NCBI Conserved Domain Search

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

963-1102

4.71e-06

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

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.71e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   963 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 1029
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914255  1030 RLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1102
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819

Smc

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

953-1107

1.45e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.45e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  953 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 1032
Cdd:COG1196   228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568914255 1033 RQQEDKDIQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQAR 1107
Cdd:COG1196   299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

PRK03918

DNA double-strand break repair ATPase Rad50;

975-1100

5.52e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDI--QMKGIISRLMSV 1052
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKkeELERLKKRLTGL 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568914255 1053 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1100
Cdd:PRK03918  385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433

Name

Accession

Description

Interval

E-value

DUF3498

pfam12004

Domain of unknown function (DUF3498); This presumed domain is functionally uncharacterized. ...

589-1102

0e+00

Pssm-ID: 463427 [Multi-domain] Cd Length: 511 Bit Score: 677.63 E-value: 0e+00

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   589 LRDVHTALSTPGSGQLPG--TNDLASTPGSGSSSVSAGLQKMVIENDLsGLIDFTRLPSPTPENKDLFFVTRSSGVQPSP 666
Cdd:pfam12004    1 LRDITTALTNPTPIQQQLrrFSEHSSSPPVPGRSISSGLQKMFEDPDD-GLSDFTRLPSPTPENKDLFFVTRPPLLQPSP 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   667 ARSSSYSEANEPDLQMANGSKSLSMVDLQDARTLDGEAgSPVGPDALPADGQVPATQLLAG---WPARAAPVSLAGLATV 743
Cdd:pfam12004   80 ARSSSYSDANEPDQQLPNGNKSLSMVDLQDSRSLQGSP-SPPLHDAPLNLSQAGSQASVGLrpaWAARTSQGNPQSAPQV 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   744 RRAVPTPTTPGTSEgapgrPQLLAPLSFQNPVYQMAAGLPLSPRGLG--DSGSEGHSSLSSHSNSEELAAAAK----LGS 817
Cdd:pfam12004  159 RRPLQTPVTQGTRP-----QQLLAPLSFQNPVYHMAAGLPVSPRGLGspDSSSETHSSFSSHSNSEDLSSAAAnkksGPS 233

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   818 FSTAAEELARRPGELARRQMSLTEKGGQPTVPRQNSAGPQRRIDQPPPPPPPPPPAPRGRtppTLLSTLQYPRPSSGTLA 897
Cdd:pfam12004  234 NSSYSEDFARRSTEFTRRQLSLTELQHQPAVPRQNSAGPQRRIDQQGLGGPPLTRGRTPP---SLLNSASYPRPSSGSLM 310

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   898 SASPDWagPGTRLRQQSSSSKGDSPELKPRAMHKQGPSPVSPNALD---RTAAWLLTMNAQLLEDEGLGPDpphrdrlrS 974
Cdd:pfam12004  311 SSSPDW--PPARLRQQSSSSKGDSPETKQRTQHQQVPSPVNPSTLSpveRTAAWVLNMNGQYEEEESSGPE--------S 380

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   975 KEELSQAEK---DLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMKGIISRLMS 1051
Cdd:pfam12004  381 REELKQAEKyeqEISKLKERLRVSNRKLEEYERRLLAQEEQTQKLLLEYQARLEDSEERLRRQQEEKDSQMKSIISRLMA 460

                          490       500       510       520       530
                   ....*....|....*....|....*....|....*....|....*....|.
gi 568914255  1052 VEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1102
Cdd:pfam12004  461 VEEELKKDHAEMQAVIDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 511

RasGAP_DAB2IP

cd05136

Ras-GTPase Activating Domain of DAB2IP and similar proteins; The DAB2IP family of Ras ...

276-599

0e+00

Pssm-ID: 213338 Cd Length: 324 Bit Score: 615.36 E-value: 0e+00

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  276 RYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIF 355
Cdd:cd05136     1 RYQSVDILPLEVYKEFLEYLTNNYLDLCEVLEPVLSVKAKEELATALVHILQSTGKAKEFLTDLVMAEVDRL-DDEHLIF 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  356 RENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPR 434
Cdd:cd05136    80 RGNTLATKAMEAYLKLVGQKYLQETLGEFIRALYESEEDCEVDPSKCPpSASLSRNQANLRRSVELAWCKILSSHCVFPR 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  435 ELKEVFASWRQECSSRGRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKE 514
Cdd:cd05136   160 ELREVFSSWRERLEERGREDIADRLISASLFLRFLCPAILSPSLFNLTQEYPSERAARNLTLIAKVIQNLANFTRFGGKE 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  515 EYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVSKLGPLPRILRDVHT 594
Cdd:cd05136   240 EYMEFMNDFVEQEWPNMKQFLQEISSPSPSSNSSDFDGYIDLGRELSLLHSLLVEIISKLNQTTLDKLGPLPRILNDITE 319


                  ....*
gi 568914255  595 ALSTP 599
Cdd:cd05136   320 ALRNP 324

PH_DAB2IP

cd13376

DOC-2/Disabled homolog 2-interacting protein Pleckstrin homology (PH) domain; DAB2IP (also ...

18-204

2.22e-115

Pssm-ID: 270179 Cd Length: 182 Bit Score: 354.78 E-value: 2.22e-115

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   18 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAaaaaaDNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 97
Cdd:cd13376     1 VTGFLSRRLKGSIKRTKSQPKLDRNSSFRHILPGFRSV-----DNERSHLMPRLKESRSHESLLSPSSAVEALDLSMEEE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   98 VIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLPAKKKYLCE 177
Cdd:cd13376    76 VVIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVENMLKLWIIEAKDLPAKKKYLCE 155

                         170       180
                  ....*....|....*....|....*..
gi 568914255  178 LCLDDVLYARTTSKLKTDNVFWGEHFE 204
Cdd:cd13376   156 LCLDDVLYARTTCKLKTDNVFWGEHFE 182

RasGAP

smart00323

GTPase-activator protein for Ras-like GTPases; All alpha-helical domain that accelerates the ...

271-589

2.75e-112

Pssm-ID: 214617 Cd Length: 344 Bit Score: 353.15 E-value: 2.75e-112

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255    271 IRIKARYQTVSILPMEMYKEFAEHITNHYLG-LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgD 349
Cdd:smart00323    9 LRLKTVYTTDFILPSEYYEELLELLLFSLDLsLASALSEVCSGLDKDELATKLVRLFLRRGRGHPFLRALIDPEVERT-D 87

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255    350 NEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSY 429
Cdd:smart00323   88 DPNTIFRGNSLATKSMEVYMKLVGNQYLHTTLKPVLKKIVESKKSCEVDPAKLEGEDLETNLENLLQYVERLFDAIINSS 167

                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255    430 CVFPRELKEVFASWRQECSSR-GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFA 508
Cdd:smart00323  168 DRLPYGLRDICKQLRQAAEKRfPDADVIYKAVSSFVFLRFFCPAIVSPKLFNLVDEHPDPTTRRTLTLIAKVLQNLANLS 247

                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255    509 KFGSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQsVVSKLGPLPRI 588
Cdd:smart00323  248 EFGSKEPWMEPLNDFLLSHKDRVKDFLDELSSVPEILVDKVSDSTTISGRELSLLHSLLLENGDALKR-ELNNEDPLGKL 326


                    .
gi 568914255    589 L 589
Cdd:smart00323  327 L 327

PH_SynGAP

cd13375

Synaptic Ras-GTPase activating protein Pleckstrin homology (PH) domain; SynGAP is a member of ...

