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Conserved domains on  [gi|26338133|dbj|BAC32752|]
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unnamed protein product [Mus musculus]

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];
3-133 5.60e-20

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 92.69  E-value: 5.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   3 GVAKLTQLRVLNLPHNSIGCV-EGLKDLVHLEWLNLAGNNLKTM-EQVNSCTALQHLDLSDNNIPQIGD-VSKLISLKTL 79
Cdd:COG4886 108 ELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEeLGNLTNLKEL 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 26338133  80 LLHGNIITSLRMAPAYLPrNLSILSLAENEIRDLNEisFLASLSELEQLSIMNN 133
Cdd:COG4886 188 DLSNNQITDLPEPLGNLT-NLEELDLSGNQLTDLPE--PLANLTNLETLDLSNN 238
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 475-503 1.79e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


:

Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.79e-04
                        10        20
                ....*....|....*....|....*....
gi 26338133 475 LQKLNAAATKLQACWRGFYTRNYNQQAKG 503
Cdd:cd23767   5 LQRMNRAATLIQALWRGYKVRKELKKKKK 33
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
3-133 5.60e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 92.69  E-value: 5.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   3 GVAKLTQLRVLNLPHNSIGCV-EGLKDLVHLEWLNLAGNNLKTM-EQVNSCTALQHLDLSDNNIPQIGD-VSKLISLKTL 79
Cdd:COG4886 108 ELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEeLGNLTNLKEL 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 26338133  80 LLHGNIITSLRMAPAYLPrNLSILSLAENEIRDLNEisFLASLSELEQLSIMNN 133
Cdd:COG4886 188 DLSNNQITDLPEPLGNLT-NLEELDLSGNQLTDLPE--PLANLTNLETLDLSNN 238
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 3-170 1.90e-15

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: 75.59  E-value: 1.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   3 GVAKLTQLRVLNLPHNSIGCVEGLKDLVHLEWLNLAGNNLKTMEQ----VNSCTA----LQHLDLSDNNIPQIGDVSKLi 74
Cdd:cd21340  63 NLENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPPGEKltfdPRSLAAlsnsLRVLNISGNNIDSLEPLAPL- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133  75 slktlllhgniitslrmapaylpRNLSILSLAENEIRDLNEIS-FLASLSELEQLSIMNNPcVMATPSipgfdYRPFIVS 153
Cdd:cd21340 142 -----------------------RNLEQLDASNNQISDLEELLdLLSSWPSLRELDLTGNP-VCKKPK-----YRDKIIL 192

                       170
                ....*....|....*..
gi 26338133 154 WCLNLRVLDGYVISQKE 170
Cdd:cd21340 193 ASKSLEVLDGKEITDTE 209
LRR_9 pfam14580
Leucine-rich repeat;
35-184 1.28e-11

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 63.63  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133    35 LNLAGNNLKTMEQVN-SCTALQHLDLSDNNIPQIGDVSKLISLKTLLLHGNIItsLRMAPA---YLPrNLSILSLAENEI 110
Cdd:pfam14580  24 LDLRGYKIPIIENLGaTLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRI--CRIGEGlgeALP-NLTELILTNNNL 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26338133   111 RDLNEISFLASLSELEQLSIMNNPcVMATPsipgfDYRPFIVSWCLNLRVLDGYVISQKESLKAEWLYSQGKGR 184
Cdd:pfam14580 101 QELGDLDPLASLKKLTFLSLLRNP-VTNKP-----HYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGK 168
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 475-503 1.79e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.79e-04
                        10        20
                ....*....|....*....|....*....
gi 26338133 475 LQKLNAAATKLQACWRGFYTRNYNQQAKG 503
Cdd:cd23767   5 LQRMNRAATLIQALWRGYKVRKELKKKKK 33
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-133 9.16e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.53  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133    4 VAKLTQLRVLNLPHNSI--GCVEGLKDLVHLEWLNLAGNNL--KTMEQVNSCTALQHLDLSDNNI-----PQIGDVSKli 74
Cdd:PLN00113 184 LTNLTSLEFLTLASNQLvgQIPRELGQMKSLKWIYLGYNNLsgEIPYEIGGLTSLNHLDLVYNNLtgpipSSLGNLKN-- 261

