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Conserved domains on  [gi|110825984|ref|NP_004216|]
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malignant fibrous histiocytoma-amplified sequence 1 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
27-434 3.38e-45

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.96  E-value: 3.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   27 SNLRQLTLTAAGACPGAGADALESPASPQLVLPANLGDIEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRFARLPPAV 106
Cdd:COG4886    12 LLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  107 AELGHHLTELDVSHNRLtalgaevVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSLSCLSRLRTL 186
Cdd:COG4886    92 LGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  187 DVDHNQLTAFPRQLLQLVALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPAGFCELASLESLMLDNNGLQALP 266
Cdd:COG4886   165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  267 aQFSCLQRLKMLNLSSNLFEEFPaALLPLAGLEELYLSRNQLTSVP----SLISGLGRLLTLWLDNNRIRYLPDSIVELT 342
Cdd:COG4886   245 -ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  343 GLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGK 422
Cdd:COG4886   323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
                         410
                  ....*....|..
gi 110825984  423 TLLRHCLTEERV 434
Cdd:COG4886   403 LTLALLDAVNTE 414
P-loop_NTPase super family cl38936
P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain ...
409-552 3.51e-14

P-loop containing Nucleoside Triphosphate Hydrolases; Members of the P-loop NTPase domain superfamily are characterized by a conserved nucleotide phosphate-binding motif, also referred to as the Walker A motif (GxxxxGK[S/T], where x is any residue), and the Walker B motif (hhhh[D/E], where h is a hydrophobic residue). The Walker A and B motifs bind the beta-gamma phosphate moiety of the bound nucleotide (typically ATP or GTP) and the Mg2+ cation, respectively. The P-loop NTPases are involved in diverse cellular functions, and they can be divided into two major structural classes: the KG (kinase-GTPase) class which includes Ras-like GTPases and its circularly permutated YlqF-like; and the ASCE (additional strand catalytic E) class which includes ATPase Binding Cassette (ABC), DExD/H-like helicases, 4Fe-4S iron sulfur cluster binding proteins of NifH family, RecA-like F1-ATPases, and ATPases Associated with a wide variety of Activities (AAA). Also included are a diverse set of nucleotide/nucleoside kinase families.


The actual alignment was detected with superfamily member cd09914:

Pssm-ID: 476819 [Multi-domain]  Cd Length: 161  Bit Score: 71.21  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  409 RLKLLLMGHKAAGKTLLRHCLTEERVEGcpgggDKEKcyppspppvSKGIEVTSWT--ADASRGLRFIVYDLAGDESYEV 486
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFDG-----DESS---------THGINVQDWKipAPERKKIRLNVWDFGGQEIYHA 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110825984  487 IQPFFLSPGALYVLVVNLATYEprhFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCL 552
Cdd:cd09914    67 THQFFLTSRSLYLLVFDLRTGD---EVSRVPYWLRQIKAFGGVSPVILVGTHIDESCDEDILKKAL 129
COR super family cl24610
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
660-727 1.83e-04

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: 43.77  E-value: 1.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110825984   660 PRSWQVLEElHFQPPQAQRLWLSWWDSARLGLQAGLT-EDRLQSALSYLHESGKLLYFEDSPALKEHVF 727
Cdd:pfam16095    1 PKSWLAVRE-ALEKERQKKPYISYEEYRKICAENGIDdEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVI 68
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
27-434 3.38e-45

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.96  E-value: 3.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   27 SNLRQLTLTAAGACPGAGADALESPASPQLVLPANLGDIEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRFARLPPAV 106
Cdd:COG4886    12 LLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  107 AELGHHLTELDVSHNRLtalgaevVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSLSCLSRLRTL 186
Cdd:COG4886    92 LGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  187 DVDHNQLTAFPRQLLQLVALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPAGFCELASLESLMLDNNGLQALP 266
Cdd:COG4886   165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  267 aQFSCLQRLKMLNLSSNLFEEFPaALLPLAGLEELYLSRNQLTSVP----SLISGLGRLLTLWLDNNRIRYLPDSIVELT 342
Cdd:COG4886   245 -ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  343 GLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGK 422
Cdd:COG4886   323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
                         410
                  ....*....|..
gi 110825984  423 TLLRHCLTEERV 434
Cdd:COG4886   403 LTLALLDAVNTE 414
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
92-343 9.81e-22

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 101.70  E-value: 9.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   92 LVLRRNRFARLPPAVAElghHLTELDVSHNRLTALGAEVVSALRELrklNLSHNQLPALPAQLGALahLEELDVSFNRLA 171
Cdd:PRK15370  183 LRLKILGLTTIPACIPE---QITTLILDNNELKSLPENLQGNIKTL---YANSNQLTSIPATLPDT--IQEMELSINRIT 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  172 HLPDSLSclSRLRTLDVDHNQLTAFPRQLLQlvALEELDVSSNRLRGLPEDI-SALRALKILWLSGAEL-GTLPAGfcel 249
Cdd:PRK15370  255 ELPERLP--SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLpSGITHLNVQSNSLTALpETLPPG---- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  250 asLESLMLDNNGLQALPAqfSCLQRLKMLNLSSNLFEEFPAALLPLagLEELYLSRNQLTSVPSLISglGRLLTLWLDNN 329
Cdd:PRK15370  327 --LKTLEAGENALTSLPA--SLPPELQVLDVSKNQITVLPETLPPT--ITTLDVSRNALTNLPENLP--AALQIMQASRN 398
                         250
                  ....*....|....
gi 110825984  330 RIRYLPDSIVELTG 343
Cdd:PRK15370  399 NLVRLPESLPHFRG 412
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
68-236 1.69e-16

