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Conserved domains on  [gi|767973121|ref|XP_011536183|]
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leucine-rich repeat serine/threonine-protein kinase 2 isoform X7 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 1334-1507 1.29e-69

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


:

Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 230.69  E-value: 1.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSdlGMQSATVGIDVKDWPIQIRDKRKrdLVLNVWDFAGREEFYSTHPHFMTQRA 1413
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFD--GDESSTHGINVQDWKIPAPERKK--IRLNVWDFGGQEIYHATHQFFLTSRS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1414 LYLAVYDLSKGqAEVDAMKPWLFNIKARASSSPVILVGTHLDVSdekqrkaCMSKITKELLNKRGFPAIRDYHFVNATEE 1493
Cdd:cd09914    77 LYLLVFDLRTG-DEVSRVPYWLRQIKAFGGVSPVILVGTHIDES-------CDEDILKKALNKKFPAIINDIHFVSCKNG 148

                         170
                  ....*....|....
gi 767973121 1494 sDALAKLRKTIINE 1507
Cdd:cd09914   149 -KGIAELKKAIAKE 161
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1009-1279 4.25e-25

Leucine-rich repeat (LRR) protein [Transcription];


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 4.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1009 HLEHLEKLELHQNALTSFPQQLcETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIgpSVVLDPTVKCPTLKQF 1088
Cdd:COG4886   111 NLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQL--TDLPEELGNLTNLKEL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1089 NLSYNQLSFVPENLTDVvEKLEQLILEGNKISGICSPL-RLKELKILNLSKNHISSLSEnfleacpkvesfsarmnfLAA 1167
Cdd:COG4886   188 DLSNNQITDLPEPLGNL-TNLEELDLSGNQLTDLPEPLaNLTNLETLDLSNNQLTDLPE------------------LGN 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1168 MPFLppsmTILKLSQNKFSCIPEaILNLPHLRSLDMSSNDIqylpgpahwKSLNLRELLFSHNQISILDLSEKAYLWSRV 1247
Cdd:COG4886   249 LTNL----EELDLSNNQLTDLPP-LANLTNLKTLDLSNNQL---------TDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                         250       260       270
                  ....*....|....*....|....*....|..
gi 767973121 1248 EKLHLSHNKLKEIPPEIGCLENLTSLDVSYNL 1279
Cdd:COG4886   315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
COR super family cl24610
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
 1527-1611 1.07e-06

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


The actual alignment was detected with superfamily member pfam16095:

Pssm-ID: 406489  Cd Length: 196  Bit Score: 51.09  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1527 YVELEKIILSERKNVPIefpvIDRKRLLQLVRENQLQlDENELPHAVHFLNESGVLLHFQDpALQLSDLYFVEPKWLCKI 1606
Cdd:pfam16095    4 WLAVREALEKERQKKPY----ISYEEYRKICAENGID-DEEDQDTLLEFLHDLGVLLYFQD-DPGLRDIVILNPQWLTNA 77


                   ....*
gi 767973121  1607 MAQFV 1611
Cdd:pfam16095   78 VYRVL 82
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
700-795 4.84e-03

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  700 AKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADAN-QAKEGSSLICQVCEKeSSPKLVELLLNSG----SREQDVRKA 774
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNaQDNDGNTPLHLAAAN-GNLEIVKLLLEAGadvnARDNDGETP 189

                          90       100
                  ....*....|....*....|.
gi 767973121  775 LTISIGKGDSQIISLLLRRLA 795
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGA 210
 
Name Accession Description Interval E-value
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 1334-1507 1.29e-69

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 230.69  E-value: 1.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSdlGMQSATVGIDVKDWPIQIRDKRKrdLVLNVWDFAGREEFYSTHPHFMTQRA 1413
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFD--GDESSTHGINVQDWKIPAPERKK--IRLNVWDFGGQEIYHATHQFFLTSRS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1414 LYLAVYDLSKGqAEVDAMKPWLFNIKARASSSPVILVGTHLDVSdekqrkaCMSKITKELLNKRGFPAIRDYHFVNATEE 1493
Cdd:cd09914    77 LYLLVFDLRTG-DEVSRVPYWLRQIKAFGGVSPVILVGTHIDES-------CDEDILKKALNKKFPAIINDIHFVSCKNG 148

                         170
                  ....*....|....
gi 767973121 1494 sDALAKLRKTIINE 1507
Cdd:cd09914   149 -KGIAELKKAIAKE 161
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 1336-1455 1.59e-39

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 142.65  E-value: 1.59e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1336 KLMIVGNTGSGKTTLLQQLMKTKKSDlgMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:pfam08477    1 KVVLLGDSGVGKTSLLKRFVDDTFDP--KYKSTIGVDFKTKTVLENDDNGKKIKLNIWDTAGQERFRSLHPFYYRGAAAA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767973121  1416 LAVYDlskgQAEVDAMKPWLFNIKARASSSPVILVGTHLD 1455
Cdd:pfam08477   79 LLVYD----SRTFSNLKYWLRELKKYAGNSPVILVGNKID 114
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1009-1279 4.25e-25

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 4.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1009 HLEHLEKLELHQNALTSFPQQLcETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIgpSVVLDPTVKCPTLKQF 1088
Cdd:COG4886   111 NLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQL--TDLPEELGNLTNLKEL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1089 NLSYNQLSFVPENLTDVvEKLEQLILEGNKISGICSPL-RLKELKILNLSKNHISSLSEnfleacpkvesfsarmnfLAA 1167
Cdd:COG4886   188 DLSNNQITDLPEPLGNL-TNLEELDLSGNQLTDLPEPLaNLTNLETLDLSNNQLTDLPE------------------LGN 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1168 MPFLppsmTILKLSQNKFSCIPEaILNLPHLRSLDMSSNDIqylpgpahwKSLNLRELLFSHNQISILDLSEKAYLWSRV 1247
Cdd:COG4886   249 LTNL----EELDLSNNQLTDLPP-LANLTNLKTLDLSNNQL---------TDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                         250       260       270
                  ....*....|....*....|....*....|..
gi 767973121 1248 EKLHLSHNKLKEIPPEIGCLENLTSLDVSYNL 1279
Cdd:COG4886   315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
1332-1504 3.97e-19

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 86.57  E-value: 3.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1332 YNRMKLMIVGNTGSGKTTLLQQLMKtKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHF--- 1408
Cdd:COG1100     1 MGEKKIVVVGTGGVGKTSLVNRLVG-DIFSLEKYLSTNGVTIDKKELKLDGLDVD---LVIWDTPGQDEFRETRQFYarq 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1409 MTQRALYLAVYDLSKGQAEVDAMKpWLFNIKARASSSPVILVGTHLDVSDEKQRKAcmskiTKELLNKRGFPAIRDYHFV 1488
Cdd:COG1100    77 LTGASLYLFVVDGTREETLQSLYE-LLESLRRLGKKSPIILVLNKIDLYDEEEIED-----EERLKEALSEDNIVEVVAT 150

                         170
                  ....*....|....*.
gi 767973121 1489 NAtEESDALAKLRKTI 1504
Cdd:COG1100   151 SA-KTGEGVEELFAAL 165
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
1015-1261 4.27e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 83.98  E-value: 4.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1015 KLELHQNALTSFPQQLCEtlkSLTHLDLHSNKFTSFPSYLlkMSCIANLDVSRNDIG--PSVVLDptvkcpTLKQFNLSY 1092
Cdd:PRK15370  182 ELRLKILGLTTIPACIPE---QITTLILDNNELKSLPENL--QGNIKTLYANSNQLTsiPATLPD------TIQEMELSI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1093 NQLSFVPENLTDVvekLEQLILEGNKISgiCSPLRL-KELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMpfL 1171
Cdd:PRK15370  251 NRITELPERLPSA---LQSLDLFHNKIS--CLPENLpEELRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALPET--L 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1172 PPSMTILKLSQNKFSCIPEAIlnLPHLRSLDMSSNDIQYLPgpahwKSL--NLRELLFSHNqiSILDLSEKayLWSRVEK 1249
Cdd:PRK15370  324 PPGLKTLEAGENALTSLPASL--PPELQVLDVSKNQITVLP-----ETLppTITTLDVSRN--ALTNLPEN--LPAALQI 392

                         250
                  ....*....|..
gi 767973121 1250 LHLSHNKLKEIP 1261
Cdd:PRK15370  393 MQASRNNLVRLP 404
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 1335-1461 4.28e-13

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 68.69  E-value: 4.28e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121   1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDlgMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSthphfMTqRAL 1414
Cdd:smart00175    1 FKIILIGDSGVGKSSLLSRFTDGKFSE--QYKSTIGVDFKTKTIEVDGKRVK---LQIWDTAGQERFRS-----IT-SSY 69

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767973121   1415 Y------LAVYDLSKGQAeVDAMKPWLFNIKARASSS-PVILVGTHLDVSDEKQ 1461
Cdd:smart00175   70 YrgavgaLLVYDITNRES-FENLENWLKELREYASPNvVIMLVGNKSDLEEQRQ 122
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 1334-1482 1.48e-12

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 67.01  E-value: 1.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSDLgmqSATVGIDVKDWPIQIRDKRKRdLVLNVWDFAGREEFYSTHPHFMTQRA 1413
Cdd:TIGR00231    1 DIKIVIVGHPNVGKSTLLNSLLGNKGSIT---EYYPGTTRNYVTTVIEEDGKT-YKFNLLDTAGQEDYDAIRRLYYPQVE 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121  1414 LYLAVYDLSKGQAEV-DAMKPWLFNIK-ARASSSPVILVGTHLDVSDEKqrkacMSKITKELLNKRGFPAI 1482
Cdd:TIGR00231   77 RSLRVFDIVILVLDVeEILEKQTKEIIhHADSGVPIILVGNKIDLKDAD-----LKTHVASEFAKLNGEPI 142
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 984-1169 1.31e-10

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.88  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  984 ITSLDLSANELRDIDALSQkCCisvhleHLEKLELHQNALTSFPQqlCETLKSLTHLDLHSNKFTSFPSyLLKMSCIANL 1063
Cdd:cd21340     4 ITHLYLNDKNITKIDNLSL-CK------NLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1064 DVSRNDIgpSVV--LDptvKCPTLKQFNLSYNQL------SFVPENLTDVVEKLEQLILEGNKISGIcSPLR-LKELKIL 1134
Cdd:cd21340    74 YLGGNRI--SVVegLE---NLTNLEELHIENQRLppgeklTFDPRSLAALSNSLRVLNISGNNIDSL-EPLApLRNLEQL 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767973121 1135 NLSKNHISSLSE--NFLEACPKVESFSARMNFLAAMP 1169
Cdd:cd21340   148 DASNNQISDLEEllDLLSSWPSLRELDLTGNPVCKKP 184
PLN03118 PLN03118
Rab family protein; Provisional
 1336-1460 6.97e-08

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 54.68  E-value: 6.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKTKKSDLgmqSATVGIDVKDWPIQIRDKRkrdLVLNVWDFAGREEFYS-THPHFMTQRAL 1414
Cdd:PLN03118   16 KILLIGDSGVGKSSLLVSFISSSVEDL---APTIGVDFKIKQLTVGGKR---LKLTIWDTAGQERFRTlTSSYYRNAQGI 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767973121 1415 YLaVYDLSKGQAEVDAMKPWLFNIKARASSSPVI--LVGTHLDVSDEK 1460
Cdd:PLN03118   90 IL-VYDVTRRETFTNLSDVWGKEVELYSTNQDCVkmLVGNKVDRESER 136
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
 1527-1611 1.07e-06

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 51.09  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1527 YVELEKIILSERKNVPIefpvIDRKRLLQLVRENQLQlDENELPHAVHFLNESGVLLHFQDpALQLSDLYFVEPKWLCKI 1606
Cdd:pfam16095    4 WLAVREALEKERQKKPY----ISYEEYRKICAENGID-DEEDQDTLLEFLHDLGVLLYFQD-DPGLRDIVILNPQWLTNA 77


                   ....*
gi 767973121  1607 MAQFV 1611
Cdd:pfam16095   78 VYRVL 82
LRR_8 pfam13855
Leucine rich repeat;
985-1047 9.26e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 9.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973121   985 TSLDLSANELRDIDALSqkcciSVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKF 1047
Cdd:pfam13855    4 RSLDLSNNRLTSLDDGA-----FKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
700-795 4.84e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  700 AKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADAN-QAKEGSSLICQVCEKeSSPKLVELLLNSG----SREQDVRKA 774
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNaQDNDGNTPLHLAAAN-GNLEIVKLLLEAGadvnARDNDGETP 189

                          90       100
                  ....*....|....*....|.
gi 767973121  775 LTISIGKGDSQIISLLLRRLA 795
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGA 210
 
Name Accession Description Interval E-value
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
 1334-1507 1.29e-69

Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein family is characterized by a superdomain containing a Ras-like GTPase domain, called Roc (Ras of complex proteins), and a characteristic second domain called COR (C-terminal of Roc). A kinase domain and diverse regulatory domains are also often found in Roco proteins. Their functions are diverse; in Dictyostelium discoideum, which encodes 11 Roco proteins, they are involved in cell division, chemotaxis and development, while in human, where 4 Roco proteins (LRRK1, LRRK2, DAPK1, and MFHAS1) are encoded, these proteins are involved in epilepsy and cancer. Mutations in LRRK2 (leucine-rich repeat kinase 2) are known to cause familial Parkinson's disease.