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338133   75 sLKTLLLHGNIITSLRMAPAYLPRNLSILSLAEN----EIRDLneisfLASLSELEQLSIMNN 133
Cdd:PLN00113 262 -LQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNslsgEIPEL-----VIQLQNLEILHLFSN 318
 
Name Accession Description Interval E-value
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
3-133 5.60e-20

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 92.69  E-value: 5.60e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   3 GVAKLTQLRVLNLPHNSIGCV-EGLKDLVHLEWLNLAGNNLKTM-EQVNSCTALQHLDLSDNNIPQIGD-VSKLISLKTL 79
Cdd:COG4886 108 ELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLpEPLGNLTNLKSLDLSNNQLTDLPEeLGNLTNLKEL 187

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 26338133  80 LLHGNIITSLRMAPAYLPrNLSILSLAENEIRDLNEisFLASLSELEQLSIMNN 133
Cdd:COG4886 188 DLSNNQITDLPEPLGNLT-NLEELDLSGNQLTDLPE--PLANLTNLETLDLSNN 238
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
5-134 9.78e-19

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 88.84  E-value: 9.78e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   5 AKLTQLRVLNLPHNSIGCV-EGLKDLVHLEWLNLAGNNLKTM-EQVNSCTALQHLDLSDNNIPQIGD-VSKLISLKTLLL 81
Cdd:COG4886 156 GNLTNLKSLDLSNNQLTDLpEELGNLTNLKELDLSNNQITDLpEPLGNLTNLEELDLSGNQLTDLPEpLANLTNLETLDL 235

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 26338133  82 HGNIITSLrmaP--AYLPrNLSILSLAENEIRDlneISFLASLSELEQLSIMNNP 134
Cdd:COG4886 236 SNNQLTDL---PelGNLT-NLEELDLSNNQLTD---LPPLANLTNLKTLDLSNNQ 283
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-133 2.96e-16

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 81.13  E-value: 2.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   4 VAKLTQLRVLNLPHNsigcvEGLKDLVHLEWLNLAGNNLKTM-EQVNSCTALQHLDLSDNNIPQIGDV-SKLISLKTLLL 81
Cdd:COG4886  92 LGDLTNLTELDLSGN-----EELSNLTNLESLDLSGNQLTDLpEELANLTNLKELDLSNNQLTDLPEPlGNLTNLKSLDL 166

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 26338133  82 HGNIITSLRMAPAYLPrNLSILSLAENEIRDLNEisFLASLSELEQLSIMNN 133
Cdd:COG4886 167 SNNQLTDLPEELGNLT-NLKELDLSNNQITDLPE--PLGNLTNLEELDLSGN 215
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 3-170 1.90e-15

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: 75.59  E-value: 1.90e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   3 GVAKLTQLRVLNLPHNSIGCVEGLKDLVHLEWLNLAGNNLKTMEQ----VNSCTA----LQHLDLSDNNIPQIGDVSKLi 74
Cdd:cd21340  63 NLENLVNLKKLYLGGNRISVVEGLENLTNLEELHIENQRLPPGEKltfdPRSLAAlsnsLRVLNISGNNIDSLEPLAPL- 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133  75 slktlllhgniitslrmapaylpRNLSILSLAENEIRDLNEIS-FLASLSELEQLSIMNNPcVMATPSipgfdYRPFIVS 153
Cdd:cd21340 142 -----------------------RNLEQLDASNNQISDLEELLdLLSSWPSLRELDLTGNP-VCKKPK-----YRDKIIL 192

                       170
                ....*....|....*..
gi 26338133 154 WCLNLRVLDGYVISQKE 170
Cdd:cd21340 193 ASKSLEVLDGKEITDTE 209
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
5-134 3.24e-14

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 74.97  E-value: 3.24e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   5 AKLTQLRVLNLPHNSIGCV-EGLKDLVHLEWLNLAGNNLKTMEQVNSCTALQHLDLSDNNIPQIGDVSKLISLKTLLLHG 83
Cdd:COG4886 202 GNLTNLEELDLSGNQLTDLpEPLANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSN 281

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 26338133  84 NIITSLRMAPAYLPRNLSILSLAENEIRDLNEISFLASLSELEQLSIMNNP 134
Cdd:COG4886 282 NQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKG 332
LRR_9 pfam14580
Leucine-rich repeat;
35-184 1.28e-11

