESLEQV 433
Cdd:pfam17380  487 KRAEEQrrkiLEKELEE--RKQAMIEEERKR---KLLEKEM----------------EERQKAIYEEER-RREAEEERRK 544
                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 157909774   434 LKHMREVAQRRQQL-EVEHEQARLSLQEKQEEVRRLQQAQAEAKREHEGAVQL 485
Cdd:pfam17380  545 QQEMEERRRIQEQMrKATEERSRLEAMEREREMMRQIVESEKARAEYEATTPI 597
DUF4686 pfam15742
Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins ...
209-501 1.18e-07

Domain of unknown function (DUF4686); This family of proteins is found in eukaryotes. Proteins in this family are typically between 498 and 775 amino acids in length. There is a conserved DLK sequence motif.


Pssm-ID: 406229 [Multi-domain]  Cd Length: 384  Bit Score: 56.23  E-value: 1.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   209 RQRARDLSETASALLAKDKQiaalqrecreLQARLSLVGK-EGPQWLHMRDFDRLLRESQREVLRLQRQI-ALRNQREPL 286
Cdd:pfam15742   47 KQHNSLLQEENIKIKAELKQ----------AQQKLLDSTKmCSSLTAEWEHCQQKIRELELEVLKQAQSIkSQNSLQEKL 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   287 RPARSpgptapsRVgapAPGAPGEAVLQDDVESPQVVLREPEKQQRVQQLESELCKKRKKCESL------EQEARKK-QR 359
Cdd:pfam15742  117 AQEKS-------KV---AEAEKKILELQQKLEHAHKVCLTETCILEKKQLEEEIKEAQENEAKLkqqyqeEQQKRKLlDQ 186
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   360 RCEELELQLRAAQNENARLVEENSRLSGRATEKE----QVEWE----------NSELKGQLLGVTQErdsallkSQGLQS 425
Cdd:pfam15742  187 NVNELQQQVRILQDKEAQLERTNSQQQLRIQQQEaqlkQLENEkrksdehlksNQELSEKLSSLQQE-------KEALQE 259
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   426 KL-ESLEQVLKHMR----------------------EVAQRRQQLE-VEHEQARLSLQEKQEEVRRLQ-QAQAEA----K 476
Cdd:pfam15742  260 ELqQFLKQLDVHVRkynekhhhhkaklrrakdrllhEVEQRDERIKqLENEIRILQSQIEKEKAFQDQvTAENETllleK 339
                          330       340       350
                   ....*....|....*....|....*....|..
gi 157909774   477 R-------EHEGAVQLLESTLDSMQARVRELE 501
Cdd:pfam15742  340 RklleqlsEQEEVIKNNKWTISSVQNRVLFLD 371
Smc COG1196
Chromosome segregation ATPase [Cell cycle control, cell division, chromosome partitioning];
332-520 1.24e-07

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


Pssm-ID: 224117 [Multi-domain]  Cd Length: 1163  Bit Score: 57.03  E-value: 1.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  332 RVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNEnARLVEENSRLsgratEKEQVEWENSELKGQLLGVTQ 411
Cdd:COG1196   173 RKEEAERKLERTEENLERLEDLLEELEKQLEKLERQAEKAERY-QELKAELREL-----ELALLLAKLKELRKELEELEE 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  412 ERDSALLKSQGLQSKLESLE---QVLKHMR-EVAQRRQQLEVEHEQARLSLQEKQEEVRRLQQAQAEAKREHEGAVQLLE 487
Cdd:COG1196   247 ELSRLEEELEELQEELEEAEkeiEELKSELeELREELEELQEELLELKEEIEELEGEISLLRERLEELENELEELEERLE 326
                         170       180       190
                  ....*....|....*....|....*....|...
gi 157909774  488 STLDSMQARVRELEGQCRSQTERFSLLAQELQA 520
Cdd:COG1196   327 ELKEKIEALKEELEERETLLEELEQLLAELEEA 359
SH3_Endophilin_A cd11803
Src homology 3 domain of Endophilin-A; Endophilins play roles in synaptic vesicle formation, ...
1762-1818 1.43e-07

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  Cd Length: 55  Bit Score: 49.57  E-value: 1.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774 1762 AAFDYNPrENspnmdvEAELPFRAGDVITVFGNMDDDgFYYGELNGQRGLVPSNFLE 1818
Cdd:cd11803     5 ALYDFEP-EN------EGELGFKEGDIITLTNQIDEN-WYEGMVNGQSGFFPVNYVE 53
SH3_GRB2_like_C cd11805
C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
1762-1818 1.48e-07

