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Conserved domains on  [gi|67944634|ref|NP_001020095|]
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exocyst complex component 1 isoform 1 [Homo sapiens]

Protein Classification

PH-EXOC1 and Sec3_C domain-containing protein( domain architecture ID 10199843)

PH-EXOC1 and Sec3_C domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Sec3_C pfam09763
Exocyst complex component Sec3; This entry is the conserved middle and C-terminus of the Sec3 ...
184-871 0e+00

Exocyst complex component Sec3; This entry is the conserved middle and C-terminus of the Sec3 protein. Sec3 binds to the C-terminal cytoplasmic domain of GLYT1 (glycine transporter protein 1). Sec3 is the exocyst component that is closest to the plasma membrane docking site and it serves as a spatial landmark in the plasma membrane for incoming secretory vesicles. Sec3 is recruited to the sites of polarised membrane growth through its interaction with Rho1p, a small GTP-binding protein.


:

Pssm-ID: 401638  Cd Length: 696  Bit Score: 602.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   184 NAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEEMLQSVKEQMDQISESNHLIHLSN 263
Cdd:pfam09763   2 DADVLEERLSRELSKLEYANIKSLLESDKRVNELMKHIDKALKECDELDPTLTLYSMELSTLSDDIEYIESQNNGLQVQS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   264 TNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNV------ALRPGHDLLLAVKQQQQRFS 337
Cdd:pfam09763  82 ANQKLLYKELESLLNTVSLPESDLHALLEGPLSSPNGLEALEAALVALFKALNAidgdkkDLDSDLGDMRALKERRARYE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   338 DLRELFARRLASHLNNVF----VQQGHDQSStlaQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDYGKYEGLTKNYMDY 413
Cdd:pfam09763 162 KVTSLFLKRLVDFLNNRFknafKSLGSDLDS---ATSNELSLPNHLNVLNNLLIYSGLMLFLKEVDPETYEALLQLYNAS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   414 LSRLYEREIKDFFEVAKIKMtgttkeskkfatlprKESAVKQETESLHgSSGKLTGSTSslnKLSVQSSGNRRSQSSSLL 493
Cdd:pfam09763 239 ASKIYEREFKDFFEYLKKQL---------------KKSSGSEESESLF-SSGQDELYTE---WLALRKSRKLTLDSSKTG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   494 DMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQhqsmpGTMAEAEDLDG-GTLSRQHNCGTPL-- 570
Cdd:pfam09763 300 ANLSTKAPQSKLSGRLRPDEAFAGALDELEPLILVEQNFIIDFFHLSS-----LTLDFNEFVKQsPPSERRAPDLVPSkg 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   571 --PVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHV-WTAQnvDPASFLSTTLGNVLVTVKRNF 647
Cdd:pfam09763 375 vePDRELARDVRQMMSKIFQFLEPELQNLVDKVLKNDPLNALGILVYLEQYIkELEE--TNQSFLSSILQKLLEKVKQLW 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   648 DKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGD----LDKAYTKLIRGVFVNVEKVA------ 717
Cdd:pfam09763 453 DKFVDEQIRSIEETKVSKKSRKGVLPFVRNFPIFVKRVEDMLSSTERQLDvrtlVDQAYEKLTEAVFELLKRIArllpgk 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   718 ----NESQKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQgI 793
Cdd:pfam09763 533 adgpEDKEKLNRHVLLIENMNHFLEELSVLNNPVLEDLRDEAKQIFDEHLELYVQAVLRRPLGKLIEFVEGVEALLQT-V 611
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   794 REEEVSYQLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHL-------CEEENLLQVVWHSMQDEFIRQYKHFEGLIA 866
Cdd:pfam09763 612 PAAEISRQAAYSKQALKKLLSSYTAKEVRKGIEKLYKRVEKHFlgdaddpGLEESLLQKVWSDMQGEFISQYLRLESIIQ 691

                  ....*
gi 67944634   867 RCYPG 871
Cdd:pfam09763 692 KCYPG 696
PH-EXOC1 cd14683
PH-like domain of Exocyst complex component 1; Exocyst complex component 1 (EXOC1, also known ...
3-120 1.48e-61