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: 79.44  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   68 LNLGNNGLEEVpEGLgSALGSLRVLVLRRNRFARLPPavaeLGH--HLTELDVSHNRLTALgaEVVSALRELRKLNLSHN 145
Cdd:cd21340     7 LYLNDKNITKI-DNL-SLCKNLKVLYLYDNKITKIEN----LEFltNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  146 QLPALpAQLGALAHLEELDVSFNRLAH------LPDSLSCLSR-LRTLDVDHNQLTAfPRQLLQLVALEELDVSSNRLRG 218
Cdd:cd21340    79 RISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALSNsLRVLNISGNNIDS-LEPLAPLRNLEQLDASNNQISD 156
                         170       180
                  ....*....|....*....|.
gi 110825984  219 LPE---DISALRALKILWLSG 236
Cdd:cd21340   157 LEElldLLSSWPSLRELDLTG 177
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
409-552 3.51e-14

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: 71.21  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  409 RLKLLLMGHKAAGKTLLRHCLTEERVEGcpgggDKEKcyppspppvSKGIEVTSWT--ADASRGLRFIVYDLAGDESYEV 486
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFDG-----DESS---------THGINVQDWKipAPERKKIRLNVWDFGGQEIYHA 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110825984  487 IQPFFLSPGALYVLVVNLATYEprhFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCL 552
Cdd:cd09914    67 THQFFLTSRSLYLLVFDLRTGD---EVSRVPYWLRQIKAFGGVSPVILVGTHIDESCDEDILKKAL 129
LRR_8 pfam13855
Leucine rich repeat;
251-308 2.93e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.07  E-value: 2.93e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   251 SLESLMLDNNGLQAL-PAQFSCLQRLKMLNLSSNLFEEF-PAALLPLAGLEELYLSRNQL 308
Cdd:pfam13855    2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
411-540 3.66e-08

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: 52.51  E-value: 3.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   411 KLLLMGHKAAGKT--LLRHClteervegcpgGGDKEKCYPPSPppvskGIEVTSWTA----DASRGLRFIVYDLAGDESY 484
Cdd:pfam08477    1 KVVLLGDSGVGKTslLKRFV-----------DDTFDPKYKSTI-----GVDFKTKTVlendDNGKKIKLNIWDTAGQERF 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110825984   485 EVIQPFFLSPGALYVLVVNLATYEprhfptTVGSFLHRVGARVPHAVVCIVGTHAD 540
Cdd:pfam08477   65 RSLHPFYYRGAAAALLVYDSRTFS------NLKYWLRELKKYAGNSPVILVGNKID 114
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
660-727 1.83e-04

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: 43.77  E-value: 1.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110825984   660 PRSWQVLEElHFQPPQAQRLWLSWWDSARLGLQAGLT-EDRLQSALSYLHESGKLLYFEDSPALKEHVF 727
Cdd:pfam16095    1 PKSWLAVRE-ALEKERQKKPYISYEEYRKICAENGIDdEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVI 68
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
27-434 3.38e-45

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 168.96  E-value: 3.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   27 SNLRQLTLTAAGACPGAGADALESPASPQLVLPANLGDIEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRFARLPPAV 106
Cdd:COG4886    12 LLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  107 AELGHHLTELDVSHNRLtalgaevVSALRELRKLNLSHNQLPALPAQLGALAHLEELDVSFNRLAHLPDSLSCLSRLRTL 186
Cdd:COG4886    92 LGDLTNLTELDLSGNEE-------LSNLTNLESLDLSGNQLTDLPEELANLTNLKELDLSNNQLTDLPEPLGNLTNLKSL 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  187 DVDHNQLTAFPRQLLQLVALEELDVSSNRLRGLPEDISALRALKILWLSGAELGTLPAGFCELASLESLMLDNNGLQALP 266
Cdd:COG4886   165 DLSNNQLTDLPEELGNLTNLKELDLSNNQITDLPEPLGNLTNLEELDLSGNQLTDLPEPLANLTNLETLDLSNNQLTDLP 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  267 aQFSCLQRLKMLNLSSNLFEEFPaALLPLAGLEELYLSRNQLTSVP----SLISGLGRLLTLWLDNNRIRYLPDSIVELT 342
Cdd:COG4886   245 -ELGNLTNLEELDLSNNQLTDLP-PLANLTNLKTLDLSNNQLTDLKlkelELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  343 GLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPLIQPPYEVCMKGIPYIAAYQKELAHSQPAVQPRLKLLLMGHKAAGK 422
Cdd:COG4886   323 LLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAGVLL 402
                         410
                  ....*....|..
gi 110825984  423 TLLRHCLTEERV 434
Cdd:COG4886   403 LTLALLDAVNTE 414
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
92-343 9.81e-22