Pssm-ID: 206741 [Multi-domain]  Cd Length: 161  Bit Score: 230.69  E-value: 1.29e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSdlGMQSATVGIDVKDWPIQIRDKRKrdLVLNVWDFAGREEFYSTHPHFMTQRA 1413
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFD--GDESSTHGINVQDWKIPAPERKK--IRLNVWDFGGQEIYHATHQFFLTSRS 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1414 LYLAVYDLSKGqAEVDAMKPWLFNIKARASSSPVILVGTHLDVSdekqrkaCMSKITKELLNKRGFPAIRDYHFVNATEE 1493
Cdd:cd09914    77 LYLLVFDLRTG-DEVSRVPYWLRQIKAFGGVSPVILVGTHIDES-------CDEDILKKALNKKFPAIINDIHFVSCKNG 148

                         170
                  ....*....|....
gi 767973121 1494 sDALAKLRKTIINE 1507
Cdd:cd09914   149 -KGIAELKKAIAKE 161
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
 1336-1455 1.59e-39

Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial Rho proteins (Miro-1, and Miro-2) and atypical Rho GTPases. Full-length proteins have a unique domain organization, with tandem GTP-binding domains and two EF hand domains (pfam00036) that may bind calcium. They are also larger than classical small GTPases. It has been proposed that they are involved in mitochondrial homeostasis and apoptosis.


Pssm-ID: 462490 [Multi-domain]  Cd Length: 114  Bit Score: 142.65  E-value: 1.59e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1336 KLMIVGNTGSGKTTLLQQLMKTKKSDlgMQSATVGIDVKDWPIQIRDKRKRDLVLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:pfam08477    1 KVVLLGDSGVGKTSLLKRFVDDTFDP--KYKSTIGVDFKTKTVLENDDNGKKIKLNIWDTAGQERFRSLHPFYYRGAAAA 78

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 767973121  1416 LAVYDlskgQAEVDAMKPWLFNIKARASSSPVILVGTHLD 1455
Cdd:pfam08477   79 LLVYD----SRTFSNLKYWLRELKKYAGNSPVILVGNKID 114
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1009-1279 4.25e-25

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 110.02  E-value: 4.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1009 HLEHLEKLELHQNALTSFPQQLcETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIgpSVVLDPTVKCPTLKQF 1088
Cdd:COG4886   111 NLTNLESLDLSGNQLTDLPEEL-ANLTNLKELDLSNNQLTDLPEPLGNLTNLKSLDLSNNQL--TDLPEELGNLTNLKEL 187

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1089 NLSYNQLSFVPENLTDVvEKLEQLILEGNKISGICSPL-RLKELKILNLSKNHISSLSEnfleacpkvesfsarmnfLAA 1167
Cdd:COG4886   188 DLSNNQITDLPEPLGNL-TNLEELDLSGNQLTDLPEPLaNLTNLETLDLSNNQLTDLPE------------------LGN 248

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1168 MPFLppsmTILKLSQNKFSCIPEaILNLPHLRSLDMSSNDIqylpgpahwKSLNLRELLFSHNQISILDLSEKAYLWSRV 1247
Cdd:COG4886   249 LTNL----EELDLSNNQLTDLPP-LANLTNLKTLDLSNNQL---------TDLKLKELELLLGLNSLLLLLLLLNLLELL 314

                         250       260       270
                  ....*....|....*....|....*....|..
gi 767973121 1248 EKLHLSHNKLKEIPPEIGCLENLTSLDVSYNL 1279
Cdd:COG4886   315 ILLLLLTTLLLLLLLLKGLLVTLTTLALSLSL 346
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
1010-1300 2.58e-23

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 104.63  E-value: 2.58e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1010 LEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLLKMSCIANLDVSRNDIGPSVVLDPTV--KCPTLKQ 1087
Cdd:COG4886    21 LTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDlgDLTNLTE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1088 FNLSYNQLSFvpeNLTDvvekLEQLILEGNKISGICSPL-RLKELKILNLSKNHISSLSENfLEACPKVESfsarmnfla 1166
Cdd:COG4886   101 LDLSGNEELS---NLTN----LESLDLSGNQLTDLPEELaNLTNLKELDLSNNQLTDLPEP-LGNLTNLKS--------- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1167 ampflppsmtiLKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGP-AHWKslNLRELLFSHNQISilDLSEKAYLWS 1245
Cdd:COG4886   164 -----------LDLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPlGNLT--NLEELDLSGNQLT--DLPEPLANLT 228

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767973121 1246 RVEKLHLSHNKLKEIpPEIGCLENLTSLDVSYNlELRSFPNEmGKLSKIWDLPLD 1300
Cdd:COG4886   229 NLETLDLSNNQLTDL-PELGNLTNLEELDLSNN-QLTDLPPL-ANLTNLKTLDLS 280
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
984-1272 7.42e-21

Leucine-rich repeat (LRR) protein [Transcription];


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 97.31  E-value: 7.42e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  984 ITSLDLSANELRDI-DALSQkccisvhLEHLEKLELHQNALTSFPQQLCEtLKSLTHLDLHSNKFTSFPSYLLKMSCIAN 1062
Cdd:COG4886   138 LKELDLSNNQLTDLpEPLGN-------LTNLKSLDLSNNQLTDLPEELGN-LTNLKELDLSNNQITDLPEPLGNLTNLEE 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1063 LDVSRNDIgpSVVLDPTVKCPTLKQFNLSYNQLSFVPE--NLTdvveKLEQLILEGNKISGICSPLRLKELKILNLSKNH 1140
Cdd:COG4886   210 LDLSGNQL--TDLPEPLANLTNLETLDLSNNQLTDLPElgNLT----NLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQ 283

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1141 ISSLSENFLEACPKVESFSaRMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSL 1220
Cdd:COG4886   284 LTDLKLKELELLLGLNSLL-LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLL 362

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767973121 1221 NLRELLFSHNQISILDLSEKAYLWSRVEKLHLSHNKLKEIPPEIGCLENLTS 1272
Cdd:COG4886   363 LTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLLLTLALLDAVNTE 414
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
1332-1504 3.97e-19

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 86.57  E-value: 3.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1332 YNRMKLMIVGNTGSGKTTLLQQLMKtKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHF--- 1408
Cdd:COG1100     1 MGEKKIVVVGTGGVGKTSLVNRLVG-DIFSLEKYLSTNGVTIDKKELKLDGLDVD---LVIWDTPGQDEFRETRQFYarq 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1409 MTQRALYLAVYDLSKGQAEVDAMKpWLFNIKARASSSPVILVGTHLDVSDEKQRKAcmskiTKELLNKRGFPAIRDYHFV 1488
Cdd:COG1100    77 LTGASLYLFVVDGTREETLQSLYE-LLESLRRLGKKSPIILVLNKIDLYDEEEIED-----EERLKEALSEDNIVEVVAT 150

                         170
                  ....*....|....*.
gi 767973121 1489 NAtEESDALAKLRKTI 1504
Cdd:COG1100   151 SA-KTGEGVEELFAAL 165
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
1015-1261 4.27e-16

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 83.98  E-value: 4.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1015 KLELHQNALTSFPQQLCEtlkSLTHLDLHSNKFTSFPSYLlkMSCIANLDVSRNDIG--PSVVLDptvkcpTLKQFNLSY 1092
Cdd:PRK15370  182 ELRLKILGLTTIPACIPE---QITTLILDNNELKSLPENL--QGNIKTLYANSNQLTsiPATLPD------TIQEMELSI 250

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1093 NQLSFVPENLTDVvekLEQLILEGNKISgiCSPLRL-KELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMpfL 1171
Cdd:PRK15370  251 NRITELPERLPSA---LQSLDLFHNKIS--CLPENLpEELRYLSVYDNSIRTLPAHLPSGITHLNVQSNSLTALPET--L 323

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1172 PPSMTILKLSQNKFSCIPEAIlnLPHLRSLDMSSNDIQYLPgpahwKSL--NLRELLFSHNqiSILDLSEKayLWSRVEK 1249
Cdd:PRK15370  324 PPGLKTLEAGENALTSLPASL--PPELQVLDVSKNQITVLP-----ETLppTITTLDVSRN--ALTNLPEN--LPAALQI 392

                         250
                  ....*....|..
gi 767973121 1250 LHLSHNKLKEIP 1261
Cdd:PRK15370  393 MQASRNNLVRLP 404
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 986-1285 1.09e-15

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 82.97  E-value: 1.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  986 SLDLSANELR-DIDALSqkccisVHLEHLEKLELHQNALT-SFPQQLCeTLKSLTHLDLHSNKFT-SFPSYLLKMSCIAN 1062
Cdd:PLN00113  288 SLDLSDNSLSgEIPELV------IQLQNLEILHLFSNNFTgKIPVALT-SLPRLQVLQLWSNKFSgEIPKNLGKHNNLTV 360

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1063 LDVSRNDIGPSVvldPTVKCPTLKQFNL---SYNQLSFVPENLTDVvEKLEQLILEGNKISGICSP--LRLKELKILNLS 1137
Cdd:PLN00113  361 LDLSTNNLTGEI---PEGLCSSGNLFKLilfSNSLEGEIPKSLGAC-RSLRRVRLQDNSFSGELPSefTKLPLVYFLDIS 436

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1138 KNHISSLSENFLEACPKVESFS-ARMNFLAAMP--FLPPSMTILKLSQNKFS-CIPEAILNLPHLRSLDMSSNDIQylpG 1213
Cdd:PLN00113  437 NNNLQGRINSRKWDMPSLQMLSlARNKFFGGLPdsFGSKRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLS---G 513

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767973121 1214 --PAHWKSL-NLRELLFSHNQIS---ILDLSEKAYLwsrvEKLHLSHNKLK-EIPPEIGCLENLTSLDVSYNLELRSFP 1285
Cdd:PLN00113  514 eiPDELSSCkKLVSLDLSHNQLSgqiPASFSEMPVL----SQLDLSQNQLSgEIPKNLGNVESLVQVNISHNHLHGSLP 588
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
 1339-1506 1.15e-13

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 70.18  E-value: 1.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1339 IVGNTGSGKTTLLQQLMKTKKSDLG-MQSATVGIDVKDWPIqirDKRKRDLVLnvWDFAGREEFYSTHPHFMTQRA---- 1413
Cdd:cd00882     2 VVGRGGVGKSSLLNALLGGEVGEVSdVPGTTRDPDVYVKEL---DKGKVKLVL--VDTPGLDEFGGLGREELARLLlrga 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1414 -LYLAVYDLSKGQAEVDAMKPWLFNIKARasSSPVILVGTHLDVSDEKQRKAcmskitKELLNKRGFPAIRDYHFVNATE 1492
Cdd:cd00882    77 dLILLVVDSTDRESEEDAKLLILRRLRKE--GIPIILVGNKIDLLEEREVEE------LLRLEELAKILGVPVFEVSAKT 148

                         170
                  ....*....|....
gi 767973121 1493 ESDaLAKLRKTIIN 1506
Cdd:cd00882   149 GEG-VDELFEKLIE 161
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
982-1200 1.76e-13

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 75.50  E-value: 1.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  982 EYITSLDLSANELR--------DIDALS----QKCCISVHL-EHLEKLELHQNALTSFPQQLCETLKSlthLDLHSNKFT 1048
Cdd:PRK15370  199 EQITTLILDNNELKslpenlqgNIKTLYansnQLTSIPATLpDTIQEMELSINRITELPERLPSALQS---LDLFHNKIS 275

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1049 SFPSYLLKMscIANLDVSRNDIGPSVVLDPTvkcpTLKQFNLSYNQLSFVPENLTdvvEKLEQLILEGNKISgiCSPLRL 1128
Cdd:PRK15370  276 CLPENLPEE--LRYLSVYDNSIRTLPAHLPS----GITHLNVQSNSLTALPETLP---PGLKTLEAGENALT--SLPASL 344

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1129 -KELKILNLSKNHISSLSENFleaCPKVESFSARMNFLAAMP-FLPPSMTILKLSQNKFSCIPEAilnLPHLRS 1200
Cdd:PRK15370  345 pPELQVLDVSKNQITVLPETL---PPTITTLDVSRNALTNLPeNLPAALQIMQASRNNLVRLPES---LPHFRG 412
RAB smart00175
Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.
 1335-1461 4.28e-13

Rab subfamily of small GTPases; Rab GTPases are implicated in vesicle trafficking.