Leucine-rich repeat;


Pssm-ID: 405295 [Multi-domain]  Cd Length: 175  Bit Score: 63.63  E-value: 1.28e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133    35 LNLAGNNLKTMEQVN-SCTALQHLDLSDNNIPQIGDVSKLISLKTLLLHGNIItsLRMAPA---YLPrNLSILSLAENEI 110
Cdd:pfam14580  24 LDLRGYKIPIIENLGaTLDQFDTIDFSDNEIRKLDGFPLLRRLKTLLLNNNRI--CRIGEGlgeALP-NLTELILTNNNL 100

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26338133   111 RDLNEISFLASLSELEQLSIMNNPcVMATPsipgfDYRPFIVSWCLNLRVLDGYVISQKESLKAEWLYSQGKGR 184
Cdd:pfam14580 101 QELGDLDPLASLKKLTFLSLLRNP-VTNKP-----HYRLYVIYKVPQLRLLDFRKVKQKERQAAEKMFRSKQGK 168
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
4-154 6.82e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 61.49  E-value: 6.82e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   4 VAKLTQLRVLNLPHNSIGCVEGLKDLVHLEWLNLAGNNLKTMEQVNSCTALQHLDLSDNNIPQIgDVSKLISLKTLLLHG 83
Cdd:COG4886 224 LANLTNLETLDLSNNQLTDLPELGNLTNLEELDLSNNQLTDLPPLANLTNLKTLDLSNNQLTDL-KLKELELLLGLNSLL 302

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338133  84 NIITSLRMAPAYLPRNLSILSLAENEIRDLNEISFLASLSELEQLSIMNNPCVMATPSIPGFDYRPFIVSW 154
Cdd:COG4886 303 LLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLG 373
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
32-133 6.31e-09

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 58.41  E-value: 6.31e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133  32 LEWLNLAGNNLKTMEQVNSCTALQHLDLSDNNipqigDVSKLISLKTLLLHGNIITSLrmaPAYLPR--NLSILSLAENE 109
Cdd:COG4886  76 LLSLLLLSLLLLGLTDLGDLTNLTELDLSGNE-----ELSNLTNLESLDLSGNQLTDL---PEELANltNLKELDLSNNQ 147

                        90       100
                ....*....|....*....|....
gi 26338133 110 IRDLNEisFLASLSELEQLSIMNN 133
Cdd:COG4886 148 LTDLPE--PLGNLTNLKSLDLSNN 169
LRR_8 pfam13855
Leucine rich repeat;
8-64 1.25e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 45.98  E-value: 1.25e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26338133     8 TQLRVLNLPHNSIGCVEG--LKDLVHLEWLNLAGNNLKTMEQV--NSCTALQHLDLSDNNI 64
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDgaFKGLSNLKVLDLSNNLLTTLSPGafSGLPSLRYLDLSGNRL 61
LRR_8 pfam13855
Leucine rich repeat;
75-134 6.74e-06

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.67  E-value: 6.74e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133    75 SLKTLLLHGNIITSLRMAPAYLPRNLSILSLAENEIRDLNEISFlASLSELEQLSIMNNP 134
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAF-SGLPSLRYLDLSGNR 60
LRR_8 pfam13855
Leucine rich repeat;
31-84 1.20e-05

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 43.28  E-value: 1.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 26338133    31 HLEWLNLAGNNLKTMEQV--NSCTALQHLDLSDNNIPQIGDVS--KLISLKTLLLHGN 84
Cdd:pfam13855   2 NLRSLDLSNNRLTSLDDGafKGLSNLKVLDLSNNLLTTLSPGAfsGLPSLRYLDLSGN 59
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 31-75 1.49e-05

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: 42.23  E-value: 1.49e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 26338133    31 HLEWLNLAGNNLKTMEQVNSCTALQHLDLSDNNipQIGDVSKLIS 75
Cdd:pfam12799   2 NLEVLDLSNNQITDIPPLAKLPNLETLDLSGNN--KITDLSDLAN 44
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 6-134 3.74e-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: 46.19  E-value: 3.74e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   6 KLTQLRVLNLPHNSIG------CVEGLKDLVHLEWLNLagNNLKTMEQ--------VNSCTALQHLDLSDNNIPQIGdVS 71
Cdd:cd00116 163 ANRDLKELNLANNGIGdagiraLAEGLKANCNLEVLDL--NNNGLTDEgasalaetLASLKSLEVLNLGDNNLTDAG-AA 239