PH-like domain of Exocyst complex component 1; Exocyst complex component 1 (EXOC1, also known as SEC3) is the higher eukaryotes homolog of yeast Sec3. The Exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


:

Pssm-ID: 270202  Cd Length: 117  Bit Score: 203.64  E-value: 1.48e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   3 AIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGdFYKRQIAWALRDLAVVDAKD 82
Cdd:cd14683   1 AIRHALQREVFTPNDERLLAVVNVSKAGKKKKTSFLCVAVTTERPVQVRLYQVKKSDKG-VYKKKRSWLLRDLKTVDGKN 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67944634  83 AIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQ 120
Cdd:cd14683  80 PKKETPEFDLHFDKVYKWVASNVQEKNAFISCLWKLCH 117
 
Name Accession Description Interval E-value
Sec3_C pfam09763
Exocyst complex component Sec3; This entry is the conserved middle and C-terminus of the Sec3 ...
184-871 0e+00

Exocyst complex component Sec3; This entry is the conserved middle and C-terminus of the Sec3 protein. Sec3 binds to the C-terminal cytoplasmic domain of GLYT1 (glycine transporter protein 1). Sec3 is the exocyst component that is closest to the plasma membrane docking site and it serves as a spatial landmark in the plasma membrane for incoming secretory vesicles. Sec3 is recruited to the sites of polarised membrane growth through its interaction with Rho1p, a small GTP-binding protein.


Pssm-ID: 401638  Cd Length: 696  Bit Score: 602.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   184 NAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEEMLQSVKEQMDQISESNHLIHLSN 263
Cdd:pfam09763   2 DADVLEERLSRELSKLEYANIKSLLESDKRVNELMKHIDKALKECDELDPTLTLYSMELSTLSDDIEYIESQNNGLQVQS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   264 TNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNV------ALRPGHDLLLAVKQQQQRFS 337
Cdd:pfam09763  82 ANQKLLYKELESLLNTVSLPESDLHALLEGPLSSPNGLEALEAALVALFKALNAidgdkkDLDSDLGDMRALKERRARYE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   338 DLRELFARRLASHLNNVF----VQQGHDQSStlaQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDYGKYEGLTKNYMDY 413
Cdd:pfam09763 162 KVTSLFLKRLVDFLNNRFknafKSLGSDLDS---ATSNELSLPNHLNVLNNLLIYSGLMLFLKEVDPETYEALLQLYNAS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   414 LSRLYEREIKDFFEVAKIKMtgttkeskkfatlprKESAVKQETESLHgSSGKLTGSTSslnKLSVQSSGNRRSQSSSLL 493
Cdd:pfam09763 239 ASKIYEREFKDFFEYLKKQL---------------KKSSGSEESESLF-SSGQDELYTE---WLALRKSRKLTLDSSKTG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   494 DMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQhqsmpGTMAEAEDLDG-GTLSRQHNCGTPL-- 570
Cdd:pfam09763 300 ANLSTKAPQSKLSGRLRPDEAFAGALDELEPLILVEQNFIIDFFHLSS-----LTLDFNEFVKQsPPSERRAPDLVPSkg 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   571 --PVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHV-WTAQnvDPASFLSTTLGNVLVTVKRNF 647
Cdd:pfam09763 375 vePDRELARDVRQMMSKIFQFLEPELQNLVDKVLKNDPLNALGILVYLEQYIkELEE--TNQSFLSSILQKLLEKVKQLW 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   648 DKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGD----LDKAYTKLIRGVFVNVEKVA------ 717
Cdd:pfam09763 453 DKFVDEQIRSIEETKVSKKSRKGVLPFVRNFPIFVKRVEDMLSSTERQLDvrtlVDQAYEKLTEAVFELLKRIArllpgk 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   718 ----NESQKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQgI 793
Cdd:pfam09763 533 adgpEDKEKLNRHVLLIENMNHFLEELSVLNNPVLEDLRDEAKQIFDEHLELYVQAVLRRPLGKLIEFVEGVEALLQT-V 611
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   794 REEEVSYQLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHL-------CEEENLLQVVWHSMQDEFIRQYKHFEGLIA 866
Cdd:pfam09763 612 PAAEISRQAAYSKQALKKLLSSYTAKEVRKGIEKLYKRVEKHFlgdaddpGLEESLLQKVWSDMQGEFISQYLRLESIIQ 691