Pssm-ID: 197555 [Multi-domain]  Cd Length: 164  Bit Score: 68.69  E-value: 4.28e-13
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121   1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDlgMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSthphfMTqRAL 1414
Cdd:smart00175    1 FKIILIGDSGVGKSSLLSRFTDGKFSE--QYKSTIGVDFKTKTIEVDGKRVK---LQIWDTAGQERFRS-----IT-SSY 69

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....
gi 767973121   1415 Y------LAVYDLSKGQAeVDAMKPWLFNIKARASSS-PVILVGTHLDVSDEKQ 1461
Cdd:smart00175   70 YrgavgaLLVYDITNRES-FENLENWLKELREYASPNvVIMLVGNKSDLEEQRQ 122
Rab cd00154
Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases ...
 1335-1461 4.73e-13

Ras-related in brain (Rab) family of small guanosine triphosphatases (GTPases); Rab GTPases form the largest family within the Ras superfamily. There are at least 60 Rab genes in the human genome, and a number of Rab GTPases are conserved from yeast to humans. Rab GTPases are small, monomeric proteins that function as molecular switches to regulate vesicle trafficking pathways. The different Rab GTPases are localized to the cytosolic face of specific intracellular membranes, where they regulate distinct steps in membrane traffic pathways. In the GTP-bound form, Rab GTPases recruit specific sets of effector proteins onto membranes. Through their effectors, Rab GTPases regulate vesicle formation, actin- and tubulin-dependent vesicle movement, and membrane fusion. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which mask C-terminal lipid binding and promote cytosolic localization. While most unicellular organisms possess 5-20 Rab members, several have been found to possess 60 or more Rabs; for many of these Rab isoforms, homologous proteins are not found in other organisms. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Since crystal structures often lack C-terminal residues, the lipid modification site is not available for annotation in many of the CDs in the hierarchy, but is included where possible.


Pssm-ID: 206640 [Multi-domain]  Cd Length: 159  Bit Score: 68.64  E-value: 4.73e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDLgmQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRAL 1414
Cdd:cd00154     1 FKIVLIGDSGVGKTSLLLRFVDNKFSEN--YKSTIGVDFKSKTIEVDGKKVK---LQIWDTAGQERFRSITSSYYRGAHG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767973121 1415 YLAVYDLSKgQAEVDAMKPWLFNIKARASSS-PVILVGTHLDVSDEKQ 1461
Cdd:cd00154    76 AILVYDVTN-RESFENLDKWLNELKEYAPPNiPIILVGNKSDLEDERQ 122
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
 1334-1482 1.48e-12

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 67.01  E-value: 1.48e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSDLgmqSATVGIDVKDWPIQIRDKRKRdLVLNVWDFAGREEFYSTHPHFMTQRA 1413
Cdd:TIGR00231    1 DIKIVIVGHPNVGKSTLLNSLLGNKGSIT---EYYPGTTRNYVTTVIEEDGKT-YKFNLLDTAGQEDYDAIRRLYYPQVE 76

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121  1414 LYLAVYDLSKGQAEV-DAMKPWLFNIK-ARASSSPVILVGTHLDVSDEKqrkacMSKITKELLNKRGFPAI 1482
Cdd:TIGR00231   77 RSLRVFDIVILVLDVeEILEKQTKEIIhHADSGVPIILVGNKIDLKDAD-----LKTHVASEFAKLNGEPI 142
Rab26 cd04112
Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, ...
 1336-1463 6.38e-12

Rab GTPase family 26 (Rab26); Rab26 subfamily. First identified in rat pancreatic acinar cells, Rab26 is believed to play a role in recruiting mature granules to the plasma membrane upon beta-adrenergic stimulation. Rab26 belongs to the Rab functional group III, which are considered key regulators of intracellular vesicle transport during exocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206695 [Multi-domain]  Cd Length: 191  Bit Score: 66.04  E-value: 6.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLmKTKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYS-THPHFMTQRAL 1414
Cdd:cd04112     2 KVMLVGDSGVGKTCLLVRF-KDGAFLAGSFIATVGIQFTNKVVTVDGVKVK---LQIWDTAGQERFRSvTHAYYRDAHAL 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767973121 1415 YLaVYDLSKgQAEVDAMKPWLFNIKARASSSPVI-LVGTHLDVSDEKQRK 1463
Cdd:cd04112    78 LL-LYDVTN-KSSFDNIRAWLTEILEYAQSDVVImLLGNKADMSGERVVK 125
Rab30 cd04114
Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi ...
 1336-1500 6.55e-12

Rab GTPase family 30 (Rab30); Rab30 subfamily. Rab30 appears to be associated with the Golgi stack. It is expressed in a wide variety of tissue types and in humans maps to chromosome 11. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133314 [Multi-domain]  Cd Length: 169  Bit Score: 65.69  E-value: 6.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKtkksdlGM----QSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYS-THPHFMT 1410
Cdd:cd04114     9 KIVLIGNAGVGKTCLVRRFTQ------GLfppgQGATIGVDFMIKTVEIKGEKIK---LQIWDTAGQERFRSiTQSYYRS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1411 QRALYLaVYDLSkGQAEVDAMKPWLFNIKARASSSPV-ILVGTHLDVSDEkqrkacmskitKELLNKRG--FPAIRDYHF 1487
Cdd:cd04114    80 ANALIL-TYDIT-CEESFRCLPEWLREIEQYANNKVItILVGNKIDLAER-----------REVSQQRAeeFSDAQDMYY 146

                         170
                  ....*....|....
gi 767973121 1488 VNAT-EESDALAKL 1500
Cdd:cd04114   147 LETSaKESDNVEKL 160
Ras pfam00071
Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop ...
 1336-1461 3.65e-11

Ras family; Includes sub-families Ras, Rab, Rac, Ral, Ran, Rap Ypt1 and more. Shares P-loop motif with GTP_EFTU, arf and myosin_head. See pfam00009 pfam00025, pfam00063. As regards Rab GTPases, these are important regulators of vesicle formation, motility and fusion. They share a fold in common with all Ras GTPases: this is a six-stranded beta-sheet surrounded by five alpha-helices.


Pssm-ID: 425451 [Multi-domain]  Cd Length: 162  Bit Score: 63.30  E-value: 3.65e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1336 KLMIVGNTGSGKTTLLQQLMK---TKKSDlgmqsATVGIDVKDWPIQIRDKRkrdLVLNVWDFAGREEFYSTHPHFMTQR 1412
Cdd:pfam00071    1 KLVLVGDGGVGKSSLLIRFTQnkfPEEYI-----PTIGVDFYTKTIEVDGKT---VKLQIWDTAGQERFRALRPLYYRGA 72

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 767973121  1413 ALYLAVYDLSKgQAEVDAMKPWLFNIKARASSS-PVILVGTHLDVSDEKQ 1461
Cdd:pfam00071   73 DGFLLVYDITS-RDSFENVKKWVEEILRHADENvPIVLVGNKCDLEDQRV 121
Rab6 cd01861
Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways ...
 1336-1461 8.81e-11

Rab GTPase family 6 (Rab6); Rab6 is involved in microtubule-dependent transport pathways through the Golgi and from endosomes to the Golgi. Rab6A of mammals is implicated in retrograde transport through the Golgi stack, and is also required for a slow, COPI-independent, retrograde transport pathway from the Golgi to the endoplasmic reticulum (ER). This pathway may allow Golgi residents to be recycled through the ER for scrutiny by ER quality-control systems. Yeast Ypt6p, the homolog of the mammalian Rab6 GTPase, is not essential for cell viability. Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde transport, and possibly also in Golgi-to-ER trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206654 [Multi-domain]  Cd Length: 161  Bit Score: 61.87  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMkTKKSDLGMQsATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:cd01861     2 KLVFLGDQSVGKTSIITRFM-YDTFDNQYQ-ATIGIDFLSKTMYVDDKTVR---LQLWDTAGQERFRSLIPSYIRDSSVA 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 767973121 1416 LAVYDLSKGQAEVDAMKpWLFNIKARASSSPVI-LVGTHLDVSDEKQ 1461
Cdd:cd01861    77 VVVYDITNRQSFDNTDK-WIDDVRDERGNDVIIvLVGNKTDLSDKRQ 122
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 984-1169 1.31e-10

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 62.88  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  984 ITSLDLSANELRDIDALSQkCCisvhleHLEKLELHQNALTSFPQqlCETLKSLTHLDLHSNKFTSFPSyLLKMSCIANL 1063
Cdd:cd21340     4 ITHLYLNDKNITKIDNLSL-CK------NLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEKIEN-LENLVNLKKL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1064 DVSRNDIgpSVV--LDptvKCPTLKQFNLSYNQL------SFVPENLTDVVEKLEQLILEGNKISGIcSPLR-LKELKIL 1134
Cdd:cd21340    74 YLGGNRI--SVVegLE---NLTNLEELHIENQRLppgeklTFDPRSLAALSNSLRVLNISGNNIDSL-EPLApLRNLEQL 147

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 767973121 1135 NLSKNHISSLSE--NFLEACPKVESFSARMNFLAAMP 1169
Cdd:cd21340   148 DASNNQISDLEEllDLLSSWPSLRELDLTGNPVCKKP 184
Rab12 cd04120
Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was ...
 1335-1461 1.34e-10

Rab GTPase family 12 (Rab12); Rab12 was first identified in canine cells, where it was localized to the Golgi complex. The specific function of Rab12 remains unknown, and inconsistent results about its cellular localization have been reported. More recent studies have identified Rab12 associated with post-Golgi vesicles, or with other small vesicle-like structures but not with the Golgi complex. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 206699 [Multi-domain]  Cd Length: 202  Bit Score: 62.72  E-value: 1.34e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLmkTKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYS-THPHFMTQRA 1413
Cdd:cd04120     1 LQVIIIGSRGVGKTSLMERF--TDDTFCEACKSTVGVDFKIKTVELRGKKIR---LQIWDTAGQERFNSiTSAYYRSAKG 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767973121 1414 LYLaVYDLSKgQAEVDAMKPWLFNIKARASS-SPVILVGTHLDVSDEKQ 1461
Cdd:cd04120    76 IIL-VYDITK-KETFDDLPKWMKMIDKYASEdAELLLVGNKLDCETDRE 122
Rab3 cd01865
Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, ...
 1336-1460 8.18e-10

Rab GTPase family 3 contains Rab3A, Rab3B, Rab3C and Rab3D; The Rab3 subfamily contains Rab3A, Rab3B, Rab3C, and Rab3D. All four isoforms were found in mouse brain and endocrine tissues, with varying levels of expression. Rab3A, Rab3B, and Rab3C localized to synaptic and secretory vesicles; Rab3D was expressed at high levels only in adipose tissue, exocrine glands, and the endocrine pituitary, where it is localized to cytoplasmic secretory granules. Rab3 appears to control Ca2+-regulated exocytosis. The appropriate GDP/GTP exchange cycle of Rab3A is required for Ca2+-regulated exocytosis to occur, and interaction of the GTP-bound form of Rab3A with effector molecule(s) is widely believed to be essential for this process. Functionally, most studies point toward a role for Rab3 in the secretion of hormones and neurotransmitters. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206657 [Multi-domain]  Cd Length: 165  Bit Score: 59.54  E-value: 8.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLqqlmkTKKSDLGMQSA---TVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQR 1412
Cdd:cd01865     3 KLLIIGNSSVGKTSFL-----FRYADDSFTSAfvsTVGIDFKVKTVYRNDKRIK---LQIWDTAGQERYRTITTAYYRGA 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767973121 1413 ALYLAVYDLSKgQAEVDAMKPWLFNIKARASSSP-VILVGTHLDVSDEK 1460
Cdd:cd01865    75 MGFILMYDITN-EESFNAVQDWSTQIKTYSWDNAqVILVGNKCDMEDER 122
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 971-1278 2.13e-09

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 62.56  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  971 SDSISSLASEREYITSLDLSANELRDidalsqkccisvhlehleklelhqnaltSFPQQLCETLKSLTHLDLHSNKFT-S 1049
Cdd:PLN00113   82 SGKISSAIFRLPYIQTINLSNNQLSG----------------------------PIPDDIFTTSSSLRYLNLSNNNFTgS 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1050 FPSYLLkmSCIANLDVSRNDIGPSVVLDPTVkCPTLKQFNLSYNQLS-FVPENLTDVVeKLEQLILEGNKISG-ICSPL- 1126
Cdd:PLN00113  134 IPRGSI--PNLETLDLSNNMLSGEIPNDIGS-FSSLKVLDLGGNVLVgKIPNSLTNLT-SLEFLTLASNQLVGqIPRELg 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1127 RLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMpfLPPSMTILK------LSQNKFS-CIPEAILNLPHLR 1199
Cdd:PLN00113  210 QMKSLKWIYLGYNNLSGEIPYEIGGLTSLNHLDLVYNNLTGP--IPSSLGNLKnlqylfLYQNKLSgPIPPSIFSLQKLI 287

