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Conserved domains on  [gi|62472946|ref|NP_001014668|]
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neurofibromin 1, isoform D [Drosophila melanogaster]

Protein Classification

neurofibromin( domain architecture ID 10142288)

neurofibromin contains a N-terminal RasGAP domain which is similar to catalytic domain of the mammalian p120RasGAP protein, followed by a Sec14-like domain, and a PH domain, and may stimulate Ras GTPase activity

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
1242-1575 0e+00

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.


:

Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 615.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1242 ETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRG 1321
Cdd:cd05130    1 ETVLADRFERLVELVTMMGDDGELPIAMALANVVPCSQMDELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTLFRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1322 NSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPP 1401
Cdd:cd05130   81 NSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEWVSYEVDPTRLEGNENLEENQRNLLQLTEKFFHAIISSSDEFPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1402 QLRSMCHCLYQVLSKRFPNllqNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSK 1481
Cdd:cd05130  161 QLRSVCHCLYQVVSHRFPN---SGLGAVGSAIFLRFINPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFTK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1482 EQHMLCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHS-MSFISDANVLALHRLLWTHQEKIGDYLSSSRDHKAVGRRPF 1560
Cdd:cd05130  238 EAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVDGPSSKyLSFINDANVLALHRLLWNNQEKIGQYLASSRDHKAVGRRPF 317
                        330
                 ....*....|....*
gi 62472946 1561 DKMATLLAYLGPPEH 1575
Cdd:cd05130  318 DKMATLLAYLGPPGH 332
PH_NF1 cd13313
Neurofibromin-1 Pleckstrin homology-like domain; Neurofibromin (NF1) contains a N-terminal ...
1759-1868 5.45e-70

Neurofibromin-1 Pleckstrin homology-like domain; Neurofibromin (NF1) contains a N-terminal RasGAP domain, followed by a Sec14-like domain, and a PH domain. Surprisingly, in neurofibromin the PH domain alone is not sufficient for phospholipid binding and instead requires the presence of the Sec-14 domain. The Sec-14 domain has been shown to bind 1-(3-sn-phosphatidyl)-sn-glycerol (PtdGro), (3-sn-phosphatidyl)-ethanolamine (PtdEtn) and -choline (PtdCho) and to a minor extent to (3-sn-phosphatidyl)-l-serine (PtdSer) and 1-(3-sn-phosphatidyl)-d-myo-inositol (PtdIns). Neurofibromatosis type 1 (also known as von Recklinghausen neurofibromatosis or NF1) is a genetic disorder caused by alterations in the tumor suppressor gene NF1. Hallmark symptoms include neural crest derived tumors, pigmentation anomalies, bone deformations, and learning disabilities. Mutations of the tumour suppressor gene NF1 are responsible for disease pathogenesis, with 90% of the alterations being nonsense codons. 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: 270123  Cd Length: 110  Bit Score: 230.46  E-value: 5.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1759 GATLSLDEDLKVFSNALKLSHKDTKVAIKVGPTALQITSAEKTKVLAHSVLLNDVYYASEIEEVCLVDDNQFTLSITNES 1838
Cdd:cd13313    1 AATLALEEDLKVFNNALKLSHKDTKVAIKVGPTAIQVTSAEKTKVLGHSVLLNDVYYASEIEEVCLVDDNQFTLTIANEG 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 62472946 1839 GQLSFIHNDCDNIVQAIIHIRNRWELSQPD 1868
Cdd:cd13313   81 GPLSFMHNDCEAIVQAIIHIRTRWELSQPD 110
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
1633-1767 6.25e-31

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


:

Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 119.74  E-value: 6.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1633 GYPVFYYIARRYKIGET---NGDLLIYHVILTL-KPFCHSPFEVVIDFTHTCSDNRFRTEFLQKWFYVLPTVAYENVHAV 1708
Cdd:pfam13716    1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472946   1709 YIYNCNSWVREYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQ--QKLPGaTLSLDED 1767
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQlpTELPG-VLSYDEE 140
MOR2-PAG1_mid super family cl20509
Cell morphogenesis central region; This family is the conserved central region of proteins ...
1931-2086 9.46e-06

Cell morphogenesis central region; This family is the conserved central region of proteins that are involved in cell morphogenesis.


The actual alignment was detected with superfamily member pfam14228:

Pssm-ID: 433790 [Multi-domain]  Cd Length: 1113  Bit Score: 51.56  E-value: 9.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1931 IPSNNTIFIKSVSEKLATNEPHLTlEFLEESIQGFQRSTIEL--KHLCLEYMTPWLKNLvkfcksndDSKKLKVS----Q 2004
Cdd:pfam14228  592 LPDSYQQFQYKLSAKLAKDHPELS-ELLCEEIMQRQLDAVDIiaQHQVLTCMAPWIENL--------NFLKLWESgwseR 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   2005 ILDKLINLTIDQKEMYPSVQAKIWGSIGQIPELIDMVLDNFLHKSITYGLGSPQVEIMADTAVALAsanvqlVSKKV--- 2081
Cdd:pfam14228  663 LLKSLYYVTWRHGDQFPDEIEKLWRTIASKPRNISPVLDFLISKGIEDCDSNASAEITGAFATYFS------VAKRVsly 736

                   ....*
gi 62472946   2082 ITRIC 2086
Cdd:pfam14228  737 LARIC 741
 
Name Accession Description Interval E-value
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
1242-1575 0e+00

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 615.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1242 ETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRG 1321
Cdd:cd05130    1 ETVLADRFERLVELVTMMGDDGELPIAMALANVVPCSQMDELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTLFRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1322 NSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPP 1401
Cdd:cd05130   81 NSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEWVSYEVDPTRLEGNENLEENQRNLLQLTEKFFHAIISSSDEFPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1402 QLRSMCHCLYQVLSKRFPNllqNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSK 1481
Cdd:cd05130  161 QLRSVCHCLYQVVSHRFPN---SGLGAVGSAIFLRFINPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFTK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1482 EQHMLCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHS-MSFISDANVLALHRLLWTHQEKIGDYLSSSRDHKAVGRRPF 1560
Cdd:cd05130  238 EAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVDGPSSKyLSFINDANVLALHRLLWNNQEKIGQYLASSRDHKAVGRRPF 317
                        330
                 ....*....|....*
gi 62472946 1561 DKMATLLAYLGPPEH 1575
Cdd:cd05130  318 DKMATLLAYLGPPGH 332
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
1227-1581 5.68e-119

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 380.89  E-value: 5.68e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1227 LTQILQQGTEFDTLAETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFY 1306
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALID 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1307 REVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEetCFEVDPARLDpTEDIEQHRNNLIALTQ 1386
Cdd:smart00323   81 PEVERTDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKK--SCEVDPAKLE-GEDLETNLENLLQYVE 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1387 KVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNlLQNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLM 1466
Cdd:smart00323  158 RLFDAIINSSDRLPYGLRDICKQLRQAAEKRFPD-ADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLI 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1467 SKILQNIANHVEF-SKEQHMLCFNDFLRDHFEAGRRFFIQIASDCET-VDQTSHSMSFIsDANVLALHRLLWTHQEKIGD 1544
Cdd:smart00323  237 AKVLQNLANLSEFgSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEIlVDKVSDSTTIS-GRELSLLHSLLLENGDALKR 315
                           330       340       350
                    ....*....|....*....|....*....|....*..
gi 62472946    1545 YLSSsrdhkavgRRPFDKMATLLAYLGPPEHKPVDSH 1581
Cdd:smart00323  316 ELNN--------EDPLGKLLFKLRYFGLTTHELTYGK 344
PH_NF1 cd13313
Neurofibromin-1 Pleckstrin homology-like domain; Neurofibromin (NF1) contains a N-terminal ...
1759-1868 5.45e-70

