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Conserved domains on  [gi|51988879|ref|NP_001004293|]
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amphoterin-induced protein 1 isoform a precursor [Mus musculus]

Protein Classification

LRR and IG_like domain-containing protein( domain architecture ID 11471650)

LRR and IG_like domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-224 2.71e-24

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 104.63  E-value: 2.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  66 LDLSHNNLSRLRAEwtPTRLTNLHSLLLSHNHLNFISSEaFVPVPNLRYLDLSSNHLHTLDEFLfSDLQALEVLLLYNNH 145
Cdd:COG4886 118 LDLSGNQLTDLPEE--LANLTNLKELDLSNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQ 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 146 IVVVDrNAFEDMAQLQKLYLSQNQISRFPVELikdgNKLPKLMLLDLSSNKLKKLP-LTDLQKLpawvkNGLYLHNNPLE 224
Cdd:COG4886 194 ITDLP-EPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTDLPeLGNLTNL-----EELDLSNNQLT 263
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 279-357 2.46e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


:

Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.35  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879    279 EAHLGDTLTIRCDTKQQGMTKVWVSPSNEQVLSQGSNGSVSVRNGD--LFFKKVQVEDGGVYTCYAMGETFNETLSVELK 356
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84


                   .
gi 51988879    357 V 357
Cdd:smart00410  85 V 85
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-224 2.71e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 104.63  E-value: 2.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  66 LDLSHNNLSRLRAEwtPTRLTNLHSLLLSHNHLNFISSEaFVPVPNLRYLDLSSNHLHTLDEFLfSDLQALEVLLLYNNH 145
Cdd:COG4886 118 LDLSGNQLTDLPEE--LANLTNLKELDLSNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQ 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 146 IVVVDrNAFEDMAQLQKLYLSQNQISRFPVELikdgNKLPKLMLLDLSSNKLKKLP-LTDLQKLpawvkNGLYLHNNPLE 224
Cdd:COG4886 194 ITDLP-EPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTDLPeLGNLTNL-----EELDLSNNQLT 263
LRR_8 pfam13855
Leucine rich repeat;
110-170 3.28e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 67.16  E-value: 3.28e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51988879   110 PNLRYLDLSSNHLHTLDEFLFSDLQALEVLLLYNNHIVVVDRNAFEDMAQLQKLYLSQNQI 170
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
30-213 5.86e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 74.35  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879   30 SVVSCPANCLCASNILSCSKQQLPNVPQSLPSYTALLDLSHNNLSRLraewtPTRL-TNLHSLLLSHNHLNFISSEafvp 108
Cdd:PRK15370 210 ELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITEL-----PERLpSALQSLDLFHNKISCLPEN---- 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  109 VPN-LRYLDLSSNHLHTLDE---------FLFSD-LQALEVLLLYNNHIVVVDRNAFEDM-----AQLQKLYLSQNQISR 172
Cdd:PRK15370 281 LPEeLRYLSVYDNSIRTLPAhlpsgithlNVQSNsLTALPETLPPGLKTLEAGENALTSLpaslpPELQVLDVSKNQITV 360

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 51988879  173 FPVELIkdgnklPKLMLLDLSSNKLKKLPltdlQKLPAWVK 213
Cdd:PRK15370 361 LPETLP------PTITTLDVSRNALTNLP----ENLPAALQ 391
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 279-357 2.46e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.35  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879    279 EAHLGDTLTIRCDTKQQGMTKVWVSPSNEQVLSQGSNGSVSVRNGD--LFFKKVQVEDGGVYTCYAMGETFNETLSVELK 356
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84


                   .
gi 51988879    357 V 357
Cdd:smart00410  85 V 85
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 83-238 1.05e-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: 52.48  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  83 TRLTNLHsllLSHNHLNFIssEAFVPVPNLRYLDLSSNHLHTLDEFLFsdLQALEVLLLYNNHIVVVDRnaFEDMAQLQK 162
Cdd:cd21340   2 KRITHLY---LNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEF--LTNLTHLYLQNNQIEKIEN--LENLVNLKK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 163 LYLSQNQISRfpVE-----------------------LIKDGNKL----PKLMLLDLSSNKLKKlpLTDLQKLPAWVKng 215
Cdd:cd21340  73 LYLGGNRISV--VEglenltnleelhienqrlppgekLTFDPRSLaalsNSLRVLNISGNNIDS--LEPLAPLRNLEQ-- 146

