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Conserved domains on  [gi|1840229252|ref|XP_034150658|]
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ras/Rap GTPase-activating protein SynGAP isoform X7 [Esox lucius]

Protein Classification

ras GTPase-activating protein( domain architecture ID 11686121)

ras GTPase-activating protein containing a DUF3498 domain, similar to Danio rerio synaptic Ras GTPase activating protein 1b

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
275-598 0e+00

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: 622.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  275 RYQTMSILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFmDREHLIF 354
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  355 RENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPR 433
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  434 ELKDVFASWRVRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKE 513
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  514 DHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLSKDAILKLGPLPRLLNDISV 593
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                   ....*
gi 1840229252  594 ALRNP 598
Cdd:cd05136    320 ALRNP 324
PH-like super family cl17171
Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like ...
5-196 3.11e-127

Pleckstrin homology-like domain; The PH-like family includes the PH domain, both the Shc-like and IRS-like PTB domains, the ran-binding domain, the EVH1 domain, a domain in neurobeachin and the third domain of FERM. All of these domains have a PH fold, but lack significant sequence similarity. They are generally involved in targeting to protein to the appropriate cellular location or interacting with a binding partner. This domain family possesses multiple functions including the ability to bind inositol phosphates and to other proteins.


The actual alignment was detected with superfamily member cd13375:

Pssm-ID: 473070  Cd Length: 189  Bit Score: 390.21  E-value: 3.11e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252    5 PIAPPQTfrQQSFLSRRLKGSIKRAKSQPKLDRTSSFrHMILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDL 84
Cdd:cd13375      1 PTAPFRP--SQGFLSRRLKSSIKRTKSQPKLDRTSSF-RQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   85 TLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKK 164
Cdd:cd13375     78 NLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKK 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1840229252  165 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 196
Cdd:cd13375    158 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 super family cl26404
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
588-1241 2.93e-107

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


The actual alignment was detected with superfamily member pfam12004:

Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 349.06  E-value: 2.93e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  588 LNDISVALRNPQLHRQashQPDRQQDRLLTRPAFNRLVSSDFQSlMMRDLNSS-IDISRLPSPTsgvsgggvhsshvnmg 666
Cdd:pfam12004    1 LRDITTALTNPTPIQQ---QLRRFSEHSSSPPVPGRSISSGLQK-MFEDPDDGlSDFTRLPSPT---------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  667 sfpdrdpRGSKDIFYVTRPPLARSSPAYCTSSSDITEPDPKVLSVNKSVSMMDLQDSRVNSIS-NLHSVGDMLNSSQASI 745
Cdd:pfam12004   61 -------PENKDLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSpSPPLHDAPLNLSQAGS 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  746 -AGLGhsfgnLGGPARVGGHLSAGSSGGSGLRLSQMggPIYHMGGPTDSLSqqqqqvaaamhfPLSFQNPLFHLAADGP- 823
Cdd:pfam12004  134 qASVG-----LRPAWAARTSQGNPQSAPQVRRPLQT--PVTQGTRPQQLLA------------PLSFQNPVYHMAAGLPv 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  824 --RGQPHGHSQGQPPPLllapepenahhqqgyarafgHGGFSRSEDLSAlrpqSSLVQPSIVHSHSYSDDYTRQNqnAEY 901
Cdd:pfam12004  195 spRGLGSPDSSSETHSS--------------------FSSHSNSEDLSS----AAANKKSGPSNSSYSEDFARRS--TEF 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  902 ARRQLSLQvqeNLQQQILMglTPQTATGTGTPTSVATPPstvhpvrhgsvaPPPPQRLKSQLSISpgatSTPPKARPQSR 981
Cdd:pfam12004  249 TRRQLSLT---ELQHQPAV--PRQNSAGPQRRIDQQGLG------------GPPLTRGRTPPSLL----NSASYPRPSSG 307
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  982 NLllQSPESSFGG---RQNSpqqqqqqqhqlSVKQSDSPApglphqsssardsqgapqggngettdtptkstkqpqqqsq 1058
Cdd:pfam12004  308 SL--MSSSPDWPParlRQQS-----------SSSKGDSPE---------------------------------------- 334
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1059 qqpppqqhlLKPTVNKQGSQSP---ATLTPTpnERTVAWVSNMPHLSADIEiLRSSSNLEDLKLKEysksmdesrmdrvk 1135
Cdd:pfam12004  335 ---------TKQRTQHQQVPSPvnpSTLSPV--ERTAAWVLNMNGQYEEEE-SSGPESREELKQAE-------------- 388
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1136 EYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMAVEDELR-- 1213
Cdd:pfam12004  389 KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKkd 468
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1840229252 1214 ---VSAIPEIKPRMFREQEEDSSSLGSADPQ 1241
Cdd:pfam12004  469 haeMQAVIDSKQKIIDAQEKRIASLDAANAR 499
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
138-284 7.57e-85

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


:

Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 272.64  E-value: 7.57e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  138 PNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYKETDKK 217
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840229252  218 RRKEKSTYLGLVSIPISSITGRQFVEQWYPVIQPSALAKGGSVGsGKVINASIRLKSRYQTMSILPM 284
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKE-GKGESPSIRIKARYQSTRVLPL 146
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
275-598 0e+00

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: 622.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  275 RYQTMSILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFmDREHLIF 354
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  355 RENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPR 433
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  434 ELKDVFASWRVRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKE 513
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  514 DHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLSKDAILKLGPLPRLLNDISV 593
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                   ....*
gi 1840229252  594 ALRNP 598
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
5-196 3.11e-127

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. 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: 270178  Cd Length: 189  Bit Score: 390.21  E-value: 3.11e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252    5 PIAPPQTfrQQSFLSRRLKGSIKRAKSQPKLDRTSSFrHMILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDL 84
Cdd:cd13375      1 PTAPFRP--SQGFLSRRLKSSIKRTKSQPKLDRTSSF-RQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   85 TLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKK 164
Cdd:cd13375     78 NLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKK 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1840229252  165 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 196
Cdd:cd13375    158 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
588-1241 2.93e-107

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 349.06  E-value: 2.93e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  588 LNDISVALRNPQLHRQashQPDRQQDRLLTRPAFNRLVSSDFQSlMMRDLNSS-IDISRLPSPTsgvsgggvhsshvnmg 666
Cdd:pfam12004    1 LRDITTALTNPTPIQQ---QLRRFSEHSSSPPVPGRSISSGLQK-MFEDPDDGlSDFTRLPSPT---------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  667 sfpdrdpRGSKDIFYVTRPPLARSSPAYCTSSSDITEPDPKVLSVNKSVSMMDLQDSRVNSIS-NLHSVGDMLNSSQASI 745
Cdd:pfam12004   61 -------PENKDLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSpSPPLHDAPLNLSQAGS 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  746 -AGLGhsfgnLGGPARVGGHLSAGSSGGSGLRLSQMggPIYHMGGPTDSLSqqqqqvaaamhfPLSFQNPLFHLAADGP- 823
Cdd:pfam12004  134 qASVG-----LRPAWAARTSQGNPQSAPQVRRPLQT--PVTQGTRPQQLLA------------PLSFQNPVYHMAAGLPv 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  824 --RGQPHGHSQGQPPPLllapepenahhqqgyarafgHGGFSRSEDLSAlrpqSSLVQPSIVHSHSYSDDYTRQNqnAEY 901
Cdd:pfam12004  195 spRGLGSPDSSSETHSS--------------------FSSHSNSEDLSS----AAANKKSGPSNSSYSEDFARRS--TEF 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  902 ARRQLSLQvqeNLQQQILMglTPQTATGTGTPTSVATPPstvhpvrhgsvaPPPPQRLKSQLSISpgatSTPPKARPQSR 981
Cdd:pfam12004  249 TRRQLSLT---ELQHQPAV--PRQNSAGPQRRIDQQGLG------------GPPLTRGRTPPSLL----NSASYPRPSSG 307
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  982 NLllQSPESSFGG---RQNSpqqqqqqqhqlSVKQSDSPApglphqsssardsqgapqggngettdtptkstkqpqqqsq 1058
Cdd:pfam12004  308 SL--MSSSPDWPParlRQQS-----------SSSKGDSPE---------------------------------------- 334
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1059 qqpppqqhlLKPTVNKQGSQSP---ATLTPTpnERTVAWVSNMPHLSADIEiLRSSSNLEDLKLKEysksmdesrmdrvk 1135
Cdd:pfam12004  335 ---------TKQRTQHQQVPSPvnpSTLSPV--ERTAAWVLNMNGQYEEEE-SSGPESREELKQAE-------------- 388
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1136 EYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMAVEDELR-- 1213
Cdd:pfam12004  389 KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKkd 468
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1840229252 1214 ---VSAIPEIKPRMFREQEEDSSSLGSADPQ 1241
Cdd:pfam12004  469 haeMQAVIDSKQKIIDAQEKRIASLDAANAR 499
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
266-590 1.30e-105