Neurofibromin-1 Pleckstrin homology-like domain; Neurofibromin (NF1) contains a N-terminal RasGAP domain, followed by a Sec14-like domain, and a PH domain. Surprisingly, in neurofibromin the PH domain alone is not sufficient for phospholipid binding and instead requires the presence of the Sec-14 domain. The Sec-14 domain has been shown to bind 1-(3-sn-phosphatidyl)-sn-glycerol (PtdGro), (3-sn-phosphatidyl)-ethanolamine (PtdEtn) and -choline (PtdCho) and to a minor extent to (3-sn-phosphatidyl)-l-serine (PtdSer) and 1-(3-sn-phosphatidyl)-d-myo-inositol (PtdIns). Neurofibromatosis type 1 (also known as von Recklinghausen neurofibromatosis or NF1) is a genetic disorder caused by alterations in the tumor suppressor gene NF1. Hallmark symptoms include neural crest derived tumors, pigmentation anomalies, bone deformations, and learning disabilities. Mutations of the tumour suppressor gene NF1 are responsible for disease pathogenesis, with 90% of the alterations being nonsense codons. 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: 270123  Cd Length: 110  Bit Score: 230.46  E-value: 5.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1759 GATLSLDEDLKVFSNALKLSHKDTKVAIKVGPTALQITSAEKTKVLAHSVLLNDVYYASEIEEVCLVDDNQFTLSITNES 1838
Cdd:cd13313    1 AATLALEEDLKVFNNALKLSHKDTKVAIKVGPTAIQVTSAEKTKVLGHSVLLNDVYYASEIEEVCLVDDNQFTLTIANEG 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 62472946 1839 GQLSFIHNDCDNIVQAIIHIRNRWELSQPD 1868
Cdd:cd13313   81 GPLSFMHNDCEAIVQAIIHIRTRWELSQPD 110
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1308-1475 4.55e-37

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 139.73  E-value: 4.55e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1308 EVEVSDCMQTLFRGNSLGSKIMA-FCFKIYGASYLQMLLEPLIRPLLDEEEETCfEVDPARL------------------ 1368
Cdd:pfam00616    9 EIESSDNPNDLLRGNSLVSKLLEtYNRRPRGQEYLKKVLGPLVRKIIEDEDLDL-ESDPRKIyeslinqeelktgrsdlp 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1369 ----------DPTED--IEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNI-GAVGTVIFL 1435
Cdd:pfam00616   88 rdvspeeaieDPEVRqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIlNAIGGFLFL 167
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 62472946   1436 RFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIAN 1475
Cdd:pfam00616  168 RFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
1633-1767 6.25e-31

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 119.74  E-value: 6.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1633 GYPVFYYIARRYKIGET---NGDLLIYHVILTL-KPFCHSPFEVVIDFTHTCSDNRFRTEFLQKWFYVLPTVAYENVHAV 1708
Cdd:pfam13716    1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472946   1709 YIYNCNSWVREYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQ--QKLPGaTLSLDED 1767
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQlpTELPG-VLSYDEE 140
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
1614-1758 1.54e-23

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 99.30  E-value: 1.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1614 EFKTLKSMNIFYQaGTSKSGYPVFYYIARRYKI-GETNGDLLIYHVILTLKPFCHSPFEVVIDFTHTCSD------NRFR 1686
Cdd:smart00516    1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFDLkSVTLEELLRYLVYVLEKILQEEKKTGGIEGFTVIFDlkglsmSNPD 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62472946    1687 TEFLQKWFYVLPTVAYENVHAVYIYNCNSWVR-EYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQqkLP 1758
Cdd:smart00516   80 LSVLRKILKILQDHYPERLGKVYIINPPWFFRvLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQ--LP 150
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
1613-1754 3.76e-13

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 69.29  E-value: 3.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1613 EEFKTLKSmNIFYQAGTSKSGYPVFYYIARRYKIGETNGDLLIYHVILTLKPFCHSPFE------VVIDFTHTCSDNRFR 1686
Cdd:cd00170    2 EELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEqvegfvVIIDLKGFSLSNLSD 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62472946 1687 TEFLQKWFYVLPTVAYENVHAVYIYNCNSWVREYTKFHDRILAPlKGNRKLLFLES-PNKLTDFIDAEQ 1754
Cdd:cd00170   81 LSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSE-KTRKKIVFLGSdLEELLEYIDPDQ 148
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1293-1475 1.52e-07

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 57.20  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1293 AKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIY--GASYLQML------------LEPLIRPLLDEEee 1358
Cdd:COG5261  433 EEHLSVSLFQMLLRTEVEATSLVQSLLRGNLPVHRNMTNYFRRSqgQAALREIRyqiindvaihedLEVDINPLLVYR-- 510
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1359 tcFEVDPARLDPTEDIEQHRNN--------------------LIALTQKVFDAIINSSDRFPPQLRSMCHcLYQVLSKRF 1418
Cdd:COG5261  511 --ALLNKGQLSPDKDLELLTSNeevseflavmnavqessaklLELSTERILDAVYNSLDEIGYGIRFVCE-LIRVVFELT 587
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472946 1419 PNLLQNNI-----------------GAVGTVIFLRFINPAIVSPQELGIVDKQVhSSAKRGLMLMSKILQNIAN 1475
Cdd:COG5261  588 PNRLFPSIsdsrclrticfaeidslGLIGGFFFLRFVNEALVSPQTSMLKDSCP-SDNVRKLATLSKILQSVFE 660
MOR2-PAG1_mid pfam14228
Cell morphogenesis central region; This family is the conserved central region of proteins ...
1931-2086 9.46e-06

Cell morphogenesis central region; This family is the conserved central region of proteins that are involved in cell morphogenesis.