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 26338133  72 KL--------ISLKTLLLHGNIITSL--RMAPAYLPRNLSI--LSLAENEI-RDLNEISFLASLSELEQLSIMNNP 134
Cdd:cd00116 240 ALasallspnISLLTLSLSCNDITDDgaKDLAEVLAEKESLleLDLRGNKFgEEGAQLLAESLLEPGNELESLWVK 315
IQCD cd23767
IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory ...
 475-503 1.79e-04

IQ (isoleucine-glutamine) motif containing D (IQCD); IQCD, also called dynein regulatory complex protein 10 (DRC10), belongs to the IQ motif-containing protein family which contains a C-terminal conserved IQ motif domain and two coiled-coil domains. The IQ motif ([ILV]QxxxRxxxx[RK]), where x stands for any amino-acid residue, interacts with calmodulin (CaM) in a calcium-independent manner and is present in proteins with a wide diversity of biological functions. The IQCD protein was found to primarily accumulate in the acrosome area of round and elongating spermatids of the testis during late stage of spermiogenesis and was then localized to the acrosome and tail regions of mature spermatozoa. The expression of IQCD follows the trajectory of acrosome development during spermatogenesis. IQCD is associated with neuroblastoma and neurodegenerative diseases, and is reported to interact with the nuclear retinoid X receptor in the presence of 9-cis-retinoic acid, thereby activating the transcriptional activity of the receptor.


Pssm-ID: 467745 [Multi-domain]  Cd Length: 37  Bit Score: 39.06  E-value: 1.79e-04
                        10        20
                ....*....|....*....|....*....
gi 26338133 475 LQKLNAAATKLQACWRGFYTRNYNQQAKG 503
Cdd:cd23767   5 LQRMNRAATLIQALWRGYKVRKELKKKKK 33
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 8-42 5.46e-04

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: 38.00  E-value: 5.46e-04
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 26338133     8 TQLRVLNLPHNSIGCVEGLKDLVHLEWLNLAGNNL 42
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLDLSGNNK 35
LRR_8 pfam13855
Leucine rich repeat;
7-42 7.76e-04

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 37.89  E-value: 7.76e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 26338133     7 LTQLRVLNLPHNSIGCVEG--LKDLVHLEWLNLAGNNL 42
Cdd:pfam13855  24 LSNLKVLDLSNNLLTTLSPgaFSGLPSLRYLDLSGNRL 61
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 4-133 9.16e-04

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 42.53  E-value: 9.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133    4 VAKLTQLRVLNLPHNSI--GCVEGLKDLVHLEWLNLAGNNL--KTMEQVNSCTALQHLDLSDNNI-----PQIGDVSKli 74
Cdd:PLN00113 184 LTNLTSLEFLTLASNQLvgQIPRELGQMKSLKWIYLGYNNLsgEIPYEIGGLTSLNHLDLVYNNLtgpipSSLGNLKN-- 261

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26338133   75 sLKTLLLHGNIITSLRMAPAYLPRNLSILSLAEN----EIRDLneisfLASLSELEQLSIMNN 133
Cdd:PLN00113 262 -LQYLFLYQNKLSGPIPPSIFSLQKLISLDLSDNslsgEIPEL-----VIQLQNLEILHLFSN 318
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 52-89 1.73e-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: 36.45  E-value: 1.73e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 26338133    52 TALQHLDLSDNNIPQIGDVSKLISLKTL-LLHGNIITSL 89
Cdd:pfam12799   1 PNLEVLDLSNNQITDIPPLAKLPNLETLdLSGNNKITDL 39
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 4-132 3.10e-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: 40.54  E-value: 3.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   4 VAKLTQLRVLNLPHNSIGC------VEGLKDLVHLEWLNLAGNN--------LKTMEQVNscTALQHLDLSDNnipQIGD 69
Cdd:COG5238 232 LKGNKSLTTLDLSNNQIGDegvialAEALKNNTTVETLYLSGNQigaegaiaLAKALQGN--TTLTSLDLSVN---RIGD 306