C-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related proteins; This family includes the adaptor protein GRB2 and related proteins including Drosophila melanogaster Downstream of receptor kinase (DRK), Caenorhabditis elegans Sex muscle abnormal protein 5 (Sem-5), GRB2-related adaptor protein (GRAP), GRAP2, and similar proteins. Family members contain an N-terminal SH3 domain, a central SH2 domain, and a C-terminal SH3 domain. GRB2/Sem-5/DRK is a critical signaling molecule that regulates the Ras pathway by linking tyrosine kinases to the Ras guanine nucleotide releasing protein Sos (son of sevenless), which converts Ras to the active GTP-bound state. GRAP2 plays an important role in T cell receptor (TCR) signaling by promoting the formation of the SLP-76:LAT complex, which couples the TCR to the Ras pathway. GRAP acts as a negative regulator of T cell receptor (TCR)-induced lymphocyte proliferation by downregulating the signaling to the Ras/ERK pathway. The C-terminal SH3 domains (SH3c) of GRB2 and GRAP2 have been shown to bind to classical PxxP motif ligands, as well as to non-classical motifs. GRB2 SH3c binds Gab2 (Grb2-associated binder 2) through epitopes containing RxxK motifs, while the SH3c of GRAP2 binds to the phosphatase-like protein HD-PTP via a RxxxxK motif. SH3 domains are protein interaction domains that typically bind to proline-rich ligands with moderate affinity and selectivity, preferentially to PxxP motifs. They play versatile and diverse roles in the cell including the regulation of enzymes, changing the subcellular localization of signaling pathway components, and mediating the formation of multiprotein complex assemblies.


Pssm-ID: 212739  Cd Length: 53  Bit Score: 49.55  E-value: 1.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 157909774 1762 AAFDYNPRENSpnmdveaELPFRAGDVITVFGNMDDDgFYYGELNGQRGLVPSNFLE 1818
Cdd:cd11805     4 ALYDFNPQEPG-------ELEFRRGDIITVLDSSDPD-WWKGELRGRVGIFPANYVQ 52
rad50 TIGR00606
rad50; All proteins in this family for which functions are known are involvedin recombination, ...
326-518 1.65e-07

rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).


Pssm-ID: 129694 [Multi-domain]  Cd Length: 1311  Bit Score: 56.59  E-value: 1.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   326 EPEKQQRVQQLESELCKKRKKCESLEQEARKKQRRCEELELQLRAAQNENARLVEE----NSRLSGRATEKEQVEWENSE 401
Cdd:TIGR00606  690 EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRRDEMLGLAPGRQSIIDLKEKEipelRNKLQKVNRDIQRLKNDIEE 769
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774   402 LKGQLLGVTQERDSAllksQGLQSKLESLEQVLKHMREVAQRRQQLEVE---------HEQARLSLQEKQEEVRRLQQAQ 472
Cdd:TIGR00606  770 QETLLGTIMPEEESA----KVCLTDVTIMERFQMELKDVERKIAQQAAKlqgsdldrtVQQVNQEKQEKQHELDTVVSKI 845
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 157909774   473 AEAKR---EHEGAVQLLESTLDSMQARVREL------EGQCRSQTERFSLLAQEL 518
Cdd:TIGR00606  846 ELNRKliqDQQEQIQHLKSKTNELKSEKLQIgtnlqrRQQFEEQLVELSTEVQSL 900
PRK02224 PRK02224
DNA double-strand break repair Rad50 ATPase;
155-520 1.72e-07

DNA double-strand break repair Rad50 ATPase;


Pssm-ID: 179385 [Multi-domain]  Cd Length: 880  Bit Score: 56.20  E-value: 1.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  155 EKVRRLKRKNAELAVIAKRLEERAQKLQETnmrvvsapvpRPGSSLELCRKALARQRARDLSETASALLAK----DKQIA 230
Cdd:PRK02224  206 ERLNGLESELAELDEEIERYEEQREQARET----------RDEADEVLEEHEERREELETLEAEIEDLRETiaetERERE 275
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  231 ALQRECRELQARLSLVGKEGPQWLHMRDFDRLLRESQrevlrLQRQIALRNQREPLRPARSPGPTAPSRVGAPAPGAPGE 310
Cdd:PRK02224  276 ELAEEVRDLRERLEELEEERDDLLAEAGLDDADAEAV-----EARREELEDRDEELRDRLEECRVAAQAHNEEAESLRED 350
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  311 AvlqDDVESpqvvlREPEKQQRVQQLESELckkrkkcESLEQEARKKQRRCEELELQLRAAQnenARLVEENSRLSGRAT 390
Cdd:PRK02224  351 A---DDLEE-----RAEELREEAAELESEL-------EEAREAVEDRREEIEELEEEIEELR---ERFGDAPVDLGNAED 412
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157909774  391 EKEQVEWENSELKGQLLGVT---QERDSALLKSQGLQS--KLESLEQVLK---HMREVAQRRQQLEvEHEQARLSLQEKQ 462
Cdd:PRK02224  413 FLEELREERDELREREAELEatlRTARERVEEAEALLEagKCPECGQPVEgspHVETIEEDRERVE-ELEAELEDLEEEV 491
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 157909774  463 EEV-RRLqqAQAEAKREHEGAVQLLESTLDSMQARVRELEGQCRSQTERFSLL---AQELQA 520
Cdd:PRK02224  492 EEVeERL--ERAEDLVEAEDRIERLEERREDLEELIAERRETIEEKRERAEELrerAAELEA 551
SH3_GRB2_like_N cd11804
N-terminal Src homology 3 domain of Growth factor receptor-bound protein 2 (GRB2) and related ...
1622-1679 2.03e-07

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