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1200 SLDMSSNDIqylpgpahwkSLNLRELLFSHNQISILDLSEKAY-------LWS--RVEKLHLSHNKLK-EIPPEIGCLEN 1269
Cdd:PLN00113  288 SLDLSDNSL----------SGEIPELVIQLQNLEILHLFSNNFtgkipvaLTSlpRLQVLQLWSNKFSgEIPKNLGKHNN 357


                  ....*....
gi 767973121 1270 LTSLDVSYN 1278
Cdd:PLN00113  358 LTVLDLSTN 366
Rab27A cd04127
Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly ...
 1335-1482 4.23e-09

Rab GTPase family 27a (Rab27a); The Rab27a subfamily consists of Rab27a and its highly homologous isoform, Rab27b. Unlike most Rab proteins whose functions remain poorly defined, Rab27a has many known functions. Rab27a has multiple effector proteins, and depending on which effector it binds, Rab27a has different functions as well as tissue distribution and/or cellular localization. Putative functions have been assigned to Rab27a when associated with the effector proteins Slp1, Slp2, Slp3, Slp4, Slp5, DmSlp, rabphilin, Dm/Ce-rabphilin, Slac2-a, Slac2-b, Slac2-c, Noc2, JFC1, and Munc13-4. Rab27a has been associated with several human diseases, including hemophagocytic syndrome (Griscelli syndrome or GS), Hermansky-Pudlak syndrome, and choroidermia. In the case of GS, a rare, autosomal recessive disease, a Rab27a mutation is directly responsible for the disorder. When Rab27a is localized to the secretory granules of pancreatic beta cells, it is believed to mediate glucose-stimulated insulin secretion, making it a potential target for diabetes therapy. When bound to JFC1 in prostate cells, Rab27a is believed to regulate the exocytosis of prostate- specific markers. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206700 [Multi-domain]  Cd Length: 180  Bit Score: 57.51  E-value: 4.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSdlGMQSATVGIDVKD--------WPIQIRDKRKRdLVLNVWDFAGREEFYSTHP 1406
Cdd:cd04127     5 IKLLALGDSGVGKTTFLYRYTDNKFN--PKFITTVGIDFREkrvvynsqGPDGTSGKAFR-VHLQLWDTAGQERFRSLTT 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767973121 1407 HFMTQRALYLAVYDLSKGQAEVDaMKPWLFNIKARA-SSSP-VILVGTHLDVSDEKQRKAcmsKITKELLNKRGFPAI 1482
Cdd:cd04127    82 AFFRDAMGFLLMFDLTSEQSFLN-VRNWMSQLQAHAyCENPdIVLIGNKADLPDQREVSE---RQARELADKYGIPYF 155
Rab35 cd04110
Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate ...
 1336-1468 7.72e-09

Rab GTPase family 35 (Rab35); Rab35 is one of several Rab proteins to be found to participate in the regulation of osteoclast cells in rats. In addition, Rab35 has been identified as a protein that interacts with nucleophosmin-anaplastic lymphoma kinase (NPM-ALK) in human cells. Overexpression of NPM-ALK is a key oncogenic event in some anaplastic large-cell lymphomas; since Rab35 interacts with N|PM-ALK, it may provide a target for cancer treatments. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133310 [Multi-domain]  Cd Length: 199  Bit Score: 57.17  E-value: 7.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKTKKSdlGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:cd04110     8 KLLIIGDSGVGKSSLLLRFADNTFS--GSYITTIGVDFKIRTVEINGERVK---LQIWDTAGQERFRTITSTYYRGTHGV 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767973121 1416 LAVYDLSKGQAEVDaMKPWLFNIKARASSSPVILVGTHldvSDEKQRKACMSK 1468
Cdd:cd04110    83 IVVYDVTNGESFVN-VKRWLQEIEQNCDDVCKVLVGNK---NDDPERKVVETE 131
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 1010-1305 4.64e-08

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 58.32  E-value: 4.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1010 LEHLEKLELHQNALT-SFPQQLCEtLKSLTHLDLHSNKFT-SFPSYLLKMSCIANLDVSRNDIG---PSVVLdptvKCPT 1084
Cdd:PLN00113  235 LTSLNHLDLVYNNLTgPIPSSLGN-LKNLQYLFLYQNKLSgPIPPSIFSLQKLISLDLSDNSLSgeiPELVI----QLQN 309

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1085 LKQFNLSYNQLS-FVPENLTDVvEKLEQLILEGNKISG-ICSPL-RLKELKILNLSKNHISS-LSENFLEA--CPKVESF 1158
Cdd:PLN00113  310 LEILHLFSNNFTgKIPVALTSL-PRLQVLQLWSNKFSGeIPKNLgKHNNLTVLDLSTNNLTGeIPEGLCSSgnLFKLILF 388

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1159 SarmNFLAAMpfLPPSMTI------LKLSQNKFSC-IPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQ 1231
Cdd:PLN00113  389 S---NSLEGE--IPKSLGAcrslrrVRLQDNSFSGeLPSEFTKLPLVYFLDISNNNLQGRINSRKWDMPSLQMLSLARNK 463

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973121 1232 IS--ILDLSEKaylwSRVEKLHLSHNKLKE-IPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDELHLN 1305
Cdd:PLN00113  464 FFggLPDSFGS----KRLENLDLSRNQFSGaVPRKLGSLSELMQLKLSENKLSGEIPDELSSCKKLVSLDLSHNQLS 536
PLN03118 PLN03118
Rab family protein; Provisional
 1336-1460 6.97e-08

Rab family protein; Provisional


Pssm-ID: 215587 [Multi-domain]  Cd Length: 211  Bit Score: 54.68  E-value: 6.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKTKKSDLgmqSATVGIDVKDWPIQIRDKRkrdLVLNVWDFAGREEFYS-THPHFMTQRAL 1414
Cdd:PLN03118   16 KILLIGDSGVGKSSLLVSFISSSVEDL---APTIGVDFKIKQLTVGGKR---LKLTIWDTAGQERFRTlTSSYYRNAQGI 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767973121 1415 YLaVYDLSKGQAEVDAMKPWLFNIKARASSSPVI--LVGTHLDVSDEK 1460
Cdd:PLN03118   90 IL-VYDVTRRETFTNLSDVWGKEVELYSTNQDCVkmLVGNKVDRESER 136
Rab23_like cd04106
Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family ...
 1335-1477 2.18e-07

Rab GTPase family 23 (Rab23)-like; Rab23-like subfamily. Rab23 is a member of the Rab family of small GTPases. In mouse, Rab23 has been shown to function as a negative regulator in the sonic hedgehog (Shh) signaling pathway. Rab23 mediates the activity of Gli2 and Gli3, transcription factors that regulate Shh signaling in the spinal cord, primarily by preventing Gli2 activation in the absence of Shh ligand. Rab23 also regulates a step in the cytoplasmic signal transduction pathway that mediates the effect of Smoothened (one of two integral membrane proteins that are essential components of the Shh signaling pathway in vertebrates). In humans, Rab23 is expressed in the retina. Mice contain an isoform that shares 93% sequence identity with the human Rab23 and an alternative splicing isoform that is specific to the brain. This isoform causes the murine open brain phenotype, indicating it may have a role in the development of the central nervous system. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133306 [Multi-domain]  Cd Length: 162  Bit Score: 52.06  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDlgMQSATVGIDVKDWPIQIRdKRKRDLVLNVWDFAGREEFYS-THPHFMTQRA 1413
Cdd:cd04106     1 IKVIVVGNGNVGKSSMIQRFVKGIFTK--DYKKTIGVDFLEKQIFLR-QSDEDVRLMLWDTAGQEEFDAiTKAYYRGAQA 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1414 LYLAVYDLSKgqAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEkqrkACMSKITKELLNKR 1477
Cdd:cd04106    78 CILVFSTTDR--ESFEAIESWKEKVEAECGDIPMVLVQTKIDLLDQ----AVITNEEAEALAKR 135
Rab8_Rab10_Rab13_like cd01867
Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to ...
 1335-1461 4.40e-07

Rab GTPase families 8, 10, 13 (Rab8, Rab10, Rab13); Rab8/Sec4/Ypt2 are known or suspected to be involved in post-Golgi transport to the plasma membrane. It is likely that these Rabs have functions that are specific to the mammalian lineage and have no orthologs in plants. Rab8 modulates polarized membrane transport through reorganization of actin and microtubules, induces the formation of new surface extensions, and has an important role in directed membrane transport to cell surfaces. The Ypt2 gene of the fission yeast Schizosaccharomyces pombe encodes a member of the Ypt/Rab family of small GTP-binding proteins, related in sequence to Sec4p of Saccharomyces cerevisiae but closer to mammalian Rab8. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206659 [Multi-domain]  Cd Length: 167  Bit Score: 51.50  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDLGMqsATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFysthpHFMTQrAL 1414
Cdd:cd01867     4 FKLLLIGDSGVGKSCLLLRFSEDSFNPSFI--STIGIDFKIRTIELDGKKIK---LQIWDTAGQERF-----RTITT-SY 72

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1415 Y------LAVYDLSKgQAEVDAMKPWLFNIKARASSSPV-ILVGTHLDVSDEKQ 1461
Cdd:cd01867    73 YrgamgiILVYDITD-EKSFENIKNWMRNIDEHASEDVErMLVGNKCDMEEKRV 125
Rab7 cd01862
Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates ...
 1335-1468 4.69e-07

Rab GTPase family 7 (Rab7); Rab7 subfamily. Rab7 is a small Rab GTPase that regulates vesicular traffic from early to late endosomal stages of the endocytic pathway. The yeast Ypt7 and mammalian Rab7 are both involved in transport to the vacuole/lysosome, whereas Ypt7 is also required for homotypic vacuole fusion. Mammalian Rab7 is an essential participant in the autophagic pathway for sequestration and targeting of cytoplasmic components to the lytic compartment. Mammalian Rab7 is also proposed to function as a tumor suppressor. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206655 [Multi-domain]  Cd Length: 172  Bit Score: 51.51  E-value: 4.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDLgmQSATVGID--VKDwpIQIRDKrkrdLV-LNVWDFAGREEFYSTHPhfmtq 1411
Cdd:cd01862     1 LKVIILGDSGVGKTSLMNQYVNKKFSNQ--YKATIGADflTKE--VTVDDR----LVtLQIWDTAGQERFQSLGV----- 67

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1412 rALY------LAVYDLSKgQAEVDAMKPWL--FNIKARASSS---PVILVGTHLDVSDEKQ---RKA---CMSK 1468
Cdd:cd01862    68 -AFYrgadccVLVYDVTN-PKSFESLDSWRdeFLIQASPRDPenfPFVVLGNKIDLEEKRQvstKKAqqwCKSK 139
Rab39 cd04111
Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell ...
 1336-1461 6.13e-07

Rab GTPase family 39 (Rab39); Found in eukaryotes, Rab39 is mainly found in epithelial cell lines, but is distributed widely in various human tissues and cell lines. It is believed to be a novel Rab protein involved in regulating Golgi-associated vesicular transport during cellular endocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins.


Pssm-ID: 133311 [Multi-domain]  Cd Length: 211  Bit Score: 52.07  E-value: 6.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKTKKSDLGmqSATVGIDVKDWPIQIRDKRKrdLVLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:cd04111     4 RLIVIGDSTVGKSSLLKRFTEGRFAEVS--DPTVGVDFFSRLIEIEPGVR--IKLQLWDTAGQERFRSITRSYYRNSVGV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767973121 1416 LAVYDLSKgQAEVDAMKPWLfnIKARAS---SSPV-ILVGTHLDVSDEKQ 1461
Cdd:cd04111    80 LLVFDITN-RESFEHVHDWL--EEARSHiqpHRPVfILVGHKCDLESQRQ 126
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 1034-1255 7.84e-07

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 51.71  E-value: 7.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1034 LKSLTHLDLHSNKFTSfpsyllkmscIANLDVsrndigpsvvldptvkCPTLKQFNLSYNQLSFVP--ENLTdvveKLEQ 1111
Cdd:cd21340     1 LKRITHLYLNDKNITK----------IDNLSL----------------CKNLKVLYLYDNKITKIEnlEFLT----NLTH 50

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1112 LILEGNKISGICSPLRLKELKILNLSKNHISSLsENfLEACPKVESFS-ARMNflaampfLPPSMTILklsqnkFSciPE 1190
Cdd:cd21340    51 LYLQNNQIEKIENLENLVNLKKLYLGGNRISVV-EG-LENLTNLEELHiENQR-------LPPGEKLT------FD--PR 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767973121 1191 AILNL-PHLRSLDMSSNDIQYLPGPAHWKslNLRELLFSHNQIS-ILDLSEKAYLWSRVEKLHLSHN 1255
Cdd:cd21340   114 SLAALsNSLRVLNISGNNIDSLEPLAPLR--NLEQLDASNNQISdLEELLDLLSSWPSLRELDLTGN 178
Rab14 cd04122
Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, ...
 1336-1461 9.69e-07

Rab GTPase family 14 (Rab14); Rab14 GTPases are localized to biosynthetic compartments, including the rough ER, the Golgi complex, and the trans-Golgi network, and to endosomal compartments, including early endosomal vacuoles and associated vesicles. Rab14 is believed to function in both the biosynthetic and recycling pathways between the Golgi and endosomal compartments. Rab14 has also been identified on GLUT4 vesicles, and has been suggested to help regulate GLUT4 translocation. In addition, Rab14 is believed to play a role in the regulation of phagocytosis. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133322 [Multi-domain]  Cd Length: 166  Bit Score: 50.61  E-value: 9.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLmkTKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:cd04122     4 KYIIIGDMGVGKSCLLHQF--TEKKFMADCPHTIGVEFGTRIIEVNGQKIK---LQIWDTAGQERFRAVTRSYYRGAAGA 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767973121 1416 LAVYDLSKgQAEVDAMKPWLFNikARASSSP---VILVGTHLDVSDEKQ 1461
Cdd:cd04122    79 LMVYDITR-RSTYNHLSSWLTD--ARNLTNPntvIFLIGNKADLEAQRD 124
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
 1527-1611 1.07e-06

C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as the putative regulator of kinase activity. It functions as a proper GTP-binding protein with a low GTPase activity somehow stimulating the kinase activity.