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 101.70  E-value: 9.81e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   92 LVLRRNRFARLPPAVAElghHLTELDVSHNRLTALGAEVVSALRELrklNLSHNQLPALPAQLGALahLEELDVSFNRLA 171
Cdd:PRK15370  183 LRLKILGLTTIPACIPE---QITTLILDNNELKSLPENLQGNIKTL---YANSNQLTSIPATLPDT--IQEMELSINRIT 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  172 HLPDSLSclSRLRTLDVDHNQLTAFPRQLLQlvALEELDVSSNRLRGLPEDI-SALRALKILWLSGAEL-GTLPAGfcel 249
Cdd:PRK15370  255 ELPERLP--SALQSLDLFHNKISCLPENLPE--ELRYLSVYDNSIRTLPAHLpSGITHLNVQSNSLTALpETLPPG---- 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  250 asLESLMLDNNGLQALPAqfSCLQRLKMLNLSSNLFEEFPAALLPLagLEELYLSRNQLTSVPSLISglGRLLTLWLDNN 329
Cdd:PRK15370  327 --LKTLEAGENALTSLPA--SLPPELQVLDVSKNQITVLPETLPPT--ITTLDVSRNALTNLPENLP--AALQIMQASRN 398
                         250
                  ....*....|....
gi 110825984  330 RIRYLPDSIVELTG 343
Cdd:PRK15370  399 NLVRLPESLPHFRG 412
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
58-243 6.41e-21

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 99.00  E-value: 6.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   58 LPANLGD-IEALNLGNNGLEEVPEGLGSALGSlrvLVLRRNRFARLPPAVAElghHLTELDVSHNRLTALGAEVVSALRE 136
Cdd:PRK15370  235 IPATLPDtIQEMELSINRITELPERLPSALQS---LDLFHNKISCLPENLPE---ELRYLSVYDNSIRTLPAHLPSGITH 308
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  137 lrkLNLSHNQLPALPAQLGalAHLEELDVSFNRLAHLPDSLSclSRLRTLDVDHNQLTAFPRQLLQlvALEELDVSSNRL 216
Cdd:PRK15370  309 ---LNVQSNSLTALPETLP--PGLKTLEAGENALTSLPASLP--PELQVLDVSKNQITVLPETLPP--TITTLDVSRNAL 379
                         170       180
                  ....*....|....*....|....*..
gi 110825984  217 RGLPEDISAlrALKILWLSGAELGTLP 243
Cdd:PRK15370  380 TNLPENLPA--ALQIMQASRNNLVRLP 404
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
68-377 4.98e-19

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 92.92  E-value: 4.98e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   68 LNLGNNGLEEVPEGLgsalgslrvlvlrrnrfarlpPAvaelghHLTELDVSHNRLTALGAevvsALRELRKLNLSHNQL 147
Cdd:PRK15387  206 LNVGESGLTTLPDCL---------------------PA------HITTLVIPDNNLTSLPA----LPPELRTLEVSGNQL 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  148 PALPAQLGALAhleELDVSFNRLAHLPDSLSCLSRLRTLDvdhNQLTAFPrqlLQLVALEELDVSSNRLRGLPEDISALR 227
Cdd:PRK15387  255 TSLPVLPPGLL---ELSIFSNPLTHLPALPSGLCKLWIFG---NQLTSLP---VLPPGLQELSVSDNQLASLPALPSELC 325
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  228 ALKILWLSGAELGTLPAGfcelasLESLMLDNNGLQALPAQFSCLQRLKMLNlssNLFEEFPAalLPlAGLEELYLSRNQ 307
Cdd:PRK15387  326 KLWAYNNQLTSLPTLPSG------LQELSVSDNQLASLPTLPSELYKLWAYN---NRLTSLPA--LP-SGLKELIVSGNR 393
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  308 LTSVPSLISGLGRLLtlwLDNNRIRYLPdsiVELTGLEELVLQGNQIAVLPDHFGQLSRVGLWKIKDNPL 377
Cdd:PRK15387  394 LTSLPVLPSELKELM---VSGNRLTSLP---MLPSGLLSLSVYRNQLTRLPESLIHLSSETTVNLEGNPL 457
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
89-331 4.56e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 86.83  E-value: 4.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   89 LRVLVLRRNRFA-RLPPAVAELGHHLTELDVSHNRLTalGAEVVSALRELRKLNLSHNQLPA-LPAQLGALAHLEELDVS 166
Cdd:PLN00113   95 IQTINLSNNQLSgPIPDDIFTTSSSLRYLNLSNNNFT--GSIPRGSIPNLETLDLSNNMLSGeIPNDIGSFSSLKVLDLG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  167 FNRL-AHLPDSLSCLSRLRTLDVDHNQLTA-FPRQLLQLVALEELDVSSNRLRG-LPEDISALRALKILWLSGAEL-GTL 242
Cdd:PLN00113  173 GNVLvGKIPNSLTNLTSLEFLTLASNQLVGqIPRELGQMKSLKWIYLGYNNLSGeIPYEIGGLTSLNHLDLVYNNLtGPI 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  243 PAGFCELASLESLMLDNNGLQA-LPAQFSCLQRLKMLNLSSN-LFEEFPAALLPLAGLEELYLSRNQLT-SVPSLISGLG 319
Cdd:PLN00113  253 PSSLGNLKNLQYLFLYQNKLSGpIPPSIFSLQKLISLDLSDNsLSGEIPELVIQLQNLEILHLFSNNFTgKIPVALTSLP 332
                         250
                  ....*....|..
gi 110825984  320 RLLTLWLDNNRI 331
Cdd:PLN00113  333 RLQVLQLWSNKF 344
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
54-285 8.08e-17