10-204

2.62e-103

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: 322.80 E-value: 2.62e-103

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   10 PSAstPFRVT-GFLSRRLKGSIKRTKSQPKLDRNHSFRHILPGFRSAaaaaaDNERSHLMPRLKESRSHESLLSPSSAVE 88
Cdd:cd13375     1 PTA--PFRPSqGFLSRRLKSSIKRTKSQPKLDRTSSFRQILPRFRSA-----DHDRARLMQSFKESHSHESLLSPSSAAE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   89 ALDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDL 168
Cdd:cd13375    74 ALDLNLDEDSIIKPVHSSILGQEFCFEVTTASGTKCFACRSAAERDKWIENLQRAVKPNKDNSRRVDNVLKLWIIEAREL 153

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 568914255  169 PAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFE 204
Cdd:cd13375   154 PPKKRYYCELCLDDMLYARTTSKPRTDTVFWGEHFE 189

C2_SynGAP_like

cd04013

C2 domain present in Ras GTPase activating protein (GAP) family; SynGAP, GAP1, RasGAP, and ...

146-285

3.99e-80

Pssm-ID: 175980 [Multi-domain] Cd Length: 146 Bit Score: 258.39 E-value: 3.99e-80

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  146 PNKDNSRRVEHILKLWVIEAKDLPAKKKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYRETDKK 225
Cdd:cd04013     1 PNRDNSRRTENSLKLWIIEAKGLPPKKRYYCELCLDKTLYARTTSKLKTDTLFWGEHFEFSNLPPVSVITVNLYRESDKK 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914255  226 KKKERNSYLGLVSLPAASVAGRQFVEKWYPVVTPNP------KGGKGPGPMIRIKARYQTVSILPM 285
Cdd:cd04013    81 KKKDKSQLIGTVNIPVTDVSSRQFVEKWYPVSTPKGngksggKEGKGESPSIRIKARYQSTRVLPL 146

RasGAP

cd04519

Ras GTPase Activating Domain; RasGAP functions as an enhancer of the hydrolysis of GTP that is ...

288-540

8.95e-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: 245.09 E-value: 8.95e-74

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  288 YKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATKAIEE 367
Cdd:cd04519     3 YRLLSLLLTESPLALLRELSQVLPVKDKEEVATALLRIFESRGLALEFLRYLVRSEVKNT-KNPNTLFRGNSLATKLLDQ 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  368 YLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQEC 447
Cdd:cd04519    82 YMKLVGQEYLKETLSPLIREILESKESCEIDTKLPVGEDLEENLENLLELVNKLVDRILSSLDRLPPELRYVFKILREFL 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  448 SSR--GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 525
Cdd:cd04519   162 AERfpEEPDEAYQAVSGFLFLRFICPAIVSPELFGLVPDEPSEQARRNLTLISKVLQSLANGVEFGDKEPFMKPLNDFIK 241

                         250
                  ....*....|....*
gi 568914255  526 HEWTNMQRFLLEISN 540
Cdd:cd04519   242 SNKPKLKQFLDELSS 256

PH_nGAP

cd13373

Neuronal growth-associated proteins Pleckstrin homology (PH) domain; nGAP (also called RASAL2 ...

15-160

1.55e-61

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: 206.12 E-value: 1.55e-61

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   15 PFRVTGFLSRRLKGSIKRTKSQPKLDRNHSFRhiLPGFRSAaaaaadNERSHLMPRLKESRSHESLLSPSSAVEALDLSM 94
Cdd:cd13373     1 PFKVSGFFSKRLKGSIKRTKSQSKLDRNTSFR--LPSLRSA------DDRSRGLPKLKESRSHESLLSPGSAVEALDLGR 72

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914255   95 EEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRVEHILKL 160
Cdd:cd13373    73 EEKVSVKPLHSSILGQDFCFEVTYSSGSKCFSCSSAAERDKWMENLRRTVQPNKDNCRRAENVLRL 138

PH_RasSynGAP-like

cd13262

Synaptic Ras-GTPase activating protein family Pleckstrin homology (PH) domain; The RasSynGAP ...

18-154

5.60e-59

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: 198.04 E-value: 5.60e-59

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   18 VTGFLSRRLKGSIKRTKSQPKLDRNHSFRhiLPGFRSAaaaaadneRSHLMPRLKESRSHESLLSPSSAveALDLSMEEE 97
Cdd:cd13262     1 ASGFFSRRLKGPLKRTKSVTKLERKSSKR--LPRTRLA--------RAPAGPRLRGSRSHESLLSSSSA--ALDLSADED 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914255   98 VIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAAERDKWMENLRRAVHPNKDNSRRV 154
Cdd:cd13262    69 VVIRPLHSSILGRKHCFQVTTSEGTRCFSCRSAAERDRWIEDLRRAAQPNKDNCRRT 125

RasGAP_CLA2_BUD2

cd05137

Ras-GTPase Activating Domain of CLA2/BUD2; CLA2/BUD2 functions as a GTPase-activating protein ...

274-525

2.82e-55

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: 196.25 E-value: 2.82e-55

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  274 KARYQTVSILPMEMYKEFAEHITNHYLGLCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVD-------- 345
Cdd:cd05137     1 KVRLDENVVLPSKNYKPLEELLHNFDLGLTLQIAELVPGDKLERLSEILLDIFQASGREDEWFMALVEDEIDgidkstsk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  346 -----RCGDNEH-LIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSA-------DLPEHQG 412
Cdd:cd05137    81 nkdmgKSSNNEAnLLFRGNSLLTKSLEKYMRRIGKEYLEKSIGDVIRKICEENKDCEVDPSRVKESdsiekeeDLEENWE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  413 NLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGRPDISE-RL--ISASLFLRFLCPAIMSPSLFNLLQEYPDDR 489
Cdd:cd05137   161 NLISLTEEIWNSIYITSNDCPPELRKILKHIRAKVEDRYGDFLRTvTLnsVSGFLFLRFFCPAILNPKLFGLLKDHPRPR 240

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 568914255  490 TARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLE 525
Cdd:cd05137   241 AQRTLTLIAKVLQNLANLTTFGQKEPWMEPMNEFLT 276

RasGAP_GAP1_like

cd05128

Ras-GTPase Activating Domain of GAP1 and similar proteins; The GAP1 family of Ras ...

301-541

1.50e-50

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: 179.75 E-value: 1.50e-50

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  301 GLCAALEPILSAKtKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDA 380
Cdd:cd05128    22 SAVYLLEELVKVD-KDDVARPLVRIFLHHGQIVPLLRALASREISKTQD-PNTLFRGNSLASKCMDEFMKLVGMQYLHET 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  381 LGEFIKALYESDENCEVDPSKCSSADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISE 457
Cdd:cd05128   100 LKPVIDEIFSEKKSCEIDPSKLKDGEVLEtNLANLRGYVERVFKAITSSARRCPTLMCEIFSDLRESAAQRfpDNEDVPY 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  458 RLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS----KEEYMS-FMNQFL-EHEWTNM 531
Cdd:cd05128   180 TAVSGFIFLRFFAPAILNPKLFGLREEHPDPQTARTLTLISKTIQTLGNLGSSSSglgvKEAYMSpLYERFTdEQHVDAV 259

                         250
                  ....*....|
gi 568914255  532 QRFLLEISNP 541
Cdd:cd05128   260 KKFLDRISSV 269

RasGAP_Neurofibromin_like

cd05392

Ras-GTPase Activating Domain of proteins similar to neurofibromin; Neurofibromin-like proteins ...