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: 338.13  E-value: 1.30e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   266 INASIRLKSRYQTMSILPMELYKEFAEYITNNYRT-LCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVD 344
Cdd:smart00323    5 DLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVE 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   345 RfMDREHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKI 424
Cdd:smart00323   85 R-TDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAI 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   425 VNSHCVFPRELKDVFASWRVRCAERGRE-DIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNL 503
Cdd:smart00323  164 INSSDRLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNL 243
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   504 ASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLsKDAILKLGP 583
Cdd:smart00323  244 ANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDAL-KRELNNEDP 322

                    ....*..
gi 1840229252   584 LPRLLND 590
Cdd:smart00323  323 LGKLLFK 329
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
138-284 7.57e-85

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 272.64  E-value: 7.57e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  138 PNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYKETDKK 217
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840229252  218 RRKEKSTYLGLVSIPISSITGRQFVEQWYPVIQPSALAKGGSVGsGKVINASIRLKSRYQTMSILPM 284
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKE-GKGESPSIRIKARYQSTRVLPL 146
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
334-505 3.89e-29

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: 116.23  E-value: 3.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  334 FLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKL-IGHRYLKDAIGEFIRALYESEE-NCEVDPMR----------- 400
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  401 --------------------TPPSVLADHQANLRMCCELALCKIVNSHCVFPREL----KDVFASWRVRCAERGREDIAd 456
Cdd:pfam00616   80 ktgrsdlprdvspeeaiedpEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1840229252  457 RLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLAS 505
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
149-245 7.55e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 60.19  E-value: 7.55e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   149 VLKLWIIEARDLPAKKRY-----YCELCLDDMLY--ARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKKRRK 220
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77
                            90       100
                    ....*....|....*....|....*
gi 1840229252   221 eKSTYLGLVSIPISSITGRQFVEQW 245
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
C2 pfam00168
C2 domain;
148-248 1.65e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.56  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  148 NVLKLWIIEARDLPAKKRY-----YCELCL-DDMLYARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKkRRK 220
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DY-DRF 76
                           90       100
                   ....*....|....*....|....*...
gi 1840229252  221 EKSTYLGLVSIPISSITGRQFVEQWYPV 248
Cdd:pfam00168   77 GRDDFIGEVRIPLSELDSGEGLDGWYPL 104
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
15-137 4.80e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 43.69  E-value: 4.80e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252    15 QSFLSRRLKGSIKRAKSqpkldrtssfRHMILprfrsadqeRTRLMQSFKESHSHESllspSSAAEALDLtlDEDAVIKP 94
Cdd:smart00233    4 EGWLYKKSGGGKKSWKK----------RYFVL---------FNSTLLYYKSKKDKKS----YKPKGSIDL--SGCTVREA 58
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1840229252    95 VHSSILGQEYCFEVTTLSG-TKCFACRSAAERDKWIENLQRAVK 137
Cdd:smart00233   59 PDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1118-1216 8.68e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1118 KLKEYSKSMDESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKI---LSQYQSRLDDSERRLRQQQVEK 1194
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRR 352
                           90       100
                   ....*....|....*....|..
gi 1840229252 1195 DsQIKGIINRLMAVEDELRVSA 1216
Cdd:TIGR02169  353 D-KLTEEYAELKEELEDLRAEL 373
PHA03247 PHA03247
large tegument protein UL36; Provisional
926-1116 1.51e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  926 TATGTGTPTSVATPPSTVHPVRHGSVAPPPPQRLKSQLSISPG----------------ATSTPPKAR-------PQSRN 982
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrrrppsrspaakpAAPARPPVRrlarpavSRSTE 2896
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  983 LLLQSPESSFGGRQNSPQQQQQQQHQLSVKQSDSPAPGLPHQSSSARDSQGAPQGGNGETTDTPTKSTKQPQQQSQQQPP 1062
Cdd:PHA03247  2897 SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840229252 1063 PQQHLLKPTVNKQGSqSPATLTPTPNERTVAWVSNMP-HLSAD------IEILRSSSNLED 1116
Cdd:PHA03247  2977 FRVPQPAPSREAPAS-STPPLTGHSLSRVSSWASSLAlHEETDpppvslKQTLWPPDDTED 3036
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1128-1232 5.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1128 ESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMA 1207
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
                           90       100
                   ....*....|....*....|....*
gi 1840229252 1208 VEDELRvsaipEIKPRMFREQEEDS 1232
Cdd:COG4717    225 LEEELE-----QLENELEAAALEER 244
 
Name Accession Description Interval E-value
RasGAP_DAB2IP cd05136
Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...
275-598 0e+00

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: 622.30  E-value: 0e+00
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  275 RYQTMSILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFmDREHLIF 354
Cdd:cd05136      1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  355 RENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPR 433
Cdd:cd05136     80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPPSaSLSRNQANLRRSVELAWCKILSSHCVFPR 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  434 ELKDVFASWRVRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKE 513
Cdd:cd05136    160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  514 DHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLSKDAILKLGPLPRLLNDISV 593
Cdd:cd05136    240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319

                   ....*
gi 1840229252  594 ALRNP 598
Cdd:cd05136    320 ALRNP 324
PH_SynGAP cd13375
Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...
5-196 3.11e-127

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and neuronal growth-associated protein (nGAP/RASAL2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. Members here include mammals, amphibians, and bony fish. 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: 270178  Cd Length: 189  Bit Score: 390.21  E-value: 3.11e-127
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252    5 PIAPPQTfrQQSFLSRRLKGSIKRAKSQPKLDRTSSFrHMILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDL 84
Cdd:cd13375      1 PTAPFRP--SQGFLSRRLKSSIKRTKSQPKLDRTSSF-RQILPRFRSADHDRARLMQSFKESHSHESLLSPSSAAEALDL 77
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   85 TLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKK 164
Cdd:cd13375     78 NLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARELPPKK 157
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1840229252  165 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 196
Cdd:cd13375    158 RYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189
DUF3498 pfam12004
Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...
588-1241 2.93e-107

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. This domain is found in eukaryotes. This domain is typically between 433 to 538 amino acids in length. This domain is found associated with pfam00616, pfam00168. This domain has two conserved sequence motifs: DLQ and PLSFQNP.