Pssm-ID: 433790 [Multi-domain]  Cd Length: 1113  Bit Score: 51.56  E-value: 9.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1931 IPSNNTIFIKSVSEKLATNEPHLTlEFLEESIQGFQRSTIEL--KHLCLEYMTPWLKNLvkfcksndDSKKLKVS----Q 2004
Cdd:pfam14228  592 LPDSYQQFQYKLSAKLAKDHPELS-ELLCEEIMQRQLDAVDIiaQHQVLTCMAPWIENL--------NFLKLWESgwseR 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   2005 ILDKLINLTIDQKEMYPSVQAKIWGSIGQIPELIDMVLDNFLHKSITYGLGSPQVEIMADTAVALAsanvqlVSKKV--- 2081
Cdd:pfam14228  663 LLKSLYYVTWRHGDQFPDEIEKLWRTIASKPRNISPVLDFLISKGIEDCDSNASAEITGAFATYFS------VAKRVsly 736

                   ....*
gi 62472946   2082 ITRIC 2086
Cdd:pfam14228  737 LARIC 741
 
Name Accession Description Interval E-value
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
1242-1575 0e+00

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the neurofibromatosis type 1 gene (NF1) and shares a region of similarity with catalytic domain of the mammalian p120RasGAP protein and an extended similarity with the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2. Neurofibromin has been shown to function as a GAP (GTPase-activating protein) which inhibits low molecular weight G proteins such as Ras by stimulating their intrinsic GTPase activity. NF1 is a common genetic disorder characterized by various symptoms ranging from predisposition for the development of tumors to learning disability or mental retardation. Loss of neurofibromin activity can be correlated to the increase in Ras-GTP concentration in neurofibromas of NF1 of patients, supporting the notion that unregulated Ras signaling may contribute to their development.


Pssm-ID: 213332 [Multi-domain]  Cd Length: 332  Bit Score: 615.49  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1242 ETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRG 1321
Cdd:cd05130    1 ETVLADRFERLVELVTMMGDDGELPIAMALANVVPCSQMDELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTLFRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1322 NSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPP 1401
Cdd:cd05130   81 NSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEWVSYEVDPTRLEGNENLEENQRNLLQLTEKFFHAIISSSDEFPP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1402 QLRSMCHCLYQVLSKRFPNllqNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSK 1481
Cdd:cd05130  161 QLRSVCHCLYQVVSHRFPN---SGLGAVGSAIFLRFINPAIVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFTK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1482 EQHMLCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHS-MSFISDANVLALHRLLWTHQEKIGDYLSSSRDHKAVGRRPF 1560
Cdd:cd05130  238 EAHMLPFNDFLRNHFEAGRRFFSSIASDCGAVDGPSSKyLSFINDANVLALHRLLWNNQEKIGQYLASSRDHKAVGRRPF 317
                        330
                 ....*....|....*
gi 62472946 1561 DKMATLLAYLGPPEH 1575
Cdd:cd05130  318 DKMATLLAYLGPPGH 332
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
1227-1581 5.68e-119

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position. Improved domain limits from structure.


Pssm-ID: 214617  Cd Length: 344  Bit Score: 380.89  E-value: 5.68e-119
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1227 LTQILQQGTEFDTLAETVLADRFEQLVQLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFY 1306
Cdd:smart00323    1 LKQGDLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLSLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALID 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1307 REVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEetCFEVDPARLDpTEDIEQHRNNLIALTQ 1386
Cdd:smart00323   81 PEVERTDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKK--SCEVDPAKLE-GEDLETNLENLLQYVE 157
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1387 KVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNlLQNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLM 1466
Cdd:smart00323  158 RLFDAIINSSDRLPYGLRDICKQLRQAAEKRFPD-ADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLI 236
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1467 SKILQNIANHVEF-SKEQHMLCFNDFLRDHFEAGRRFFIQIASDCET-VDQTSHSMSFIsDANVLALHRLLWTHQEKIGD 1544
Cdd:smart00323  237 AKVLQNLANLSEFgSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEIlVDKVSDSTTIS-GRELSLLHSLLLENGDALKR 315
                           330       340       350
                    ....*....|....*....|....*....|....*..
gi 62472946    1545 YLSSsrdhkavgRRPFDKMATLLAYLGPPEHKPVDSH 1581
Cdd:smart00323  316 ELNN--------EDPLGKLLFKLRYFGLTTHELTYGK 344
PH_NF1 cd13313
Neurofibromin-1 Pleckstrin homology-like domain; Neurofibromin (NF1) contains a N-terminal ...
1759-1868 5.45e-70

Neurofibromin-1 Pleckstrin homology-like domain; Neurofibromin (NF1) contains a N-terminal RasGAP domain, followed by a Sec14-like domain, and a PH domain. Surprisingly, in neurofibromin the PH domain alone is not sufficient for phospholipid binding and instead requires the presence of the Sec-14 domain. The Sec-14 domain has been shown to bind 1-(3-sn-phosphatidyl)-sn-glycerol (PtdGro), (3-sn-phosphatidyl)-ethanolamine (PtdEtn) and -choline (PtdCho) and to a minor extent to (3-sn-phosphatidyl)-l-serine (PtdSer) and 1-(3-sn-phosphatidyl)-d-myo-inositol (PtdIns). Neurofibromatosis type 1 (also known as von Recklinghausen neurofibromatosis or NF1) is a genetic disorder caused by alterations in the tumor suppressor gene NF1. Hallmark symptoms include neural crest derived tumors, pigmentation anomalies, bone deformations, and learning disabilities. Mutations of the tumour suppressor gene NF1 are responsible for disease pathogenesis, with 90% of the alterations being nonsense codons. 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: 270123  Cd Length: 110  Bit Score: 230.46  E-value: 5.45e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1759 GATLSLDEDLKVFSNALKLSHKDTKVAIKVGPTALQITSAEKTKVLAHSVLLNDVYYASEIEEVCLVDDNQFTLSITNES 1838
Cdd:cd13313    1 AATLALEEDLKVFNNALKLSHKDTKVAIKVGPTAIQVTSAEKTKVLGHSVLLNDVYYASEIEEVCLVDDNQFTLTIANEG 80
                         90       100       110
                 ....*....|....*....|....*....|
gi 62472946 1839 GQLSFIHNDCDNIVQAIIHIRNRWELSQPD 1868
Cdd:cd13313   81 GPLSFMHNDCEAIVQAIIHIRTRWELSQPD 110
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
1247-1543 1.69e-59

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins include the Saccharomyces cerevisiae RasGAP proteins Ira1 and Ira2, the closest homolog of neurofibromin, which is responsible for the human autosomal dominant disease neurofibromatosis type I (NF1). The RasGAP Ira1/2 proteins are negative regulators of the Ras-cAMP signaling pathway and conserved from yeast to human. In yeast Ras proteins are activated by GEFs, and inhibited by two GAPs, Ira1 and Ira2. Ras proteins activate the cAMP/protein kinase A (PKA) pathway, which controls metabolism, stress resistance, growth, and meiosis. Recent studies showed that the kelch proteins Gpb1 and Gpb2 inhibit Ras activity via association with Ira1 and Ira2. Gpb1/2 bind to a conserved C-terminal domain of Ira1/2, and loss of Gpb1/2 results in a destabilization of Ira1 and Ira2, leading to elevated levels of Ras2-GTP and uninhibited cAMP-PKA signaling. Since the Gpb1/2 binding domain on Ira1/2 is conserved in the human neurofibromin protein, the studies suggest that an analogous signaling mechanism may contribute to the neoplastic development of NF1.


