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Conserved domains on  [gi|960139137|ref|NP_001304695|]
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capping protein, Arp2/3 and myosin-I linker protein 2 [Danio rerio]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Carm_PH super family cl39358
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 24-117 1.26e-27

Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.


The actual alignment was detected with superfamily member pfam17888:

Pssm-ID: 436119  Cd Length: 94  Bit Score: 108.14  E-value: 1.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137    24 VQFMSLVHLNQGKGRADSRVLVISQWRAHVFYSKQPVKVESSFSYLEIYAITIDSIEQVVIETDRQIYSLGLMSVRDLEA 103
Cdd:pfam17888    1 IKLVKSVKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDH 80

                           90
                   ....*....|....
gi 960139137   104 VVSHVTASLKKIFP 117
Cdd:pfam17888   81 VVGHILTALKKIFP 94
CARMIL_C super family cl24538
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 783-1139 3.18e-17

CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).


The actual alignment was detected with superfamily member pfam16000:

Pssm-ID: 464966 [Multi-domain]  Cd Length: 299  Bit Score: 84.44  E-value: 3.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   783 CPRVVQRSSVNEQLADRVAKKTRQAAHFIQNTM-HEAENSIRNKLSELKLSVSVSLVESIINEVHQDLFVAQEKLDKHMR 861
Cdd:pfam16000    5 CPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLlEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLARHLS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   862 EfsqsssikanvPQLRVMEHEFPTDDYVPviwRNSFHSRSIRPAPSIKSLLDVEgeqqaraaTHPQQEPEERGGGGGGGV 941
Cdd:pfam16000   85 Q-----------RGRTLLEPESLPDGDRP---ESSPLGPGKRHEGEIERLEELE--------TPMATLKSKRKSIHSRKL 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   942 PQVSRVGTEERRRAQSLPLATGLSVTTAGQLKPGSPSywrreadaaaapaaaaaalSNREPRRSEPAPPQPPMDLPIEGH 1021
Cdd:pfam16000  143 RPVSVAFSVSELDLDKAPEEVPIHVEDASSGPPLPSS-------------------SPSEPELSASESLDSLSELPTEGQ 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1022 TLRHYTRSRPRPNRRNRQPPSKPQEQAAEiENEANENMGRVDEGVEEFFTKKIIPDDPLKHQREEPlikaqpaeptcvtt 1101
Cdd:pfam16000  204 KLQHLTKGRPKRNKTRAPTRPPGKVGPAQ-DGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEP-------------- 268

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 960139137  1102 appttstTTPIPTTAPSKNIKKKFGDFFAFKKVRAGRG 1139
Cdd:pfam16000  269 -------SSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 super family cl34950
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-613 3.45e-17

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


The actual alignment was detected with superfamily member COG5238:

Pssm-ID: 444072 [Multi-domain]  Cd Length: 434  Bit Score: 86.38  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  250 SLEASGLKMDFAIRMATALRESTasaVHIINLSVNAIEDKGVIALSQSLGKlSCCLSQLHLSKVSMSSKGLGCLVQVLHQ 329
Cdd:COG5238   159 LGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKG 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  330 STflcnTLTHLDLSGNtgCLATEEAMSLYRFLSAPNSVSHLDLSCTDCPLDTLfVSLS--LGCCTTLNYLNLSRNPfslr 407
Cdd:COG5238   235 NK----SLTTLDLSNN--QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGA-IALAkaLQGNTTLTSLDLSVNR---- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  408 kvrevtrsvrdffskstvlkyVGFSGTklppealRLLLQGLATNTHLSELelDISSCELRSAGAQVIQEHIFEAKAISSL 487
Cdd:COG5238   304 ---------------------IGDEGA-------IALAEGLQGNKTLHTL--NLAYNGIGAQGAIALAKALQENTTLHSL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  488 DLSDNgfesnmvtlilsigrshsikhlsigrnfamksrALTDvlhrlvqliqeeecpleslsvcdsklkTGTTILINSLG 567
Cdd:COG5238   354 DLSDN---------------------------------QIGD---------------------------EGAIALAKYLE 373