Pssm-ID: 406489  Cd Length: 196  Bit Score: 51.09  E-value: 1.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1527 YVELEKIILSERKNVPIefpvIDRKRLLQLVRENQLQlDENELPHAVHFLNESGVLLHFQDpALQLSDLYFVEPKWLCKI 1606
Cdd:pfam16095    4 WLAVREALEKERQKKPY----ISYEEYRKICAENGID-DEEDQDTLLEFLHDLGVLLYFQD-DPGLRDIVILNPQWLTNA 77


                   ....*
gi 767973121  1607 MAQFV 1611
Cdd:pfam16095   78 VYRVL 82
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 1006-1294 1.08e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 53.70  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1006 ISVHLEHLEKLELhqnaLTSFPQQLCETLKSLTHLDlHSNKFTSFPSYLL-KMSCIANLDVSRNDIGPSVVLdPTVKCPT 1084
Cdd:PLN00113   21 LNFSMLHAEELEL----LLSFKSSINDPLKYLSNWN-SSADVCLWQGITCnNSSRVVSIDLSGKNISGKISS-AIFRLPY 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1085 LKQFNLSYNQLSF-VPENltdvvekleqlilegnkISGICSPLRLkelkiLNLSKNhisslsenfleacpkvesfsarmN 1163
Cdd:PLN00113   95 IQTINLSNNQLSGpIPDD-----------------IFTTSSSLRY-----LNLSNN-----------------------N 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1164 FLAAMP--FLPpSMTILKLSQNKFSC-IPEAILNLPHLRSLDMSSNdiqYLPG--PAHWKSL-NLRELLFSHNQISILDL 1237
Cdd:PLN00113  130 FTGSIPrgSIP-NLETLDLSNNMLSGeIPNDIGSFSSLKVLDLGGN---VLVGkiPNSLTNLtSLEFLTLASNQLVGQIP 205

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973121 1238 SEKAYLWSrVEKLHLSHNKLK-EIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKI 1294
Cdd:PLN00113  206 RELGQMKS-LKWIYLGYNNLSgEIPYEIGGLTSLNHLDLVYNNLTGPIPSSLGNLKNL 262
PLN03108 PLN03108
Rab family protein; Provisional
 1336-1460 1.12e-06

Rab family protein; Provisional


Pssm-ID: 178655 [Multi-domain]  Cd Length: 210  Bit Score: 51.10  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLmkTKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRALY 1415
Cdd:PLN03108    8 KYIIIGDTGVGKSCLLLQF--TDKRFQPVHDLTIGVEFGARMITIDNKPIK---LQIWDTAGQESFRSITRSYYRGAAGA 82

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767973121 1416 LAVYDLSKGQAeVDAMKPWLFNIKARASSS-PVILVGTHLDVSDEK 1460
Cdd:PLN03108   83 LLVYDITRRET-FNHLASWLEDARQHANANmTIMLIGNKCDLAHRR 127
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 986-1208 2.44e-06

Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 residue sequence motifs present in many proteins that participate in protein-protein interactions and have different functions and cellular locations. LRRs correspond to structural units consisting of a beta strand (LxxLxLxxN/CxL conserved pattern) and an alpha helix. This alignment contains 12 strands corresponding to 11 full repeats, consistent with the extent observed in the subfamily acting as Ran GTPase Activating Proteins (RanGAP1).


Pssm-ID: 238064 [Multi-domain]  Cd Length: 319  Bit Score: 51.20  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  986 SLDLSANELRDIDALSQkccISVhLEHLEKLELHQNALT-SFPQQLCETL---KSLTHLDLHSNKFTSFP-------SYL 1054
Cdd:cd00116     2 QLSLKGELLKTERATEL---LPK-LLCLQVLRLEGNTLGeEAAKALASALrpqPSLKELCLSLNETGRIPrglqsllQGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1055 LKMSCIANLDVSRNDIGP--SVVLDPTVKCPTLKQFNLSYNQLS-----FVPENLTDVVEKLEQLILEGNKISGICSPLR 1127
Cdd:cd00116    78 TKGCGLQELDLSDNALGPdgCGVLESLLRSSSLQELKLNNNGLGdrglrLLAKGLKDLPPALEKLVLGRNRLEGASCEAL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1128 LKE------LKILNLSKNHIS-----SLSENFLEACpKVESFSARMN--------FLAAMPFLPPSMTILKLSQNKFS-- 1186
Cdd:cd00116   158 AKAlranrdLKELNLANNGIGdagirALAEGLKANC-NLEVLDLNNNgltdegasALAETLASLKSLEVLNLGDNNLTda 236

                         250       260
                  ....*....|....*....|....*.
gi 767973121 1187 CIPEAILNLPH----LRSLDMSSNDI 1208
Cdd:cd00116   237 GAAALASALLSpnisLLTLSLSCNDI 262
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 986-1301 5.92e-06

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 51.39  E-value: 5.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  986 SLDLSANEL-----RDIDALSQkccisvhlehLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFT-SFPSYLLKMSC 1059
Cdd:PLN00113  144 TLDLSNNMLsgeipNDIGSFSS----------LKVLDLGGNVLVGKIPNSLTNLTSLEFLTLASNQLVgQIPRELGQMKS 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1060 IANLDVSRNDIGPSVvldPTV--KCPTLKQFNLSYNQLSF-VPENLTDVvEKLEQLILEGNKISGICSP----------- 1125
Cdd:PLN00113  214 LKWIYLGYNNLSGEI---PYEigGLTSLNHLDLVYNNLTGpIPSSLGNL-KNLQYLFLYQNKLSGPIPPsifslqklisl 289

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1126 ---------------LRLKELKILNLSKNHISSLSENFLEACPKVESFSARMNFLAAMpfLPP------SMTILKLSQNK 1184
Cdd:PLN00113  290 dlsdnslsgeipelvIQLQNLEILHLFSNNFTGKIPVALTSLPRLQVLQLWSNKFSGE--IPKnlgkhnNLTVLDLSTNN 367

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1185 FSC-IPEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQIS--------------ILDLSEKAYL------ 1243
Cdd:PLN00113  368 LTGeIPEGLCSSGNLFKLILFSNSLEGEIPKSLGACRSLRRVRLQDNSFSgelpseftklplvyFLDISNNNLQgrinsr 447

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121 1244 -WS--RVEKLHLSHNKLKEIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLDE 1301
Cdd:PLN00113  448 kWDmpSLQMLSLARNKFFGGLPDSFGSKRLENLDLSRNQFSGAVPRKLGSLSELMQLKLSE 508
Rop_like cd04133
Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) ...
 1390-1461 9.16e-06

Rho-related protein from plants (Rop)-like; The Rop (Rho-related protein from plants) subfamily plays a role in diverse cellular processes, including cytoskeletal organization, pollen and vegetative cell growth, hormone responses, stress responses, and pathogen resistance. Rops are able to regulate several downstream pathways to amplify a specific signal by acting as master switches early in the signaling cascade. They transmit a variety of extracellular and intracellular signals. Rops are involved in establishing cell polarity in root-hair development, root-hair elongation, pollen-tube growth, cell-shape formation, responses to hormones such as abscisic acid (ABA) and auxin, responses to abiotic stresses such as oxygen deprivation, and disease resistance and disease susceptibility. An individual Rop can have a unique function or an overlapping function shared with other Rop proteins; in addition, a given Rop-regulated function can be controlled by one or multiple Rop proteins. For example, Rop1, Rop3, and Rop5 are all involved in pollen-tube growth; Rop2 plays a role in response to low-oxygen environments, cell-morphology, and root-hair development; root-hair development is also regulated by Rop4 and Rop6; Rop6 is also responsible for ABA response, and ABA response is also regulated by Rop10. Plants retain some of the regulatory mechanisms that are shared by other members of the Rho family, but have also developed a number of unique modes for regulating Rops. Unique RhoGEFs have been identified that are exclusively active toward Rop proteins, such as those containing the domain PRONE (plant-specific Rop nucleotide exchanger). Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206705 [Multi-domain]  Cd Length: 173  Bit Score: 47.92  E-value: 9.16e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767973121 1390 LNVWDFAGREEFYSTHPhfMTQRA---LYLAVYDLSKGQAEvDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQ 1461
Cdd:cd04133    51 LGLWDTAGQEDYNRLRP--LSYRGadvFLLAFSLISKASYE-NVLKKWIPELRHYAPGVPIVLVGTKLDLRDDKQ 122
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 1108-1297 2.68e-05

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 47.09  E-value: 2.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1108 KLEQLILEGNKISGICSPLRLKELKILNLSKNHISSLsENfLEACPKvesfsarmnflaampflppsMTILKLSQNKFSC 1187
Cdd:cd21340     3 RITHLYLNDKNITKIDNLSLCKNLKVLYLYDNKITKI-EN-LEFLTN--------------------LTHLYLQNNQIEK 60

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1188 IpEAILNLPHLRSLDMSSNDIQYLPGpahwksL----NLRELLFSHNQisiLDLSEK--------AYLWSRVEKLHLSHN 1255
Cdd:cd21340    61 I-ENLENLVNLKKLYLGGNRISVVEG------LenltNLEELHIENQR---LPPGEKltfdprslAALSNSLRVLNISGN 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 767973121 1256 KLKEIPPeIGCLENLTSLDVSYNL--ELRSFPNEMGKLSKIWDL 1297
Cdd:cd21340   131 NIDSLEP-LAPLRNLEQLDASNNQisDLEELLDLLSSWPSLREL 173
Rnd cd04131
Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd ...
 1334-1480 3.39e-05

Rho family GTPase subfamily Rnd includes Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8; The Rnd subfamily contains Rnd1/Rho6, Rnd2/Rho7, and Rnd3/RhoE/Rho8. These novel Rho family proteins have substantial structural differences compared to other Rho members, including N- and C-terminal extensions relative to other Rhos. Rnd3/RhoE is farnesylated at the C-terminal prenylation site, unlike most other Rho proteins that are geranylgeranylated. In addition, Rnd members are unable to hydrolyze GTP and are resistant to GAP activity. They are believed to exist only in the GTP-bound conformation, and are antagonists of RhoA activity. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206703 [Multi-domain]  Cd Length: 176  Bit Score: 46.27  E-value: 3.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSDLGM----QSATVGIDVkdwpiqirDKRKRDLVLnvWDFAGREEFYSTHPHFM 1409
Cdd:cd04131     1 RCKIVLVGDSQCGKTALLQVFAKDSFPENYVptvfENYTASFEV--------DKQRIELSL--WDTSGSPYYDNVRPLSY 70

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121 1410 TQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEkqrkacmSKITKELLNKRGFP 1480
Cdd:cd04131    71 PDSDAVLICFDISRPETLDSVLKKWKGEVREFCPNTPVLLVGCKSDLRTD-------LSTLTELSNKRQIP 134
RAN smart00176
Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the ...
 1340-1511 3.88e-05

Ran (Ras-related nuclear proteins) /TC4 subfamily of small GTPases; Ran is involved in the active transport of proteins through nuclear pores.