                  ....*
gi 67944634   867 RCYPG 871
Cdd:pfam09763 692 KCYPG 696
PH-EXOC1 cd14683
PH-like domain of Exocyst complex component 1; Exocyst complex component 1 (EXOC1, also known ...
3-120 1.48e-61

PH-like domain of Exocyst complex component 1; Exocyst complex component 1 (EXOC1, also known as SEC3) is the higher eukaryotes homolog of yeast Sec3. The Exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270202  Cd Length: 117  Bit Score: 203.64  E-value: 1.48e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   3 AIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGdFYKRQIAWALRDLAVVDAKD 82
Cdd:cd14683   1 AIRHALQREVFTPNDERLLAVVNVSKAGKKKKTSFLCVAVTTERPVQVRLYQVKKSDKG-VYKKKRSWLLRDLKTVDGKN 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67944634  83 AIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQ 120
Cdd:cd14683  80 PKKETPEFDLHFDKVYKWVASNVQEKNAFISCLWKLCH 117
Sec3-PIP2_bind pfam15277
Exocyst complex component SEC3 N-terminal PIP2 binding PH; This is the N-terminal domain of ...
31-121 1.56e-20

Exocyst complex component SEC3 N-terminal PIP2 binding PH; This is the N-terminal domain of fungal and eukaryotic Sec3 proteins. Sec3 is a component of the exocyst complex that is involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.This N-terminal domain contains a cryptic pleckstrin homology (PH) fold, and all six positively charged lysine and arginine residues in the PH domain predicted to bind the PIP2 head group are conserved. The exocyst complex is essential for many exocytic events, by tethering vesicles at the plasma membrane for fusion. In fission yeast, polarised exocytosis for growth relies on the combined action of the exocyst at cell poles and myosin-driven transport along actin cables.


Pssm-ID: 464608  Cd Length: 85  Bit Score: 86.80  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634    31 KKKKNCFLCATVTTERPVQVKVVKVkkSDKGDFYKRQIaWALRDLAVVDAKDaikENPEFDLHFEKIYKWVASSTAEKNA 110
Cdd:pfam15277   1 KKKKPRYLCLSVTKSGRVFLHKVKE--NSNGSFSIGKT-WPLKELRLVEGIN---PDKGFDLTFDKPYYWQANSPKEKNA 74
                          90
                  ....*....|.
gi 67944634   111 FISCIWKLNQR 121
Cdd:pfam15277  75 FIRSLVKLYRK 85
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
154-256 8.40e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634  154 EEVVDEYQELNaREEQDIEIMMEGCEYAISNAEAFAEKLSRELQVLDG--ANIQSIMASEKQVNILMKLLDEALKEVDQI 231
Cdd:PRK03918 234 EELKEEIEELE-KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvKELKELKEKAEEYIKLSEFYEEYLDELREI 312
                         90       100
                 ....*....|....*....|....*
gi 67944634  232 ELKLSSYEEMLQSVKEQMDQISESN 256
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKE 337
 
Name Accession Description Interval E-value
Sec3_C pfam09763
Exocyst complex component Sec3; This entry is the conserved middle and C-terminus of the Sec3 ...
184-871 0e+00

Exocyst complex component Sec3; This entry is the conserved middle and C-terminus of the Sec3 protein. Sec3 binds to the C-terminal cytoplasmic domain of GLYT1 (glycine transporter protein 1). Sec3 is the exocyst component that is closest to the plasma membrane docking site and it serves as a spatial landmark in the plasma membrane for incoming secretory vesicles. Sec3 is recruited to the sites of polarised membrane growth through its interaction with Rho1p, a small GTP-binding protein.