Pssm-ID: 213341  Cd Length: 317  Bit Score: 208.68  E-value: 1.69e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1247 DRFEQLVQLVTmisdkGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGS 1326
Cdd:cd05392    4 EAYDELLELLI-----EDPQLLLAIAEVCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISHTSRAADLFRRNSVAT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1327 KIMAFCFKIYGASYLQMLLEPLIRPLLDEEEEtcFEVDPARLDPtEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSM 1406
Cdd:cd05392   79 RLLTLYAKSVGNKYLRKVLRPLLTEIVDNKDY--FEVEKIKPDD-ENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1407 CHCLYQVLSKRFPNLLQNnigAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFS-KEQHM 1485
Cdd:cd05392  156 CNTIYESVSKKFPDAALI---AVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSlKEPYL 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 62472946 1486 LCFNDFLRDHFEAGRRFFIQIASDCETVDQTSHSMSFISDANVLALHRLLWTHQEKIG 1543
Cdd:cd05392  233 ESLNEFLKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHKFLYLHFLEIR 290
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
1254-1508 9.18e-59

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin, among others. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP exhibit no similarity at their amino acid sequence level. RasGTPases function as molecular switches in a large number of signaling pathways. They are in the on state when bound to GTP, and in the off state when bound to GDP. The RasGAP domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213328  Cd Length: 256  Bit Score: 204.26  E-value: 9.18e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1254 QLVTMISDKGELPIAMALANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCF 1333
Cdd:cd04519    4 RLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKNPNTLFRGNSLATKLLDQYM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1334 KIYGASYLQMLLEPLIRPLLDEEEEtcFEVDPaRLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQV 1413
Cdd:cd04519   84 KLVGQEYLKETLSPLIREILESKES--CEIDT-KLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1414 LSKRFPNLLQNNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFS-KEQHMLCFNDFL 1492
Cdd:cd04519  161 LAERFPEEPDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGdKEPFMKPLNDFI 240
                        250
                 ....*....|....*.
gi 62472946 1493 RDHFEAGRRFFIQIAS 1508
Cdd:cd04519  241 KSNKPKLKQFLDELSS 256
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
1249-1508 4.27e-39

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras GTPase-activating proteins includes GAP1(m) (or RASA2), GAP1_IP4BP (or RASA3), Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), and Ras GTPase activating-like proteins (RASAL) or RASAL1. The members are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin homology domain that is associated with a Bruton's tyrosine kinase motif. While this domain structure is conserved, a small change in the function of each individual domain and the interaction between domains has a marked effect on the regulation of each protein.


Pssm-ID: 213330  Cd Length: 269  Bit Score: 147.78  E-value: 4.27e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1249 FEQLVQLVTMISDKGELPIAMA--LANVVTTSQMDeLARVLVTLFDAKHLLSPLLWNMFYREVevSDCMQ--TLFRGNSL 1324
Cdd:cd05128    3 YEPLLNLLLESLDVPPFTASAVylLEELVKVDKDD-VARPLVRIFLHHGQIVPLLRALASREI--SKTQDpnTLFRGNSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1325 GSKIMAFCFKIYGASYLQMLLepliRPLLDE--EEETCFEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQ 1402
Cdd:cd05128   80 ASKCMDEFMKLVGMQYLHETL----KPVIDEifSEKKSCEIDPSKLKDGEVLETNLANLRGYVERVFKAITSSARRCPTL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1403 LRSMCHCLYQVLSKRFPNllQNNIG--AVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFS 1480
Cdd:cd05128  156 MCEIFSDLRESAAQRFPD--NEDVPytAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSS 233
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 62472946 1481 -----KEQHMLCFND--FLRDHFEAGRRFFIQIAS 1508
Cdd:cd05128  234 sglgvKEAYMSPLYErfTDEQHVDAVKKFLDRISS 268
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
1317-1508 8.89e-38

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein (GAP) for BUD1/RSR1 and is necessary for proper bud-site selection in yeast. BUD2 has sequence similarity to the catalytic domain of RasGAPs, and stimulates the hydrolysis of BUD1-GTP to BUD1-GDP. Elimination of Bud2p activity by mutation causes a random budding pattern with no growth defect. Overproduction of Bud2p also alters the budding pattern.


Pssm-ID: 213339 [Multi-domain]  Cd Length: 356  Bit Score: 146.94  E-value: 8.89e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1317 TLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLDEEEEtcFEVDPARLDPT------EDIEQHRNNLIALTQKVFD 1390
Cdd:cd05137   94 LLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKD--CEVDPSRVKESdsiekeEDLEENWENLISLTEEIWN 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1391 AIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKI 1469
Cdd:cd05137  172 SIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTVTlNSVSGFLFLRFFCPAILNPKLFGLLKDHPRPRAQRTLTLIAKV 251
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 62472946 1470 LQNIANHVEFS-KEQHMLCFNDFLRDHFEAGRRFFIQIAS 1508
Cdd:cd05137  252 LQNLANLTTFGqKEPWMEPMNEFLTTHREELKDYIDKITG 291
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
1281-1537 1.39e-37

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras GTPase-activating proteins includes DAB2IP, nGAP, and Syn GAP. Disabled 2 interactive protein, (DAB2IP; also known as ASK-interacting protein 1 (AIP1)), is a member of the GTPase-activating proteins, down-regulates Ras-mediated signal pathways, and mediates TNF-induced activation of ASK1-JNK signaling pathways. The mechanism by which TNF signaling is coupled to DAB2IP is not known.


Pssm-ID: 213338  Cd Length: 324  Bit Score: 145.42  E-value: 1.39e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1281 DELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLdEEEETC 1360
Cdd:cd05136   41 EELATALVHILQSTGKAKEFLTDLVMAEVDRLDDEHLIFRGNTLATKAMEAYLKLVGQKYLQETLGEFIRALY-ESEEDC 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1361 fEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRF-PNLLQNNIGAvgtVIFLRFIN 1439
Cdd:cd05136  120 -EVDPSKCPPSASLSRNQANLRRSVELAWCKILSSHCVFPRELREVFSSWRERLEERGrEDIADRLISA---SLFLRFLC 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1440 PAIVSPQELGIVdkQVHSSAK--RGLMLMSKILQNIANHVEF-SKEQHMLCFNDFLRDHFEAGRRFFIQIASdcetVDQT 1516
Cdd:cd05136  196 PAILSPSLFNLT--QEYPSERaaRNLTLIAKVIQNLANFTRFgGKEEYMEFMNDFVEQEWPNMKQFLQEISS----PSPS 269
                        250       260
                 ....*....|....*....|....*
gi 62472946 1517 SHSMSF---ISDANVLA-LHRLLWT 1537
Cdd:cd05136  270 SNSSDFdgyIDLGRELSlLHSLLVE 294
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
1308-1475 4.55e-37

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the GTPase activity of Ras, thereby "switching" it into an "off" position.