Pssm-ID: 128473 [Multi-domain]  Cd Length: 200  Bit Score: 46.54  E-value: 3.88e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121   1340 VGNTGSGKTTLLQQLMK---TKKSDlgmqsATVGIDVKdwPIQIRDKRKRdLVLNVWDFAGREEFYSTHPHFMTQRALYL 1416
Cdd:smart00176    1 VGDGGTGKTTFVKRHLTgefEKKYV-----ATLGVEVH--PLVFHTNRGP-IRFNVWDTAGQEKFGGLRDGYYIQGQCAI 72

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121   1417 AVYDLSkGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQRKACMSKITKELLNKRGFPAIRDYHFvnateESDA 1496
Cdd:smart00176   73 IMFDVT-ARVTYKNVPNWHRDLVRVCENIPIVLCGNKVDVKDRKVKAKSITFHRKKNLQYYDISAKSNYNF-----EKPF 146

                           170
                    ....*....|....*
gi 767973121   1497 LAKLRKTIINESLNF 1511
Cdd:smart00176  147 LWLARKLIGDPNLEF 161
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
972-1208 4.13e-05

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 48.23  E-value: 4.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  972 DSISSLASEREYITSLDLSANELRDIDALS----QKCCISVHLEHLE-------KLELHQNALTSFPQqLCETLKSLTHL 1040
Cdd:PRK15387  232 NNLTSLPALPPELRTLEVSGNQLTSLPVLPpgllELSIFSNPLTHLPalpsglcKLWIFGNQLTSLPV-LPPGLQELSVS 310

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1041 DLHSNKFTSFPSYLLKMSCIANLDVSRndigpsvvldPTVkcPT-LKQFNLSYNQLSFVPEnltdVVEKLEQLILEGNKI 1119
Cdd:PRK15387  311 DNQLASLPALPSELCKLWAYNNQLTSL----------PTL--PSgLQELSVSDNQLASLPT----LPSELYKLWAYNNRL 374

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1120 SGICS-PLRLKELKIlnlSKNHISSLSenfleACP-KVESFSARMNFLAAMPFLPPSMTILKLSQNKFSCIPEAILNLPH 1197
Cdd:PRK15387  375 TSLPAlPSGLKELIV---SGNRLTSLP-----VLPsELKELMVSGNRLTSLPMLPSGLLSLSVYRNQLTRLPESLIHLSS 446

                         250
                  ....*....|.
gi 767973121 1198 LRSLDMSSNDI 1208
Cdd:PRK15387  447 ETTVNLEGNPL 457
Spg1 cd04128
Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in ...
 1335-1455 6.04e-05

Septum-promoting GTPase (Spg1); Spg1p. Spg1p (septum-promoting GTPase) was first identified in the fission yeast S. pombe, where it regulates septum formation in the septation initiation network (SIN) through the cdc7 protein kinase. Spg1p is an essential gene that localizes to the spindle pole bodies. When GTP-bound, it binds cdc7 and causes it to translocate to spindle poles. Sid4p (septation initiation defective) is required for localization of Spg1p to the spindle pole body, and the ability of Spg1p to promote septum formation from any point in the cell cycle depends on Sid4p. Spg1p is negatively regulated by Byr4 and cdc16, which form a two-component GTPase activating protein (GAP) for Spg1p. The existence of a SIN-related pathway in plants has been proposed. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 206701 [Multi-domain]  Cd Length: 182  Bit Score: 45.46  E-value: 6.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQsaTVGIDVKDWPIQIRDKRkrdLVLNVWDFAGREEFYSTHPHFMTQRAL 1414
Cdd:cd04128     1 LKIGLLGDAQIGKTSLMVKYVEGEFDEEYIQ--TLGVNFMEKTISIRGTE---ITFSIWDLGGQREFINMLPLVCKDAVA 75

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 767973121 1415 YLAVYDLSKgQAEVDAMKPWLFNIKARASSSPVILVGTHLD 1455
Cdd:cd04128    76 ILFMFDLTR-KSTLNSIKEWYRQARGFNKTAIPILVGTKYD 115
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 1188-1299 7.13e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.54  E-value: 7.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1188 IPEAILNLPHLRSLDMSSNDIQY-LPGPAHWKSLNLRELLFSHNQISildLSEKAYLWSRVEKLHLSHNKLK-EIPPEIG 1265
Cdd:PLN00113   85 ISSAIFRLPYIQTINLSNNQLSGpIPDDIFTTSSSLRYLNLSNNNFT---GSIPRGSIPNLETLDLSNNMLSgEIPNDIG 161

                          90       100       110
                  ....*....|....*....|....*....|....
gi 767973121 1266 CLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPL 1299
Cdd:PLN00113  162 SFSSLKVLDLGGNVLVGKIPNSLTNLTSLEFLTL 195
LRR_8 pfam13855
Leucine rich repeat;
985-1047 9.26e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 41.74  E-value: 9.26e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767973121   985 TSLDLSANELRDIDALSqkcciSVHLEHLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKF 1047
Cdd:pfam13855    4 RSLDLSNNRLTSLDDGA-----FKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
Rab15 cd04117
Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early ...
 1336-1461 1.17e-04

Rab GTPase family 15 (Rab15); Rab15 colocalizes with the transferrin receptor in early endosome compartments, but not with late endosomal markers. It codistributes with Rab4 and Rab5 on early/sorting endosomes, and with Rab11 on pericentriolar recycling endosomes. It is believed to function as an inhibitory GTPase that regulates distinct steps in early endocytic trafficking. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization. Most Rab GTPases contain a lipid modification site at the C-terminus, with sequence motifs CC, CXC, or CCX. Lipid binding is essential for membrane attachment, a key feature of most Rab proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206698 [Multi-domain]  Cd Length: 164  Bit Score: 44.20  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLmkTKKSDLGMQSATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYS-THPHFMTQRAL 1414
Cdd:cd04117     2 RLLLIGDSGVGKTCLLCRF--TDNEFHSSHISTIGVDFKMKTIEVDGIKVR---IQIWDTAGQERYQTiTKQYYRRAQGI 76

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767973121 1415 YLaVYDLSKGQAEVDAMKpWLFNIKARA-SSSPVILVGTHLDVSDEKQ 1461
Cdd:cd04117    77 FL-VYDISSERSYQHIMK-WVSDVDEYApEGVQKILIGNKADEEQKRQ 122
RabL4 cd04101
Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins ...
 1335-1461 1.97e-04

Rab GTPase-like family 4 (Rab-like4); RabL4 (Rab-like4) subfamily. RabL4s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL4 lacks a prenylation site at the C-terminus. The specific function of RabL4 remains unknown.


Pssm-ID: 206688 [Multi-domain]  Cd Length: 167  Bit Score: 43.67  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQL----MKTKKSDLgmqsATVGID--VKDWPIqirDKRKRDLVLNVWDFAGREEFYSTHPHF 1408
Cdd:cd04101     1 AQCAVVGDPAVGKSALVQMFhsdgATFQKNYT----MTTGCDlvVKTVPV---PDTSDSVELFIFDSAGQELFSDMVENV 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767973121 1409 MTQRALYLAVYDLSKgQAEVDAMKPWLFNIK--ARASSSPVILVGTHLDVSDEKQ 1461
Cdd:cd04101    74 WEQPAVVCVVYDVTN-EVSFNNCSRWINRVRthSHGLHTPGVLVGNKCDLTDRRE 127
Ran cd00877
Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in ...
 1336-1470 2.14e-04

Ras-related nuclear proteins (Ran)/TC4 family of small GTPases; Ran GTPase is involved in diverse biological functions, such as nuclear transport, spindle formation during mitosis, DNA replication, and cell division. Among the Ras superfamily, Ran is a unique small G protein. It does not have a lipid modification motif at the C-terminus to bind to the membrane, which is often observed within the Ras superfamily. Ran may therefore interact with a wide range of proteins in various intracellular locations. Like other GTPases, Ran exists in GTP- and GDP-bound conformations that interact differently with effectors. Conversion between these forms and the assembly or disassembly of effector complexes requires the interaction of regulator proteins. The intrinsic GTPase activity of Ran is very low, but it is greatly stimulated by a GTPase-activating protein (RanGAP1) located in the cytoplasm. By contrast, RCC1, a guanine nucleotide exchange factor that generates RanGTP, is bound to chromatin and confined to the nucleus. Ran itself is mobile and is actively imported into the nucleus by a mechanism involving NTF-2. Together with the compartmentalization of its regulators, this is thought to produce a relatively high concentration of RanGTP in the nucleus.


Pssm-ID: 206643 [Multi-domain]  Cd Length: 166  Bit Score: 43.44  E-value: 2.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMK---TKKSDlgmqsATVGIDVKdwPIQIRDKRKrDLVLNVWDFAGREEF------YSTHP 1406
Cdd:cd00877     2 KLVLVGDGGTGKTTFVKRHLTgefEKKYV-----ATLGVEVH--PLDFHTNRG-KIRFNVWDTAGQEKFgglrdgYYIQG 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1407 H---FM---TQRALYLAVYDlskgqaevdamkpWLFNIKARASSSPVILVGTHLDVSDeKQRKAcmSKIT 1470
Cdd:cd00877    74 QcaiIMfdvTSRVTYKNVPN-------------WHRDLVRVCENIPIVLCGNKVDIKD-RKVKP--KQIT 127
LRR_8 pfam13855
Leucine rich repeat;
1130-1208 2.43e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.59  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1130 ELKILNLSKNHISSLSenfleacpkVESFSArmnflaampflPPSMTILKLSQNKFSCI-PEAILNLPHLRSLDMSSNDI 1208
Cdd:pfam13855    2 NLRSLDLSNNRLTSLD---------DGAFKG-----------LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
RJL cd04119
Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with ...
 1336-1455 2.64e-04

Rab GTPase family J-like (RabJ-like); RJLs are found in many protists and as chimeras with C-terminal DNAJ domains in deuterostome metazoa. They are not found in plants, fungi, and protostome metazoa, suggesting a horizontal gene transfer between protists and deuterostome metazoa. RJLs lack any known membrane targeting signal and contain a degenerate phosphate/magnesium-binding 3 (PM3) motif, suggesting an impaired ability to hydrolyze GTP. GTPase activating proteins (GAPs) interact with GTP-bound Rab and accelerate the hydrolysis of GTP to GDP. Guanine nucleotide exchange factors (GEFs) interact with GDP-bound Rabs to promote the formation of the GTP-bound state. Rabs are further regulated by guanine nucleotide dissociation inhibitors (GDIs), which facilitate Rab recycling by masking C-terminal lipid binding and promoting cytosolic localization.


Pssm-ID: 133319 [Multi-domain]  Cd Length: 168  Bit Score: 43.50  E-value: 2.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLmkTKKSDLGMQSATVGID--VKdwPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRA 1413
Cdd:cd04119     2 KVISMGNSGVGKSCIIKRY--CEGRFVSKYLPTIGIDygVK--KVSVRNKEVR---VNFFDLSGHPEYLEVRNEFYKDTQ 74

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 767973121 1414 LYLAVYDLSKGQAeVDAMKPWLFNIK------ARASSSPVILVGTHLD 1455
Cdd:cd04119    75 GVLLVYDVTDRQS-FEALDSWLKEMKqeggphGNMENIVVVVCANKID 121
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 984-1232 2.89e-04

Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ribosomal structure and biogenesis];


Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 45.17  E-value: 2.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  984 ITSLDLSANELRDI------DALSQKCciSVHLEHLEKLELHQNALTSFPQQLCEtLKSLTHLDLHSNK-----FTSFPS 1052
Cdd:COG5238   182 VETVYLGCNQIGDEgieelaEALTQNT--TVTTLWLKRNPIGDEGAEILAEALKG-NKSLTTLDLSNNQigdegVIALAE 258

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1053 YLLKMSCIANLDVSRNDIGP--SVVLDPTVK-CPTLKQFNLSYNQLSFvpenltDVVEKLEQLiLEGNKIsgicsplrlk 1129
Cdd:COG5238   259 ALKNNTTVETLYLSGNQIGAegAIALAKALQgNTTLTSLDLSVNRIGD------EGAIALAEG-LQGNKT---------- 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1130 eLKILNLSKNHISslsenfleacpkvesfSARMNFLAAMPFLPPSMTILKLSQNKFS-----CIPEAILNLPHLRSLDMS 1204
Cdd:COG5238   322 -LHTLNLAYNGIG----------------AQGAIALAKALQENTTLHSLDLSDNQIGdegaiALAKYLEGNTTLRELNLG 384

                         250       260       270
                  ....*....|....*....|....*....|...
gi 767973121 1205 SNDI-----QYLpgPAHWKSLNLRELLFSHNQI 1232
Cdd:COG5238   385 KNNIgkqgaEAL--IDALQTNRLHTLILDGNLI 415
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 976-1064 3.17e-04

protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 (PPP1R42), also known as leucine-rich repeat-containing protein 67 (lrrc67) or testis leucine-rich repeat (TLRR) protein, plays a role in centrosome separation. PPP1R42 has been shown to interact with the well-conserved signaling protein phosphatase-1 (PP1) and thereby increasing PP1's activity, which counters centrosome separation. Inhibition of PPP1R42 expression increases the number of centrosomes per cell while its depletion reduces the activity of PP1 leading to activation of NEK2, the kinase responsible for phosphorylation of centrosomal linker proteins promoting centrosome separation.