                       170       180
                ....*....|....*....|...
gi 51988879 216 LYLHNNPLECDCKLYQLFSHWQY 238
Cdd:cd21340 147 LDASNNQISDLEELLDLLSSWPS 169
I-set pfam07679
Immunoglobulin I-set domain;
279-357 8.08e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.17  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879   279 EAHLGDTLTIRCDTKQQGMTKV-WVSpsNEQVLSQGSNGSVSVRNGD--LFFKKVQVEDGGVYTCYAMGETFNETLSVEL 355
Cdd:pfam07679  11 EVQEGESARFTCTVTGTPDPEVsWFK--DGQPLRSSDRFKVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88


                  ..
gi 51988879   356 KV 357
Cdd:pfam07679  89 TV 90
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 311-357 1.20e-04

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 41.22  E-value: 1.20e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 51988879 311 SQGSNGsvsvrNGDLFFKKVQVEDGGVYTCYAMGETFNETLSVELKV 357
Cdd:cd16091  66 DQISNG-----NASLLLRRVQLQDEGRYKCYTSTIIGNQESFVNLKV 107
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
66-224 2.71e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 104.63  E-value: 2.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  66 LDLSHNNLSRLRAEwtPTRLTNLHSLLLSHNHLNFISSEaFVPVPNLRYLDLSSNHLHTLDEFLfSDLQALEVLLLYNNH 145
Cdd:COG4886 118 LDLSGNQLTDLPEE--LANLTNLKELDLSNNQLTDLPEP-LGNLTNLKSLDLSNNQLTDLPEEL-GNLTNLKELDLSNNQ 193

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 146 IVVVDrNAFEDMAQLQKLYLSQNQISRFPVELikdgNKLPKLMLLDLSSNKLKKLP-LTDLQKLpawvkNGLYLHNNPLE 224
Cdd:COG4886 194 ITDLP-EPLGNLTNLEELDLSGNQLTDLPEPL----ANLTNLETLDLSNNQLTDLPeLGNLTNL-----EELDLSNNQLT 263
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
44-235 7.71e-24

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 103.47  E-value: 7.71e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  44 ILSCSKQQLPNVPQSLPSYTAL--LDLSHNNLSRLRAEWTPtrLTNLHSLLLSHNHLNFISsEAFVPVPNLRYLDLSSNH 121
Cdd:COG4886 140 ELDLSNNQLTDLPEPLGNLTNLksLDLSNNQLTDLPEELGN--LTNLKELDLSNNQITDLP-EPLGNLTNLEELDLSGNQ 216

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 122 LHTLDEFLfSDLQALEVLLLYNNHIVVVDrnAFEDMAQLQKLYLSQNQISRFPVELikdgnKLPKLMLLDLSSNKLKKLP 201
Cdd:COG4886 217 LTDLPEPL-ANLTNLETLDLSNNQLTDLP--ELGNLTNLEELDLSNNQLTDLPPLA-----NLTNLKTLDLSNNQLTDLK 288

                       170       180       190
                ....*....|....*....|....*....|....
gi 51988879 202 LTDLQKLPAWVKNGLYLHNNPLECDCKLYQLFSH 235
Cdd:COG4886 289 LKELELLLGLNSLLLLLLLLNLLELLILLLLLTT 322
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
43-224 2.14e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 93.07  E-value: 2.14e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  43 NILSCSKQQLPNVPQSLPSYTALLDLSHNNLSRLRAEWTPTRLTNLHSLLLSHNHLNFIsSEAFVPVPNLRYLDLSSNHL 122
Cdd:COG4886  70 SLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLESLDLSGNQLTDL-PEELANLTNLKELDLSNNQL 148

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 123 HTLDEFLfSDLQALEVLLLYNNHIVVVDrNAFEDMAQLQKLYLSQNQISRFPVELikdgNKLPKLMLLDLSSNKLKKLP- 201
Cdd:COG4886 149 TDLPEPL-GNLTNLKSLDLSNNQLTDLP-EELGNLTNLKELDLSNNQITDLPEPL----GNLTNLEELDLSGNQLTDLPe 222