284-580

6.41e-46

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: 168.23 E-value: 6.41e-46

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  284 PMEMYKEFAEHITNHYLGLCAALEpILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCgDNEHLIFRENTLATK 363
Cdd:cd05392     2 KSEAYDELLELLIEDPQLLLAIAE-VCPSSEVDLLAQSLLNLFETRNRLLPLISWLIEDEISHT-SRAADLFRRNSVATR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  364 AIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASW 443
Cdd:cd05392    80 LLTLYAKSVGNKYLRKVLRPLLTEIVDNKDYFEVEKIKPDDENLEENADLLMKYAQMLLDSITDSVDQLPPSFRYICNTI 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  444 RQECSSRgRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEEYMSFMNQF 523
Cdd:cd05392   160 YESVSKK-FPDAALIAVGGFLFLRFICPAIVSPESENLLDPPPTPEARRSLILIAKVLQNIANGVLFSLKEPYLESLNEF 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914255  524 LEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLGRELSSLHSLLWEAVSQLDQSVVS 580
Cdd:cd05392   239 LKKNSDRIQQFLSEVSTIPPTDPIFDESDEEPITADLRYLHKFLYLHFLEIRKEVLK 295

RasGAP_p120GAP

cd05391

Ras-GTPase Activating Domain of p120; p120GAP is a negative regulator of Ras that stimulates ...

282-566

6.10e-43

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: 159.96 E-value: 6.10e-43

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  282 ILPMEMYKEFAEHITNHYLGLCAALEPiLSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRcGDNEHLIFRENTLA 361
Cdd:cd05391     4 IMPEEEYSELKELILQKELHVVYALAH-VCGQDRTLLASILLRIFRHEKLESLLLRTLNDREISM-EDEATTLFRATTLA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  362 TKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSKCSSADlpEHQGNLKMCCELAFC---KIINSYCVFPRELKE 438
Cdd:cd05391    82 STLMEQYMKATATPFVHHALKDTILKILESKQSCELNPSKLEKNE--DVNTNLEHLLNILSElveKIFMAAEILPPTLRY 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  439 VFaSWRQECSSRGRPD---ISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGSKEE 515
Cdd:cd05391   160 IY-GCLQKSVQQKWPTnttVRTRVVSGFVFLRLICPAILNPRMFNIISETPSPTAARTLTLVAKSLQNLANLVEFGAKEP 238

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568914255  516 YMSFMNQFLEHEWTNMQRFLLEISN-PETLSNTAGFEGyiDLGRELSSLHSL 566
Cdd:cd05391   239 YMEGVNPFIKKNKERMIMFLDELGNvPELPDTTEHSRT--DLSRDLAALHEI 288

RasGAP_RASA3

cd05134

Ras-GTPase Activating Domain of RASA3; RASA3 (or GAP1_IP4BP) is a member of the GAP1 family ...

313-540

7.32e-39

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: 145.94 E-value: 7.32e-39

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  313 KTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESD 392
Cdd:cd05134    33 REKQEAAIPLVRLFLHYGKIVPFISAIASAEVNRTQD-PNTIFRGNSLTSKCIDETMKLAGMHYLQVTLKPIIDEICQEH 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  393 ENCEVDPSKCS-SADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFL 469
Cdd:cd05134   112 KPCEIDPVKLKdGENLENNRENLRQYVDRIFRVITKSGVSCPTVMCDIFFSLRESAAKRfqVDPDVRYTAVSSFIFLRFF 191

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914255  470 CPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS---KEEYM-SFMNQFLEHEWTN-MQRFLLEISN 540
Cdd:cd05134   192 APAILSPNLFQLTPHHPDPQTSRTLTLISKTIQTLGSLSKSKSanfKESYMaAFYDYFNEQKYADaVKNFLDLISS 267

RasGAP_Neurofibromin

cd05130

Ras-GTPase Activating Domain of neurofibromin; Neurofibromin is the product of the ...

317-569

1.55e-33

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: 132.45 E-value: 1.55e-33

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  317 EMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDE--N 394
Cdd:cd05130    41 ELARVLVTLFDSKHLLYQLLWNMFSKEVELADSMQTL-FRGNSLASKIMTFCFKVYGATYLQSLLEPLLRTMITSSEwvS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  395 CEVDPSKC-SSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSRGrPDISERLISASLFLRFLCPAI 473
Cdd:cd05130   120 YEVDPTRLeGNENLEENQRNLLQLTEKFFHAIISSSDEFPPQLRSVCHCLYQVVSHRF-PNSGLGAVGSAIFLRFINPAI 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  474 MSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEI-SNPETLSNTAG-FE 551
Cdd:cd05130   199 VSPYEYGILDREPPPRVKRGLKLMSKILQNIANHVLF-TKEAHMLPFNDFLRNHFEAGRRFFSSIaSDCGAVDGPSSkYL 277

                         250
                  ....*....|....*...
gi 568914255  552 GYIDLGrELSSLHSLLWE 569
Cdd:cd05130   278 SFINDA-NVLALHRLLWN 294

PH_RASAL3

cd13374

RAS protein activator like-3 Pleckstrin homology (PH) domain; RASAL3 is thought to be a Ras ...

67-169

2.56e-31

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: 120.12 E-value: 2.56e-31

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   67 LMPRLKESRSHESLL------SPSSAVEA---------LDLSMEEEVIIKPVHSSILGQDYCFEVTTSSGSKCFSCRSAA 131
Cdd:cd13374    25 LLKRLKEKKKAKAEStgtgrdGPPSALGSreslatiseLDLGAERDVRVWPLHPSLLGEPHCFQVTWPGGSRCFSCRSAA 104

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 568914255  132 ERDKWMENLRRAVHPNKDNSRRVEHILKLWVIEAKDLP 169
Cdd:cd13374   105 ERDRWIEDLRRSFQPHQDNVEREETWLSVWVHEAKGLP 142

RasGAP_RASAL

cd05135

Ras-GTPase Activating Domain of RASAL1 and similar proteins; Ras GTPase activating-like ...

304-535

1.09e-29

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: 119.92 E-value: 1.09e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  304 AALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDALGE 383
Cdd:cd05135    29 AMLEEVTTGESRQDVATKLVKIFLGQGLVVPFLDYLNTREVGRTTDPNTL-FRSNSLASKSMEQFMKVVGMPYLHEVLKP 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  384 FIKALYESDENCEVDPSK--------------CSSADLPEH-----QGNLKMCCElafcKIINSYCVFPRELKEVFASWR 444
Cdd:cd05135   108 VINRIFEEKKYVELDPCKidlnrtrrisfkgsLSEAQVRESslellQGYLGSIID----AIVGSVDQCPPVMRVAFKQLH 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  445 QECSSR----GRPDISERLISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANF-AKFGS-KEEYMS 518
Cdd:cd05135   184 KRVEERfpeaEHQDVKYLAISGFLFLRFFAPAILTPKLFQLREQHADPRTSRTLLLLAKAVQSIGNLgLQLGQgKEQWMA 263

                         250
                  ....*....|....*..
gi 568914255  519 FMNQFLEHEWTNMQRFL 535
Cdd:cd05135   264 PLHPFILQSVARVKDFL 280

RasGAP_RASA2

cd05394

Ras-GTPase Activating Domain of RASA2; RASA2 (or GAP1(m)) is a member of the GAP1 family of ...