Pssm-ID: 401638  Cd Length: 696  Bit Score: 602.01  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   184 NAEAFAEKLSRELQVLDGANIQSIMASEKQVNILMKLLDEALKEVDQIELKLSSYEEMLQSVKEQMDQISESNHLIHLSN 263
Cdd:pfam09763   2 DADVLEERLSRELSKLEYANIKSLLESDKRVNELMKHIDKALKECDELDPTLTLYSMELSTLSDDIEYIESQNNGLQVQS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   264 TNNVKLLSEIEFLVNHMDLAKGHIKALQEGDLASSRGIEACTNAADALLQCMNV------ALRPGHDLLLAVKQQQQRFS 337
Cdd:pfam09763  82 ANQKLLYKELESLLNTVSLPESDLHALLEGPLSSPNGLEALEAALVALFKALNAidgdkkDLDSDLGDMRALKERRARYE 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   338 DLRELFARRLASHLNNVF----VQQGHDQSStlaQHSVELTLPNHHPFHRDLLRYAKLMEWLKSTDYGKYEGLTKNYMDY 413
Cdd:pfam09763 162 KVTSLFLKRLVDFLNNRFknafKSLGSDLDS---ATSNELSLPNHLNVLNNLLIYSGLMLFLKEVDPETYEALLQLYNAS 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   414 LSRLYEREIKDFFEVAKIKMtgttkeskkfatlprKESAVKQETESLHgSSGKLTGSTSslnKLSVQSSGNRRSQSSSLL 493
Cdd:pfam09763 239 ASKIYEREFKDFFEYLKKQL---------------KKSSGSEESESLF-SSGQDELYTE---WLALRKSRKLTLDSSKTG 299
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   494 DMGNMSASDLDVADRTKFDKIFEQVLSELEPLCLAEQDFISKFFKLQQhqsmpGTMAEAEDLDG-GTLSRQHNCGTPL-- 570
Cdd:pfam09763 300 ANLSTKAPQSKLSGRLRPDEAFAGALDELEPLILVEQNFIIDFFHLSS-----LTLDFNEFVKQsPPSERRAPDLVPSkg 374
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   571 --PVSSEKDMIRQMMIKIFRCIEPELNNLIALGDKIDSFNSLYMLVKMSHHV-WTAQnvDPASFLSTTLGNVLVTVKRNF 647
Cdd:pfam09763 375 vePDRELARDVRQMMSKIFQFLEPELQNLVDKVLKNDPLNALGILVYLEQYIkELEE--TNQSFLSSILQKLLEKVKQLW 452
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   648 DKCISNQIRQMEEVKISKKSKVGILPFVAEFEEFAGLAESIFKNAERRGD----LDKAYTKLIRGVFVNVEKVA------ 717
Cdd:pfam09763 453 DKFVDEQIRSIEETKVSKKSRKGVLPFVRNFPIFVKRVEDMLSSTERQLDvrtlVDQAYEKLTEAVFELLKRIArllpgk 532
                         570       580       590       600       610       620       630       640
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   718 ----NESQKTPRDVVMMENFHHIFATLSRLKISCLEAEKKEAKQKYTDHLQSYVIYSLGQPLEKLNHFFEGVEARVAQgI 793
Cdd:pfam09763 533 adgpEDKEKLNRHVLLIENMNHFLEELSVLNNPVLEDLRDEAKQIFDEHLELYVQAVLRRPLGKLIEFVEGVEALLQT-V 611
                         650       660       670       680       690       700       710       720
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   794 REEEVSYQLAFNKQELRKVIKEYPGKEVKKGLDNLYKKVDKHL-------CEEENLLQVVWHSMQDEFIRQYKHFEGLIA 866
Cdd:pfam09763 612 PAAEISRQAAYSKQALKKLLSSYTAKEVRKGIEKLYKRVEKHFlgdaddpGLEESLLQKVWSDMQGEFISQYLRLESIIQ 691