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 960139137  568 CNASLSKIDISGNCIGDTGAKMLAKALMMNtKLKTLVWDRNNVTAG 613
Cdd:COG5238   374 GNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAE 418
PHA03247 super family cl33720
large tegument protein UL36; Provisional
 1224-1663 8.72e-08

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1224 DKMSPRAPSPVPTPALTPPASTPTPPASSPSKTEEVPALSPAAPPTKTPSPVPVVSPS---EREKSRTLEK--------S 1292
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASsppQRPRRRAARPtvgsltslA 2699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1293 RTPDGERRPKPIRRSL------------REGKSQSLILLSDVLPEQDGTAMHAKKHASESSSSFEQRLHVMLHRMGVTKT 1360
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALvsatplppgpaaARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1361 SPTDTKQSQSKDEELRKA---NSEGAILDKPEPPPTFMKPRTMSTSSDTRRPTRVTqsvtdfqrterPQLPERPIGPLPP 1437
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESlpsPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-----------PTAPPPPPGPPPP 2848

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1438 KPTMKPILFPTSETARTATATPKLPSPSQDGQPEVSE--AISVSQPQEKEKEPPTPSPRKEAPPAPSPRRilstdIRERA 1515
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQ-----PQPQP 2923

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1516 ERAQSVTEETLPIPRPRMKPSPQRRAVSVHEDSLLQHAAMLDP-EELKAALPRRQKSPGRKKGNVGELTTCSedlPEGEP 1594
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlVPGRVAVPRFRVPQPAPSREAPASSTPP---LTGHS 3000

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960139137 1595 VK--SAGKDSTGQVEETDSTTVTDSQSEQSPTGSSEqvtnQERDESVVSEEHTTQGETSDQRTESP-SPEKH 1663
Cdd:PHA03247 3001 LSrvSSWASSLALHEETDPPPVSLKQTLWPPDDTED----SDADSLFDSDSERSDLEALDPLPPEPhDPFAH 3068
 
Name Accession Description Interval E-value
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 24-117 1.26e-27

Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.


Pssm-ID: 436119  Cd Length: 94  Bit Score: 108.14  E-value: 1.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137    24 VQFMSLVHLNQGKGRADSRVLVISQWRAHVFYSKQPVKVESSFSYLEIYAITIDSIEQVVIETDRQIYSLGLMSVRDLEA 103
Cdd:pfam17888    1 IKLVKSVKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDH 80

                           90
                   ....*....|....
gi 960139137   104 VVSHVTASLKKIFP 117
Cdd:pfam17888   81 VVGHILTALKKIFP 94
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 783-1139 3.18e-17

CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).


Pssm-ID: 464966 [Multi-domain]  Cd Length: 299  Bit Score: 84.44  E-value: 3.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   783 CPRVVQRSSVNEQLADRVAKKTRQAAHFIQNTM-HEAENSIRNKLSELKLSVSVSLVESIINEVHQDLFVAQEKLDKHMR 861
Cdd:pfam16000    5 CPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLlEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLARHLS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   862 EfsqsssikanvPQLRVMEHEFPTDDYVPviwRNSFHSRSIRPAPSIKSLLDVEgeqqaraaTHPQQEPEERGGGGGGGV 941
Cdd:pfam16000   85 Q-----------RGRTLLEPESLPDGDRP---ESSPLGPGKRHEGEIERLEELE--------TPMATLKSKRKSIHSRKL 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   942 PQVSRVGTEERRRAQSLPLATGLSVTTAGQLKPGSPSywrreadaaaapaaaaaalSNREPRRSEPAPPQPPMDLPIEGH 1021
Cdd:pfam16000  143 RPVSVAFSVSELDLDKAPEEVPIHVEDASSGPPLPSS-------------------SPSEPELSASESLDSLSELPTEGQ 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1022 TLRHYTRSRPRPNRRNRQPPSKPQEQAAEiENEANENMGRVDEGVEEFFTKKIIPDDPLKHQREEPlikaqpaeptcvtt 1101
Cdd:pfam16000  204 KLQHLTKGRPKRNKTRAPTRPPGKVGPAQ-DGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEP-------------- 268