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 86.06  E-value: 8.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   54 PQLVlpANLGDIEALNL-GNNGLEEVPEGLGSaLGSLRVLVLRRNRFARLPPAvaELGHH--LTELDVSHNRLT------ 124
Cdd:PLN00113  301 PELV--IQLQNLEILHLfSNNFTGKIPVALTS-LPRLQVLQLWSNKFSGEIPK--NLGKHnnLTVLDLSTNNLTgeipeg 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  125 ---------------ALGAEV---VSALRELRKLNLSHNQLPA-LPAQLGALAHLEELDVSFNRL--------------- 170
Cdd:PLN00113  376 lcssgnlfklilfsnSLEGEIpksLGACRSLRRVRLQDNSFSGeLPSEFTKLPLVYFLDISNNNLqgrinsrkwdmpslq 455
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  171 ----------AHLPDSLSClSRLRTLDVDHNQLT-AFPRQLLQLVALEELDVSSNRLRG-LPEDISALRALKILWLSGAE 238
Cdd:PLN00113  456 mlslarnkffGGLPDSFGS-KRLENLDLSRNQFSgAVPRKLGSLSELMQLKLSENKLSGeIPDELSSCKKLVSLDLSHNQ 534
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 110825984  239 L-GTLPAGFCELASLESLMLDNNGLQA-LPAQFSCLQRLKMLNLSSNLF 285
Cdd:PLN00113  535 LsGQIPASFSEMPVLSQLDLSQNQLSGeIPKNLGNVESLVQVNISHNHL 583
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
68-236 1.69e-16

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: 79.44  E-value: 1.69e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   68 LNLGNNGLEEVpEGLgSALGSLRVLVLRRNRFARLPPavaeLGH--HLTELDVSHNRLTALgaEVVSALRELRKLNLSHN 145
Cdd:cd21340     7 LYLNDKNITKI-DNL-SLCKNLKVLYLYDNKITKIEN----LEFltNLTHLYLQNNQIEKI--ENLENLVNLKKLYLGGN 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  146 QLPALpAQLGALAHLEELDVSFNRLAH------LPDSLSCLSR-LRTLDVDHNQLTAfPRQLLQLVALEELDVSSNRLRG 218
Cdd:cd21340    79 RISVV-EGLENLTNLEELHIENQRLPPgekltfDPRSLAALSNsLRVLNISGNNIDS-LEPLAPLRNLEQLDASNNQISD 156
                         170       180
                  ....*....|....*....|.
gi 110825984  219 LPE---DISALRALKILWLSG 236
Cdd:cd21340   157 LEElldLLSSWPSLRELDLTG 177
RocCOR cd09914
Ras of complex proteins (Roc) C-terminal of Roc (COR) domain family; RocCOR (or Roco) protein ...
409-552 3.51e-14

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: 71.21  E-value: 3.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  409 RLKLLLMGHKAAGKTLLRHCLTEERVEGcpgggDKEKcyppspppvSKGIEVTSWT--ADASRGLRFIVYDLAGDESYEV 486
Cdd:cd09914     1 EAKLMLVGQGGVGKTSLCKQLIGEKFDG-----DESS---------THGINVQDWKipAPERKKIRLNVWDFGGQEIYHA 66
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110825984  487 IQPFFLSPGALYVLVVNLATYEprhFPTTVGSFLHRVGARVPHAVVCIVGTHADLCGERELEEKCL 552
Cdd:cd09914    67 THQFFLTSRSLYLLVFDLRTGD---EVSRVPYWLRQIKAFGGVSPVILVGTHIDESCDEDILKKAL 129
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
124-354 1.68e-12

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: 69.69  E-value: 1.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  124 TALGAEVVSALRELRKLNLSHNQL-----PALPAQLGALAHLEELDVSFNRLAHLPDSLSCL-------SRLRTLDVDHN 191
Cdd:cd00116    12 TERATELLPKLLCLQVLRLEGNTLgeeaaKALASALRPQPSLKELCLSLNETGRIPRGLQSLlqgltkgCGLQELDLSDN 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  192 QLT----AFPRQLLQLVALEELDVSSNRL---------RGLPEDISALRALkILW---LSGAELGTLPAGFCELASLESL 255
Cdd:cd00116    92 ALGpdgcGVLESLLRSSSLQELKLNNNGLgdrglrllaKGLKDLPPALEKL-VLGrnrLEGASCEALAKALRANRDLKEL 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  256 MLDNNGL---------QALPAQfsclQRLKMLNLSSNLFEE-----FPAALLPLAGLEELYLSRNQLTSV------PSLI 315
Cdd:cd00116   171 NLANNGIgdagiralaEGLKAN----CNLEVLDLNNNGLTDegasaLAETLASLKSLEVLNLGDNNLTDAgaaalaSALL 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 110825984  316 SGLGRLLTLWLDNNRI---------RYLPDSIVeltgLEELVLQGNQI 354
Cdd:cd00116   247 SPNISLLTLSLSCNDItddgakdlaEVLAEKES----LLELDLRGNKF 290
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
65-210 2.40e-11