Pssm-ID: 411060 [Multi-domain]  Cd Length: 220  Bit Score: 44.01  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  976 SLASEREYITSLDLSANELRDIDALSqkccisvHLEHLEKLELHQNALTSFpQQLCETLKS---LTHLDLHSNKFTSFPS 1052
Cdd:cd21340   114 SLAALSNSLRVLNISGNNIDSLEPLA-------PLRNLEQLDASNNQISDL-EELLDLLSSwpsLRELDLTGNPVCKKPK 185

                          90
                  ....*....|....*.
gi 767973121 1053 Y----LLKMSCIANLD 1064
Cdd:cd21340   186 YrdkiILASKSLEVLD 201
Rac1_like cd01871
Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like ...
 1335-1461 4.36e-04

Ras-related C3 botulinum toxin substrate 1 (rho family, small GTP binding protein Rac1)-like consists of Rac1, Rac2 and Rac3; The Rac1-like subfamily consists of Rac1, Rac2, and Rac3 proteins, plus the splice variant Rac1b that contains a 19-residue insertion near switch II relative to Rac1. While Rac1 is ubiquitously expressed, Rac2 and Rac3 are largely restricted to hematopoietic and neural tissues respectively. Rac1 stimulates the formation of actin lamellipodia and membrane ruffles. It also plays a role in cell-matrix adhesion and cell anoikis. In intestinal epithelial cells, Rac1 is an important regulator of migration and mediates apoptosis. Rac1 is also essential for RhoA-regulated actin stress fiber and focal adhesion complex formation. In leukocytes, Rac1 and Rac2 have distinct roles in regulating cell morphology, migration, and invasion, but are not essential for macrophage migration or chemotaxis. Rac3 has biochemical properties that are closely related to Rac1, such as effector interaction, nucleotide binding, and hydrolysis; Rac2 has a slower nucleotide association and is more efficiently activated by the RacGEF Tiam1. Both Rac1 and Rac3 have been implicated in the regulation of cell migration and invasion in human metastatic breast cancer. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206663 [Multi-domain]  Cd Length: 174  Bit Score: 42.88  E-value: 4.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLqqLMKTKKSDLG--------MQSATVGIDVKdwPIQirdkrkrdlvLNVWDFAGREEFYSTHP 1406
Cdd:cd01871     2 IKCVVVGDGAVGKTCLL--ISYTTNAFPGeyiptvfdNYSANVMVDGK--PVN----------LGLWDTAGQEDYDRLRP 67

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767973121 1407 HFMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDEKQ 1461
Cdd:cd01871    68 LSYPQTDVFLICFSLVSPASFENVRAKWYPEVRHHCPNTPIILVGTKLDLRDDKD 122
Rnd2_Rho7 cd04173
Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1 ...
 1334-1456 5.08e-04

Rnd2/Rho7 GTPases; Rnd2/Rho7 is a member of the novel Rho subfamily Rnd, together with Rnd1/Rho6 and Rnd3/RhoE/Rho8. Rnd2/Rho7 is transiently expressed in radially migrating cells in the brain while they are within the subventricular zone of the hippocampus and cerebral cortex. These migrating cells typically develop into pyramidal neurons. Cells that exogenously expressed Rnd2/Rho7 failed to migrate to upper layers of the brain, suggesting that Rnd2/Rho7 plays a role in the radial migration and morphological changes of developing pyramidal neurons, and that Rnd2/Rho7 degradation is necessary for proper cellular migration. The Rnd2/Rho7 GEF Rapostlin is found primarily in the brain and together with Rnd2/Rho7 induces dendrite branching. Unlike Rnd1/Rho6 and Rnd3/RhoE/Rho8, which are RhoA antagonists, Rnd2/Rho7 binds the GEF Pragmin and significantly stimulates RhoA activity and Rho-A mediated cell contraction. Rnd2/Rho7 is also found to be expressed in spermatocytes and early spermatids, with male-germ-cell Rac GTPase-activating protein (MgcRacGAP), where it localizes to the Golgi-derived pro-acrosomal vesicle. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins.


Pssm-ID: 206736 [Multi-domain]  Cd Length: 221  Bit Score: 43.48  E-value: 5.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSD------LGMQSATVGIDvkdwpiqirdkrKRDLVLNVWDFAGREEFYSTHPH 1407
Cdd:cd04173     1 RCKIVVVGDTQCGKTALLHVFAKDNYPEsyvptvFENYTASFEID------------KHRIELNMWDTSGSSYYDNVRPL 68

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767973121 1408 FMTQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDV 1456
Cdd:cd04173    69 AYPDSDAVLICFDISRPETLDSVLKKWQGETQEFCPNAKLVLVGCKLDM 117
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
1163-1295 5.17e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 44.77  E-value: 5.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1163 NFLAAMPFLPPSMTILKLSQNKFSCIPeaiLNLPHLRSLDMSSNDIQYLPG-PAHWKSL---------------NLRELL 1226
Cdd:PRK15387  232 NNLTSLPALPPELRTLEVSGNQLTSLP---VLPPGLLELSIFSNPLTHLPAlPSGLCKLwifgnqltslpvlppGLQELS 308

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121 1227 FSHNQISILDL--SEKAYLWSrveklhlSHNKLKEIPPEIGCLENLTsldVSYNlELRSFPNEMGKLSKIW 1295
Cdd:PRK15387  309 VSDNQLASLPAlpSELCKLWA-------YNNQLTSLPTLPSGLQELS---VSDN-QLASLPTLPSELYKLW 368
PLN03071 PLN03071
GTP-binding nuclear protein Ran; Provisional
 1330-1464 5.60e-04

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 178620 [Multi-domain]  Cd Length: 219  Bit Score: 43.20  E-value: 5.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1330 VPYNRMKLMIVGNTGSGKTTLLQQLMK---TKKSDlgmqsATVGIDVkdWPIQIRDKRKRdLVLNVWDFAGREEF----- 1401
Cdd:PLN03071    9 VDYPSFKLVIVGDGGTGKTTFVKRHLTgefEKKYE-----PTIGVEV--HPLDFFTNCGK-IRFYCWDTAGQEKFgglrd 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1402 -YSTHPH-----F-MTQRALYLAV----YDLSKgqaevdamkpWLFNIkarasssPVILVGTHLDVSDeKQRKA 1464
Cdd:PLN03071   81 gYYIHGQcaiimFdVTARLTYKNVptwhRDLCR----------VCENI-------PIVLCGNKVDVKN-RQVKA 136
Rnd1_Rho6 cd04174
Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2 ...
 1334-1461 6.96e-04

Rnd1/Rho6 GTPases; Rnd1/Rho6 is a member of the novel Rho subfamily Rnd, together with Rnd2/Rho7 and Rnd3/RhoE/Rho8. Rnd1/Rho6 binds GTP but does not hydrolyze it to GDP, indicating that it is constitutively active. In rat, Rnd1/Rho6 is highly expressed in the cerebral cortex and hippocampus during synapse formation, and plays a role in spine formation. Rnd1/Rho6 is also expressed in the liver and in endothelial cells, and is upregulated in uterine myometrial cells during pregnancy. Like Rnd3/RhoE/Rho8, Rnd1/Rho6 is believed to function as an antagonist to RhoA. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206737 [Multi-domain]  Cd Length: 232  Bit Score: 43.12  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1334 RMKLMIVGNTGSGKTTLLQQLMKTKKSDLGM----QSATVGIDVKDWPIQirdkrkrdlvLNVWDFAGREEFYSTHPHFM 1409
Cdd:cd04174    13 RCKLVLVGDVQCGKTAMLQVLAKDCYPETYVptvfENYTACLETEEQRVE----------LSLWDTSGSPYYDNVRPLCY 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767973121 1410 TQRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVG----------THLDVSDEKQ 1461
Cdd:cd04174    83 SDSDAVLLCFDISRPEIFDSALKKWRAEILDYCPSTRILLIGcktdlrtdlsTLMELSNQKQ 144
PTZ00099 PTZ00099
rab6; Provisional
 1367-1461 6.99e-04

rab6; Provisional


Pssm-ID: 185444 [Multi-domain]  Cd Length: 176  Bit Score: 42.42  E-value: 6.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1367 ATVGIDVKDWPIQIRDKRKRdlvLNVWDFAGREEFYSTHPHFMTQRALYLAVYDLSKGQAEVDAMKpWLFNI-KARASSS 1445
Cdd:PTZ00099   11 STIGIDFLSKTLYLDEGPVR---LQLWDTAGQERFRSLIPSYIRDSAAAIVVYDITNRQSFENTTK-WIQDIlNERGKDV 86

                          90
                  ....*....|....*.
gi 767973121 1446 PVILVGTHLDVSDEKQ 1461
Cdd:PTZ00099   87 IIALVGNKTDLGDLRK 102
RabL3 cd04102
Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins ...
 1335-1462 7.93e-04

Rab GTPase-like family 3 (Rab-like3); RabL3 (Rab-like3) subfamily. RabL3s are novel proteins that have high sequence similarity with Rab family members, but display features that are distinct from Rabs, and have been termed Rab-like. As in other Rab-like proteins, RabL3 lacks a prenylation site at the C-terminus. The specific function of RabL3 remains unknown.


Pssm-ID: 206689  Cd Length: 204  Bit Score: 42.58  E-value: 7.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTkkSDLGMQSATVG--IDVKDWPIQIRDKRKRDLVLNVWDFAG----REEFYSTHPHF 1408
Cdd:cd04102     1 VKVLVLGDSGVGKSSLVHLLCKN--QVLGNPSWTVGcsVDVRHHTYGEGTPEEKTFYVELWDVGGsvgsAESVKSTRAVF 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1409 MTQRALYLAVYDLSKGQAEVDAMKpWLFNIKARASSS--------------------PVILVGTHLDVSDEKQR 1462
Cdd:cd04102    79 YNQINGIIFVHDLTNKKSSQNLYR-WSLEALNRDTFPagllvtngdydseqfagnpvPLLVIGTKLDQIPEAKR 151
PTZ00132 PTZ00132
GTP-binding nuclear protein Ran; Provisional
 1336-1460 9.56e-04

GTP-binding nuclear protein Ran; Provisional


Pssm-ID: 240284 [Multi-domain]  Cd Length: 215  Bit Score: 42.37  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMK---TKKsdlgmQSATVGIDVKDWPIQIrdkRKRDLVLNVWDFAGREEF------YSTHP 1406
Cdd:PTZ00132   11 KLILVGDGGVGKTTFVKRHLTgefEKK-----YIPTLGVEVHPLKFYT---NCGPICFNVWDTAGQEKFgglrdgYYIKG 82

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1407 H-----F-MTQRALYLAVydlskgqaevdamKPWLFNIKARASSSPVILVGTHLDVSDEK 1460
Cdd:PTZ00132   83 QcaiimFdVTSRITYKNV-------------PNWHRDIVRVCENIPIVLVGNKVDVKDRQ 129
PLN03150 PLN03150
hypothetical protein; Provisional
 1244-1300 1.35e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.27  E-value: 1.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121 1244 WSRVEKL---HLSHNKLK-EIPPEIGCLENLTSLDVSYNLELRSFPNEMGKLSKIWDLPLD 1300
Cdd:PLN03150  438 ISKLRHLqsiNLSGNSIRgNIPPSLGSITSLEVLDLSYNSFNGSIPESLGQLTSLRILNLN 498
LRR_8 pfam13855
Leucine rich repeat;
1221-1279 1.48e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 38.27  E-value: 1.48e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121  1221 NLRELLFSHNqiSILDLSEKAYL-WSRVEKLHLSHNKLKEIPPE-IGCLENLTSLDVSYNL 1279
Cdd:pfam13855    2 NLRSLDLSNN--RLTSLDDGAFKgLSNLKVLDLSNNLLTTLSPGaFSGLPSLRYLDLSGNR 60
PLN00023 PLN00023
GTP-binding protein; Provisional
 1331-1423 1.88e-03

GTP-binding protein; Provisional


Pssm-ID: 177661  Cd Length: 334  Bit Score: 42.54  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1331 PYNRMKLMIVGNTGSGKTTLLQQLMKTkkSDLGMQSATVGIDVKDWPIQ----------IRDKRKRDLVLNVWDFAGREE 1400
Cdd:PLN00023   18 PCGQVRVLVVGDSGVGKSSLVHLIVKG--SSIARPPQTIGCTVGVKHITygspgsssnsIKGDSERDFFVELWDVSGHER 95

                          90       100
                  ....*....|....*....|...
gi 767973121 1401 FYSTHPHFMTQRALYLAVYDLSK 1423
Cdd:PLN00023   96 YKDCRSLFYSQINGVIFVHDLSQ 118
Rap2 cd04176
Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap ...
 1336-1461 1.90e-03

Rap2 family GTPase consists of Rap2a, Rap2b, and Rap2c; The Rap2 subgroup is part of the Rap subfamily of the Ras family. It consists of Rap2a, Rap2b, and Rap2c. Both isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK) are putative effectors of Rap2 in mediating the activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton. In human platelets, Rap2 was shown to interact with the cytoskeleton by binding the actin filaments. In embryonic Xenopus development, Rap2 is necessary for the Wnt/beta-catenin signaling pathway. The Rap2 interacting protein 9 (RPIP9) is highly expressed in human breast carcinomas and correlates with a poor prognosis, suggesting a role for Rap2 in breast cancer oncogenesis. Rap2b, but not Rap2a, Rap2c, Rap1a, or Rap1b, is expressed in human red blood cells, where it is believed to be involved in vesiculation. A number of additional effector proteins for Rap2 have been identified, including the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133376 [Multi-domain]  Cd Length: 163  Bit Score: 40.59  E-value: 1.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKtkksdlgmqsatvGIDVKDWPIQIRDKRKRDL-------VLNVWDFAGREEFYSTHPHF 1408
Cdd:cd04176     3 KVVVLGSGGVGKSALTVQFVS-------------GTFIEKYDPTIEDFYRKEIevdsspsVLEILDTAGTEQFASMRDLY 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767973121 1409 MTQRALYLAVYDLSKGQA--EVDAMKPWLFNIKaRASSSPVILVGTHLDVSDEKQ 1461
Cdd:cd04176    70 IKNGQGFIVVYSLVNQQTfqDIKPMRDQIVRVK-GYEKVPIILVGNKVDLESERE 123
LRR_8 pfam13855
Leucine rich repeat;
1012-1070 1.97e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 1.97e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  1012 HLEKLELHQNALTSFPQQLCETLKSLTHLDLHSNKFTSFPSYLL-KMSCIANLDVSRNDI 1070
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFsGLPSLRYLDLSGNRL 61
GBP cd01851
Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), ...
 1339-1528 2.04e-03

Guanylate-binding protein (GBP) family (N-terminal domain); Guanylate-binding protein (GBP), N-terminal domain. Guanylate-binding proteins (GBPs) define a group of proteins that are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. Furthermore, two unique regions around the base and the phosphate-binding areas, the guanine and the phosphate caps, respectively, give the nucleotide-binding site a unique appearance not found in the canonical GTP-binding proteins. The phosphate cap, which constitutes the region analogous to switch I, completely shields the phosphate-binding site from solvent such that a potential GTPase-activating protein (GAP) cannot approach.