Pssm-ID: 463427 [Multi-domain]  Cd Length: 511  Bit Score: 349.06  E-value: 2.93e-107
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  588 LNDISVALRNPQLHRQashQPDRQQDRLLTRPAFNRLVSSDFQSlMMRDLNSS-IDISRLPSPTsgvsgggvhsshvnmg 666
Cdd:pfam12004    1 LRDITTALTNPTPIQQ---QLRRFSEHSSSPPVPGRSISSGLQK-MFEDPDDGlSDFTRLPSPT---------------- 60
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  667 sfpdrdpRGSKDIFYVTRPPLARSSPAYCTSSSDITEPDPKVLSVNKSVSMMDLQDSRVNSIS-NLHSVGDMLNSSQASI 745
Cdd:pfam12004   61 -------PENKDLFFVTRPPLLQPSPARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSpSPPLHDAPLNLSQAGS 133
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  746 -AGLGhsfgnLGGPARVGGHLSAGSSGGSGLRLSQMggPIYHMGGPTDSLSqqqqqvaaamhfPLSFQNPLFHLAADGP- 823
Cdd:pfam12004  134 qASVG-----LRPAWAARTSQGNPQSAPQVRRPLQT--PVTQGTRPQQLLA------------PLSFQNPVYHMAAGLPv 194
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  824 --RGQPHGHSQGQPPPLllapepenahhqqgyarafgHGGFSRSEDLSAlrpqSSLVQPSIVHSHSYSDDYTRQNqnAEY 901
Cdd:pfam12004  195 spRGLGSPDSSSETHSS--------------------FSSHSNSEDLSS----AAANKKSGPSNSSYSEDFARRS--TEF 248
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  902 ARRQLSLQvqeNLQQQILMglTPQTATGTGTPTSVATPPstvhpvrhgsvaPPPPQRLKSQLSISpgatSTPPKARPQSR 981
Cdd:pfam12004  249 TRRQLSLT---ELQHQPAV--PRQNSAGPQRRIDQQGLG------------GPPLTRGRTPPSLL----NSASYPRPSSG 307
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  982 NLllQSPESSFGG---RQNSpqqqqqqqhqlSVKQSDSPApglphqsssardsqgapqggngettdtptkstkqpqqqsq 1058
Cdd:pfam12004  308 SL--MSSSPDWPParlRQQS-----------SSSKGDSPE---------------------------------------- 334
                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1059 qqpppqqhlLKPTVNKQGSQSP---ATLTPTpnERTVAWVSNMPHLSADIEiLRSSSNLEDLKLKEysksmdesrmdrvk 1135
Cdd:pfam12004  335 ---------TKQRTQHQQVPSPvnpSTLSPV--ERTAAWVLNMNGQYEEEE-SSGPESREELKQAE-------------- 388
                          570       580       590       600       610       620       630       640
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1136 EYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMAVEDELR-- 1213
Cdd:pfam12004  389 KYEQEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMAVEEELKkd 468
                          650       660       670
                   ....*....|....*....|....*....|.
gi 1840229252 1214 ---VSAIPEIKPRMFREQEEDSSSLGSADPQ 1241
Cdd:pfam12004  469 haeMQAVIDSKQKIIDAQEKRIASLDAANAR 499
RasGAP smart00323
GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...
266-590 1.30e-105

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: 338.13  E-value: 1.30e-105
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   266 INASIRLKSRYQTMSILPMELYKEFAEYITNNYRT-LCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVD 344
Cdd:smart00323    5 DLGSLRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVE 84
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   345 RfMDREHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKI 424
Cdd:smart00323   85 R-TDDPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAI 163
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   425 VNSHCVFPRELKDVFASWRVRCAERGRE-DIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNL 503
Cdd:smart00323  164 INSSDRLPYGLRDICKQLRQAAEKRFPDaDVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNL 243
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   504 ASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGRELSMLHSLLWEVMAQLsKDAILKLGP 583
Cdd:smart00323  244 ANLSEFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDAL-KRELNNEDP 322

                    ....*..
gi 1840229252   584 LPRLLND 590
Cdd:smart00323  323 LGKLLFK 329
PH_DAB2IP cd13376
DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...
17-196 1.66e-91

DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also called AIP1/ASK1-interacting protein-1 and DIP1/2) is a member of the RasSynGAP family along with Synaptic Ras-GTPase activating protein (SynGAP) and neuronal growth-associated protein (nGAP/RASAL2). DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. Human DAB2IP is expressed in the adrenal gland, pancreas, endocardium, stomach, kidney, testis, small intestine, liver, trachea, skin, ovary, endometrium, lung, esophagus and bladder. No expression was observed in the cerebrum, parotid gland, thymus, thyroid gland and spleen. 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: 270179  Cd Length: 182  Bit Score: 292.76  E-value: 1.66e-91
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   17 FLSRRLKGSIKRAKSQPKLDRTSSFRHmILPRFRSADQERTRLMQSFKESHSHESLLSPSSAAEALDLTLDEDAVIKPVH 96
Cdd:cd13376      4 FLSRRLKGSIKRTKSQPKLDRNSSFRH-ILPGFRSVDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEEVVIKPVH 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   97 SSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDML 176
Cdd:cd13376     83 SSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCELCLDDVL 162
                          170       180
                   ....*....|....*....|
gi 1840229252  177 YARTTSKPRTDTVFWGEHFE 196
Cdd:cd13376    163 YARTTCKLKTDNVFWGEHFE 182
C2_SynGAP_like cd04013
C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...
138-284 7.57e-85

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and neurofibromin are all members of the Ras-specific GAP (GTPase-activating protein) family. SynGAP regulates the MAP kinase signaling pathway and is critical for cognition and synapse function. Mutations in this gene causes mental retardation in humans. SynGAP contains a PH-like domain, a C2 domain, and a Ras-GAP domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175980 [Multi-domain]  Cd Length: 146  Bit Score: 272.64  E-value: 7.57e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  138 PNKDNSRRVDNVLKLWIIEARDLPAKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYKETDKK 217
Cdd:cd04013      1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840229252  218 RRKEKSTYLGLVSIPISSITGRQFVEQWYPVIQPSALAKGGSVGsGKVINASIRLKSRYQTMSILPM 284
Cdd:cd04013     81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGNGKSGGKE-GKGESPSIRIKARYQSTRVLPL 146
RasGAP cd04519
Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...
285-539 5.84e-74

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: 246.63  E-value: 5.84e-74
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  285 ELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAI 364
Cdd:cd04519      1 EEYRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNTKN-PNTLFRGNSLATKLL 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  365 EEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKIVNSHCVFPRELKDVFASWRV 444
Cdd:cd04519     80 DQYMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILRE 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  445 RCAERGRED--IADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEF 522
Cdd:cd04519    160 FLAERFPEEpdEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDF 239
                          250
                   ....*....|....*..
gi 1840229252  523 LEMEWGSMQQFLYEISN 539
Cdd:cd04519    240 IKSNKPKLKQFLDELSS 256
PH_RasSynGAP-like cd13262
Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...
17-146 1.25e-52

Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP family is composed of members: DAB2IP, nGAP, and SynGAP. Neuronal growth-associated proteins (nGAPs) are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). SynGAP, a neuronal Ras-GAP, has been shown display both Ras-GAP activity and Ras-related protein (Rap)-GAP activity. Saccharomyces cerevisiae Bud2 and GAP1 members CAPRI (Ca2+-promoted Ras inactivator) and RASAL (Ras-GTPase-activating-like protein) also possess this dual activity. Human DOC-2/DAB2-interacting protein (DAB2IP) is encoded by a tumor suppressor gene and a newly recognized member of the Ras-GTPase-activating family. DAB2IP is a critical component of many signal transduction pathways mediated by Ras and tumor necrosis factors including apoptosis pathways, and it is involved in the formation of many types of tumors. DAB2IP participates in regulation of gene expression and pluripotency of cells. It has been reported that DAB2IP was expressed in different tumor tissues. Little information is available concerning the expression levels of DAB2IP in normal tissues and cells, however, and no studies of its expression patterns during the development of human embryos have been reported. DAB2IP was expressed primarily in cell cytoplasm throughout the fetal development. The expression levels varied among tissues and different gestational ages. 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: 270082  Cd Length: 125  Bit Score: 180.32  E-value: 1.25e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   17 FLSRRLKGSIKRAKSQPKLDRTSSFRhmiLPRFRSADQERtrlMQSFKESHSHESLLSPSSAAEalDLTLDEDAVIKPVH 96
Cdd:cd13262      4 FFSRRLKGPLKRTKSVTKLERKSSKR---LPRTRLARAPA---GPRLRGSRSHESLLSSSSAAL--DLSADEDVVIRPLH 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1840229252   97 SSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRV 146
Cdd:cd13262     76 SSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125
PH_nGAP cd13373
Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...
12-152 2.78e-52

Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2/RAS protein activator like-3) is a member of the RasSynGAP family along with DOC-2/DAB2-interacting protein (DAB2IP) and synaptic RasGAP (SynGAP). nGAPs are growth cone markers found in multiple types of neurons. There are many nGAPs including Cap1 (Adenylate cyclase-associated protein 1), Capzb (Capping protein (actin filament) muscle Z-line, beta), Clptm1 (Cleft lip and palate associated transmembrane protein 1), Cotl1 (Coactosin-like 1), Crmp1 (Collapsin response mediator protein 1), Cyfip1 (Cytoplasmic FMR1 interacting protein 1), Fabp7 (Fatty acid binding protein 7, brain), Farp2 (FERM, RhoGEF and pleckstrin domain protein 2), Gap43 (Growth associated protein 43), Gnao1 (Guanine nucleotide binding protein (G protein), alpha activating activity polypeptide O), Gnai2 (Guanine nucleotide binding protein (G protein), alpha inhibiting 2), Pacs1 (Phosphofurin acidic cluster sorting protein 1), Rtn1 (Reticulon 1), Sept2 (Septin 2), Snap25 (Synaptosomal-associated protein 25), Strap (Serine/threonine kinase receptor associated protein), Stx7 (Syntaxin 7), and Tmod2 (Tropomodulin 2). PH domains are only found in eukaryotes. They share little sequence conservation, but all have a common fold, which is electrostatically polarized. 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: 270176  Cd Length: 138  Bit Score: 179.92  E-value: 2.78e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   12 FRQQSFLSRRLKGSIKRAKSQPKLDRTSSFRhmiLPRFRSADqERTRLMQSFKESHSHESLLSPSSAAEALDLTLDEDAV 91
Cdd:cd13373      2 FKVSGFFSKRLKGSIKRTKSQSKLDRNTSFR---LPSLRSAD-DRSRGLPKLKESRSHESLLSPGSAVEALDLGREEKVS 77
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840229252   92 IKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKL 152
Cdd:cd13373     78 VKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138
RasGAP_GAP1_like cd05128
Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...
298-538 2.90e-51

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: 182.07  E-value: 2.90e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  298 YRTLCAVLEPLLSVkSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAIEEYLKLIGHRYLK 377
Cdd:cd05128     20 TASAVYLLEELVKV-DKDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLH 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  378 DAIGEFIRALYESEENCEVDPMRTP-PSVLADHQANLRMCCELALCKIVNS--HCvfPRELKDVFASWRVRCAER--GRE 452
Cdd:cd05128     98 ETLKPVIDEIFSEKKSCEIDPSKLKdGEVLETNLANLRGYVERVFKAITSSarRC--PTLMCEIFSDLRESAAQRfpDNE 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  453 DIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASF----SKFSGKEDHMC-FMNEFLEMEW 527
Cdd:cd05128    176 DVPYTAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLgsssSGLGVKEAYMSpLYERFTDEQH 255
                          250
                   ....*....|..
gi 1840229252  528 -GSMQQFLYEIS 538
Cdd:cd05128    256 vDAVKKFLDRIS 267
RasGAP_CLA2_BUD2 cd05137
Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...
281-524 3.18e-50

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: 181.99  E-value: 3.18e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  281 ILPMELYKEFAEYITNNYRTLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVD-------------RFM 347
Cdd:cd05137      9 VLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsknkdmgKSS 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  348 DREH-LIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSV-------LADHQANLRMCCEL 419
Cdd:cd05137     89 NNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESDsiekeedLEENWENLISLTEE 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  420 ALCKIVNSHCVFPRELKDVFASWRvRCAERGREDIADRL----ISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTL 495
Cdd:cd05137    169 IWNSIYITSNDCPPELRKILKHIR-AKVEDRYGDFLRTVtlnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPRAQRTLTL 247
                          250       260
                   ....*....|....*....|....*....
gi 1840229252  496 IAKVVQNLASFSKFSGKEDHMCFMNEFLE 524
Cdd:cd05137    248 IAKVLQNLANLTTFGQKEPWMEPMNEFLT 276
RasGAP_Neurofibromin_like cd05392
Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...
283-542 2.21e-42

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: 158.22  E-value: 2.21e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  283 PMELYKEFAEYITNNYRTLCAVLEpLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRfMDREHLIFRENTLATK 362
Cdd:cd05392      2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISH-TSRAADLFRRNSVATR 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  363 AIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSVLADHQANLRMCCELALCKIVNSHCVFPRELKDVFASW 442
Cdd:cd05392     80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  443 RvRCAERGREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEF 522
Cdd:cd05392    160 Y-ESVSKKFPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238
                          250       260
                   ....*....|....*....|
gi 1840229252  523 LEMEWGSMQQFLYEISNMDT 542
Cdd:cd05392    239 LKKNSDRIQQFLSEVSTIPP 258
RasGAP_RASA3 cd05134
Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...
312-539 3.49e-37

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: 141.31  E-value: 3.49e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  312 KSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESE 391
Cdd:cd05134     33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  392 ENCEVDPMRTPPSV-LADHQANLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAERGREDIADRL--ISSSLFLRFL 468
Cdd:cd05134    112 KPCEIDPVKLKDGEnLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRFQVDPDVRYtaVSSFIFLRFF 191
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1840229252  469 CPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSK---FSGKEDHMC-FMNEFLEMEWG-SMQQFLYEISN 539
Cdd:cd05134    192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKsksANFKESYMAaFYDYFNEQKYAdAVKNFLDLISS 267
RasGAP_RASAL cd05135
Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...
300-541 7.72e-32

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: 126.47  E-value: 7.72e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  300 TLCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKLIGHRYLKDA 379
Cdd:cd05135     26 TPLAMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEV 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  380 IGEFIRALYESEENCEVDPMRTPPS---------VLADHQ------ANLRMCCELALCKIVNSHCVFPRELKDVFASWRV 444
Cdd:cd05135    105 LKPVINRIFEEKKYVELDPCKIDLNrtrrisfkgSLSEAQvresslELLQGYLGSIIDAIVGSVDQCPPVMRVAFKQLHK 184
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  445 RCAER----GREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSK--FSGKEDHMCF 518
Cdd:cd05135    185 RVEERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLGLqlGQGKEQWMAP 264
                          250       260
                   ....*....|....*....|...
gi 1840229252  519 MNEFLEMEWGSMQQFLYEISNMD 541
Cdd:cd05135    265 LHPFILQSVARVKDFLDRLIDID 287
RasGAP_p120GAP cd05391
Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...
281-565 1.05e-31

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: 127.22  E-value: 1.05e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  281 ILPMELYKEFAEYITNnyrtlcavlEPLLSVKSKEEV--------AYALVHILQSTGKAKDFLSDMAMCEVDRfMDREHL 352
Cdd:cd05391      4 IMPEEEYSELKELILQ---------KELHVVYALAHVcgqdrtllASILLRIFRHEKLESLLLRTLNDREISM-EDEATT 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  353 IFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEENCEVDPMRTPPSvlADHQANLRMCCELALC---KIVNSHC 429
Cdd:cd05391     74 LFRATTLASTLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKN--EDVNTNLEHLLNILSElveKIFMAAE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  430 VFPRELKDVFASWRVRCAERGRED--IADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFS 507
Cdd:cd05391    152 ILPPTLRYIYGCLQKSVQQKWPTNttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLV 231
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1840229252  508 KFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNM-DTGSNVGGFEGyiDLGRELSMLHSL 565
Cdd:cd05391    232 EFGAKEPYMEGVNPFIKKNKERMIMFLDELGNVpELPDTTEHSRT--DLSRDLAALHEI 288
RasGAP_Neurofibromin cd05130
Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...
316-568 7.74e-30