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: 64.42  E-value: 2.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   65 IEALNLGNNGLEEVpEGLGSaLGSLRVLVLRRNRFARlppaVAELG--HHLTELDVSHNRLtALGAEV------VSALRE 136
Cdd:cd21340    48 LTHLYLQNNQIEKI-ENLEN-LVNLKKLYLGGNRISV----VEGLEnlTNLEELHIENQRL-PPGEKLtfdprsLAALSN 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  137 -LRKLNLSHNQLPALpAQLGALAHLEELDVSFNRLAHLPD---SLSCLSRLRTLDVDHNQLTAFPRQLLQLVA----LEE 208
Cdd:cd21340   121 sLRVLNISGNNIDSL-EPLAPLRNLEQLDASNNQISDLEElldLLSSWPSLRELDLTGNPVCKKPKYRDKIILasksLEV 199

                  ..
gi 110825984  209 LD 210
Cdd:cd21340   200 LD 201
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
157-355 2.49e-10

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 64.87  E-value: 2.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  157 LAHLEELDVSFNRLA-HLPDSLSCLS-RLRTLDVDHNQLT-AFPRQLLQLvaLEELDVSSNRLRG-LPEDISALRALKIL 232
Cdd:PLN00113   92 LPYIQTINLSNNQLSgPIPDDIFTTSsSLRYLNLSNNNFTgSIPRGSIPN--LETLDLSNNMLSGeIPNDIGSFSSLKVL 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  233 WLSGAEL-GTLPAGFCELASLESLMLDNNGLQAlpaqfsclqrlkmlnlssnlfeEFPAALLPLAGLEELYLSRNQLT-S 310
Cdd:PLN00113  170 DLGGNVLvGKIPNSLTNLTSLEFLTLASNQLVG----------------------QIPRELGQMKSLKWIYLGYNNLSgE 227
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 110825984  311 VPSLISGLGRLLTLWL-DNNRIRYLPDSIVELTGLEELVLQGNQIA 355
Cdd:PLN00113  228 IPYEIGGLTSLNHLDLvYNNLTGPIPSSLGNLKNLQYLFLYQNKLS 273
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
113-312 5.30e-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: 60.57  E-value: 5.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  113 LTELDVSHNRLTALgaEVVSALRELRKLNLSHNQLPALPaQLGALAHLEELDVSFNRLAHLpDSLSCLSRLRTLDVDHNQ 192
Cdd:cd21340     4 ITHLYLNDKNITKI--DNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKI-ENLENLVNLKKLYLGGNR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  193 LTafpR--QLLQLVALEELDVSSNRLRglPEDISALRALKILWLSGaelgtlpagfcelaSLESLMLDNNGLQALpAQFS 270
Cdd:cd21340    80 IS---VveGLENLTNLEELHIENQRLP--PGEKLTFDPRSLAALSN--------------SLRVLNISGNNIDSL-EPLA 139
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 110825984  271 CLQRLKMLNLSSNLFEEFPAALLPLAG---LEELYLSRNQLTSVP 312
Cdd:cd21340   140 PLRNLEQLDASNNQISDLEELLDLLSSwpsLRELDLTGNPVCKKP 184
LRR_8 pfam13855
Leucine rich repeat;
251-308 2.93e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.07  E-value: 2.93e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   251 SLESLMLDNNGLQAL-PAQFSCLQRLKMLNLSSNLFEEF-PAALLPLAGLEELYLSRNQL 308
Cdd:pfam13855    2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
88-147 3.04e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 54.07  E-value: 3.04e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984    88 SLRVLVLRRNRFARLPPAVAELGHHLTELDVSHNRLTALGAEVVSALRELRKLNLSHNQL 147
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
112-170 8.42e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.53  E-value: 8.42e-09
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   112 HLTELDVSHNRLTALGAEVVSALRELRKLNLSHNQLPAL-PAQLGALAHLEELDVSFNRL 170
Cdd:pfam13855    2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
68-308 3.66e-08

