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Conserved domains on  [gi|325077017|gb|EGC30759|]
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hypothetical protein DICPUDRAFT_157468 [Dictyostelium purpureum]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 13-79 6.31e-27

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


:

Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 103.64  E-value: 6.31e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325077017   13 IGERIQSDDGYIGTIRYEGSVDGFDGNWYGIEWDDPkRGKHFGTVKGKQYFQCQyNGSGSFMKPEKL 79
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
Elongin_A pfam06881
RNA polymerase II transcription factor SIII (Elongin) subunit A; This family represents a ...
 414-515 1.03e-19

RNA polymerase II transcription factor SIII (Elongin) subunit A; This family represents a conserved region within RNA polymerase II transcription factor SIII (Elongin) subunit A. In mammals, the Elongin complex activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin is a heterotrimer composed of A, B, and C subunits of 110, 18, and 15 kilodaltons, respectively. Subunit A has been shown to function as the transcriptionally active component of Elongin.


:

Pssm-ID: 462026  Cd Length: 105  Bit Score: 84.58  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017  414 IKGLGRIPDKLLIVILDKCPPQQLIAIENKI-GRNVDTEELWKRHC---F-NLSPNQSVSPEDNDveTWRELYVVLERNY 488
Cdd:pfam06881   1 IDDVGDVPYHLLRPILLKCSPEQLRRIEENSpHLAGDTDELWKRFIkrdFpNWAEEKDYEPKNPK--SWRKLYEKLKEER 78

                          90       100
                  ....*....|....*....|....*..
gi 325077017  489 LDKARKTGDKLRNTYNNAAKNRQSKQI 515
Cdd:pfam06881  79 EEKLKAAAERLRQAYAGLQKEKQSKQI 105
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
159-435 7.26e-15

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


:

Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.90  E-value: 7.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 159 TEIKKSNDNNIELPSKTKSLVLNNLFISDfaflLPICKEIFSNLETLVVSNNSIENISnSSLDVFSKLVSLDLAHNKIK- 237
Cdd:COG4886   99 TELDLSGNEELSNLTNLESLDLSGNQLTD----LPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTd 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 238 ----------------SFNDIT----AIGFLEHLQELNLNNNQIDSIEFS----------DINKNQDDSTTTTKLFKNLK 287
Cdd:COG4886  174 lpeelgnltnlkeldlSNNQITdlpePLGNLTNLEELDLSGNQLTDLPEPlanltnletlDLSNNQLTDLPELGNLTNLE 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 288 ILYLSNNNISDwrhVEELDYLQNLEELSFRENPIIDSLLLDAAAIKDQNQQDETNNTKTVTTSTGVKKISVNKNIYLNRL 367
Cdd:COG4886  254 ELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLL 330

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325077017 368 NIIPRISKLTKLNLSHKIMDNLFGDEIEVPTLLSICTQRIKDSLDNIKGLGRIPDKLLIVILDKCPPQ 435
Cdd:COG4886  331 KGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTA 398
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 13-79 6.31e-27

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 103.64  E-value: 6.31e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325077017   13 IGERIQSDDGYIGTIRYEGSVDGFDGNWYGIEWDDPkRGKHFGTVKGKQYFQCQyNGSGSFMKPEKL 79
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 13-79 8.85e-23

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 91.88  E-value: 8.85e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325077017    13 IGERIQ-SDDGYIGTIRYEGSVDGFDGNWYGIEWDDPKRGKHFGTVKGKQYFQCQyNGSGSFMKPEKL 79
Cdd:smart01052   1 VGDRVEvGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Elongin_A pfam06881
RNA polymerase II transcription factor SIII (Elongin) subunit A; This family represents a ...
 414-515 1.03e-19

RNA polymerase II transcription factor SIII (Elongin) subunit A; This family represents a conserved region within RNA polymerase II transcription factor SIII (Elongin) subunit A. In mammals, the Elongin complex activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin is a heterotrimer composed of A, B, and C subunits of 110, 18, and 15 kilodaltons, respectively. Subunit A has been shown to function as the transcriptionally active component of Elongin.