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: 122.05  E-value: 7.74e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  316 EVAYALVHILQSTGKAKDFLSDMAMCEVDrFMDREHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESEE--N 393
Cdd:cd05130     41 ELARVLVTLFDSKHLLYQLLWNMFSKEVE-LADSMQTLFRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  394 CEVDPMRTPPS-VLADHQANLRMCCELALCKIVNSHCVFPRELKDV-FASWRVRCAeRGREDIADRLiSSSLFLRFLCPA 471
Cdd:cd05130    120 YEVDPTRLEGNeNLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVcHCLYQVVSH-RFPNSGLGAV-GSAIFLRFINPA 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  472 IMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSgKEDHMCFMNEFLEMEWGSMQQFLYEISNMdtGSNVGGFEG 551
Cdd:cd05130    198 IVSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLFT-KEAHMLPFNDFLRNHFEAGRRFFSSIASD--CGAVDGPSS 274
                          250       260
                   ....*....|....*....|.
gi 1840229252  552 ----YIDLGRELSmLHSLLWE 568
Cdd:cd05130    275 kylsFINDANVLA-LHRLLWN 294
RasGAP pfam00616
GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...
334-505 3.89e-29

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: 116.23  E-value: 3.89e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  334 FLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKL-IGHRYLKDAIGEFIRALYESEE-NCEVDPMR----------- 400
Cdd:pfam00616    1 LISELIEEEIESSDNPNDL-LRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  401 --------------------TPPSVLADHQANLRMCCELALCKIVNSHCVFPREL----KDVFASWRVRCAERGREDIAd 456
Cdd:pfam00616   80 ktgrsdlprdvspeeaiedpEVRQIFEDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKFPDASEEEIL- 158
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1840229252  457 RLISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLAS 505
Cdd:pfam00616  159 NAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207
RasGAP_RASA2 cd05394
Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...
312-539 6.93e-28

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: 114.61  E-value: 6.93e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  312 KSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDrEHLIFRENTLATKAIEEYLKLIGHRYLKDAIGEFIRALYESE 391
Cdd:cd05394     33 RDKYDAVLPLVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESP 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  392 ENCEVDPMRTPPSVLAD-HQANLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAERGRED--IADRLISSSLFLRFL 468
Cdd:cd05394    112 KPCEIDPIKLKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRFPNDphVQYSAVSSFVFLRFF 191
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1840229252  469 CPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSG------KEDHMC-FMNEFLEMEW-GSMQQFLYEISN 539
Cdd:cd05394    192 AVAVVSPHTFQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMCdFFKMFQEEKYiEKVKKFLDEISS 270
PH_RASAL3 cd13374
RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...
68-161 4.66e-27

RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras GTPase-activating protein. It is involved in positive regulation of Ras GTPase activity and of small GTPase mediated signal transduction as well as negative regulation of Ras protein signal transduction. It contains a PH domain, a C2 domain, and a Ras-GAP domain. 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: 270177  Cd Length: 146  Bit Score: 108.18  E-value: 4.66e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   68 SHESLLSPSSAAEaLDLTLDEDAVIKPVHSSILGQEYCFEVTTLSGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVD 147
Cdd:cd13374     50 ALGSRESLATISE-LDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAAERDRWIEDLRRSFQPHQDNVEREE 128
                           90
                   ....*....|....
gi 1840229252  148 NVLKLWIIEARDLP 161
Cdd:cd13374    129 TWLSVWVHEAKGLP 142
RasGAP_RASA4 cd05395
Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...
301-516 1.65e-22

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: 99.18  E-value: 1.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  301 LCAVLEPLLSVKSKEEVAYALVHILQSTGKAKDFLSDMAMCEVDRFMDREHLiFRENTLATKAIEEYLKLIGHRYLKDAI 380
Cdd:cd05395     27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  381 GEFIRALYESEENCEVDP---------------MRTPPSVLADHQANLRMCCELALCKIVNSHCVFPRELKDVFASWRVR 445
Cdd:cd05395    106 GPTINRVFEEKKYVELDPskveikdvgcsglhrIQTESEVIEQSAQLLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1840229252  446 CAERGREDIADRL----ISSSLFLRFLCPAIMSPSLFNLTQEYPGERTSRTLTLIAKVVQNLASFSKFSG--KEDHM 516
Cdd:cd05395    186 VQERFPENQHQNVkfiaVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraKEAWM 262
RasGAP_GAPA cd05132
Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...
372-623 4.67e-19

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: 90.49  E-value: 4.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  372 GHRYLKDAIGEFIRALYESEE-NCEVDPMR-----------------------TPPSVLADH------QANLRMCCELA- 420
Cdd:cd05132     67 GQSYLKTVLADRINDLISLKDlNLEINPLKvyeqmindieldtglpsnlprgiTPEEAAENPavqniiEPRLEMLEEITn 146
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  421 --LCKIVNSHCVFP----------RELKdvfaswRVRCAERGREDIADrLISSSLFLRFLCPAIMSPSLFNLTQEYPGER 488
Cdd:cd05132    147 sfLEAIINSLDEVPygirwickqiRSLT------RRKFPDASDETICS-LIGGFFLLRFINPAIVSPQAYMLVDGKPSDN 219
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  489 TSRTLTLIAKVVQNLASFSKFSgKEDHMCFMNEFLEMEWGSMQQFLYEISNMDTGSNVGGFEGYIDLGR----------E 558
Cdd:cd05132    220 TRRTLTLIAKLLQNLANKPSYS-KEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALSKkdlsinitlnE 298
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1840229252  559 LSMLHSLLWEVMAQLSKDAILKLGPLPRLLNdisvalrnpqlhrQASHQPDRQQDRLLTRPAFNR 623
Cdd:cd05132    299 IYNTHSLLVKHLAELAPDHNDHLRLILQELG-------------PAPPQVPRKENRTIELPLYSR 350
C2 cd00030
C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...
150-247 9.77e-13

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 175973 [Multi-domain]  Cd Length: 102  Bit Score: 65.55  E-value: 9.77e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  150 LKLWIIEARDLPAKKR-----YYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNL-PAIRSLRLHLYketDKKRRKeKS 223
Cdd:cd00030      1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLdPESDTLTVEVW---DKDRFS-KD 76
                           90       100
                   ....*....|....*....|....*
gi 1840229252  224 TYLGLVSIPISSITGR-QFVEQWYP 247
Cdd:cd00030     77 DFLGEVEIPLSELLDSgKEGELWLP 101
C2_Ras_p21A1 cd08400
C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating ...
150-276 1.47e-12

C2 domain present in RAS p21 protein activator 1 (RasA1); RasA1 is a GAP1 (GTPase activating protein 1), a Ras-specific GAP member, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA1 contains a C2 domain, a Ras-GAP domain, a pleckstrin homology (PH)-like domain, a SH3 domain, and 2 SH2 domains. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176045 [Multi-domain]  Cd Length: 126  Bit Score: 65.85  E-value: 1.47e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  150 LKLWIIEARDLPAKK--RYYCELCLDDMLYARTTSKPRTDTVfWGEHFEFNNLPA-IRSLRLHLYKetdkKRRKEKSTYL 226
Cdd:cd08400      6 LQLNVLEAHKLPVKHvpHPYCVISLNEVKVARTKVREGPNPV-WSEEFVFDDLPPdVNSFTISLSN----KAKRSKDSEI 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1840229252  227 GLVSIPISSITGRQFVEQWYPVIqPSALAKGGSVGsgkvinaSIRLKSRY 276
Cdd:cd08400     81 AEVTVQLSKLQNGQETDEWYPLS-SASPLKGGEWG-------SLRIRARY 122
C2 smart00239
Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...
149-245 7.55e-11

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, protein kinases C, and synaptotagmins (among others). Some do not appear to contain Ca2+-binding sites. Particular C2s appear to bind phospholipids, inositol polyphosphates, and intracellular proteins. Unusual occurrence in perforin. Synaptotagmin and PLC C2s are permuted in sequence with respect to N- and C-terminal beta strands. SMART detects C2 domains using one or both of two profiles.