Pssm-ID: 459871  Cd Length: 207  Bit Score: 139.73  E-value: 4.55e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1308 EVEVSDCMQTLFRGNSLGSKIMA-FCFKIYGASYLQMLLEPLIRPLLDEEEETCfEVDPARL------------------ 1368
Cdd:pfam00616    9 EIESSDNPNDLLRGNSLVSKLLEtYNRRPRGQEYLKKVLGPLVRKIIEDEDLDL-ESDPRKIyeslinqeelktgrsdlp 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1369 ----------DPTED--IEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNI-GAVGTVIFL 1435
Cdd:pfam00616   88 rdvspeeaieDPEVRqiFEDNLQKLRELADEFLDAIYSSLNQLPYGIRYICKQLYELLEEKFPDASEEEIlNAIGGFLFL 167
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 62472946   1436 RFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIAN 1475
Cdd:pfam00616  168 RFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
1264-1542 5.74e-33

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates hydrolysis of bound GTP to GDP. Once the Ras regulator p120GAP, a member of the GAP protein family, is recruited to the membrane, it is transiently immobilized to interact with Ras-GTP. The down-regulation of Ras by p120GAP is a critical step in the regulation of many cellular processes, which is disrupted in approximately 30% of human cancers. p120GAP contains SH2, SH3, PH, calcium- and lipid-binding domains, suggesting its involvement in a complex network of cellular interactions in vivo.


Pssm-ID: 213340  Cd Length: 328  Bit Score: 132.23  E-value: 5.74e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1264 ELPIAMALANVVTTSQMdELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQM 1343
Cdd:cd05391   21 ELHVVYALAHVCGQDRT-LLASILLRIFRHEKLESLLLRTLNDREISMEDEATTLFRATTLASTLMEQYMKATATPFVHH 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1344 LLEPLIRPLLdEEEETCfEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQ 1423
Cdd:cd05391  100 ALKDTILKIL-ESKQSC-ELNPSKLEKNEDVNTNLEHLLNILSELVEKIFMAAEILPPTLRYIYGCLQKSVQQKWPTNTT 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1424 NNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEF-SKEQHMLCFNDFLRDHFEAGRRF 1502
Cdd:cd05391  178 VRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFgAKEPYMEGVNPFIKKNKERMIMF 257
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 62472946 1503 FIQIASDCETVDQTSHSMSFISdANVLALHRLLWTHQEKI 1542
Cdd:cd05391  258 LDELGNVPELPDTTEHSRTDLS-RDLAALHEICVAHSDEL 296
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
1633-1767 6.25e-31

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 119.74  E-value: 6.25e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1633 GYPVFYYIARRYKIGET---NGDLLIYHVILTL-KPFCHSPFEVVIDFTHTCSDNRFRTEFLQKWFYVLPTVAYENVHAV 1708
Cdd:pfam13716    1 GRPVLVFISKLLPSRPAsldDLDRLLFYLLKTLsEKLKGKPFVVVVDHTGVTSENFPSLSFLKKAYDLLPRAFKKNLKAV 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 62472946   1709 YIYNCNSWVREYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQ--QKLPGaTLSLDED 1767
Cdd:pfam13716   81 YVVHPSTFLRTFLKTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQlpTELPG-VLSYDEE 140
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
1266-1502 1.13e-25

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like protein (RASAL) or RASAL1 is a member of the GAP1 family, and a Ca2+ sensor responding in-phase to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. It contains a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL, like Ca2+ -promoted Ras inactivator (CAPRI, or RASAL4), is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to receptor-mediated elevation in the concentration of intracellular free Ca2+, a translocation that activates its ability to function as a RasGAP. However, unlike RASAL4, RASAL undergoes an oscillatory translocation to the plasma membrane that occurs in synchrony with repetitive Ca2+ spikes.


Pssm-ID: 213337  Cd Length: 287  Bit Score: 109.52  E-value: 1.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1266 PIAMaLANVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQMLL 1345
Cdd:cd05135   27 PLAM-LEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTLFRSNSLASKSMEQFMKVVGMPYLHEVL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1346 EPLIRPLLDEEEETcfEVDPARLDP----------TEDIEQHRNNLIALTQ----KVFDAIINSSDRFPPQLRSMCHCLY 1411
Cdd:cd05135  106 KPVINRIFEEKKYV--ELDPCKIDLnrtrrisfkgSLSEAQVRESSLELLQgylgSIIDAIVGSVDQCPPVMRVAFKQLH 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1412 QVLSKRFPNLLQNNIG--AVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIAN---HVEFSKEQHML 1486
Cdd:cd05135  184 KRVEERFPEAEHQDVKylAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNlglQLGQGKEQWMA 263
                        250
                 ....*....|....*.
gi 62472946 1487 CFNDFLRDHFEAGRRF 1502
Cdd:cd05135  264 PLHPFILQSVARVKDF 279
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
1337-1542 4.98e-25

Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family represents IQ motif containing GTPase activating protein (IQGAP) which associated with the Ras GTP-binding protein. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 213329 [Multi-domain]  Cd Length: 331  Bit Score: 108.83  E-value: 4.98e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1337 GASYLQMLLEPLIRPLLDEEEeTCFEVDP-----ARLDPTE-------------DIEQ-------------HRNNLIALT 1385
Cdd:cd05127   52 GQKYLRELLGPVVKEILDDDD-LDLETDPvdiykAWINQEEsrtgepsklpydvTREQalkdpevrkrlieHLEKLRAIT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1386 QKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVDKQVHSS----AK 1460
Cdd:cd05127  131 DKFLTAITESLDKMPYGMRYIAKVLKEALREKFPDAPEEEIlKIVGNLLYYRYMNPAIVAPEAFDIIDLSVGGQlsplQR 210
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1461 RGLMLMSKILQNIANHVEFSKE-QHMLCFNDFLRDHFEAGRRFFIQIAS--DCET---VDQ-TSHSMS-----FISDANV 1528
Cdd:cd05127  211 RNLGSIAKVLQQAASGKLFGGEnPYLSPLNPYISESHEKFKKFFLEACTvpEAEEhfnIDEySDLTMLtkptiYISLQEI 290
                        250
                 ....*....|....
gi 62472946 1529 LALHRLLWTHQEKI 1542
Cdd:cd05127  291 FATHKLLLEHQDEI 304
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
1266-1508 6.03e-25

Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family and has been shown to specifically bind 1,3,4,5-tetrakisphosphate (IP4). Thus, RASA3 may function as an IP4 receptor. The members of GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. Purified RASA3 stimulates GAP activity on Ras with about a five-fold lower potency than p120RasGAP, but shows no GAP-stimulating activity at all against Rac or Rab3A.


Pssm-ID: 213336  Cd Length: 269  Bit Score: 107.03  E-value: 6.03e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1266 PIAMALANVV--TTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQM 1343
Cdd:cd05134   19 PVSASAAHILgeVCREKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQDPNTIFRGNSLTSKCIDETMKLAGMHYLQV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1344 LLEPLIRPLLdEEEETCfEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQ 1423
Cdd:cd05134   99 TLKPIIDEIC-QEHKPC-EIDPVKLKDGENLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1424 NNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNI-----ANHVEFsKEQHMLCFNDFLRD--HF 1496
Cdd:cd05134  177 VRYTAVSSFIFLRFFAPAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLgslskSKSANF-KESYMAAFYDYFNEqkYA 255
                        250
                 ....*....|..
gi 62472946 1497 EAGRRFFIQIAS 1508
Cdd:cd05134  256 DAVKNFLDLISS 267
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
1340-1573 6.12e-25

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to bind to small GTPases, which are yet to be identified. IQGAP proteins are integral components of cytoskeletal regulation. Results from truncated GAPAs indicated that almost the entire region of GAPA homologous to IQGAP is required for cytokinesis in Dictyostelium. More members of the IQGAP family are emerging, and evidence suggests that there are both similarities and differences in their function.