                       170       180
                ....*....|....*....|....
gi 51988879 202 -LTDLQKLpawvkNGLYLHNNPLE 224
Cdd:COG4886 223 pLANLTNL-----ETLDLSNNQLT 241
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
45-247 4.08e-17

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 83.44  E-value: 4.08e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  45 LSCSKQQLPNVPQSLPSYTAL--LDLSHNNLSRLRAEWTptRLTNLHSLLLSHNHLNFISSEaFVPVPNLRYLDLSSNHL 122
Cdd:COG4886 164 LDLSNNQLTDLPEELGNLTNLkeLDLSNNQITDLPEPLG--NLTNLEELDLSGNQLTDLPEP-LANLTNLETLDLSNNQL 240

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 123 HTLDEFlfSDLQALEVLLLYNNHIVVVDRNAfeDMAQLQKLYLSQNQISRFPVELIKDGNKLPKLMLLDLSSNKLKKLPL 202
Cdd:COG4886 241 TDLPEL--GNLTNLEELDLSNNQLTDLPPLA--NLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLIL 316

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*
gi 51988879 203 TDLQKLPAWVKNGLYLHNNPLECDCKLYQLFSHWQYRQLSSVMDF 247
Cdd:COG4886 317 LLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSL 361
LRR_8 pfam13855
Leucine rich repeat;
110-170 3.28e-14

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 67.16  E-value: 3.28e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51988879   110 PNLRYLDLSSNHLHTLDEFLFSDLQALEVLLLYNNHIVVVDRNAFEDMAQLQKLYLSQNQI 170
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
PRK15370 PRK15370
type III secretion system effector E3 ubiquitin transferase SlrP;
30-213 5.86e-14

type III secretion system effector E3 ubiquitin transferase SlrP;


Pssm-ID: 185268 [Multi-domain]  Cd Length: 754  Bit Score: 74.35  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879   30 SVVSCPANCLCASNILSCSKQQLPNVPQSLPSYTALLDLSHNNLSRLraewtPTRL-TNLHSLLLSHNHLNFISSEafvp 108
Cdd:PRK15370 210 ELKSLPENLQGNIKTLYANSNQLTSIPATLPDTIQEMELSINRITEL-----PERLpSALQSLDLFHNKISCLPEN---- 280

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  109 VPN-LRYLDLSSNHLHTLDE---------FLFSD-LQALEVLLLYNNHIVVVDRNAFEDM-----AQLQKLYLSQNQISR 172
Cdd:PRK15370 281 LPEeLRYLSVYDNSIRTLPAhlpsgithlNVQSNsLTALPETLPPGLKTLEAGENALTSLpaslpPELQVLDVSKNQITV 360

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 51988879  173 FPVELIkdgnklPKLMLLDLSSNKLKKLPltdlQKLPAWVK 213
Cdd:PRK15370 361 LPETLP------PTITTLDVSRNALTNLP----ENLPAALQ 391
LRR_8 pfam13855
Leucine rich repeat;
86-146 4.56e-12

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 61.00  E-value: 4.56e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 51988879    86 TNLHSLLLSHNHLNFISSEAFVPVPNLRYLDLSSNHLHTLDEFLFSDLQALEVLLLYNNHI 146
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
66-122 1.99e-11

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 59.08  E-value: 1.99e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 51988879    66 LDLSHNNLSRLRAEWtPTRLTNLHSLLLSHNHLNFISSEAFVPVPNLRYLDLSSNHL 122
Cdd:pfam13855   6 LDLSNNRLTSLDDGA-FKGLSNLKVLDLSNNLLTTLSPGAFSGLPSLRYLDLSGNRL 61
IG_like smart00410
Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.
 279-357 2.46e-08

Immunoglobulin like; IG domains that cannot be classified into one of IGv1, IGc1, IGc2, IG.