Pssm-ID: 214577 [Multi-domain]  Cd Length: 101  Bit Score: 60.19  E-value: 7.55e-11
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252   149 VLKLWIIEARDLPAKKRY-----YCELCLDDMLY--ARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKKRRK 220
Cdd:smart00239    1 TLTVKIISARNLPPKDKGgksdpYVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77
                            90       100
                    ....*....|....*....|....*
gi 1840229252   221 eKSTYLGLVSIPISSITGRQFVEQW 245
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101
C2A_RasGAP cd08383
C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...
150-276 1.29e-10

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. The proteins here all contain either a single C2 domain or two tandem C2 domains, a Ras-GAP domain, and a pleckstrin homology (PH)-like domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-I topology.


Pssm-ID: 176029 [Multi-domain]  Cd Length: 117  Bit Score: 59.97  E-value: 1.29e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  150 LKLWIIEARDLPAKK--RYYCELCLDDMLYARTTSKPRTDTvFWGEHFEFNNLPA-IRSLRLHLY-KETDKKRRKeksty 225
Cdd:cd08383      2 LRLRILEAKNLPSKGtrDPYCTVSLDQVEVARTKTVEKLNP-FWGEEFVFDDPPPdVTFFTLSFYnKDKRSKDRD----- 75
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1840229252  226 LGLVSIPISSITGRQFVEQWYPVIqpSALAKGGSVGsgkvinaSIRLKSRY 276
Cdd:cd08383     76 IVIGKVALSKLDLGQGKDEWFPLT--PVDPDSEVQG-------SVRLRARY 117
C2 pfam00168
C2 domain;
148-248 1.65e-09

C2 domain;


Pssm-ID: 425499 [Multi-domain]  Cd Length: 104  Bit Score: 56.56  E-value: 1.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  148 NVLKLWIIEARDLPAKKRY-----YCELCL-DDMLYARTTSKPRTDTVFWGEHFEFN-NLPAIRSLRLHLYketDKkRRK 220
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGNgtsdpYVKVYLlDGKQKKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DY-DRF 76
                           90       100
                   ....*....|....*....|....*...
gi 1840229252  221 EKSTYLGLVSIPISSITGRQFVEQWYPV 248
Cdd:pfam00168   77 GRDDFIGEVRIPLSELDSGEGLDGWYPL 104
RasGAP_IQGAP_like cd05127
Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...
342-591 2.69e-07

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: 54.13  E-value: 2.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  342 EVDRFMDREHLIFRENTLATKAIEEYLK-LIGHRYLKDAIGEFIRALYESEE-NCEVDP------------MRT------ 401
Cdd:cd05127     21 EIESKVSLPEDIVTGNPTVIKLVVNYNRgPRGQKYLRELLGPVVKEILDDDDlDLETDPvdiykawinqeeSRTgepskl 100
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  402 PPSV--------------LADHQANLRMCCELALCKIVNSHCVFP-------RELKDvfaSWRVRCAERGREDIAdRLIS 460
Cdd:cd05127    101 PYDVtreqalkdpevrkrLIEHLEKLRAITDKFLTAITESLDKMPygmryiaKVLKE---ALREKFPDAPEEEIL-KIVG 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  461 SSLFLRFLCPAIMSPSLFNLTQEYPGERTS----RTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYE 536
Cdd:cd05127    177 NLLYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLE 256
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1840229252  537 IS---------NMDTGSNVGGFEG---YIDLgRELSMLHSLLWEVMAQLSKD------AILK-LGPLPRLLNDI 591
Cdd:cd05127    257 ACtvpeaeehfNIDEYSDLTMLTKptiYISL-QEIFATHKLLLEHQDEIAPDpddplrELLDdLGPAPTIESLL 329
RasGAP_IQGAP2 cd05131
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...
401-578 5.23e-07

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: 53.46  E-value: 5.23e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  401 TPPSVLADHQA---NLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAER---GREDIADRLISSSLFLRFLCPAIMS 474
Cdd:cd05131    121 THPEVVNKLESsiqSLRSVTDKVLGSIFSSLDLIPYGMRYIAKVLKNSLHEKfpdATEDELLKIVGNLLYYRYMNPAIVA 200
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  475 PSLFNLTQEYPG----ERTSRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLYEISNM---DTGSNVG 547
Cdd:cd05131    201 PDGFDIIDMTAGgqihSEQRRNLGSVAKVLQHAASNKLFEGENAHLSSMNSYLSQTYQKFRKFFQAACDVpepEEKFNID 280
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1840229252  548 GFEGYIDLGR--------ELSMLHSLLWEvmaqlSKDAI 578
Cdd:cd05131    281 EYSDMVTLSKpviyisieEIINTHSLLLE-----HQDAI 314
C2A_RasA2_RasA3 cd08401
C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...
149-251 1.97e-06

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase activating protein 1s ), Ras-specific GAP members, which suppresses Ras function by enhancing the GTPase activity of Ras proteins resulting in the inactive GDP-bound form of Ras. In this way it can control cellular proliferation and differentiation. RasA2 and RasA3 are both inositol 1,3,4,5-tetrakisphosphate-binding proteins and contain an N-terminal C2 domain, a Ras-GAP domain, a pleckstrin-homology (PH) domain which localizes it to the plasma membrane, and Bruton's Tyrosine Kinase (BTK) a zinc binding domain. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 176046 [Multi-domain]  Cd Length: 121  Bit Score: 48.20  E-value: 1.97e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  149 VLKLWIIEARDLPAKKR------YYCELCLDDMLYARTTSKPRTDTVFWGEHFEFNNLPAIRSLRLHLYkETDKKRRkek 222
Cdd:cd08401      1 SLKIKIGEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIY-DRDVLRR--- 76
                           90       100
                   ....*....|....*....|....*....
gi 1840229252  223 STYLGLVSIPISSITGRQFVEQWYPvIQP 251
Cdd:cd08401     77 DSVIGKVAIKKEDLHKYYGKDTWFP-LQP 104
C2A_MCTP_PRT_plant cd04022
C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...
154-247 2.26e-06

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); plant subset; MCTPs are involved in Ca2+ signaling at the membrane. Plant-MCTPs are composed of a variable N-terminal sequence, four C2 domains, two transmembrane regions (TMRs), and a short C-terminal sequence. It is one of four protein classes that are anchored to membranes via a transmembrane region; the others being synaptotagmins, extended synaptotagmins, and ferlins. MCTPs are the only membrane-bound C2 domain proteins that contain two functional TMRs. MCTPs are unique in that they bind Ca2+ but not phospholipids. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-II topology.