322-542

4.19e-29

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: 118.07 E-value: 4.19e-29

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  322 LVHILQSTGKVKDFLTDLMMSEVDRCGDnEHLIFRENTLATKAIEEYLKLVGQKYLQDALGEFIKALYESDENCEVDPSK 401
Cdd:cd05394    42 LVRLLLHHNKLVPFVAAVAALDLKDTQE-ANTIFRGNSLATRCLDEMMKIVGKHYLKVTLKPVLDEICESPKPCEIDPIK 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  402 CSSADLPE-HQGNLKMCCELAFCKIINSYCVFPRELKEVFASWRQECSSR--GRPDISERLISASLFLRFLCPAIMSPSL 478
Cdd:cd05394   121 LKEGDNVEnNKENLRYYVDKVFFSIVKSSMSCPTLMCDVFRSLRHLAVKRfpNDPHVQYSAVSSFVFLRFFAVAVVSPHT 200

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914255  479 FNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS------KEEYM-SFMNQFLEHEWT-NMQRFLLEISNPE 542
Cdd:cd05394   201 FQLRPHHPDAQTSRTLTLISKTIQTLGSWGSLSKsklssfKETFMcDFFKMFQEEKYIeKVKKFLDEISSTE 272

RasGAP

pfam00616

GTPase-activator protein for Ras-like GTPase; All alpha-helical domain that accelerates the ...

335-506

1.68e-28

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: 113.92 E-value: 1.68e-28

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   335 FLTDLMMSEVDRCgDNEHLIFRENTLATKAIEEYLKL-VGQKYLQDALGEFIKALYESDE-NCEVDPSK----------- 401
Cdd:pfam00616    1 LISELIEEEIESS-DNPNDLLRGNSLVSKLLETYNRRpRGQEYLKKVLGPLVRKIIEDEDlDLESDPRKiyeslinqeel 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   402 -CSSADLP-------------------EHQGNLKMCCELAFCKIINSYCVFPREL----KEVFASWRQECssrgrPDISE 457
Cdd:pfam00616   80 kTGRSDLPrdvspeeaiedpevrqifeDNLQKLRELADEFLDAIYSSLNQLPYGIryicKQLYELLEEKF-----PDASE 154

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 568914255   458 R----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLAN 506
Cdd:pfam00616  155 EeilnAIGGFLFLRFFCPAIVNPDLFGLVDHQISPKQRRNLTLIAKVLQNLAN 207

RasGAP_RASA4

cd05395

Ras-GTPase Activating Domain of RASA4; Ras GTPase activating-like 4 protein (RASAL4), also ...

302-542

3.22e-25

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: 106.88 E-value: 3.22e-25

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  302 LCAALEPILSAKTKEEMASALVHILQSTGKVKDFLTDLMMSEVDRCGDNEHLiFRENTLATKAIEEYLKLVGQKYLQDAL 381
Cdd:cd05395    27 LISLIDETTTAECRQEVATNLVKLFLGQGLAKEFLDLLFQLELDKTTEPNTL-FRSNSLASKSMESFLKVAGMQYLHSVL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  382 GEFIKALYESDENCEVDPSK-------CSSADLPEHQGN--------LKMCCELAFCKIINSYCVFPRELKEVFASWRQE 446
Cdd:cd05395   106 GPTINRVFEEKKYVELDPSKveikdvgCSGLHRIQTESEvieqsaqlLQSYLGELLSAISKSVKYCPAVIRATFRQLFKR 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  447 CSSRgRPDISER-----LISASLFLRFLCPAIMSPSLFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFGS--KEEYMSF 519
Cdd:cd05395   186 VQER-FPENQHQnvkfiAVTSFLCLRFFSPAIMSPKLFHLREKHADARTSRTLLLLAKAVQNVGNMDTLASraKEAWMAP 264

                         250       260
                  ....*....|....*....|...
gi 568914255  520 MNQFLEHEWTNMQRFLLEISNPE 542
Cdd:cd05395   265 LQPAIQQGVAQLKDFITKLVDIE 287

RasGAP_GAPA

cd05132

Ras-GTPase Activating Domain of GAPA; GAPA is an IQGAP-related protein and is predicted to ...

356-586

1.28e-24

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: 106.67 E-value: 1.28e-24

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  356 RENTLATKAIEEYLKLV-GQKYLQDALGEFIKALYE-SDENCEVDPSKC-------------------------SSADLP 408
Cdd:cd05132    49 RANTAVSRMMTTYTRRGpGQSYLKTVLADRINDLISlKDLNLEINPLKVyeqmindieldtglpsnlprgitpeEAAENP 128

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  409 EHQG----NLKMCCELA---FCKIINSYCVFPRELKEVFASWRQECSSRgRPDISER----LISASLFLRFLCPAIMSPS 477
Cdd:cd05132   129 AVQNiiepRLEMLEEITnsfLEAIINSLDEVPYGIRWICKQIRSLTRRK-FPDASDEticsLIGGFFLLRFINPAIVSPQ 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  478 LFNLLQEYPDDRTARTLTLIAKVTQNLANFAKFgSKEEYMSFMNQFLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDLG 557
Cdd:cd05132   208 AYMLVDGKPSDNTRRTLTLIAKLLQNLANKPSY-SKEPYMAPLQPFVEENKERLNKFLNDLCEVDDFYESLELDQYIALS 286

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 568914255  558 R----------ELSSLHSLLWEAVSQLDQS-------VVSKLGPLP 586
Cdd:cd05132   287 KkdlsinitlnEIYNTHSLLVKHLAELAPDhndhlrlILQELGPAP 332

C2A_RasGAP

cd08383

C2 domain (first repeat) of Ras GTPase activating proteins (GAPs); RasGAPs suppress Ras ...

158-277

1.59e-11

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: 62.28 E-value: 1.59e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  158 LKLWVIEAKDLPAKKK---YlCELCLDDVLYARTTSKLKTdNVFWGEHFEFHNLPPL---RTVTVHLYretdKKKKKERN 231
Cdd:cd08383     2 LRLRILEAKNLPSKGTrdpY-CTVSLDQVEVARTKTVEKL-NPFWGEEFVFDDPPPDvtfFTLSFYNK----DKRSKDRD 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914255  232 SYLGLVSLpaASVAGRQFVEKWYPVVTPNPKGGKgPGpMIRIKARY 277
Cdd:cd08383    76 IVIGKVAL--SKLDLGQGKDEWFPLTPVDPDSEV-QG-SVRLRARY 117

cd00030

C2 domain; The C2 domain was first identified in PKC. C2 domains fold into an 8-standed ...

158-255

4.87e-11

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: 60.54 E-value: 4.87e-11

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  158 LKLWVIEAKDLPAKKK-----YLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPL-RTVTVHLYretDKKKKKeRN 231
Cdd:cd00030     1 LRVTVIEARNLPAKDLngksdPYVKVSLGGKQKFKTKVVKNTLNPVWNETFEFPVLDPEsDTLTVEVW---DKDRFS-KD 76

                          90       100
                  ....*....|....*....|....*
gi 568914255  232 SYLGLVSLPAASVAGR-QFVEKWYP 255
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 ...

158-277

1.11e-10

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: 60.07 E-value: 1.11e-10

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  158 LKLWVIEAKDLPAKK---KYlCELCLDDVLYARTTSKLKTDNVfWGEHFEFHNLPP-LRTVTVHLYretdKKKKKERNSY 233
Cdd:cd08400     6 LQLNVLEAHKLPVKHvphPY-CVISLNEVKVARTKVREGPNPV-WSEEFVFDDLPPdVNSFTISLS----NKAKRSKDSE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 568914255  234 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKGPGpMIRIKARY 277
Cdd:cd08400    80 IAEVTVQLSKLQNGQETDEWYPLSSASPLKGGEWG-SLRIRARY 122

smart00239

Protein kinase C conserved region 2 (CalB); Ca2+-binding motif present in phospholipases, ...