Pssm-ID: 462026  Cd Length: 105  Bit Score: 84.58  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017  414 IKGLGRIPDKLLIVILDKCPPQQLIAIENKI-GRNVDTEELWKRHC---F-NLSPNQSVSPEDNDveTWRELYVVLERNY 488
Cdd:pfam06881   1 IDDVGDVPYHLLRPILLKCSPEQLRRIEENSpHLAGDTDELWKRFIkrdFpNWAEEKDYEPKNPK--SWRKLYEKLKEER 78

                          90       100
                  ....*....|....*....|....*..
gi 325077017  489 LDKARKTGDKLRNTYNNAAKNRQSKQI 515
Cdd:pfam06881  79 EEKLKAAAERLRQAYAGLQKEKQSKQI 105
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
159-435 7.26e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.90  E-value: 7.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 159 TEIKKSNDNNIELPSKTKSLVLNNLFISDfaflLPICKEIFSNLETLVVSNNSIENISnSSLDVFSKLVSLDLAHNKIK- 237
Cdd:COG4886   99 TELDLSGNEELSNLTNLESLDLSGNQLTD----LPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTd 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 238 ----------------SFNDIT----AIGFLEHLQELNLNNNQIDSIEFS----------DINKNQDDSTTTTKLFKNLK 287
Cdd:COG4886  174 lpeelgnltnlkeldlSNNQITdlpePLGNLTNLEELDLSGNQLTDLPEPlanltnletlDLSNNQLTDLPELGNLTNLE 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 288 ILYLSNNNISDwrhVEELDYLQNLEELSFRENPIIDSLLLDAAAIKDQNQQDETNNTKTVTTSTGVKKISVNKNIYLNRL 367
Cdd:COG4886  254 ELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLL 330

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325077017 368 NIIPRISKLTKLNLSHKIMDNLFGDEIEVPTLLSICTQRIKDSLDNIKGLGRIPDKLLIVILDKCPPQ 435
Cdd:COG4886  331 KGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTA 398
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 178-321 4.82e-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: 62.88  E-value: 4.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 178 LVLNNLFISDFAfLLPICKeifsNLETLVVSNNSIENISNssLDVFSKLVSLDLAHNKIK----------------SFND 241
Cdd:cd21340    7 LYLNDKNITKID-NLSLCK----NLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEkienlenlvnlkklylGGNR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 242 ITAI-GF--LEHLQELNLNNNQID---SIEFS--------------DINKNQDDSTTTTKLFKNLKILYLSNNNISDWRH 301
Cdd:cd21340   80 ISVVeGLenLTNLEELHIENQRLPpgeKLTFDprslaalsnslrvlNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEE 159

                        170       180
                 ....*....|....*....|.
gi 325077017 302 VEE-LDYLQNLEELSFRENPI 321
Cdd:cd21340  160 LLDlLSSWPSLRELDLTGNPV 180
LRR_8 pfam13855
Leucine rich repeat;
200-261 5.98e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.53  E-value: 5.98e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325077017  200 SNLETLVVSNNSIENISNSSLDVFSKLVSLDLAHNKIKSFNDITAIGfLEHLQELNLNNNQI 261
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSG-LPSLRYLDLSGNRL 61
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 22-76 3.27e-07

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 53.54  E-value: 3.27e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 325077017  22 GYIGTIRYEGSVDGFDGNWYGIEWDDPKrGKHFGTVKGKQYFQCQyNGSGSFMKP 76
Cdd:COG5244   14 DKFGTVRFIGKTKFKDGIWIGLELDDPV-GKNDGSVNGVRYFHCK-KRHGIFIRP 66
PLN03150 PLN03150
hypothetical protein; Provisional
 199-259 9.22e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 9.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325077017 199 FSNLETLVVSNNSIENISNSSLDVFSKLVSLDLAHNkikSFNDIT--AIGFLEHLQELNLNNN 259
Cdd:PLN03150 441 LRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYN---SFNGSIpeSLGQLTSLRILNLNGN 500
 