Pssm-ID: 175989 [Multi-domain]  Cd Length: 127  Bit Score: 48.10  E-value: 2.26e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  154 IIEARDLPAKKRY-----YCELCLDDMLYaRTTSKPRTDTVFWGEHFEFN--NLPAIRSLRLHLYKEtDKKRRKEKSTYL 226
Cdd:cd04022      6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFNvsDPSRLSNLVLEVYVY-NDRRSGRRRSFL 83
                           90       100
                   ....*....|....*....|..
gi 1840229252  227 GLVSIPISSITGRQ-FVEQWYP 247
Cdd:cd04022     84 GRVRISGTSFVPPSeAVVQRYP 105
RasGAP_IQGAP1 cd05133
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...
412-591 3.62e-06

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: 50.81  E-value: 3.62e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  412 NLRMCCELALCKIVNSHCVFPRELKDVFASWRVRCAER---GREDIADRLISSSLFLRFLCPAIMSPSLFNLTQEYPGER 488
Cdd:cd05133    135 NMRMVTDKFLSAIISSVDKIPYGMRFIAKVLKDTLHEKfpdAGEDELLKIVGNLLYYRYMNPAIVAPDAFDIIDLSAGGQ 214
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  489 TS----RTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEMEWGSMQQFLY---EISNMDTGSNVGGFEG---------Y 552
Cdd:cd05133    215 LTtdqrRNLGSIAKMLQHAASNKMFLGDNAHLSPINEYLSQSYQKFRRFFQaacDVPELEDKFNVDEYSDlvtltkpviY 294
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1840229252  553 IDLGrELSMLHSLLWEvmaqlSKDAILKL--GPLPRLLNDI 591
Cdd:cd05133    295 ISIG-EIINTHTLLLD-----HQDAIAPEhnDPIHELLDDL 329
C2A_C2C_Synaptotagmin_like cd08391
C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...
149-267 4.01e-06

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains either the first or third repeat in Synaptotagmin-like proteins with a type-I topology.


Pssm-ID: 176037 [Multi-domain]  Cd Length: 121  Bit Score: 47.29  E-value: 4.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  149 VLKLWIIEARDLPAKKRY-----------YCELCLDDMLYARTTSKPRTDTVfWGEHFEF--NNLPAiRSLRLHLY-KET 214
Cdd:cd08391      2 VLRIHVIEAQDLVAKDKFvgglvkgksdpYVIVRVGAQTFKSKVIKENLNPK-WNEVYEAvvDEVPG-QELEIELFdEDP 79
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1840229252  215 DKkrrkekSTYLGLVSIPISSITGRQFVEQWYPVIqpsalakggSVGSGKVIN 267
Cdd:cd08391     80 DK------DDFLGRLSIDLGSVEKKGFIDEWLPLE---------DVKSGRLHL 117
RasGAP_IQGAP3 cd12207
Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...
452-591 6.81e-06

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: 49.83  E-value: 6.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  452 EDIADRLISSSLFLRFLCPAIMSPSLFNLTQE------YPGERtsRTLTLIAKVVQNLASFSKFSGKEDHMCFMNEFLEM 525
Cdd:cd12207    178 EDEVYKVVGNLLYYRFMNPAVVAPDGFDIVDCsaggalQPEQR--RMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEE 255
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1840229252  526 EWGSMQQFLY---------EISNMDTGS---NVGGFEGYIDLGrELSMLHSLLWEVMAQLSKDailKLGPLPRLLNDI 591
Cdd:cd12207    256 THVKFRKFILqaccvpepeERFNVDEYSemvAVAKPVIYITVG-ELINTHKLLLEHQDSIAPD---HSDPLHELLEDL 329
C2A_Synaptotagmin-like cd04024
C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a ...
149-265 1.94e-05

C2 domain first repeat present in Synaptotagmin-like proteins; Synaptotagmin is a membrane-trafficking protein characterized by a N-terminal transmembrane region, a linker, and 2 C-terminal C2 domains. Previously all synaptotagmins were thought to be calcium sensors in the regulation of neurotransmitter release and hormone secretion, but it has been shown that not all of them bind calcium. Of the 17 identified synaptotagmins only 8 bind calcium (1-3, 5-7, 9, 10). The function of the two C2 domains that bind calcium are: regulating the fusion step of synaptic vesicle exocytosis (C2A) and binding to phosphatidyl-inositol-3,4,5-triphosphate (PIP3) in the absence of calcium ions and to phosphatidylinositol bisphosphate (PIP2) in their presence (C2B). C2B also regulates also the recycling step of synaptic vesicles. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. This cd contains the first C2 repeat, C2A, and has a type-I topology.


Pssm-ID: 175990 [Multi-domain]  Cd Length: 128  Bit Score: 45.49  E-value: 1.94e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  149 VLKLWIIEARDLPAKKRY-------YCELCLDDmlyarttSKPRTDTVF------WGEHFEFNNLPAIRSLrLHLyKETD 215
Cdd:cd04024      2 VLRVHVVEAKDLAAKDRSgkgksdpYAILSVGA-------QRFKTQTIPntlnpkWNYWCEFPIFSAQNQL-LKL-ILWD 72
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1840229252  216 KKRRKEKStYLGLVSIPISSITGRQFVEQ---WYPViqPSALAKGGSVGSGKV 265
Cdd:cd04024     73 KDRFAGKD-YLGEFDIALEEVFADGKTGQsdkWITL--KSTRPGKTSVVSGEI 122
PH smart00233
Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...
15-137 4.80e-05

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The domain family possesses multiple functions including the abilities to bind inositol phosphates, and various proteins. PH domains have been found to possess inserted domains (such as in PLC gamma, syntrophins) and to be inserted within other domains. Mutations in Brutons tyrosine kinase (Btk) within its PH domain cause X-linked agammaglobulinaemia (XLA) in patients. Point mutations cluster into the positively charged end of the molecule around the predicted binding site for phosphatidylinositol lipids.


Pssm-ID: 214574 [Multi-domain]  Cd Length: 102  Bit Score: 43.69  E-value: 4.80e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252    15 QSFLSRRLKGSIKRAKSqpkldrtssfRHMILprfrsadqeRTRLMQSFKESHSHESllspSSAAEALDLtlDEDAVIKP 94
Cdd:smart00233    4 EGWLYKKSGGGKKSWKK----------RYFVL---------FNSTLLYYKSKKDKKS----YKPKGSIDL--SGCTVREA 58
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|....
gi 1840229252    95 VHSSILGQEYCFEVTTLSG-TKCFACRSAAERDKWIENLQRAVK 137
Cdd:smart00233   59 PDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
1118-1216 8.68e-05

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 46.98  E-value: 8.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1118 KLKEYSKSMDESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKI---LSQYQSRLDDSERRLRQQQVEK 1194
Cdd:TIGR02169  273 LLEELNKKIKDLGEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLeaeIDKLLAEIEELEREIEEERKRR 352
                           90       100
                   ....*....|....*....|..
gi 1840229252 1195 DsQIKGIINRLMAVEDELRVSA 1216
Cdd:TIGR02169  353 D-KLTEEYAELKEELEDLRAEL 373
C2_fungal_Inn1p-like cd08681
C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 ...
154-248 1.27e-03

C2 domain found in fungal Ingression 1 (Inn1) proteins; Saccharomyces cerevisiae Inn1 associates with the contractile actomyosin ring at the end of mitosis and is needed for cytokinesis. The C2 domain of Inn1, located at the N-terminus, is required for ingression of the plasma membrane. The C-terminus is relatively unstructured and contains eight PXXP motifs that are thought to mediate interaction of Inn1 with other proteins with SH3 domains in the cytokinesis proteins Hof1 (an F-BAR protein) and Cyk3 (whose overexpression can restore primary septum formation in Inn1Delta cells) as well as recruiting Inn1 to the bud-neck by binding to Cyk3. Inn1 and Cyk3 appear to cooperate in activating chitin synthase Chs2 for primary septum formation, which allows coordination of actomyosin ring contraction with ingression of the cleavage furrow. It is thought that the C2 domain of Inn1 helps to preserve the link between the actomyosin ring and the plasma membrane, contributing both to membrane ingression, as well as to stability of the contracting ring. Additionally, Inn1 might induce curvature of the plasma membrane adjacent to the contracting ring, thereby promoting ingression of the membrane. It has been shown that the C2 domain of human synaptotagmin induces curvature in target membranes and thereby contributes to fusion of these membranes with synaptic vesicles. The C2 domain was first identified in PKC. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions.