157-253

3.46e-09

Pssm-ID: 214577 [Multi-domain] Cd Length: 101 Bit Score: 55.19 E-value: 3.46e-09

                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255    157 ILKLWVIEAKDLPAKKKYL-----CELCLDDVLY--ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKKK 228
Cdd:smart00239    1 TLTVKIISARNLPPKDKGGksdpyVKVSLDGDPKekKKTKVVKNTLNPVWNETFEFEvPPPELAELEIEVY---DKDRFG 77

                            90       100
                    ....*....|....*....|....*
gi 568914255    229 eRNSYLGLVSLPAASVAGRQFVEKW 253
Cdd:smart00239   78 -RDDFIGQVTIPLSDLLLGGRHEKL 101

pfam00168

C2 domain;

156-256

8.30e-09

C2 domain;

Pssm-ID: 425499 [Multi-domain] Cd Length: 104 Bit Score: 54.25 E-value: 8.30e-09

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   156 HILKLWVIEAKDLPAKKK------YlCELCLDDVLY-ARTTSKLKTDNVFWGEHFEFH-NLPPLRTVTVHLYretDKKKK 227
Cdd:pfam00168    1 GRLTVTVIEAKNLPPKDGngtsdpY-VKVYLLDGKQkKKTKVVKNTLNPVWNETFTFSvPDPENAVLEIEVY---DYDRF 76

                           90       100
                   ....*....|....*....|....*....
gi 568914255   228 KeRNSYLGLVSLPAASVAGRQFVEKWYPV 256
Cdd:pfam00168   77 G-RDDFIGEVRIPLSELDSGEGLDGWYPL 104

RasGAP_IQGAP2

cd05131

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 2; IQGAP2 is a ...

362-610

1.94e-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: 54.62 E-value: 1.94e-07

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  362 TKAIEEYLKLVGQkyLQDALGEFIKALYE-SDENCEVDPSkcSSADLPEHQGNLKMCCELAFCKIINSYCVFPRELKEVF 440
Cdd:cd05131    87 TNPVEVYKAWVNQ--LETATGEASKLPYDvTTEQALTHPE--VVNKLESSIQSLRSVTDKVLGSIFSSLDLIPYGMRYIA 162

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  441 ASWRQECSSRgRPDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKF 510
Cdd:cd05131   163 KVLKNSLHEK-FPDATEdellKIVGNLLYYRYMNPAIVAPDGFDIIdmtaggQIHSEQR--RNLGSVAKVLQHAASNKLF 239

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  511 GSKEEYMSFMNQFLEHEWTNMQRFL---LEISNPETLSNTAGFEGYIDLGR--------ELSSLHSLLWE---AVSQlDQ 576
Cdd:cd05131   240 EGENAHLSSMNSYLSQTYQKFRKFFqaaCDVPEPEEKFNIDEYSDMVTLSKpviyisieEIINTHSLLLEhqdAIAP-DQ 318

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 568914255  577 S-----VVSKLGPLPrilrDVHTALstpGSGQLpGTNDL 610
Cdd:cd05131   319 NdllheLLKDLGEVP----DVESFL---GEGTV-DPNDP 349

smart00233

Pleckstrin homology domain; Domain commonly found in eukaryotic signalling proteins. The ...

92-145

2.55e-06

Pssm-ID: 214574 [Multi-domain] Cd Length: 102 Bit Score: 47.16 E-value: 2.55e-06

                            10        20        30        40        50
                    ....*....|....*....|....*....|....*....|....*....|....*
gi 568914255     92 LSMEEEVIIKPVHSSILGQDYCFEVTTSSG-SKCFSCRSAAERDKWMENLRRAVH 145
Cdd:smart00233   48 IDLSGCTVREAPDPDSSKKPHCFEIKTSDRkTLLLQAESEEEREKWVEALRKAIA 102

RasGAP_IQGAP_like

cd05127

Ras-GTPase Activating Domain of IQ motif containing GTPase activating proteins; This family ...

464-591

4.32e-06

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: 50.28 E-value: 4.32e-06

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  464 LFLRFLCPAIMSPSLFNLLQEYPDDRTA----RTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLEIS 539
Cdd:cd05127   179 LYYRYMNPAIVAPEAFDIIDLSVGGQLSplqrRNLGSIAKVLQQAASGKLFGGENPYLSPLNPYISESHEKFKKFFLEAC 258

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 568914255  540 NPETLSNTAGFEGYIDLG-----------RELSSLHSLLWEavsQLDQSVVSKLGPLPRILRD 591
Cdd:cd05127   259 TVPEAEEHFNIDEYSDLTmltkptiyislQEIFATHKLLLE---HQDEIAPDPDDPLRELLDD 318

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

963-1102

4.71e-06

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 51.21 E-value: 4.71e-06

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   963 GPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLF-----------KCQEETTQKLVLEYQ--ARLEEGEE 1029
Cdd:TIGR02168  664 GSAKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELeeleeeleqlrKELEELSRQISALRKdlARLEAEVE 743

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914255  1030 RLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKI---IDAQEKRIASLDAANARLMSALTQLKERY 1102
Cdd:TIGR02168  744 QLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELeaqIEQLKEELKALREALDELRAELTLLNEEA 819

C2A_C2C_Synaptotagmin_like

cd08391

C2 domain first and third repeat in Synaptotagmin-like proteins; Synaptotagmin is a ...

156-255

1.17e-05

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: 45.75 E-value: 1.17e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  156 HILKLWVIEAKDLPAKKKYLCEL--------CLDDVLYARTTSKLKTDNV--FWGEHFEF--HNLPPLrTVTVHLYretD 223
Cdd:cd08391     1 GVLRIHVIEAQDLVAKDKFVGGLvkgksdpyVIVRVGAQTFKSKVIKENLnpKWNEVYEAvvDEVPGQ-ELEIELF---D 76

                          90       100       110
                  ....*....|....*....|....*....|..
gi 568914255  224 KKKKKErnSYLGLVSLPAASVAGRQFVEKWYP 255
Cdd:cd08391    77 EDPDKD--DFLGRLSIDLGSVEKKGFIDEWLP 106

C2A_MCTP_PRT_plant

cd04022

C2 domain first repeat found in Multiple C2 domain and Transmembrane region Proteins (MCTP); ...

162-255

1.40e-05

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: 45.79 E-value: 1.40e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  162 VIEAKDLPAKKKY-----LCELCLDDVLYaRTTSKLKTDNVFWGEHFEF--HNLPPLRTVTVHLYRETDKKKKKeRNSYL 234
Cdd:cd04022     6 VVDAQDLMPKDGQgsssaYVELDFDGQKK-RTRTKPKDLNPVWNEKLVFnvSDPSRLSNLVLEVYVYNDRRSGR-RRSFL 83

                          90       100
                  ....*....|....*....|..
gi 568914255  235 GLVSLPAASVAGRQ-FVEKWYP 255
Cdd:cd04022    84 GRVRISGTSFVPPSeAVVQRYP 105

Smc

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

953-1107

1.45e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 49.55 E-value: 1.45e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  953 NAQLLEDEGLgpdppHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLR 1032
Cdd:COG1196   228 ELLLLKLREL-----EAELEELEAELEELEAELEELEAELAELEAELEELRL----ELEELELELEEAQAEEYELLAELA 298

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568914255 1033 RQQEDKDIQMKGIIsRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQAR 1107
Cdd:COG1196   299 RLEQDIARLEERRR-ELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEA 372

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

975-1103

2.34e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.97 E-value: 2.34e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDKDiQMKGIISRLMSVEE 1054
Cdd:COG4372    51 REELEQAREELEQLEEELEQARSELEQLEE----ELEELNEQLQAAQAELAQAQEELESLQEEAE-ELQEELEELQKERQ 125

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914255 1055 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1103
Cdd:COG4372   126 DLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQ 174

Smc

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

975-1100

3.60e-05

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.01 E-value: 3.60e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEyQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEE 1054
Cdd:COG1196   273 RLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEER-LEELEEELAELEEELEELEEELEELEEELEEAEE 351

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 568914255 1055 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1100
Cdd:COG1196   352 ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAE 397

RasGAP_IQGAP1

cd05133

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 1; IQGAP1 is a ...