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: 56.21  E-value: 3.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   68 LNLGNNGL-EEVPEGLGSAL--GSLRVLVLRRNRFARLP-----PAVAELGHHLTELDVSHNRLTALG----AEVVSALR 135
Cdd:cd00116    86 LDLSDNALgPDGCGVLESLLrsSSLQELKLNNNGLGDRGlrllaKGLKDLPPALEKLVLGRNRLEGAScealAKALRANR 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  136 ELRKLNLSHNQL--PALPAQLGALAHleeldvsfnrlahlpdslscLSRLRTLDVDHNQLT-----AFPRQLLQLVALEE 208
Cdd:cd00116   166 DLKELNLANNGIgdAGIRALAEGLKA--------------------NCNLEVLDLNNNGLTdegasALAETLASLKSLEV 225
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  209 LDVSSNRLRGlpEDISALraLKILWLSGAELGTLPAGFCELASLESLMLdnngLQALPAQfsclQRLKMLNLSSNLF--- 285
Cdd:cd00116   226 LNLGDNNLTD--AGAAAL--ASALLSPNISLLTLSLSCNDITDDGAKDL----AEVLAEK----ESLLELDLRGNKFgee 293
                         250       260
                  ....*....|....*....|....*.
gi 110825984  286 ---EEFPAALLPLAGLEELYLSRNQL 308
Cdd:cd00116   294 gaqLLAESLLEPGNELESLWVKDDSF 319
Roc pfam08477
Ras of Complex, Roc, domain of DAPkinase; Roc, or Ras of Complex, proteins are mitochondrial ...
411-540 3.66e-08

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: 52.51  E-value: 3.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   411 KLLLMGHKAAGKT--LLRHClteervegcpgGGDKEKCYPPSPppvskGIEVTSWTA----DASRGLRFIVYDLAGDESY 484
Cdd:pfam08477    1 KVVLLGDSGVGKTslLKRFV-----------DDTFDPKYKSTI-----GVDFKTKTVlendDNGKKIKLNIWDTAGQERF 64
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 110825984   485 EVIQPFFLSPGALYVLVVNLATYEprhfptTVGSFLHRVGARVPHAVVCIVGTHAD 540
Cdd:pfam08477   65 RSLHPFYYRGAAAALLVYDSRTFS------NLKYWLRELKKYAGNSPVILVGNKID 114
LRR_8 pfam13855
Leucine rich repeat;
159-216 1.93e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 48.67  E-value: 1.93e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   159 HLEELDVSFNRLAHL-PDSLSCLSRLRTLDVDHNQLTAF-PRQLLQLVALEELDVSSNRL 216
Cdd:pfam13855    2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
297-354 3.99e-07

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 47.90  E-value: 3.99e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   297 GLEELYLSRNQLTSV-PSLISGLGRLLTLWLDNNRIRYL-PDSIVELTGLEELVLQGNQI 354
Cdd:pfam13855    2 NLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
131-194 8.67e-07

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 52.90  E-value: 8.67e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 110825984  131 VSALRELRKLNLSHNQLP-ALPAQLGALAHLEELDVSFNRL-AHLPDSLSCLSRLRTLDVDHNQLT 194
Cdd:PLN03150  438 ISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSFnGSIPESLGQLTSLRILNLNGNSLS 503
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
57-193 1.03e-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: 51.97  E-value: 1.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   57 VLPANlGDIEALNLGNNGLEEvpEGL------GSALGSLRVLVLRRNRFAR-----LPPAVAELgHHLTELDVSHNRLTA 125
Cdd:cd00116   160 ALRAN-RDLKELNLANNGIGD--AGIralaegLKANCNLEVLDLNNNGLTDegasaLAETLASL-KSLEVLNLGDNNLTD 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  126 LG-AEVVSALRE----LRKLNLSHNQLPALPAQ-----LGALAHLEELDVSFNRLAHLPDSLSCLSR------LRTLDVD 189
Cdd:cd00116   236 AGaAALASALLSpnisLLTLSLSCNDITDDGAKdlaevLAEKESLLELDLRGNKFGEEGAQLLAESLlepgneLESLWVK 315

                  ....
gi 110825984  190 HNQL 193
Cdd:cd00116   316 DDSF 319
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
221-381 5.47e-06

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: 48.63  E-value: 5.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  221 EDISALRALKILWLSGAELGTLPaGFCELASLESLMLDNNGLQALPaQFSCLQRLKMLNLSSNLFEEfpaallpLAGLE- 299
Cdd:cd21340    18 DNLSLCKNLKVLYLYDNKITKIE-NLEFLTNLTHLYLQNNQIEKIE-NLENLVNLKKLYLGGNRISV-------VEGLEn 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  300 -----ELYLSRNQL------TSVPSLISGLGRLLTLwLD--NNRIRYLpDSIVELTGLEELVLQGNQIAVLPDHFGQLSR 366
Cdd:cd21340    89 ltnleELHIENQRLppgeklTFDPRSLAALSNSLRV-LNisGNNIDSL-EPLAPLRNLEQLDASNNQISDLEELLDLLSS 166
                         170
                  ....*....|....*...
gi 110825984  367 VG-LWKI--KDNPLIQPP 381
Cdd:cd21340   167 WPsLRELdlTGNPVCKKP 184
PLN03150 PLN03150
hypothetical protein; Provisional
205-355 5.88e-06