Name Accession Description Interval E-value
CAP_GLY pfam01302
CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of ...
 13-79 6.31e-27

CAP-Gly domain; Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 460154 [Multi-domain]  Cd Length: 65  Bit Score: 103.64  E-value: 6.31e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 325077017   13 IGERIQSDDGYIGTIRYEGSVDGFDGNWYGIEWDDPkRGKHFGTVKGKQYFQCQyNGSGSFMKPEKL 79
Cdd:pfam01302   1 VGDRVEVPGGRRGTVRYVGPVPFAPGVWVGVELDEP-VGKNDGSVKGVRYFECP-PKHGVFVRPSKV 65
CAP_GLY smart01052
Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and ...
 13-79 8.85e-23

Cytoskeleton-associated proteins (CAPs) are involved in the organisation of microtubules and transportation of vesicles and organelles along the cytoskeletal network; A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of Caenorhabditis elegans F53F4.3 protein CAP-Gly domain was recently solved. The domain contains three beta-strands. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove.


Pssm-ID: 214997 [Multi-domain]  Cd Length: 68  Bit Score: 91.88  E-value: 8.85e-23
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325077017    13 IGERIQ-SDDGYIGTIRYEGSVDGFDGNWYGIEWDDPKRGKHFGTVKGKQYFQCQyNGSGSFMKPEKL 79
Cdd:smart01052   1 VGDRVEvGGGGRRGTVRYVGPTPFAPGVWVGVELDEPLRGKNDGSVKGVRYFECP-PKHGIFVRPSKV 67
Elongin_A pfam06881
RNA polymerase II transcription factor SIII (Elongin) subunit A; This family represents a ...
 414-515 1.03e-19

RNA polymerase II transcription factor SIII (Elongin) subunit A; This family represents a conserved region within RNA polymerase II transcription factor SIII (Elongin) subunit A. In mammals, the Elongin complex activates elongation by RNA polymerase II by suppressing transient pausing of the polymerase at many sites within transcription units. Elongin is a heterotrimer composed of A, B, and C subunits of 110, 18, and 15 kilodaltons, respectively. Subunit A has been shown to function as the transcriptionally active component of Elongin.


Pssm-ID: 462026  Cd Length: 105  Bit Score: 84.58  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017  414 IKGLGRIPDKLLIVILDKCPPQQLIAIENKI-GRNVDTEELWKRHC---F-NLSPNQSVSPEDNDveTWRELYVVLERNY 488
Cdd:pfam06881   1 IDDVGDVPYHLLRPILLKCSPEQLRRIEENSpHLAGDTDELWKRFIkrdFpNWAEEKDYEPKNPK--SWRKLYEKLKEER 78

                          90       100
                  ....*....|....*....|....*..
gi 325077017  489 LDKARKTGDKLRNTYNNAAKNRQSKQI 515
Cdd:pfam06881  79 EEKLKAAAERLRQAYAGLQKEKQSKQI 105
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
159-435 7.26e-15

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 76.90  E-value: 7.26e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 159 TEIKKSNDNNIELPSKTKSLVLNNLFISDfaflLPICKEIFSNLETLVVSNNSIENISnSSLDVFSKLVSLDLAHNKIK- 237
Cdd:COG4886   99 TELDLSGNEELSNLTNLESLDLSGNQLTD----LPEELANLTNLKELDLSNNQLTDLP-EPLGNLTNLKSLDLSNNQLTd 173

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 238 ----------------SFNDIT----AIGFLEHLQELNLNNNQIDSIEFS----------DINKNQDDSTTTTKLFKNLK 287
Cdd:COG4886  174 lpeelgnltnlkeldlSNNQITdlpePLGNLTNLEELDLSGNQLTDLPEPlanltnletlDLSNNQLTDLPELGNLTNLE 253

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 288 ILYLSNNNISDwrhVEELDYLQNLEELSFRENPIIDSLLLDAAAIKDQNQQDETNNTKTVTTSTGVKKISVNKNIYLNRL 367
Cdd:COG4886  254 ELDLSNNQLTD---LPPLANLTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLL 330