453-556

3.85e-05

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: 47.35 E-value: 3.85e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  453 PDISE----RLISASLFLRFLCPAIMSPSLFNLL------QEYPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQ 522
Cdd:cd05133   174 PDAGEdellKIVGNLLYYRYMNPAIVAPDAFDIIdlsaggQLTTDQR--RNLGSIAKMLQHAASNKMFLGDNAHLSPINE 251

                          90       100       110
                  ....*....|....*....|....*....|....
gi 568914255  523 FLEHEWTNMQRFLLEISNPETLSNTAGFEGYIDL 556
Cdd:cd05133   252 YLSQSYQKFRRFFQAACDVPELEDKFNVDEYSDL 285

PRK03918

DNA double-strand break repair ATPase Rad50;

975-1100

5.52e-05

DNA double-strand break repair ATPase Rad50;

Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 47.37 E-value: 5.52e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQQEDKDI--QMKGIISRLMSV 1052
Cdd:PRK03918  306 LDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLK-ELEKRLEELEERHELYEEAKAKkeELERLKKRLTGL 384

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568914255 1053 E-EELKKdhaEMQAAVDSKQKIIDAQEK---RIASLDAANARLMSALTQLKE 1100
Cdd:PRK03918  385 TpEKLEK---ELEELEKAKEEIEEEISKitaRIGELKKEIKELKKAIEELKK 433

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

970-1101

5.53e-05

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 46.07 E-value: 5.53e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  970 DRLRSK-----EELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQE---ETTQKLVLEYQARLEEG------------EE 1029
Cdd:COG1579    20 DRLEHRlkelpAELAELEDELAALEARLEAAKTELEDLEKEIKRLEleiEEVEARIKKYEEQLGNVrnnkeyealqkeIE 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 568914255 1030 RLRRQQEDKDIQMKGIISRLmsveEELKKDHAEMQAAVDSKQKIIDAQEKRiasLDAANARLMSALTQLKER 1101
Cdd:COG1579   100 SLKRRISDLEDEILELMERI----EELEEELAELEAELAELEAELEEKKAE---LDEELAELEAELEELEAE 164

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

970-1108

5.92e-05

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 47.36 E-value: 5.92e-05

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   970 DRLRS-KEELSQAEKDLAVLQDKLRISTKKLEEYETLF----------KCQEETTQKLVLEYQARLEEGEERLRRQQE-- 1036
Cdd:TIGR02168  232 LRLEElREELEELQEELKEAEEELEELTAELQELEEKLeelrlevselEEEIEELQKELYALANEISRLEQQKQILRErl 311

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568914255  1037 ---DKDIQMK-GIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARN 1108
Cdd:TIGR02168  312 anlERQLEELeAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

973-1106

6.54e-05

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 46.43 E-value: 6.54e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  973 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkcQEETTQKLvleyqARLEEGEERLRRQQEdkdiQMKGIISRLMSV 1052
Cdd:COG4372    63 QLEEELEQARSELEQLEEELEELNEQLQAAQAE---LAQAQEEL-----ESLQEEAEELQEELE----ELQKERQDLEQQ 130

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568914255 1053 EEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQA 1106
Cdd:COG4372   131 RKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAEQA 184

RasGAP_IQGAP3

cd12207

Ras-GTPase Activating Domain of IQ motif containing GTPase activating protein 3; This family ...

464-601

6.96e-05

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: 46.36 E-value: 6.96e-05

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  464 LFLRFLCPAIMSPSLFNLLQE------YPDDRtaRTLTLIAKVTQNLANFAKFGSKEEYMSFMNQFLEHEWTNMQRFLLE 537
Cdd:cd12207   189 LYYRFMNPAVVAPDGFDIVDCsaggalQPEQR--RMLGSVAKVLQHAAANKHFQGDSEHLQALNQYLEETHVKFRKFILQ 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  538 ---ISNPETLSNTAGFEG---------YIDLGrELSSLHSLLWEAVSQL--DQS-----VVSKLGPLPRILRDVHTALST 598
Cdd:cd12207   267 accVPEPEERFNVDEYSEmvavakpviYITVG-ELINTHKLLLEHQDSIapDHSdplheLLEDLGEVPTVQSLIGESWAD 345


                  ...
gi 568914255  599 PGS 601
Cdd:cd12207   346 LGD 348

C2A_Rasal1_RasA4

cd04054

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 ...

162-253

3.14e-04

C2 domain first repeat present in RasA1 and RasA4; Rasal1 and RasA4 are both members of GAP1 (GTPase activating protein 1). Rasal1 responds to repetitive Ca2+ signals by associating with the plasma membrane and deactivating Ras. RasA4 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. Both of these proteins contains two C2 domains, a Ras-GAP domain, a plextrin homology (PH)-like domain, and a Bruton's Tyrosine Kinase (BTK) 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: 176018 [Multi-domain] Cd Length: 121 Bit Score: 41.73 E-value: 3.14e-04

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  162 VIEAKDLPAK-----KKYLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYREtdkkKKKERNSYLGL 236
Cdd:cd04054     6 IVEGKNLPAKditgsSDPYCIVKVDNEVIIRTATVWKTLNPFWGEEYTVHLPPGFHTVSFYVLDE----DTLSRDDVIGK 81

                          90
                  ....*....|....*...
gi 568914255  237 VSLPAASVAGR-QFVEKW 253
Cdd:cd04054    82 VSLTREVISAHpRGIDGW 99

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

974-1100

1.01e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.97 E-value: 1.01e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  974 SKEELSQAEKDLAVLQDKLRISTKKLEEYET--------LFKCQEE--TTQKLVLEYQARLEEGEERLRRQQEdkdiQMK 1043
Cdd:COG4372    29 LSEQLRKALFELDKLQEELEQLREELEQAREeleqleeeLEQARSEleQLEEELEELNEQLQAAQAELAQAQE----ELE 104

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914255 1044 GIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKE 1100
Cdd:COG4372   105 SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLES 161

Smc

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

975-1101

1.03e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.39 E-value: 1.03e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRisTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEERLRRQQEDkdiqmkgiISRLMSVEE 1054
Cdd:COG1196   219 KEELKELEAELLLLKLREL--EAELEELEA----ELEELEAELEELEAELAELEAELEELRLE--------LEELELELE 284

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914255 1055 ELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1101
Cdd:COG1196   285 EAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEE 331

C2A_RasA2_RasA3

cd08401

C2 domain first repeat present in RasA2 and RasA3; RasA2 and RasA3 are GAP1s (GTPase ...

160-256

1.22e-03

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: 40.11 E-value: 1.22e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  160 LWVI-EAKDLPAKKK------YLCELCLDDVLYARTTSKLKTDNVFWGEHFEFHNLPPLRTVTVHLYretdKKKKKERNS 232
Cdd:cd08401     3 KIKIgEAKNLPPRSGpnkmrdCYCTVNLDQEEVFRTKTVEKSLCPFFGEDFYFEIPRTFRHLSFYIY----DRDVLRRDS 78

                          90       100
                  ....*....|....*....|....
gi 568914255  233 YLGLVSLPAASVAGRQFVEKWYPV 256
Cdd:cd08401    79 VIGKVAIKKEDLHKYYGKDTWFPL 102

DR0291

COG1579

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...