Pssm-ID: 213334  Cd Length: 352  Bit Score: 108.98  E-value: 6.12e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1340 YLQMLLEPLIRPLLDEEEETCFEVDPARLDPTED--IEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKR 1417
Cdd:cd05132   98 YEQMINDIELDTGLPSNLPRGITPEEAAENPAVQniIEPRLEMLEEITNSFLEAIINSLDEVPYGIRWICKQIRSLTRRK 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1418 FPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFSKEQHMLCFNDFLRDHF 1496
Cdd:cd05132  178 FPDASDETIcSLIGGFFLLRFINPAIVSPQAYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSYSKEPYMAPLQPFVEENK 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1497 EAGRRFFIQIasdCETVD-QTSHSMSF------------ISDANVLALHRLLWTHQEKIgdylssSRDHKavgrrpfDKM 1563
Cdd:cd05132  258 ERLNKFLNDL---CEVDDfYESLELDQyialskkdlsinITLNEIYNTHSLLVKHLAEL------APDHN-------DHL 321
                        250
                 ....*....|
gi 62472946 1564 ATLLAYLGPP 1573
Cdd:cd05132  322 RLILQELGPA 331
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
1614-1758 1.54e-23

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 99.30  E-value: 1.54e-23
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946    1614 EFKTLKSMNIFYQaGTSKSGYPVFYYIARRYKI-GETNGDLLIYHVILTLKPFCHSPFEVVIDFTHTCSD------NRFR 1686
Cdd:smart00516    1 ELELLKAYIPGGR-GYDKDGRPVLIERAGRFDLkSVTLEELLRYLVYVLEKILQEEKKTGGIEGFTVIFDlkglsmSNPD 79
                            90       100       110       120       130       140       150
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62472946    1687 TEFLQKWFYVLPTVAYENVHAVYIYNCNSWVR-EYTKFHDRILAPLKGNRKLLFLESPNKLTDFIDAEQqkLP 1758
Cdd:smart00516   80 LSVLRKILKILQDHYPERLGKVYIINPPWFFRvLWKIIKPFLDEKTREKIRFVGNDSKEELLEYIDKEQ--LP 150
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
1266-1508 4.18e-23

Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of Ras GTPase-activating proteins that includes GAP1_IP4BP (or RASA3), CAPRI, and RASAL. In vitro, RASA2 has been shown to bind inositol 1,3,4,5-tetrakisphosphate (IP4), the water soluble inositol head group of the lipid second messenger phosphatidylinositol 3,4,5-trisphosphate (PIP3). In vivo studies also demonstrated that RASA2 binds PIP3, and it is recruited to the plasma membrane following agonist stimulation of PI 3-kinase. Furthermore, the membrane translocation is a consequence of the ability of its pleckstrin homology (PH) domain to bind PIP3.


Pssm-ID: 213342  Cd Length: 272  Bit Score: 101.51  E-value: 4.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1266 PIAMALANVVTTSQMDELARVL--VTLFDAKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIYGASYLQM 1343
Cdd:cd05394   19 PISASAAHILGEICRDKYDAVLplVRLLLHHNKLVPFVAAVAALDLKDTQEANTIFRGNSLATRCLDEMMKIVGKHYLKV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1344 LLEPLIRPLLdEEEETCfEVDPARLDPTEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQ 1423
Cdd:cd05394   99 TLKPVLDEIC-ESPKPC-EIDPIKLKEGDNVENNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDPH 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1424 NNIGAVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGLMLMSKILQNIANHVEFS-------KEQHMlC--FNDFLRD 1494
Cdd:cd05394  177 VQYSAVSSFVFLRFFAVAVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSksklssfKETFM-CdfFKMFQEE 255
                        250
                 ....*....|....*
gi 62472946 1495 HF-EAGRRFFIQIAS 1508
Cdd:cd05394  256 KYiEKVKKFLDEISS 270
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
1240-1475 2.25e-21

Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also known as Ca2+ -promoted Ras inactivator (CAPRI), is a member of the GAP1 family. Members of the GAP1 family are characterized by a conserved domain structure comprising N-terminal tandem C2 domains, a highly conserved central RasGAP domain, and a C-terminal pleckstrin-homology domain that is associated with a Bruton's tyrosine kinase motif. RASAL4, like RASAL, is a cytosolic protein that undergoes a rapid translocation to the plasma membrane in response to a receptor-mediated elevation in the concentration of intracellular free Ca2+ ([Ca2+]i). However, unlike RASAL, RASAL4 does not sense oscillations in [Ca2+]i.


Pssm-ID: 213343 [Multi-domain]  Cd Length: 287  Bit Score: 96.86  E-value: 2.25e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1240 LAETVLADRFEQLVQLVTMISDkgelpiamalanVVTTSQMDELARVLVTLFDAKHLLSPLLWNMFYREVEVSDCMQTLF 1319
Cdd:cd05395   12 LCQEVKLGHQAGPVQLISLIDE------------TTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTLF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1320 RGNSLGSKIMAFCFKIYGASYLQMLLEPLIRPLLdeEEETCFEVDPARLD--------------PTEDIEQHRNNLIALT 1385
Cdd:cd05395   80 RSNSLASKSMESFLKVAGMQYLHSVLGPTINRVF--EEKKYVELDPSKVEikdvgcsglhriqtESEVIEQSAQLLQSYL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1386 QKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNIG--AVGTVIFLRFINPAIVSPQELGIVDKQVHSSAKRGL 1463
Cdd:cd05395  158 GELLSAISKSVKYCPAVIRATFRQLFKRVQERFPENQHQNVKfiAVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTL 237
                        250
                 ....*....|..
gi 62472946 1464 MLMSKILQNIAN 1475
Cdd:cd05395  238 LLLAKAVQNVGN 249
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
1286-1542 1.05e-19

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a member of the IQGAP family that contains a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeat, a single WW domain, four IQ motifs which mediate interactions with calmodulin, and a Ras-GTPase-activating protein (GAP)-related domain that binds Rho family GTPases. IQGAP2 and IQGAP3 play important roles in the regulation of the cytoskeleton for axon outgrowth in hippocampal neurons and are thought to stay in a common regulatory pathway. The results of RNA interference studies indicated that IQGAP3 partially compensates functions of IQGAP2, but has lesser ability than IQGAP2 to promote axon outgrowth in hippocampal neuron. Moreover, IQGAP2 is required for the cadherin-mediated cell-to-cell adhesion in Xenopus laevis embryos.