Pssm-ID: 214653 [Multi-domain]  Cd Length: 85  Bit Score: 51.35  E-value: 2.46e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879    279 EAHLGDTLTIRCDTKQQGMTKVWVSPSNEQVLSQGSNGSVSVRNGD--LFFKKVQVEDGGVYTCYAMGETFNETLSVELK 356
Cdd:smart00410   5 TVKEGESVTLSCEASGSPPPEVTWYKQGGKLLAESGRFSVSRSGSTstLTISNVTPEDSGTYTCAATNSSGSASSGTTLT 84


                   .
gi 51988879    357 V 357
Cdd:smart00410  85 V 85
LRR_8 pfam13855
Leucine rich repeat;
136-197 4.11e-08

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 49.83  E-value: 4.11e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51988879   136 LEVLLLYNNHIVVVDRNAFEDMAQLQKLYLSQNQISRFPVELIKDgnkLPKLMLLDLSSNKL 197
Cdd:pfam13855   3 LRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSG---LPSLRYLDLSGNRL 61
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 83-238 1.05e-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: 52.48  E-value: 1.05e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  83 TRLTNLHsllLSHNHLNFIssEAFVPVPNLRYLDLSSNHLHTLDEFLFsdLQALEVLLLYNNHIVVVDRnaFEDMAQLQK 162
Cdd:cd21340   2 KRITHLY---LNDKNITKI--DNLSLCKNLKVLYLYDNKITKIENLEF--LTNLTHLYLQNNQIEKIEN--LENLVNLKK 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 163 LYLSQNQISRfpVE-----------------------LIKDGNKL----PKLMLLDLSSNKLKKlpLTDLQKLPAWVKng 215
Cdd:cd21340  73 LYLGGNRISV--VEglenltnleelhienqrlppgekLTFDPRSLaalsNSLRVLNISGNNIDS--LEPLAPLRNLEQ-- 146

                       170       180
                ....*....|....*....|...
gi 51988879 216 LYLHNNPLECDCKLYQLFSHWQY 238
Cdd:cd21340 147 LDASNNQISDLEELLDLLSSWPS 169
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 66-197 7.20e-06

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: 48.25  E-value: 7.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  66 LDLSHNNLSRLRAEWTPTRL---TNLHSLLLSHNHLNFISSEAFVP----VPNLRYLDLSSNHLHTLD-EFLFSDLQA-- 135
Cdd:COG5238 269 LYLSGNQIGAEGAIALAKALqgnTTLTSLDLSVNRIGDEGAIALAEglqgNKTLHTLNLAYNGIGAQGaIALAKALQEnt 348

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51988879 136 -LEVLLLYNNHI----VVVDRNAFEDMAQLQKLYLSQNQISRFPVELIKDGNKLPKLMLLDLSSNKL 197
Cdd:COG5238 349 tLHSLDLSDNQIgdegAIALAKYLEGNTTLRELNLGKNNIGKQGAEALIDALQTNRLHTLILDGNLI 415
I-set pfam07679
Immunoglobulin I-set domain;
279-357 8.08e-06

Immunoglobulin I-set domain;


Pssm-ID: 400151 [Multi-domain]  Cd Length: 90  Bit Score: 44.17  E-value: 8.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879   279 EAHLGDTLTIRCDTKQQGMTKV-WVSpsNEQVLSQGSNGSVSVRNGD--LFFKKVQVEDGGVYTCYAMGETFNETLSVEL 355
Cdd:pfam07679  11 EVQEGESARFTCTVTGTPDPEVsWFK--DGQPLRSSDRFKVTYEGGTytLTISNVQPDDSGKYTCVATNSAGEAEASAEL 88


                  ..
gi 51988879   356 KV 357
Cdd:pfam07679  89 TV 90
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 64-198 1.73e-05

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: 46.58  E-value: 1.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  64 ALLDLSHNNLS----RLRAEWTPTRLTNLHSLLLSHNHLNFISSEA----FVPVPNLRYLDLSSNHLH-----TLDEFLf 130
Cdd:cd00116 111 QELKLNNNGLGdrglRLLAKGLKDLPPALEKLVLGRNRLEGASCEAlakaLRANRDLKELNLANNGIGdagirALAEGL- 189