969-1101

1.34e-03

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];

Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 41.83 E-value: 1.34e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  969 RDRL-RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkcQEE-TTQKlvlEYQARLEEgEERLRRQQEDKDIQMKGII 1046
Cdd:COG1579    44 EARLeAAKTELEDLEKEIKRLELEIEEVEARIKKYEEQ---LGNvRNNK---EYEALQKE-IESLKRRISDLEDEILELM 116

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 568914255 1047 SRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1101
Cdd:COG1579   117 ERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREELAAK 171

YhaN

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

983-1111

1.39e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.83 E-value: 1.39e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  983 KDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVlEYQARLEEGEERLRRQqeDKDIQMKGIISRLMSVEEELKKDHAE 1062
Cdd:COG4717    71 KELKELEEELKEAEEKEEEYAELQEELEELEEELE-ELEAELEELREELEKL--EKLLQLLPLYQELEALEAELAELPER 147

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914255 1063 MQAAVDSKQKIIDAQEkRIASLDAANARLMSALTQLKERYSMQARNGVS 1111
Cdd:COG4717   148 LEELEERLEELRELEE-ELEELEAELAELQEELEELLEQLSLATEEELQ 195

RasGAP_RAP6

cd05129

Ras-GTPase Activating Domain of Rab5-activating protein 6; Rab5-activating protein 6 (RAP6) is ...

368-582

1.58e-03

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

Pssm-ID: 213331 Cd Length: 365 Bit Score: 42.33 E-value: 1.58e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  368 YLKLVGQKYLQDALGEFIKALYESDE-NCEVDPSKC-------------SSADLPEHQGNLKMCCE------LAFCKII- 426
Cdd:cd05129   104 ELLFSAKLYLTAALHKPIMQVLVDDEiFLETDPQKAlcrfspaeqekrfGEEGTPEQQRKLQQYRAeflsrlVALVNKFi 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  427 -----NSYCvFPRELKE-VFASWRQECSSRGRPDISERLISASL-FLRFLCPAIMSPSLFNLLQEYPDDRTAR-TLTLIA 498
Cdd:cd05129   184 sslrqSVYC-FPQSLRWiVRQLRKILTRSGDDEEAEARALCTDLlFTNFICPAIVNPEQYGIISDAPISEVARhNLMQVA 262

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  499 KVTQNLAnFAKFGSKE-EYMSFMNQFLEHEWTNMQRFLLE----------ISNPETLSNTAGFEGYIDLGRELSSLHSLL 567
Cdd:cd05129   263 QILQVLA-LTEFESPDpRLKELLSKFDKDCVSAFLDVVIVgravetpppsSSALLEGSRTAVLITESDLATLVEFLRSVK 341

                         250
                  ....*....|....*
gi 568914255  568 WEAVSQLDQSVVSKL 582
Cdd:cd05129   342 TGDEEKEDQMALDNL 356

COG4372

Uncharacterized protein, contains DUF3084 domain [Function unknown];

969-1093

1.63e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];

Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 42.20 E-value: 1.63e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  969 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQaRLEEGEERLRRQQEDKDIQMKGIISR 1048
Cdd:COG4372    73 SELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQ-DLEQQRKQLEAQIAELQSEIAEREEE 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914255 1049 LMSVEEELKKDHAEMQAAVDSKQKIIDAQ-EKRIASL-DAANARLMS 1093
Cdd:COG4372   152 LKELEEQLESLQEELAALEQELQALSEAEaEQALDELlKEANRNAEK 198

Caldesmon

pfam02029

Caldesmon;

909-1124

1.68e-03

Caldesmon;

Pssm-ID: 460421 [Multi-domain] Cd Length: 495 Bit Score: 42.16 E-value: 1.68e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   909 RLRQ-QSSSSKGDSPELKPRAMHKQGPS-----PVSPNALDRTAAWLLTMnaQLLEDeglgpdpphRDRLRSKEELS-QA 981
Cdd:pfam02029   19 RRRQkEEEEPSGQVTESVEPNEHNSYEEdselkPSGQGGLDEEEAFLDRT--AKREE---------RRQKRLQEALErQK 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   982 EKDLAVLQDKLRISTKK----LEEYET----------LFKCQEETTQKLVLEYQARL---------EEGEERLRRQQEDK 1038
Cdd:pfam02029   88 EFDPTIADEKESVAERKenneEEENSSwekeekrdsrLGRYKEEETEIREKEYQENKwstevrqaeEEGEEEEDKSEEAE 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  1039 DIQmkgiisRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYSMQARNGVSPTNPTKL 1118
Cdd:pfam02029  168 EVP------TENFAKEEVKDEKIKKEKKVKYESKVFLDQKRGHPEVKSQNGEEEVTKLKVTTKRRQGGLSQSQEREEEAE 241


                   ....*.
gi 568914255  1119 QITENG 1124
Cdd:pfam02029  242 VFLEAE 247

YhaN

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

976-1091

1.77e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 42.45 E-value: 1.77e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  976 EELSQAEKDLAVLQDKLRISTKKLEEYETLfkcqEETTQKLvleyQARLEEGEERLRRQQEDKDIQMKGIISRLMSVEEE 1055
Cdd:COG4717   132 QELEALEAELAELPERLEELEERLEELREL----EEELEEL----EAELAELQEELEELLEQLSLATEEELQDLAEELEE 203

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 568914255 1056 LKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARL 1091
Cdd:COG4717   204 LQQRLAELEEELEEAQEELEELEEELEQLENELEAA 239

C2_plant_PLD

cd04015

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds ...

234-277

2.40e-03

C2 domain present in plant phospholipase D (PLD); PLD hydrolyzes terminal phosphodiester bonds in diester glycerophospholipids resulting in the degradation of phospholipids. In vitro PLD transfers phosphatidic acid to primary alcohols. In plants PLD plays a role in germination, seedling growth, phosphatidylinositol metabolism, and changes in phospholipid composition. There is a single Ca(2+)/phospholipid-binding C2 domain in PLD. 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: 175982 [Multi-domain] Cd Length: 158 Bit Score: 39.98 E-value: 2.40e-03

                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 568914255  234 LGLVSLPAASVAGRQFVEKWYPVVTPNPKGGKgPGPMIRIKARY 277
Cdd:cd04015   115 IGRAYIPVEDLLSGEPVEGWLPILDSNGKPPK-PGAKIRVSLQF 157

YhaN

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

949-1102

2.66e-03

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

Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 41.68 E-value: 2.66e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  949 LLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFkcQEETTQKLVLEYQARLEEGE 1028
Cdd:COG4717   368 LEQEIAALLAEAGVEDEEELRAALEQAEEYQELKEELEELEEQLEELLGELEELLEAL--DEEELEEELEELEEELEELE 445

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568914255 1029 ERLRRQQEDKdIQMKGIISRLMSvEEELkkdhAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1102
Cdd:COG4717   446 EELEELREEL-AELEAELEQLEE-DGEL----AELLQELEELKAELRELAEEWAALKLALELLEEAREEYREER 513

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

949-1105

2.95e-03

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: 41.98 E-value: 2.95e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   949 LLTMNAQLLEDEGL---GPDPPHRDRLRSKEELSQAEKdlavLQDKLristKKLE-EYETLFKCQEETtQKLVLEYQARL 1024
Cdd:TIGR02169  641 MVTLEGELFEKSGAmtgGSRAPRGGILFSRSEPAELQR----LRERL----EGLKrELSSLQSELRRI-ENRLDELSQEL 711

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  1025 EEGEERLRRQQedKDIQM-KGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERYS 1103
Cdd:TIGR02169  712 SDASRKIGEIE--KEIEQlEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLS 789


                   ..
gi 568914255  1104 MQ 1105
Cdd:TIGR02169  790 HS 791

SMC_prok_A

TIGR02169

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...