Pssm-ID: 213333 [Multi-domain]  Cd Length: 359  Bit Score: 93.52  E-value: 1.05e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1286 VLVTLFD------AKHLLSPLLWNMFYREVEVS-DCMQTLFRGNSLGSK-IMAFCFKIYGASYLQMLLEPLIRPLLD--- 1354
Cdd:cd05131    3 VIFTLYNyasnqrEEYLLLKLFETALEEEIKSKvDQIQDIVTGNPTVIKmVVSFNRGARGQNTLRQLLAPVVKEIIEdks 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1355 -----------------------EEEETCFEVDP--ARLDP--TEDIEQHRNNLIALTQKVFDAIINSSDRFPPQLRSMC 1407
Cdd:cd05131   83 liintnpvevykawvnqletatgEASKLPYDVTTeqALTHPevVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYIA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1408 HCLYQVLSKRFPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVDK----QVHSSAKRGLMLMSKILQNIANHVEFSKE 1482
Cdd:cd05131  163 KVLKNSLHEKFPDATEDELlKIVGNLLYYRYMNPAIVAPDGFDIIDMtaggQIHSEQRRNLGSVAKVLQHAASNKLFEGE 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62472946 1483 -QHMLCFNDFLRDHFEAGRRFFiQIASDCE------TVDQTSHSMS------FISDANVLALHRLLWTHQEKI 1542
Cdd:cd05131  243 nAHLSSMNSYLSQTYQKFRKFF-QAACDVPepeekfNIDEYSDMVTlskpviYISIEEIINTHSLLLEHQDAI 314
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
1380-1571 2.75e-19

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family represents the IQ motif containing GTPase activating protein 3 (IQGAP3), which associates with Ras GTP-binding proteins. A primary function of IQGAP proteins is to modulate cytoskeletal architecture. There are three known IQGAP family members: IQGAP1, IQGAP2 and IQGAP3. Human IQGAP1 and IQGAP2 share 62% identity. IQGAPs are multi-domain molecules having a calponin-homology (CH) domain which binds F-actin, IQGAP-specific repeats, a single WW domain, four IQ motifs that mediate interactions with calmodulin, and a RasGAP related domain that binds active Rho family GTPases. IQGAP is an essential regulator of cytoskeletal function. IQGAP1 negatively regulates Ras family GTPases by stimulating their intrinsic GTPase activity, the protein actually lacks GAP activity. Both IQGAP1 and IQGAP2 specifically bind to Cdc42 and Rac1, but not to RhoA. Despite of their similarities to part of the sequence of RasGAP, neither IQGAP1 nor IQGAP2 interacts with Ras. IQGAP3, only present in mammals, regulates the organization of the cytoskeleton under the regulation of Rac1 and Cdc42 in neuronal cells. The depletion of IQGAP3 is shown to impair neurite or axon outgrowth in neuronal cells with disorganized cytoskeleton.


Pssm-ID: 213346 [Multi-domain]  Cd Length: 350  Bit Score: 92.20  E-value: 2.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1380 NLIALTQKVFDAIINSSDRFPPQLRSMCHCLYQVLSKRFPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVD----KQ 1454
Cdd:cd12207  135 NLLAVTDKFLSAITSSVDKIPYGMRYVAKVLRDSLQEKFPGASEDEVyKVVGNLLYYRFMNPAVVAPDGFDIVDcsagGA 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1455 VHSSAKRGLMLMSKILQNIANHVEFSKE-QHMLCFNDFLRDHFEAGRRFFIQIASDCE-----TVDQTSHSMS------F 1522
Cdd:cd12207  215 LQPEQRRMLGSVAKVLQHAAANKHFQGDsEHLQALNQYLEETHVKFRKFILQACCVPEpeerfNVDEYSEMVAvakpviY 294
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 62472946 1523 ISDANVLALHRLLWTHQEKIgdylssSRDHKavgrrpfDKMATLLAYLG 1571
Cdd:cd12207  295 ITVGELINTHKLLLEHQDSI------APDHS-------DPLHELLEDLG 330
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
1286-1543 1.13e-17

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a homodimeric protein that is widely expressed among vertebrate cell types from early embryogenesis. Mammalian IQGAP1 protein is the best characterized member of the IQGAP family, and contains several protein-interacting domains. Human IQGAP1 is most similar to mouse Iqgap1 (94% identity) and has 62% identity to human IQGAP2. IQGAP1 binds and cross-links actin filaments in vitro and has been implicated in Ca2+/calmodulin signaling, E-cadherin-dependent cell adhesion, cell motility, and invasion. Yeast IQGAP homologs have a role in the recruitment of actin filaments, are components of the spindle pole body, and are required for actomyosin ring assembly and cytokinesis. Furthermore, IQGAP1 over-expression has also been detected in gastric and colorectal carcinomas and gastric cancer cell lines.


Pssm-ID: 213335  Cd Length: 380  Bit Score: 87.79  E-value: 1.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1286 VLVTLFD------AKHLLSPLLWNMFYREVEVS-DCMQTLFRGNSLGSK-IMAFCFKIYGASYLQMLLEPLIRPLLD--- 1354
Cdd:cd05133    3 VIFTLYNyasnqrEEYLLLRLFKTALQEEIKSKvDQIQEIVTGNPTVIKmVVSFNRGARGQNALRQILAPVVKEIMDdks 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1355 -----------------------EEEETCFEVDPARLDPTEDI----EQHRNNLIALTQKVFDAIINSSDRFPPQLRSMC 1407
Cdd:cd05133   83 lniktdpvdiykswvnqmesqtgEASKLPYDVTPEQAMSHEEVrtrlDASIKNMRMVTDKFLSAIISSVDKIPYGMRFIA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1408 HCLYQVLSKRFPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVD----KQVHSSAKRGLMLMSKILQNIANHVEF-SK 1481
Cdd:cd05133  163 KVLKDTLHEKFPDAGEDELlKIVGNLLYYRYMNPAIVAPDAFDIIDlsagGQLTTDQRRNLGSIAKMLQHAASNKMFlGD 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472946 1482 EQHMLCFNDFLRDHFEAGRRFFiQIASDCET------VDQTSHSMS------FISDANVLALHRLLWTHQEKIG 1543
Cdd:cd05133  243 NAHLSPINEYLSQSYQKFRRFF-QAACDVPEledkfnVDEYSDLVTltkpviYISIGEIINTHTLLLDHQDAIA 315
SEC14 cd00170
Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory ...
1613-1754 3.76e-13

Sec14p-like lipid-binding domain; Sec14p-like lipid-binding domains are found in secretory proteins, such as S. cerevisiae phosphatidylinositol transfer protein (Sec14p), and in lipid regulated proteins such as RhoGAPs, RhoGEFs and neurofibromin (NF1). SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 469559 [Multi-domain]  Cd Length: 156  Bit Score: 69.29  E-value: 3.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1613 EEFKTLKSmNIFYQAGTSKSGYPVFYYIARRYKIGETNGDLLIYHVILTLKPFCHSPFE------VVIDFTHTCSDNRFR 1686
Cdd:cd00170    2 EELLELLG-GIGYLGGRDKEGRPVLVFRAGWDPPKLLDLEELLRYLVYLLEKALRELEEqvegfvVIIDLKGFSLSNLSD 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62472946 1687 TEFLQKWFYVLPTVAYENVHAVYIYNCNSWVREYTKFHDRILAPlKGNRKLLFLES-PNKLTDFIDAEQ 1754
Cdd:cd00170   81 LSLLKKLLKILQDHYPERLKKIYIVNAPWIFSALWKIVKPFLSE-KTRKKIVFLGSdLEELLEYIDPDQ 148
IQG1 COG5261
Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and ...
1293-1475 1.52e-07