                  ....*
gi 67944634   867 RCYPG 871
Cdd:pfam09763 692 KCYPG 696
PH-EXOC1 cd14683
PH-like domain of Exocyst complex component 1; Exocyst complex component 1 (EXOC1, also known ...
3-120 1.48e-61

PH-like domain of Exocyst complex component 1; Exocyst complex component 1 (EXOC1, also known as SEC3) is the higher eukaryotes homolog of yeast Sec3. The Exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270202  Cd Length: 117  Bit Score: 203.64  E-value: 1.48e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   3 AIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTTERPVQVKVVKVKKSDKGdFYKRQIAWALRDLAVVDAKD 82
Cdd:cd14683   1 AIRHALQREVFTPNDERLLAVVNVSKAGKKKKTSFLCVAVTTERPVQVRLYQVKKSDKG-VYKKKRSWLLRDLKTVDGKN 79
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67944634  83 AIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQ 120
Cdd:cd14683  80 PKKETPEFDLHFDKVYKWVASNVQEKNAFISCLWKLCH 117
PH-SEC3_like cd14675
PH-like domain of Sec3-like protein; Fungal Sec3, as well as its homolog in higher eukaryotes ...
3-120 1.74e-43

PH-like domain of Sec3-like protein; Fungal Sec3, as well as its homolog in higher eukaryotes Exocyst complex component 1 (EXOC1) are part of the exocyst is a conserved octameric complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270194  Cd Length: 115  Bit Score: 153.14  E-value: 1.74e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   3 AIKHALQRDIFTPNDERLLSIVNVCKAGKKKKNCFLCATVTteRPVQVKVVKVKKSDKGdFYKRQIAWALRDLAVVDAKD 82
Cdd:cd14675   1 AIKQAIQRSLFSPAHERLIEDVEVSKGGKKKRILFLCVSVT--KPGQVRLHKVKKNDNG-SFKIGKTWNLKDLKKVDGKD 77
                        90       100       110
                ....*....|....*....|....*....|....*...
gi 67944634  83 AIKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLNQ 120
Cdd:cd14675  78 PDKDTPEFDLHFDKTYKWEASSVAEKEAFISSLVKLYR 115
Sec3-PIP2_bind pfam15277
Exocyst complex component SEC3 N-terminal PIP2 binding PH; This is the N-terminal domain of ...
31-121 1.56e-20

Exocyst complex component SEC3 N-terminal PIP2 binding PH; This is the N-terminal domain of fungal and eukaryotic Sec3 proteins. Sec3 is a component of the exocyst complex that is involved in the docking of exocytic vesicles with fusion sites on the plasma membrane.This N-terminal domain contains a cryptic pleckstrin homology (PH) fold, and all six positively charged lysine and arginine residues in the PH domain predicted to bind the PIP2 head group are conserved. The exocyst complex is essential for many exocytic events, by tethering vesicles at the plasma membrane for fusion. In fission yeast, polarised exocytosis for growth relies on the combined action of the exocyst at cell poles and myosin-driven transport along actin cables.


Pssm-ID: 464608  Cd Length: 85  Bit Score: 86.80  E-value: 1.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634    31 KKKKNCFLCATVTTERPVQVKVVKVkkSDKGDFYKRQIaWALRDLAVVDAKDaikENPEFDLHFEKIYKWVASSTAEKNA 110
Cdd:pfam15277   1 KKKKPRYLCLSVTKSGRVFLHKVKE--NSNGSFSIGKT-WPLKELRLVEGIN---PDKGFDLTFDKPYYWQANSPKEKNA 74
                          90
                  ....*....|.
gi 67944634   111 FISCIWKLNQR 121
Cdd:pfam15277  75 FIRSLVKLYRK 85
PH-STXBP6 cd14681
PH-like domain of Syntaxin binding protein 6; Syntaxin binding protein 6 (STXBP6, also called ...
4-112 9.44e-18