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 51988879 131 SDLQALEVLLLYNNHI----VVVDRNAFEDMAQLQKLYLSQNQISRFPVELIKDGNKLP--KLMLLDLSSNKLK 198
Cdd:cd00116 190 KANCNLEVLDLNNNGLtdegASALAETLASLKSLEVLNLGDNNLTDAGAAALASALLSPniSLLTLSLSCNDIT 263
LRR_8 pfam13855
Leucine rich repeat;
159-223 2.08e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 42.13  E-value: 2.08e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51988879   159 QLQKLYLSQNQISRFPVELIKDgnkLPKLMLLDLSSNKLKKLPLTDLQKLPAWVKngLYLHNNPL 223
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKG---LSNLKVLDLSNNLLTTLSPGAFSGLPSLRY--LDLSGNRL 61
IgV_HHLA2 cd16091
Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are ...
 311-357 1.20e-04

Immunoglobulin Variable (IgV) domain in HERV-H LTR-associating 2 (HHLA2); The members here are composed of the immunoglobulin variable (IgV) region in HERV-H LTR-associating 2 (HHLA2; also known as B7-H7/B7 homolog 7). HHLA2 is a member of the B7 family of immune regulatory proteins. Mature human HHLA2 consists of an extracellular domain (ECD) with three immunoglobulin-like domains, a transmembrane segment, and a cytoplasmic domain. HHLA2 is widely expressed in human cancers including non-small cell lung carcinoma (NSCLS), triple negative breast cancer (TNBC), and melanoma, but has limited expression on normal tissues. Interestingly, unlike other members of B7 family, HHLA2 is not expressed in mice or rats. HHLA2 functions as a T cell coinhibitory molecules as it inhibits the proliferation of activated CD4(+) and CD8(+) T cells and their cytokine production. Furthermore, HHLA2 is constitutively expressed on the surface of human monocytes and is induced on B cells after stimulation, however it is not inducible on T cells.


Pssm-ID: 409512  Cd Length: 107  Bit Score: 41.22  E-value: 1.20e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 51988879 311 SQGSNGsvsvrNGDLFFKKVQVEDGGVYTCYAMGETFNETLSVELKV 357
Cdd:cd16091  66 DQISNG-----NASLLLRRVQLQDEGRYKCYTSTIIGNQESFVNLKV 107
Ig cd00096
Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found ...
 286-342 1.35e-04

Immunoglobulin domain; The members here are composed of the immunoglobulin (Ig) domain found in the Ig superfamily. The Ig superfamily is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. Members of this group are components of immunoglobulin, neuroglia, cell surface glycoproteins, including T-cell receptors, CD2, CD4, CD8, and membrane glycoproteins, including butyrophilin and chondroitin sulfate proteoglycan core protein. A predominant feature of most Ig domains is a disulfide bridge connecting the two beta-sheets with a tryptophan residue packed against the disulfide bond. Ig superfamily (IgSF) domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Typically, the V-set domains have A, B, E, and D strands in one sheet and A', G, F, C, C' and C" in the other. The structures in C1-set are smaller than those in the V-set; they have one beta sheet that is formed by strands A, B, E, and D and the other by strands G, F, C, and C'. Moreover, a C1-set Ig domain contains a short C' strand (three residues) and lacks A' and C" strand. Unlike other Ig domain sets, C2-set structures do not have a D strand. Like the V-set Ig domains, members of the I-set have a discontinuous A strand, but lack a C" strand.


Pssm-ID: 409353 [Multi-domain]  Cd Length: 70  Bit Score: 40.01  E-value: 1.35e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 51988879 286 LTIRCDTKQQGMTKV-WVSPSNEQVLSQGSNGSVSVRNGDLFFKKVQVEDGGVYTCYA 342
Cdd:cd00096   1 VTLTCSASGNPPPTItWYKNGKPLPPSSRDSRRSELGNGTLTISNVTLEDSGTYTCVA 58
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 66-174 2.44e-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: 42.47  E-value: 2.44e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  66 LDLSHNNLSR---LraewtpTRLTNLHSLLLSHNHLNfiSSEAFVPVPN--------LRYLDLSSNHLHTLDEflFSDLQ 134
Cdd:cd21340  73 LYLGGNRISVvegL------ENLTNLEELHIENQRLP--PGEKLTFDPRslaalsnsLRVLNISGNNIDSLEP--LAPLR 142