Protein involved in regulation of cellular morphogenesis/cytokinesis [Cell division and chromosome partitioning / Signal transduction mechanisms];


Pssm-ID: 227586 [Multi-domain]  Cd Length: 1054  Bit Score: 57.20  E-value: 1.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1293 AKHLLSPLLWNMFYREVEVSDCMQTLFRGNSLGSKIMAFCFKIY--GASYLQML------------LEPLIRPLLDEEee 1358
Cdd:COG5261  433 EEHLSVSLFQMLLRTEVEATSLVQSLLRGNLPVHRNMTNYFRRSqgQAALREIRyqiindvaihedLEVDINPLLVYR-- 510
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1359 tcFEVDPARLDPTEDIEQHRNN--------------------LIALTQKVFDAIINSSDRFPPQLRSMCHcLYQVLSKRF 1418
Cdd:COG5261  511 --ALLNKGQLSPDKDLELLTSNeevseflavmnavqessaklLELSTERILDAVYNSLDEIGYGIRFVCE-LIRVVFELT 587
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472946 1419 PNLLQNNI-----------------GAVGTVIFLRFINPAIVSPQELGIVDKQVhSSAKRGLMLMSKILQNIAN 1475
Cdd:COG5261  588 PNRLFPSIsdsrclrticfaeidslGLIGGFFFLRFVNEALVSPQTSMLKDSCP-SDNVRKLATLSKILQSVFE 660
RasGAP_RAP6 cd05129
Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...
1277-1474 2.95e-07

Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is an endosomal protein with a role in the regulation of receptor-mediated endocytosis. RAP6 contains a Vps9 domain, which is involved in the activation of Rab5, and a Ras GAP domain (RGD). Rab5 is a small GTPase required for the control of the endocytic route, and its activity is regulated by guanine nucleotide exchange factor, such as Rabex5, and GAPs, such as RN-tre. Human Rap6 protein is localized on the plasma membrane and on the endosome. RAP6 binds to Rab5 and Ras through the Vps9 and RGD domains, respectively.


Pssm-ID: 213331  Cd Length: 365  Bit Score: 55.43  E-value: 2.95e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1277 TSQMDELARVLVTL--------FDAKHLLSpLLWNMFYREVEVSDCMQTLFRGNSLGSKIM--AFCFKIYGAS-YLQMLL 1345
Cdd:cd05129   39 LEQTQNVIQTIVTSlygncimpEDERLLLQ-LLRELMELQLKKSDNPRRLLRKGSCAFSRVfkLFTELLFSAKlYLTAAL 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1346 EPLIRPLLDEEEETcFEVDP----ARLDPTE---------------DIEQHR----NNLIALTQKVFDAIINSSDRFPPQ 1402
Cdd:cd05129  118 HKPIMQVLVDDEIF-LETDPqkalCRFSPAEqekrfgeegtpeqqrKLQQYRaeflSRLVALVNKFISSLRQSVYCFPQS 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 62472946 1403 LRSMCHCLYQVLSKRFpNLLQNNIGAVGT-VIFLRFINPAIVSPQELGIVDKQVHSSAKR-GLMLMSKILQNIA 1474
Cdd:cd05129  197 LRWIVRQLRKILTRSG-DDEEAEARALCTdLLFTNFICPAIVNPEQYGIISDAPISEVARhNLMQVAQILQVLA 269
MOR2-PAG1_mid pfam14228
Cell morphogenesis central region; This family is the conserved central region of proteins ...
1931-2086 9.46e-06

Cell morphogenesis central region; This family is the conserved central region of proteins that are involved in cell morphogenesis.


Pssm-ID: 433790 [Multi-domain]  Cd Length: 1113  Bit Score: 51.56  E-value: 9.46e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   1931 IPSNNTIFIKSVSEKLATNEPHLTlEFLEESIQGFQRSTIEL--KHLCLEYMTPWLKNLvkfcksndDSKKLKVS----Q 2004
Cdd:pfam14228  592 LPDSYQQFQYKLSAKLAKDHPELS-ELLCEEIMQRQLDAVDIiaQHQVLTCMAPWIENL--------NFLKLWESgwseR 662
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946   2005 ILDKLINLTIDQKEMYPSVQAKIWGSIGQIPELIDMVLDNFLHKSITYGLGSPQVEIMADTAVALAsanvqlVSKKV--- 2081
Cdd:pfam14228  663 LLKSLYYVTWRHGDQFPDEIEKLWRTIASKPRNISPVLDFLISKGIEDCDSNASAEITGAFATYFS------VAKRVsly 736

                   ....*
gi 62472946   2082 ITRIC 2086
Cdd:pfam14228  737 LARIC 741
RasGAP_IQGAP_related cd12206
Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating ...
1341-1551 4.27e-04

Ras-GTPase Activating Domain of proteins related to IQGAPs; RasGAP: Ras-GTPase Activating Domain. RasGAP functions as an enhancer of the hydrolysis of GTP that is bound to Ras-GTPases. Proteins having a RasGAP domain include p120GAP, IQGAP, Rab5-activating protein 6, and Neurofibromin. Although the Rho (Ras homolog) GTPases are most closely related to members of the Ras family, RhoGAP and RasGAP show no sequence homology at their amino acid level. RasGTPases function as molecular switches in a myriad of signaling pathways. When bound to GTP they are in the on state and when bound to GDP they are in the off state. The RasGap domain speeds up the hydrolysis of GTP in Ras-like proteins acting as a negative regulator.


Pssm-ID: 213345 [Multi-domain]  Cd Length: 359  Bit Score: 45.40  E-value: 4.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1341 LQMLLEPLIRPLLDEEEETcFEVDPAR----------LDPTEDIEQHRN---------NLIALTQKVFDAIINSSDRFPP 1401
Cdd:cd12206   76 LKSIFGPLLVQYLENQEID-FESDPSViykslhgrppLSSEEAIEDDRVsdkfvenltNLREAVEMVAEIIFKNVDKIPV 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1402 QLRSMCHCLYQVLSKRFPNLLQNNI-GAVGTVIFLRFINPAIVSPQELGIVD---------KQVHSSAKRGLMLMSK--- 1468
Cdd:cd12206  155 EIRYLCTKAYIAFADKFPDESEEDIlRAISKILIKSYVAPILVNPENYGFVDneednlnekARVLLQILSMVFFLKNfdg 234
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62472946 1469 ------------------ILQNIANHVEFSKEQHMLCFND---FLRDHFEAGRRFFIQIasdCETVDQTShsmSFISDAN 1527
Cdd:cd12206  235 ylkplnqyieeikpsirdLLKELLDVPEEEQEYDKLIYYDimsTTRPCLEILLDKVIEI---IQILKENL---DEFTPDD 308
                        250       260
                 ....*....|....*....|....
gi 62472946 1528 vlALHRLLwthqEKIGDYLSSSRD 1551
Cdd:cd12206  309 --QLVQLL----EKIVDLSSSSND 326
 
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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