Pssm-ID: 206650  Cd Length: 224  Bit Score: 41.54  E-value: 2.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1339 IVGNTGSGKTTLLQQLMKTKKS-DLG--MQSATVGIdvkdW----PIQIRDKRKRDLVLnvWDFAGreefysthphfmtq 1411
Cdd:cd01851    12 VFGSQSSGKSFLLNHLFGTSDGfDVMdtSQQTTKGI----WmwsdPFKDTDGKKHAVLL--LDTEG-------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1412 ralylaVYDLSKGQAEVDAmkpWLFNIkARASSSPVI--LVGTHLDvsDEKQRKACMSKITKELLNKRG-------FP-- 1480
Cdd:cd01851    72 ------TDGRERGEFENDA---RLFAL-ATLLSSVLIynMWQTILG--DDLDKLMGLLKTALETLGLAGlhnfskpKPll 139

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 767973121 1481 --AIRDyHFVNATEESDALAKLRKTIINEsLNfKIRDQLVVGQLIPDCYV 1528
Cdd:cd01851   140 lfVVRD-FTGPTPLEGLDVTEKSETLIEE-LN-KIWSSIRKPFTPITCFV 186
Rap_like cd04136
Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, ...
 1336-1460 2.55e-03

Rap-like family consists of Rap1, Rap2 and RSR1; The Rap subfamily consists of the Rap1, Rap2, and RSR1. Rap subfamily proteins perform different cellular functions, depending on the isoform and its subcellular localization. For example, in rat salivary gland, neutrophils, and platelets, Rap1 localizes to secretory granules and is believed to regulate exocytosis or the formation of secretory granules. Rap1 has also been shown to localize in the Golgi of rat fibroblasts, zymogen granules, plasma membrane, and microsomal membrane of the pancreatic acini, as well as in the endocytic compartment of skeletal muscle cells and fibroblasts. Rap1 localizes in the nucleus of human oropharyngeal squamous cell carcinomas (SCCs) and cell lines. Rap1 plays a role in phagocytosis by controlling the binding of adhesion receptors (typically integrins) to their ligands. In yeast, Rap1 has been implicated in multiple functions, including activation and silencing of transcription and maintenance of telomeres. Rap2 is involved in multiple functions, including activation of c-Jun N-terminal kinase (JNK) to regulate the actin cytoskeleton and activation of the Wnt/beta-catenin signaling pathway in embryonic Xenopus. A number of effector proteins for Rap2 have been identified, including isoform 3 of the human mitogen-activated protein kinase kinase kinase kinase 4 (MAP4K4) and Traf2- and Nck-interacting kinase (TNIK), and the RalGEFs RalGDS, RGL, and Rlf, which also interact with Rap1 and Ras. RSR1 is the fungal homolog of Rap1 and Rap2. In budding yeasts, it is involved in selecting a site for bud growth, which directs the establishment of cell polarization. The Rho family GTPase Cdc42 and its GEF, Cdc24, then establish an axis of polarized growth. It is believed that Cdc42 interacts directly with RSR1 in vivo. In filamentous fungi such as Ashbya gossypii, RSR1 is a key regulator of polar growth in the hypha. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 206708 [Multi-domain]  Cd Length: 164  Bit Score: 40.24  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMKtkksdlgmqsatvGIDVKDWPIQIRDKRKRDL-------VLNVWDFAGREEFYSTHPHF 1408
Cdd:cd04136     3 KLVVLGSGGVGKSALTVQFVQ-------------GIFVDKYDPTIEDSYRKQIevdcqqcMLEILDTAGTEQFTAMRDLY 69

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767973121 1409 MTQRALYLAVYDLSKGQA--EVDAMKPWLFNIKaRASSSPVILVGTHLDVSDEK 1460
Cdd:cd04136    70 IKNGQGFALVYSITAQQSfnDLQDLREQILRVK-DTEDVPMILVGNKCDLEDER 122
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 1246-1286 2.92e-03

Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a number of proteins with diverse functions and cellular locations. These repeats are usually involved in protein-protein interactions. Each Leucine Rich Repeat is composed of a beta-alpha unit. These units form elongated non-globular structures. Leucine Rich Repeats are often flanked by cysteine rich domains.


Pssm-ID: 463713 [Multi-domain]  Cd Length: 44  Bit Score: 37.22  E-value: 2.92e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 767973121  1246 RVEKLHLSHNKLKEIPPeIGCLENLTSLDVSYNLELRSFPN 1286
Cdd:pfam12799    2 NLEVLDLSNNQITDIPP-LAKLPNLETLDLSGNNKITDLSD 41
PTZ00369 PTZ00369
Ras-like protein; Provisional
 1333-1461 3.33e-03

Ras-like protein; Provisional


Pssm-ID: 240385 [Multi-domain]  Cd Length: 189  Bit Score: 40.62  E-value: 3.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1333 NRMKLMIVGNTGSGKTTLLQQLMKTKKSDlgmqsatvgidvkDWPIQIRDKRKRDLV-------LNVWDFAGREEFYSTH 1405
Cdd:PTZ00369    4 TEYKLVVVGGGGVGKSALTIQFIQNHFID-------------EYDPTIEDSYRKQCVideetclLDILDTAGQEEYSAMR 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 767973121 1406 PHFMTQRALYLAVYDLSKGQA--EVDAMKPWLFNIKARaSSSPVILVGTHLDVSDEKQ 1461
Cdd:PTZ00369   71 DQYMRTGQGFLCVYSITSRSSfeEIASFREQILRVKDK-DRVPMILVGNKCDLDSERQ 127
LRR_8 pfam13855
Leucine rich repeat;
1173-1232 3.63e-03

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.12  E-value: 3.63e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767973121  1173 PSMTILKLSQNKFSCI-PEAILNLPHLRSLDMSSNDIQYLPGPAHWKSLNLRELLFSHNQI 1232
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
700-795 4.84e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.71  E-value: 4.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121  700 AKVAMDDYLKNVMLERACDQNNSIMVECLLLLGADAN-QAKEGSSLICQVCEKeSSPKLVELLLNSG----SREQDVRKA 774
Cdd:COG0666   111 ADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNaQDNDGNTPLHLAAAN-GNLEIVKLLLEAGadvnARDNDGETP 189

                          90       100
                  ....*....|....*....|.
gi 767973121  775 LTISIGKGDSQIISLLLRRLA 795
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGA 210
Wrch_1 cd04130
Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 ...
 1335-1459 5.56e-03

Wnt-1 responsive Cdc42 homolog (Wrch-1) is a Rho family GTPase similar to Cdc42; Wrch-1 (Wnt-1 responsive Cdc42 homolog) is a Rho family GTPase that shares significant sequence and functional similarity with Cdc42. Wrch-1 was first identified in mouse mammary epithelial cells, where its transcription is upregulated in Wnt-1 transformation. Wrch-1 contains N- and C-terminal extensions relative to cdc42, suggesting potential differences in cellular localization and function. The Wrch-1 N-terminal extension contains putative SH3 domain-binding motifs and has been shown to bind the SH3 domain-containing protein Grb2, which increases the level of active Wrch-1 in cells. Unlike Cdc42, which localizes to the cytosol and perinuclear membranes, Wrch-1 localizes extensively with the plasma membrane and endosomes. The membrane association, localization, and biological activity of Wrch-1 indicate an atypical model of regulation distinct from other Rho family GTPases. Most Rho proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Rho proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133330 [Multi-domain]  Cd Length: 173  Bit Score: 39.69  E-value: 5.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1335 MKLMIVGNTGSGKTTLLQQLMKTKKSDLGMQSA----TVGIDVKDWPIQIRdkrkrdlvlnVWDFAGREEFYSTHPHFMT 1410
Cdd:cd04130     1 LKCVLVGDGAVGKTSLIVSYTTNGYPTEYVPTAfdnfSVVVLVDGKPVRLQ----------LCDTAGQDEFDKLRPLCYP 70

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 767973121 1411 QRALYLAVYDLSKGQAEVDAMKPWLFNIKARASSSPVILVGTHLDVSDE 1459
Cdd:cd04130    71 DTDVFLLCFSVVNPSSFQNISEKWIPEIRKHNPKAPIILVGTQADLRTD 119
M_R_Ras_like cd04145
R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, ...
 1336-1461 5.68e-03

R-Ras2/TC21, M-Ras/R-Ras3; The M-Ras/R-Ras-like subfamily contains R-Ras2/TC21, M-Ras/R-Ras3, and related members of the Ras family. M-Ras is expressed in lympho-hematopoetic cells. It interacts with some of the known Ras effectors, but appears to also have its own effectors. Expression of mutated M-Ras leads to transformation of several types of cell lines, including hematopoietic cells, mammary epithelial cells, and fibroblasts. Overexpression of M-Ras is observed in carcinomas from breast, uterus, thyroid, stomach, colon, kidney, lung, and rectum. In addition, expression of a constitutively active M-Ras mutant in murine bone marrow induces a malignant mast cell leukemia that is distinct from the monocytic leukemia induced by H-Ras. TC21, along with H-Ras, has been shown to regulate the branching morphogenesis of ureteric bud cell branching in mice. Most Ras proteins contain a lipid modification site at the C-terminus, with a typical sequence motif CaaX, where a = an aliphatic amino acid and X = any amino acid. Lipid binding is essential for membrane attachment, a key feature of most Ras proteins. Due to the presence of truncated sequences in this CD, the lipid modification site is not available for annotation.


Pssm-ID: 133345 [Multi-domain]  Cd Length: 164  Bit Score: 39.31  E-value: 5.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLMktkksdlgmQSatvgIDVKDWPIQIRDK-RKRDLVLNVW------DFAGREEFYSTHPHF 1408
Cdd:cd04145     4 KLVVVGGGGVGKSALTIQFI---------QS----YFVTDYDPTIEDSyTKQCEIDGQWarldilDTAGQEEFSAMREQY 70

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767973121 1409 MTQRALYLAVYDLSKGQA--EVDAMKPWLFNIKARaSSSPVILVGTHLDVSDEKQ 1461
Cdd:cd04145    71 MRTGEGFLLVFSVTDRGSfeEVDKFHTQILRVKDR-DEFPMILVGNKADLEHQRQ 124
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
 1336-1401 5.84e-03

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 39.10  E-value: 5.84e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767973121 1336 KLMIVGNTGSGKTTLLQQLmktKKSDLGMQSATVGIDVKDwpIQIRDKRkrdlvLNVWDFAGREEF 1401
Cdd:cd00878     1 RILMLGLDGAGKTTILYKL---KLGEVVTTIPTIGFNVET--VEYKNVK-----FTVWDVGGQDKI 56
PRK11784 PRK11784
tRNA 2-selenouridine synthase; Provisional
 1320-1354 6.23e-03

tRNA 2-selenouridine synthase; Provisional


Pssm-ID: 236982 [Multi-domain]  Cd Length: 345  Bit Score: 40.58  E-value: 6.23e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 767973121 1320 RFLQQRLKKAVPYNRMKLmIVGNTGSGKTTLLQQL 1354
Cdd:PRK11784  128 RFVIDTLEEAPAQFPLVV-LGGNTGSGKTELLQAL 161
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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