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 51988879 135 ALEVLLLYNNHIVVVDR--NAFEDMAQLQKLYLSQNQISRFP 174
Cdd:cd21340 143 NLEQLDASNNQISDLEEllDLLSSWPSLRELDLTGNPVCKKP 184
Ig2_IL1R-like cd05757
Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; ...
 318-357 2.86e-04

Second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R), and similar domains; The members here are composed of the second immunoglobulin (Ig)-like domain of interleukin-1 receptor (IL1R; also known as cluster of differentiation (CD) 121). IL-1 alpha and IL-1 beta are cytokines which participate in the regulation of inflammation, immune responses, and hematopoiesis. These cytokines bind to the IL-1 receptor type 1 (IL1R1), which is activated on additional association with interleukin-1 receptor accessory protein (IL1RAP). IL-1 also binds a second receptor designated type II (IL1R2). Mature IL1R1 consists of three IG-like domains, a transmembrane domain, and a large cytoplasmic domain. Mature IL1R2 is organized similarly except that it has a short cytoplasmic domain. The latter does not initiate signal transduction. A naturally occurring cytokine IL-1RA (IL-1 receptor antagonist) is widely expressed and binds to IL-1 receptors, inhibiting the binding of IL-1 alpha and IL-1 beta. This group also contains ILIR-like 1 (IL1R1L) which maps to the same chromosomal location as IL1R1 and IL1R2.


Pssm-ID: 409415  Cd Length: 92  Bit Score: 40.00  E-value: 2.86e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 51988879 318 VSVRNGDLFFKKVQVEDGGVYTCYA----MGETFNETLSVELKV 357
Cdd:cd05757  47 FIPKGSKLLIQNVTEEDAGNYTCKFtythNGKQYNVTRTISLTV 90
Ig_3 pfam13927
Immunoglobulin domain; This family contains immunoglobulin-like domains.
 279-342 6.68e-04

Immunoglobulin domain; This family contains immunoglobulin-like domains.


Pssm-ID: 464046 [Multi-domain]  Cd Length: 78  Bit Score: 38.32  E-value: 6.68e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 51988879   279 EAHLGDTLTIRCDTKQQGMTKV-WVSPSNEQVLSQGSNGSVSVRNGDLFFKKVQVEDGGVYTCYA 342
Cdd:pfam13927  12 TVREGETVTLTCEATGSPPPTItWYKNGEPISSGSTRSRSLSGSNSTLTISNVTRSDAGTYTCVA 76
IgI_Lingo-1 cd20969
Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing ...
 283-357 2.47e-03

Immunoglobulin I-set domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1); The members here are composed of the immunoglobulin I-set (IgI) domain of the Leucine-rich repeat and immunoglobin-like domain-containing protein 1 (Lingo-1). Human Lingo-1 is a central nervous system-specific transmembrane glycoprotein also known as LERN-1, which functions as a negative regulator of neuronal survival, axonal regeneration, and oligodendrocyte differentiation and myelination. Lingo-1 is a key component of the Nogo receptor signaling complex (RTN4R/NGFR) in RhoA activation responsible for some inhibition of axonal regeneration by myelin-associated factors. The ligand-binding ectodomain of human Lingo-1 contains a bimodular, kinked structure composed of leucine-rich repeat (LRR) and immunoglobulin (Ig)-like modules. Diseases associated with Lingo-1 include mental retardation, autosomal recessive 64 and essential tremor. The Ig superfamily (IgSF) is a heterogenous group of proteins, built on a common fold comprised of a sandwich of two beta sheets. IgSF domains can be divided into 4 main classes based on their structures and sequences: the Variable (V), Constant 1 (C1), Constant 2 (C2), and Intermediate (I) sets. Unlike the V-set, one of the distinctive features of I-set domains is the lack of a C" strand. The structure of the Lingo-1 lacks this strand and thus it belongs to the I-set of the IgSF. I-set domains are found in several cell adhesion molecules (such as VCAM, ICAM, and MADCAM), and are also present in numerous other diverse protein families, including several tyrosine-protein kinase receptors, the hemolymph protein hemolin, the muscle proteins titin, telokin, and twitchin, the neuronal adhesion molecule axonin-1, and the signaling molecule semaphorin 4D that is involved in axonal guidance, immune function and angiogenesis.