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 50.20  E-value: 5.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  205 ALEELDVSSNRLRGLPEDISALRALKilwlsgAELGtLPAGF------------------CELAS------LESLMLDNN 260
Cdd:PLN03150  356 AIEVFEIITAESKTLLEEVSALQTLK------SSLG-LPLRFgwngdpcvpqqhpwsgadCQFDStkgkwfIDGLGLDNQ 428
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  261 GLQA-LPAQFSCLQRLKMLNLSSNLFE-EFPAALLPLAGLEELYLSRNQLtsvpsliSGLgrlltlwldnnriryLPDSI 338
Cdd:PLN03150  429 GLRGfIPNDISKLRHLQSINLSGNSIRgNIPPSLGSITSLEVLDLSYNSF-------NGS---------------IPESL 486
                         170
                  ....*....|....*..
gi 110825984  339 VELTGLEELVLQGNQIA 355
Cdd:PLN03150  487 GQLTSLRILNLNGNSLS 503
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
249-355 1.44e-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: 47.47  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  249 LASLESLMLDNNGLQALPAqFSCLQRLKMLNLSSNLFEEFPAaLLPLAGLEELYLSRNQLTSVPSLiSGLGRLLTLWLDN 328
Cdd:cd21340     1 LKRITHLYLNDKNITKIDN-LSLCKNLKVLYLYDNKITKIEN-LEFLTNLTHLYLQNNQIEKIENL-ENLVNLKKLYLGG 77
                          90       100       110
                  ....*....|....*....|....*....|.
gi 110825984  329 NRIrylpdSIVE----LTGLEELVLQGNQIA 355
Cdd:cd21340    78 NRI-----SVVEglenLTNLEELHIENQRLP 103
LRR_8 pfam13855
Leucine rich repeat;
273-331 2.37e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.90  E-value: 2.37e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110825984   273 QRLKMLNLSSNLFEEF-PAALLPLAGLEELYLSRNQLTSV-PSLISGLGRLLTLWLDNNRI 331
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLdDGAFKGLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNRL 61
PLN03150 PLN03150
hypothetical protein; Provisional
65-157 4.20e-05

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 47.50  E-value: 4.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   65 IEALNLGNNGLEEVPEGLGSALGSLRVLVLRRNRF-ARLPPAVAELGHhLTELDVSHNRLTALGAEVVSALRELRKLNLS 143
Cdd:PLN03150  420 IDGLGLDNQGLRGFIPNDISKLRHLQSINLSGNSIrGNIPPSLGSITS-LEVLDLSYNSFNGSIPESLGQLTSLRILNLN 498
                          90
                  ....*....|....*
gi 110825984  144 HNQLPA-LPAQLGAL 157
Cdd:PLN03150  499 GNSLSGrVPAALGGR 513
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
234-364 4.72e-05

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 47.54  E-value: 4.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  234 LSGAEL-GTLPAGFCELASLESLMLDNNGLQA-LPAQ-FSCLQRLKMLNLSSNLFE-EFPAALLPlaGLEELYLSRNQLT 309
Cdd:PLN00113   76 LSGKNIsGKISSAIFRLPYIQTINLSNNQLSGpIPDDiFTTSSSLRYLNLSNNNFTgSIPRGSIP--NLETLDLSNNMLS 153
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 110825984  310 -SVPSLISGLGRLLTLWLDNNRIR-YLPDSIVELTGLEELVLQGNQ-IAVLPDHFGQL 364
Cdd:PLN00113  154 gEIPNDIGSFSSLKVLDLGGNVLVgKIPNSLTNLTSLEFLTLASNQlVGQIPRELGQM 211
PRK15387 PRK15387
type III secretion system effector E3 ubiquitin transferase SspH2;
58-202 1.19e-04

type III secretion system effector E3 ubiquitin transferase SspH2;


Pssm-ID: 185285 [Multi-domain]  Cd Length: 788  Bit Score: 46.31  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   58 LPANLGDIEALNLGNNGLEEVPeglgSALGSLRVLVLRRNRFARLPPavaeLGHHLTELDVSHNRLTALgaEVVSAlrEL 137
Cdd:PRK15387  337 LPTLPSGLQELSVSDNQLASLP----TLPSELYKLWAYNNRLTSLPA----LPSGLKELIVSGNRLTSL--PVLPS--EL 404
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 110825984  138 RKLNLSHNQLPALPAQLGALAhleELDVSFNRLAHLPDSLSCLSRLRTLDVDHNQLTAFPRQLLQ 202
Cdd:PRK15387  405 KELMVSGNRLTSLPMLPSGLL---SLSVYRNQLTRLPESLIHLSSETTVNLEGNPLSERTLQALR 466
LRR_8 pfam13855
Leucine rich repeat;
181-236 1.32e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 40.97  E-value: 1.32e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 110825984   181 SRLRTLDVDHNQLTAFPRQLLQ-LVALEELDVSSNRLRGL-PEDISALRALKILWLSG 236
Cdd:pfam13855    1 PNLRSLDLSNNRLTSLDDGAFKgLSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSG 58
COR pfam16095
C-terminal of Roc, COR, domain; The C-terminal of Roc domain, COR, along with Roc functions as ...
660-727 1.83e-04