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 325077017 368 NIIPRISKLTKLNLSHKIMDNLFGDEIEVPTLLSICTQRIKDSLDNIKGLGRIPDKLLIVILDKCPPQ 435
Cdd:COG4886  331 KGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTA 398
PPP1R42 cd21340
protein phosphatase 1 regulatory subunit 42; Protein phosphatase 1 regulatory subunit 42 ...
 178-321 4.82e-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: 62.88  E-value: 4.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 178 LVLNNLFISDFAfLLPICKeifsNLETLVVSNNSIENISNssLDVFSKLVSLDLAHNKIK----------------SFND 241
Cdd:cd21340    7 LYLNDKNITKID-NLSLCK----NLKVLYLYDNKITKIEN--LEFLTNLTHLYLQNNQIEkienlenlvnlkklylGGNR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 242 ITAI-GF--LEHLQELNLNNNQID---SIEFS--------------DINKNQDDSTTTTKLFKNLKILYLSNNNISDWRH 301
Cdd:cd21340   80 ISVVeGLenLTNLEELHIENQRLPpgeKLTFDprslaalsnslrvlNISGNNIDSLEPLAPLRNLEQLDASNNQISDLEE 159

                        170       180
                 ....*....|....*....|.
gi 325077017 302 VEE-LDYLQNLEELSFRENPI 321
Cdd:cd21340  160 LLDlLSSWPSLRELDLTGNPV 180
LRR_8 pfam13855
Leucine rich repeat;
200-261 5.98e-09

Leucine rich repeat;


Pssm-ID: 404697 [Multi-domain]  Cd Length: 61  Bit Score: 52.53  E-value: 5.98e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 325077017  200 SNLETLVVSNNSIENISNSSLDVFSKLVSLDLAHNKIKSFNDITAIGfLEHLQELNLNNNQI 261
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDDGAFKGLSNLKVLDLSNNLLTTLSPGAFSG-LPSLRYLDLSGNRL 61
NIP100 COG5244
Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle ...
 22-76 3.27e-07

Dynactin complex subunit involved in mitotic spindle partitioning in anaphase B [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 227569 [Multi-domain]  Cd Length: 669  Bit Score: 53.54  E-value: 3.27e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 325077017  22 GYIGTIRYEGSVDGFDGNWYGIEWDDPKrGKHFGTVKGKQYFQCQyNGSGSFMKP 76
Cdd:COG5244   14 DKFGTVRFIGKTKFKDGIWIGLELDDPV-GKNDGSVNGVRYFHCK-KRHGIFIRP 66
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
133-323 4.08e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 52.63  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 133 QQKIISASHLLISEIDEYPAIFNYFKTEIKKSNDNNIELPSKTKSLVLNNLFISDFAFLLPICKEIFSNLETLVVSNNSI 212
Cdd:COG4886    2 LLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLL 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 213 ENISNSSLDVFSKLVSLdlahnKIKSFNDITAIGFLEHLQELNLNNNQIDSIeFSDINKnqddsttttklFKNLKILYLS 292
Cdd:COG4886   82 LSLLLLGLTDLGDLTNL-----TELDLSGNEELSNLTNLESLDLSGNQLTDL-PEELAN-----------LTNLKELDLS 144

                        170       180       190
                 ....*....|....*....|....*....|.
gi 325077017 293 NNNISDWRhvEELDYLQNLEELSFRENPIID 323
Cdd:COG4886  145 NNQLTDLP--EPLGNLTNLKSLDLSNNQLTD 173
LRR_8 pfam13855
Leucine rich repeat;
224-296 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        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 325077017  224 SKLVSLDLAHNKIKSFNDiTAIGFLEHLQELNLNNNQIDSIE---FSDINknqddsttttklfkNLKILYLSNNNI 296
Cdd:pfam13855   1 PNLRSLDLSNNRLTSLDD-GAFKGLSNLKVLDLSNNLLTTLSpgaFSGLP--------------SLRYLDLSGNRL 61
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 196-299 8.61e-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: 45.04  E-value: 8.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 196 KEIFSNLETLVVSNNSIENISNSSL-DVFS---KLVSLDLAHNKIKSFNdITAI--GFLE--HLQELNLNNNQIDSIEFS 267
Cdd:cd00116  133 KDLPPALEKLVLGRNRLEGASCEALaKALRanrDLKELNLANNGIGDAG-IRALaeGLKAncNLEVLDLNNNGLTDEGAS 211