973-1122

3.13e-03

Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 41.98 E-value: 3.13e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   973 RSKEELSQAEKDLAVLQ----------DKLRISTKKLEEYETLFKCQEETTQKLVL-EYQARLEEGE------ERLRRQQ 1035
Cdd:TIGR02169  174 KALEELEEVEENIERLDliidekrqqlERLRREREKAERYQALLKEKREYEGYELLkEKEALERQKEaierqlASLEEEL 253

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  1036 EDKDIQMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIdaqEKRIASLDAANARLMSALTQLK---ERYSMQARNGVSP 1112
Cdd:TIGR02169  254 EKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRV---KEKIGELEAEIASLERSIAEKErelEDAEERLAKLEAE 330

                          170
                   ....*....|
gi 568914255  1113 TNPTKLQITE 1122
Cdd:TIGR02169  331 IDKLLAEIEE 340

Smc

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

969-1101

3.19e-03

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

Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.85 E-value: 3.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  969 RDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVLEYQARLEEGEERLRRQQEDKDIQMkgiisR 1048
Cdd:COG1196   316 ERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELL-----E 390

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568914255 1049 LMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1101
Cdd:COG1196   391 ALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

CwlO1

COG3883

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...

975-1101

3.36e-03

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

Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 41.35 E-value: 3.36e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRISTKKLEEYETlfkcQEETTQKLVLEYQARLEEGEE----RLRRQQED------------- 1037
Cdd:COG3883    36 QAELDALQAELEELNEEYNELQAELEALQA----EIDKLQAEIAEAEAEIEERREelgeRARALYRSggsvsyldvllgs 111

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 568914255 1038 KDI---------------QMKGIISRLMSVEEELKKDHAEMQAAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1101
Cdd:COG3883   112 ESFsdfldrlsalskiadADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQAEQEALLAQLSAE 190

GOLGA2L5

pfam15070

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein ...

942-1064

4.02e-03

Putative golgin subfamily A member 2-like protein 5; The function of the GOLGA2L5 protein family remains unknown. This family of proteins is thought to be found in the Golgi apparatus of eukaryotes.

Pssm-ID: 464485 [Multi-domain] Cd Length: 521 Bit Score: 41.20 E-value: 4.02e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   942 LDRTAAWLLTMNAQLLEDEGLGPDPPHRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLfkCQEETTQKLVLEYQ 1021
Cdd:pfam15070   55 LETSLAELKNQAAVPPAEEEQPPAGPSEEEQRLQEEAEQLQKELEALAGQLQAQVQDNEQLSRL--NQEQEQRLLELERA 132

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 568914255  1022 ARLEeGEERLRRQQEDKDIQM-KGIISRLMSVEEELKKDHAEMQ 1064
Cdd:pfam15070  133 AERW-GEQAEDRKQILEDMQSdRATISRALSQNRELKEQLAELQ 175

SMC_prok_B

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...

953-1102

4.51e-03

Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 41.20 E-value: 4.51e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   953 NAQLLEDEglgpdpphRDRLRSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKL--VLEYQAR----LEE 1026
Cdd:TIGR02168  322 EAQLEELE--------SKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELeeQLETLRSkvaqLEL 393

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 568914255  1027 GEERLRRQQEDKDIQMKGIISRLMSVEEELKKDHAEMQ-AAVDSKQKIIDAQEKRIASLDAANARLMSALTQLKERY 1102
Cdd:TIGR02168  394 QIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEeAELKELQAELEELEEELEELQEELERLEEALEELREEL 470

cd00821

Pleckstrin homology (PH) domain; PH domains have diverse functions, but in general are ...

92-140

6.25e-03

Pleckstrin homology (PH) 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: 275388 [Multi-domain] Cd Length: 92 Bit Score: 37.14 E-value: 6.25e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 568914255   92 LSMEEEVIIKPVHSSilGQDYCFEVTTSSGSK-CFSCRSAAERDKWMENL 140
Cdd:cd00821    45 IPLSGILEVEEVSPK--ERPHCFELVTPDGRTyYLQADSEEERQEWLKAL 92

COG4913

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

975-1101

7.19e-03

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

Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 40.67 E-value: 7.19e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  975 KEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEEttQKLVLEYQARLEEGEERLRRQQEDKDIqmkgiISRLMSVEE 1054
Cdd:COG4913   623 EEELAEAEERLEALEAELDALQERREALQRLAEYSWD--EIDVASAEREIAELEAELERLDASSDD-----LAALEEQLE 695

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 568914255 1055 ELKKDHAEMQAAvdskqkiIDAQEKRIASLDAANARLMSALTQLKER 1101
Cdd:COG4913   696 ELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDR 735

HEC1

COG5185

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ...

973-1101

7.39e-03

Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];

Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 40.33 E-value: 7.39e-03

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255  973 RSKEELSQAEKDLAVLQDKLRISTKKLEEYETLFKCQEETTQKLVleyqarlEEGEERLRRQQEDKDIQMKGIISRLMSV 1052
Cdd:COG5185   374 KSSEELDSFKDTIESTKESLDEIPQNQRGYAQEILATLEDTLKAA-------DRQIEELQRQIEQATSSNEEVSKLLNEL 446

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 568914255 1053 EEELKKDHAEMQaaVDSKQKIIDAQEKRIASLDAANARLMSALTQLKER 1101
Cdd:COG5185   447 ISELNKVMREAD--EESQSRLEEAYDEINRSVRSKKEDLNEELTQIESR 493

RNase_Y_N

pfam12072

RNase Y N-terminal region;

970-1063

8.04e-03

RNase Y N-terminal region;

Pssm-ID: 463456 [Multi-domain] Cd Length: 201 Bit Score: 39.10 E-value: 8.04e-03

                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568914255   970 DRLRSKEE--------LSQAEKDLAVLQDKLRISTKKLEEyetlfkcQEETTQKLVLEYQARLEE--GeerlRRQQEDKD 1039
Cdd:pfam12072   85 RRLLQKEEtldrkdesLEKKEESLEKKEKELEAQQQQLEE-------KEEELEELIEEQRQELERisG----LTSEEAKE 153

                           90       100
                   ....*....|....*....|....
gi 568914255  1040 IQMKgiisrlmSVEEELKKDHAEM 1063
Cdd:pfam12072  154 ILLD-------EVEEELRHEAAVM 170

PH_RASA1

cd13260

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 ...

90-142

8.12e-03

RAS p21 protein activator (GTPase activating protein) 1 Pleckstrin homology (PH) domain; RASA1 (also called RasGap1 or p120) is a member of the RasGAP family of GTPase-activating proteins. RASA1 contains N-terminal SH2-SH3-SH2 domains, followed by two C2 domains, a PH domain, a RasGAP domain, and a BTK domain. Splice variants lack the N-terminal domains. It is a cytosolic vertebrate protein that acts as a suppressor of RAS via its C-terminal GAP domain function, enhancing the weak intrinsic GTPase activity of RAS proteins resulting in the inactive GDP-bound form of RAS, allowing control of cellular proliferation and differentiation. Additionally, it is involved in mitogenic signal transmission towards downstream interacting partners through its N-terminal SH2-SH3-SH2 domains. RASA1 interacts with a number of proteins including: G3BP1, SOCS3, ANXA6, Huntingtin, KHDRBS1, Src, EPHB3, EPH receptor B2, Insulin-like growth factor 1 receptor, PTK2B, DOK1, PDGFRB, HCK, Caveolin 2, DNAJA3, HRAS, GNB2L1 and NCK1. 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: 270080 Cd Length: 103 Bit Score: 36.94 E-value: 8.12e-03

                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568914255   90 LDLSmeeEVIIKPVHSSILGQDYCFEVTTSSGSKC----FSCRSAAERDKWMENLRR 142
Cdd:cd13260    48 IDLS---YCSLYPVHDSLFGRPNCFQIVVRALNEStityLCADTAELAQEWMRALRA 101

YhaN