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 26338133  70 VSkLISLKTLLLHGNIITSLRMAPAYLP--------------RNLSILSLAENEIRDLNEISFLASLSELEQLSIMN 132
Cdd:COG5238 307 EG-AIALAEGLQGNKTLHTLNLAYNGIGaqgaialakalqenTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLRELN 382
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 3-112 3.10e-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: 40.54  E-value: 3.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   3 GVAKLTQLRVLNLPHNSIG------CVEGLKDLVHLEWLNLAGNNLKTMEQVNSCTALQH------LDLSDNnipQIGDV 70
Cdd:COG5238 287 ALQGNTTLTSLDLSVNRIGdegaiaLAEGLQGNKTLHTLNLAYNGIGAQGAIALAKALQEnttlhsLDLSDN---QIGDE 363

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 26338133  71 S-----KLI----SLKTLLLHGNIITSL---RMAPAYLPRNLSILSLAENEIRD 112
Cdd:COG5238 364 GaialaKYLegntTLRELNLGKNNIGKQgaeALIDALQTNRLHTLILDGNLIGA 417
PLN03150 PLN03150
hypothetical protein; Provisional
 29-84 3.34e-03

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 40.57  E-value: 3.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 26338133   29 LVHLEWLNLAGNNLK--TMEQVNSCTALQHLDLSDN----NIPQigDVSKLISLKTLLLHGN 84
Cdd:PLN03150 441 LRHLQSINLSGNSIRgnIPPSLGSITSLEVLDLSYNsfngSIPE--SLGQLTSLRILNLNGN 500
Adgb_C_mid-like cd22307
C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted ...
 479-502 5.92e-03

C-terminal middle region of Androglobins (Adgbs) and related proteins; including permuted globin domain and IQ motif; Androglobin (Adgb, also known as Calpain-7-like protein, CAPN7L) is a large multidomain protein consisting of an N-terminal peptidase C2 family calpain-like domain, an IQ calmodulin-binding motif, and an internal, circularly permuted globin domain. The canonical secondary structure of hemoglobins is an 3-over-3 alpha-helical sandwich structure, where the eight alpha-helical segments are conventionally labeled, A-H, according to their sequential order; Adgbs differ from this in having helices C-H followed by A-B. Adgbs and other phylogenetically ancient globins, such as neuroglobins and globin X, form hexacoordinated heme iron complexes. Globins contain various highly conserved residues of the heme pocket: including a Phe in the interhelical position CD1 (Phe CD1, first position in the loop between the helices C and D) that is packed against the heme, a His at the 7th position of the E-helix (His E7) that binds the heme iron distally, and a His at the 8th position of the F-helix (His F8) that binds the heme iron proximally. Unlike other hexacoordinated globins, Adgbs have an E7 Gln; their hexacoordination scheme is [Gln]-Fe-[His]. In mammals, Adgb is mainly expressed in the testes and may play an important role in spermatogenesis. Arthropod Adgbs have degenerate globin domains (DOI:10.3389/fgene.2020.00858). This model spans the permuted globin domain, the IQ motif, and a conserved region of about 200 amino acid residues located C-terminal to the globin domain; it does not include the N-terminal protease domain or the large uncharacterized C-terminal domain of approximately 500 residues.


Pssm-ID: 412094  Cd Length: 416  Bit Score: 39.46  E-value: 5.92e-03
                        10        20
                ....*....|....*....|....
gi 26338133 479 NAAATKLQACWRGFYTRNYNQQAK 502
Cdd:cd22307 147 HEAATKIQAFFRGTLVRKLLKAHK 170
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 32-110 7.95e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.45  E-value: 7.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26338133   32 LEWLNLAGNNLKTMEQVNSCTALQHLDLSDN----NIPQigDVSKLISLKTLLLHGNIITSlrMAPAYLPR--NLSILSL 105
Cdd:PLN00113 120 LRYLNLSNNNFTGSIPRGSIPNLETLDLSNNmlsgEIPN--DIGSFSSLKVLDLGGNVLVG--KIPNSLTNltSLEFLTL 195


                 ....*
gi 26338133  106 AENEI 110
Cdd:PLN00113 196 ASNQL 200
 
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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