                         90       100       110
                 ....*....|....*....|....*....|..
gi 325077017 268 DInknqddsTTTTKLFKNLKILYLSNNNISDW 299
Cdd:cd00116  212 AL-------AETLASLKSLEVLNLGDNNLTDA 236
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 284-325 3.96e-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: 38.38  E-value: 3.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 325077017  284 KNLKILYLSNNNISDwrhVEELDYLQNLEELSFRENPIIDSL 325
Cdd:pfam12799   1 PNLEVLDLSNNQITD---IPPLAKLPNLETLDLSGNNKITDL 39
PLN03150 PLN03150
hypothetical protein; Provisional
 199-259 9.22e-04

hypothetical protein; Provisional


Pssm-ID: 178695 [Multi-domain]  Cd Length: 623  Bit Score: 42.11  E-value: 9.22e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325077017 199 FSNLETLVVSNNSIENISNSSLDVFSKLVSLDLAHNkikSFNDIT--AIGFLEHLQELNLNNN 259
Cdd:PLN03150 441 LRHLQSINLSGNSIRGNIPPSLGSITSLEVLDLSYN---SFNGSIpeSLGQLTSLRILNLNGN 500
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
199-351 1.41e-03

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 41.46  E-value: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 199 FSNLETLVVSNNSIENISNSSLdvFSKLVSLDLAHNKIKSFNDITAIGFLEHLQELNLNNNQIDSIEFSDINKNQDDSTT 278
Cdd:COG4886  249 LTNLEELDLSNNQLTDLPPLAN--LTNLKTLDLSNNQLTDLKLKELELLLGLNSLLLLLLLLNLLELLILLLLLTTLLLL 326

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 325077017 279 TTKLFKNLKILYLSNNNISDWRHVEELDYLQNLEELSFRENPIIDSLLLDAAAIKDQNQQDETNNTKTVTTST 351
Cdd:COG4886  327 LLLLKGLLVTLTTLALSLSLLALLTLLLLLNLLSLLLTLLLTLGLLGLLEATLLTLALLLLTLLLLLLTTTAG 399
LRR_4 pfam12799
Leucine Rich repeats (2 copies); Leucine rich repeats are short sequence motifs present in a ...
 225-266 4.33e-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: 4.33e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 325077017  225 KLVSLDLAHNKIKsfnDITAIGFLEHLQELNL-NNNQIDSIEF 266
Cdd:pfam12799   2 NLEVLDLSNNQIT---DIPPLAKLPNLETLDLsGNNKITDLSD 41
PLN00113 PLN00113
leucine-rich repeat receptor-like protein kinase; Provisional
 151-297 5.96e-03

leucine-rich repeat receptor-like protein kinase; Provisional


Pssm-ID: 215061 [Multi-domain]  Cd Length: 968  Bit Score: 39.83  E-value: 5.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 325077017 151 PAIFN--YFKTEIKKSNDNNIELPSK--TKSLVLNNLFISDFAFLLPICKEIFSNLETLVVSNNSIENISNSSLDVFSKL 226
Cdd:PLN00113  87 SAIFRlpYIQTINLSNNQLSGPIPDDifTTSSSLRYLNLSNNNFTGSIPRGSIPNLETLDLSNNMLSGEIPNDIGSFSSL 166

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 325077017 227 VSLDLAHNKIKSFNDITaIGFLEHLQELNLNNNQIDSIEFSDINKnqddsttttklFKNLKILYLSNNNIS 297
Cdd:PLN00113 167 KVLDLGGNVLVGKIPNS-LTNLTSLEFLTLASNQLVGQIPRELGQ-----------MKSLKWIYLGYNNLS 225
 
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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