Pssm-ID: 176063 [Multi-domain]  Cd Length: 118  Bit Score: 39.92  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  154 IIEARDLPAKKRY-----YCELCLDDMlyarttsKPRTDTVF-------WGEHFEFNNLPAI-RSLRLHLYKETdkkrrK 220
Cdd:cd08681      7 VLKARNLPNKRKLdkqdpYCVLRIGGV-------TKKTKTDFrggqhpeWDEELRFEITEDKkPILKVAVFDDD-----K 74
                           90       100
                   ....*....|....*....|....*...
gi 1840229252  221 EKSTYLGLVSIPISSITGRQFVEQWYPV 248
Cdd:cd08681     75 RKPDLIGDTEVDLSPALKEGEFDDWYEL 102
PHA03247 PHA03247
large tegument protein UL36; Provisional
926-1116 1.51e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 43.39  E-value: 1.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  926 TATGTGTPTSVATPPSTVHPVRHGSVAPPPPQRLKSQLSISPG----------------ATSTPPKAR-------PQSRN 982
Cdd:PHA03247  2817 ALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGgdvrrrppsrspaakpAAPARPPVRrlarpavSRSTE 2896
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252  983 LLLQSPESSFGGRQNSPQQQQQQQHQLSVKQSDSPAPGLPHQSSSARDSQGAPQGGNGETTDTPTKSTKQPQQQSQQQPP 1062
Cdd:PHA03247  2897 SFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPR 2976
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1840229252 1063 PQQHLLKPTVNKQGSqSPATLTPTPNERTVAWVSNMP-HLSAD------IEILRSSSNLED 1116
Cdd:PHA03247  2977 FRVPQPAPSREAPAS-STPPLTGHSLSRVSSWASSLAlHEETDpppvslKQTLWPPDDTED 3036
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
1096-1229 1.63e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1096 SNMPHLSADIEILR-------------SSSNLEDLKLKEYSKSMDE---SRMDRVKEYEEEIHSLKER---------LIM 1150
Cdd:PRK03918   214 SELPELREELEKLEkevkeleelkeeiEELEKELESLEGSKRKLEEkirELEERIEELKKEIEELEEKvkelkelkeKAE 293
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1151 SHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQvEKDSQIKGIINRLMAVEDEL-----RVSAIPEIKPRMF 1225
Cdd:PRK03918   294 EYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELE-EKEERLEELKKKLKELEKRLeeleeRHELYEEAKAKKE 372

                   ....
gi 1840229252 1226 REQE 1229
Cdd:PRK03918   373 ELER 376
C2_PKC_epsilon cd04014
C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The ...
150-196 2.27e-03

C2 domain in Protein Kinase C (PKC) epsilon; A single C2 domain is found in PKC epsilon. The PKC family of serine/threonine kinases regulates apoptosis, proliferation, migration, motility, chemo-resistance, and differentiation. There are 3 groups: group 1 (alpha, betaI, beta II, gamma) which require phospholipids and calcium, group 2 (delta, epsilon, theta, eta) which do not require calcium for activation, and group 3 (xi, iota/lambda) which are atypical and can be activated in the absence of diacylglycerol and calcium. C2 domains fold into an 8-standed beta-sandwich that can adopt 2 structural arrangements: Type I and Type II, distinguished by a circular permutation involving their N- and C-terminal beta strands. Many C2 domains are Ca2+-dependent membrane-targeting modules that bind a wide variety of substances including bind phospholipids, inositol polyphosphates, and intracellular proteins. Most C2 domain proteins are either signal transduction enzymes that contain a single C2 domain, such as protein kinase C, or membrane trafficking proteins which contain at least two C2 domains, such as synaptotagmin 1. However, there are a few exceptions to this including RIM isoforms and some splice variants of piccolo/aczonin and intersectin which only have a single C2 domain. C2 domains with a calcium binding region have negatively charged residues, primarily aspartates, that serve as ligands for calcium ions. Members here have a type-II topology.


Pssm-ID: 175981 [Multi-domain]  Cd Length: 132  Bit Score: 39.56  E-value: 2.27e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840229252  150 LKLWIIEARDL-PAK--KRY------------YCELCLDDMLYARTTSKPRTDTVFWGEHFE 196
Cdd:cd04014      6 LKIKICEAVDLkPTDwsTRHavpkkgsqlldpYVSIDVDDTHIGKTSTKPKTNSPVWNEEFT 67
PRK12704 PRK12704
phosphodiesterase; Provisional
1116-1232 2.57e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 42.07  E-value: 2.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1116 DLKLKEYSKSMDESRMDRVKEYEEEIHSLKERLIMSHR----KLEEYERRMLSQEQQTSK---ILSQYQSRLDDSERRLR 1188
Cdd:PRK12704    41 KRILEEAKKEAEAIKKEALLEAKEEIHKLRNEFEKELRerrnELQKLEKRLLQKEENLDRkleLLEKREEELEKKEKELE 120
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*..
gi 1840229252 1189 QQQVEKDSQIKGIINRLMAVEDEL-RVSAI--PEIKPRMFREQEEDS 1232
Cdd:PRK12704   121 QKQQELEKKEEELEELIEEQLQELeRISGLtaEEAKEILLEKVEEEA 167
PRK00409 PRK00409
recombination and DNA strand exchange inhibitor protein; Reviewed
1111-1199 4.75e-03

recombination and DNA strand exchange inhibitor protein; Reviewed


Pssm-ID: 234750 [Multi-domain]  Cd Length: 782  Bit Score: 41.35  E-value: 4.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1111 SSNLEDL--KLKEYSKSMDESRmDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLS-QEQQTSKILSQYQSRLDDSERRL 1187
Cdd:PRK00409   515 KEKLNELiaSLEELERELEQKA-EEAEALLKEAEKLKEELEEKKEKLQEEEDKLLEeAEKEAQQAIKEAKKEADEIIKEL 593
                           90
                   ....*....|..
gi 1840229252 1188 RQQQVEKDSQIK 1199
Cdd:PRK00409   594 RQLQKGGYASVK 605
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
1128-1232 5.16e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 41.29  E-value: 5.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1128 ESRMDRVKEYEEEIHSLKERLIMSHRKLEEYERRMLSQEQQTSKILSQYQSRLDDSERRLRQQQVEKDSQIKGIINRLMA 1207
Cdd:COG4717    145 PERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEE 224
                           90       100
                   ....*....|....*....|....*
gi 1840229252 1208 VEDELRvsaipEIKPRMFREQEEDS 1232
Cdd:COG4717    225 LEEELE-----QLENELEAAALEER 244
Mitofilin pfam09731
Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. ...
1101-1239 8.72e-03

Mitochondrial inner membrane protein; Mitofilin controls mitochondrial cristae morphology. Mitofilin is enriched in the narrow space between the inner boundary and the outer membranes, where it forms a homotypic interaction and assembles into a large multimeric protein complex. The first 78 amino acids contain a typical amino-terminal-cleavable mitochondrial presequence rich in positive-charged and hydroxylated residues and a membrane anchor domain. In addition, it has three centrally located coiled coil domains.


Pssm-ID: 430783 [Multi-domain]  Cd Length: 618  Bit Score: 40.51  E-value: 8.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1840229252 1101 LSADIEILRSSSNLEDLKLKEysksmdESRMDR-VKEYEEEIHSLKERLIMS-HRKLEEYERRM-LSQEQQTSKILSQYQ 1177
Cdd:pfam09731  290 AHAHREIDQLSKKLAELKKRE------EKHIERaLEKQKEELDKLAEELSARlEEVRAADEAQLrLEFEREREEIRESYE 363
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1840229252 1178 SRLDDSERRLRQQQVEKdsqikgIINRLMAVEDELRVSAIPEIKPRMFREQEEDSSSLGSAD 1239
Cdd:pfam09731  364 EKLRTELERQAEAHEEH------LKDVLVEQEIELQREFLQDIKEKVEEERAGRLLKLNELL 419
 
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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