PH-like domain of Syntaxin binding protein 6; Syntaxin binding protein 6 (STXBP6, also called Amisyn) contains, beside the N-terminal PH-like domain, a C-terminal R-SNARE-like domain, which allows it to assemble into SNARE complexes, which in turn makes the complexes inactive and inhibits exocytosis. SNARE complexes mediate membrane fusion, important for trafficking of newly synthesized proteins, recycling of pre-existing proteins and organelle formation. SNARE proteins are classified into four groups, Qa-, Qb-, Qc- and R-SNAREs, with STXBP6 being a R-SNARE. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270200  Cd Length: 130  Bit Score: 80.38  E-value: 9.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   4 IKHALQRDIFTPNDERLLSIVNVCKAGKKK-----------KNCFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWAL 72
Cdd:cd14681   2 AKSAISKEIFAPRDERMLGAVQVKRRTKKKipflatggqgeYLTYICLSVTNKKPAQVFITKVKQFEGSTSFVRRSQWML 81
                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 67944634  73 RDLAVVDAKDAIKENPEFDLHFEKIY-KWVASSTAEKNAFI 112
Cdd:cd14681  82 EQLRQVNGIDPNKDSPEFDLVFDNGFdQWVASSASEKCTFF 122
PH-EXOC1_like cd14682
PH-like domain of Exocyst complex component 1-like; Exocyst complex component 1-like proteins ...
4-119 5.78e-17

PH-like domain of Exocyst complex component 1-like; Exocyst complex component 1-like proteins are short, higher eukaryotic proteins that show homology to the PH-domain of higher eukaryotic EXOC1 and yeast SEC3 which are part of the exocyst complex involved in the docking of post-Golgi transport vesicles to sites of membrane remodeling during cellular processes such as polarization, migration, and division. Their function is unknown. PH domains have diverse functions, but in general are involved in targeting proteins to the appropriate cellular location or in the interaction with a binding partner. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. Less than 10% of PH domains bind phosphoinositide phosphates (PIPs) with high affinity and specificity. PH domains are distinguished from other PIP-binding domains by their specific high-affinity binding to PIPs with two vicinal phosphate groups: PtdIns(3,4)P2, PtdIns(4,5)P2 or PtdIns(3,4,5)P3 which results in targeting some PH domain proteins to the plasma membrane. A few display strong specificity in lipid binding. Any specificity is usually determined by loop regions or insertions in the N-terminus of the domain, which are not conserved across all PH domains. PH domains are found in cellular signaling proteins such as serine/threonine kinase, tyrosine kinases, regulators of G-proteins, endocytotic GTPases, adaptors, as well as cytoskeletal associated molecules and in lipid associated enzymes.


Pssm-ID: 270201  Cd Length: 118  Bit Score: 77.53  E-value: 5.78e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634   4 IKHALQRDIFTPNDERLLSIVNVCKAGKKKKncFLCATVTTERPVQVKVVKVKKSDKGDFYKRQIAWALRDLAVVDAKDA 83
Cdd:cd14682   4 VKEDMQKKLFRPLGQTLYEFIEIEEQSHGRH--YLCASVAKDKEVQISMVKHYRVCLDEKYERTEIWSLKDLEMIDGKDA 81
                        90       100       110
                ....*....|....*....|....*....|....*.
gi 67944634  84 IKENPEFDLHFEKIYKWVASSTAEKNAFISCIWKLN 119
Cdd:cd14682  82 DTDNPCFDMHFEEVRSVEAYSCASKYAFARTLNKLN 117
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
154-256 8.40e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.13  E-value: 8.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 67944634  154 EEVVDEYQELNaREEQDIEIMMEGCEYAISNAEAFAEKLSRELQVLDG--ANIQSIMASEKQVNILMKLLDEALKEVDQI 231
Cdd:PRK03918 234 EELKEEIEELE-KELESLEGSKRKLEEKIRELEERIEELKKEIEELEEkvKELKELKEKAEEYIKLSEFYEEYLDELREI 312
                         90       100
                 ....*....|....*....|....*
gi 67944634  232 ELKLSSYEEMLQSVKEQMDQISESN 256
Cdd:PRK03918 313 EKRLSRLEEEINGIEERIKELEEKE 337
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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