Pssm-ID: 409561  Cd Length: 92  Bit Score: 37.37  E-value: 2.47e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 51988879 283 GDTLTIRCdtKQQGM---TKVWVSPsNEQVLSQGSNGSVSV-RNGDLFFKKVQVEDGGVYTCYAMGETFNETLSVELKV 357
Cdd:cd20969  17 GHTVQFVC--RADGDpppAILWLSP-RKHLVSAKSNGRLTVfPDGTLEVRYAQVQDNGTYLCIAANAGGNDSMPAHLHV 92
Ig_2 pfam13895
Immunoglobulin domain; This domain contains immunoglobulin-like domains.
 283-357 2.62e-03

Immunoglobulin domain; This domain contains immunoglobulin-like domains.


Pssm-ID: 464026 [Multi-domain]  Cd Length: 79  Bit Score: 36.60  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51988879   283 GDTLTIRCDTKQQGMTKV-WVSpsNEQVLSQGSNgsvsvrngdLFFKKVQVEDGGVYTCYA-MGETFNETLSVELKV 357
Cdd:pfam13895  14 GEPVTLTCSAPGNPPPSYtWYK--DGSAISSSPN---------FFTLSVSAEDSGTYTCVArNGRGGKVSNPVELTV 79
Ig4_Contactin-2-like cd05728
Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The ...
 279-357 2.66e-03

Fourth Ig domain of the neural cell adhesion molecule contactin-2, and similar domains; The members here are composed of the fourth Ig domain of the neural cell adhesion molecule contactin-2. Contactins are comprised of six Ig domains followed by four fibronectin type III (FnIII) domains anchored to the membrane by glycosylphosphatidylinositol. Contactin-2 (also called TAG-1, axonin-1) facilitates cell adhesion by homophilic binding between molecules in apposed membranes. The first four Ig domains form the intermolecular binding fragment which arranges as a compact U-shaped module by contacts between Ig domains 1 and 4, and domains 2 and 3. It has been proposed that a linear zipper-like array forms, from contactin-2 molecules alternatively provided by the two apposed membranes.


Pssm-ID: 143205 [Multi-domain]  Cd Length: 85  Bit Score: 36.81  E-value: 2.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 279 EAHLGDTLTIRCDTKQQGMTKV-WVSpsNEQVLSqgSNGSVSVRNGDLFFKKVQVEDGGVYTCYAMGETFNETLSVELKV 357
Cdd:cd05728  10 EADIGSSLRWECKASGNPRPAYrWLK--NGQPLA--SENRIEVEAGDLRITKLSLSDSGMYQCVAENKHGTIYASAELAV 85
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 110-146 4.70e-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: 34.91  E-value: 4.70e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 51988879   110 PNLRYLDLSSNHLHTLDefLFSDLQALEVL-LLYNNHI 146
Cdd:pfam12799   1 PNLEVLDLSNNQITDIP--PLAKLPNLETLdLSGNNKI 36
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
44-225 5.09e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 39.15  E-value: 5.09e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879  44 ILSCSKQQLPNVPqSLPSYTAL--LDLSHNNLSRLRAEwtpTRLTNLHSLLLSHNH---LNFISSEAFVPVPNLRYLDLS 118
Cdd:COG4886 232 TLDLSNNQLTDLP-ELGNLTNLeeLDLSNNQLTDLPPL---ANLTNLKTLDLSNNQltdLKLKELELLLGLNSLLLLLLL 307

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51988879 119 SNHLHTLDEFLFSDLQALEVLLLYNNHIVVVDRNAFEDMAQLQKLYLSQNQISRFPVELIKDGNKLPKLMLLDLSSNKLK 198
Cdd:COG4886 308 LNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLL 387

                       170       180
                ....*....|....*....|....*..
gi 51988879 199 KLPLTDLQKLPAWVKNGLYLHNNPLEC 225
Cdd:COG4886 388 TLLLLLLTTTAGVLLLTLALLDAVNTE 414
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 86-128 5.78e-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: 34.91  E-value: 5.78e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 51988879    86 TNLHSLLLSHNHLNFIssEAFVPVPNLRYLDLSSN-HLHTLDEF 128
Cdd:pfam12799   1 PNLEVLDLSNNQITDI--PPLAKLPNLETLDLSGNnKITDLSDL 42
 
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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