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: 43.77  E-value: 1.83e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110825984   660 PRSWQVLEElHFQPPQAQRLWLSWWDSARLGLQAGLT-EDRLQSALSYLHESGKLLYFEDSPALKEHVF 727
Cdd:pfam16095    1 PKSWLAVRE-ALEKERQKKPYISYEEYRKICAENGIDdEEDQDTLLEFLHDLGVLLYFQDDPGLRDIVI 68
LRR_8 pfam13855
Leucine rich repeat;
206-285 3.86e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 39.43  E-value: 3.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   206 LEELDVSSNRLRGLPEDisalralkilWLSGaelgtlpagfceLASLESLMLDNNGLQAL-PAQFSCLQRLKMLNLSSNL 284
Cdd:pfam13855    3 LRSLDLSNNRLTSLDDG----------AFKG------------LSNLKVLDLSNNLLTTLsPGAFSGLPSLRYLDLSGNR 60

                   .
gi 110825984   285 F 285
Cdd:pfam13855   61 L 61
PLN03150 PLN03150
hypothetical protein; Provisional
150-218 5.59e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 44.04  E-value: 5.59e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 110825984  150 LPAQLGALAHLEELDVSFNRL-AHLPDSLSCLSRLRTLDVDHNQLT-AFPRQLLQLVALEELDVSSNRLRG 218
Cdd:PLN03150  434 IPNDISKLRHLQSINLSGNSIrGNIPPSLGSITSLEVLDLSYNSFNgSIPESLGQLTSLRILNLNGNSLSG 504
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
140-354 6.70e-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: 43.24  E-value: 6.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  140 LNLSHN-QLPALPAQLGALAHLEELDVSFNRLAHLPD-SLSCLSRLRTLDVDHNQLTAFPRQLLQLVALEELDVSSNRLR 217
Cdd:COG5238   119 LRRIMAkTLEDSLILYLALPRRINLIQVLKDPLGGNAvHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIE 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  218 GLPEDISALRALKILWLSGAELGTLPAGF-----CELASLESLMLDNN--GLQALPAQFSCLQ---RLKMLNLSSNLFEE 287
Cdd:COG5238   199 ELAEALTQNTTVTTLWLKRNPIGDEGAEIlaealKGNKSLTTLDLSNNqiGDEGVIALAEALKnntTVETLYLSGNQIGA 278
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  288 FPAALLP--LAG---LEELYLSRNQLT--SVPSLISGLGR---LLTLWLDNNRI-----RYLPDSIVELTGLEELVLQGN 352
Cdd:COG5238   279 EGAIALAkaLQGnttLTSLDLSVNRIGdeGAIALAEGLQGnktLHTLNLAYNGIgaqgaIALAKALQENTTLHSLDLSDN 358

                  ..
gi 110825984  353 QI 354
Cdd:COG5238   359 QI 360
PLN03150 PLN03150
hypothetical protein; Provisional
129-267 8.13e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 43.27  E-value: 8.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  129 EVVSALRELRK-----LNLSHNQLPALPAQlgalaH-LEELDVSFnrlahlpDSLSCLSRLRTLDVDHNQLTAF-PRQLL 201
Cdd:PLN03150  372 EEVSALQTLKSslglpLRFGWNGDPCVPQQ-----HpWSGADCQF-------DSTKGKWFIDGLGLDNQGLRGFiPNDIS 439
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 110825984  202 QLVALEELDVSSNRLRG-LPEDISALRALKILWLSGAEL-GTLPAGFCELASLESLMLDNNGLQA-LPA 267
Cdd:PLN03150  440 KLRHLQSINLSGNSIRGnIPPSLGSITSLEVLDLSYNSFnGSIPESLGQLTSLRILNLNGNSLSGrVPA 508
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
68-240 1.52e-03

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: 42.08  E-value: 1.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984   68 LNLGNNGL-EEVPEGLGSALG---SLRVLVLRRNRFArlPPAVAELGHHLTE------LDVSHNRLTALGAE-VVSALR- 135
Cdd:COG5238   213 LWLKRNPIgDEGAEILAEALKgnkSLTTLDLSNNQIG--DEGVIALAEALKNnttvetLYLSGNQIGAEGAIaLAKALQg 290
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 110825984  136 --ELRKLNLSHNQLP-----ALPAQLGALAHLEELDVSFNRLAH-----LPDSLSCLSRLRTLDVDHNQLT-----AFPR 198
Cdd:COG5238   291 ntTLTSLDLSVNRIGdegaiALAEGLQGNKTLHTLNLAYNGIGAqgaiaLAKALQENTTLHSLDLSDNQIGdegaiALAK 370
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 110825984  199 QLLQLVALEELDVSSNRL--RGLPEDISALRA--LKILWLSGAELG 240
Cdd:COG5238   371 YLEGNTTLRELNLGKNNIgkQGAEALIDALQTnrLHTLILDGNLIG 416
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
298-336 6.87e-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: 35.30  E-value: 6.87e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 110825984   298 LEELYLSRNQLTSVPSLiSGLGRLLTLWL-DNNRIRYLPD 336
Cdd:pfam12799    3 LEVLDLSNNQITDIPPL-AKLPNLETLDLsGNNKITDLSD 41
 
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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