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 960139137  1102 appttstTTPIPTTAPSKNIKKKFGDFFAFKKVRAGRG 1139
Cdd:pfam16000  269 -------SSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-613 3.45e-17

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: 86.38  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  250 SLEASGLKMDFAIRMATALRESTasaVHIINLSVNAIEDKGVIALSQSLGKlSCCLSQLHLSKVSMSSKGLGCLVQVLHQ 329
Cdd:COG5238   159 LGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKG 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  330 STflcnTLTHLDLSGNtgCLATEEAMSLYRFLSAPNSVSHLDLSCTDCPLDTLfVSLS--LGCCTTLNYLNLSRNPfslr 407
Cdd:COG5238   235 NK----SLTTLDLSNN--QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGA-IALAkaLQGNTTLTSLDLSVNR---- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  408 kvrevtrsvrdffskstvlkyVGFSGTklppealRLLLQGLATNTHLSELelDISSCELRSAGAQVIQEHIFEAKAISSL 487
Cdd:COG5238   304 ---------------------IGDEGA-------IALAEGLQGNKTLHTL--NLAYNGIGAQGAIALAKALQENTTLHSL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  488 DLSDNgfesnmvtlilsigrshsikhlsigrnfamksrALTDvlhrlvqliqeeecpleslsvcdsklkTGTTILINSLG 567
Cdd:COG5238   354 DLSDN---------------------------------QIGD---------------------------EGAIALAKYLE 373

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 960139137  568 CNASLSKIDISGNCIGDTGAKMLAKALMMNtKLKTLVWDRNNVTAG 613
Cdd:COG5238   374 GNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAE 418
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 397-648 7.80e-13

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: 71.62  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  397 LNLSRNPFSLRKVREVTRSVRDffskstvLKYVGFSGTKLPPEALRLLLQGLATNTHLSELELdiSSCELRSAGAQVIQE 476
Cdd:cd00116     3 LSLKGELLKTERATELLPKLLC-------LQVLRLEGNTLGEEAAKALASALRPQPSLKELCL--SLNETGRIPRGLQSL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  477 -HIFEAKA-ISSLDLSDNGFESNMVTLILSIGRSHSIKHLSIGRN------FAMKSRALTDVLHRLVQLIQEEeCPLESL 548
Cdd:cd00116    74 lQGLTKGCgLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNglgdrgLRLLAKGLKDLPPALEKLVLGR-NRLEGA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  549 SVCD--------SKLKT-----------GTTILINSLGCNASLSKIDISGNCIGDTGAKMLAKALMMNTKLKTLVWDRNN 609
Cdd:cd00116   153 SCEAlakalranRDLKElnlanngigdaGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 960139137  610 VTAGGFMDVANALE------KNLTLQNISIPMSDVLQAHRSAPEK 648
Cdd:cd00116   233 LTDAGAAALASALLspnislLTLSLSCNDITDDGAKDLAEVLAEK 277
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1224-1663 8.72e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1224 DKMSPRAPSPVPTPALTPPASTPTPPASSPSKTEEVPALSPAAPPTKTPSPVPVVSPS---EREKSRTLEK--------S 1292
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASsppQRPRRRAARPtvgsltslA 2699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1293 RTPDGERRPKPIRRSL------------REGKSQSLILLSDVLPEQDGTAMHAKKHASESSSSFEQRLHVMLHRMGVTKT 1360
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALvsatplppgpaaARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1361 SPTDTKQSQSKDEELRKA---NSEGAILDKPEPPPTFMKPRTMSTSSDTRRPTRVTqsvtdfqrterPQLPERPIGPLPP 1437
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESlpsPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-----------PTAPPPPPGPPPP 2848

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1438 KPTMKPILFPTSETARTATATPKLPSPSQDGQPEVSE--AISVSQPQEKEKEPPTPSPRKEAPPAPSPRRilstdIRERA 1515
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQ-----PQPQP 2923

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1516 ERAQSVTEETLPIPRPRMKPSPQRRAVSVHEDSLLQHAAMLDP-EELKAALPRRQKSPGRKKGNVGELTTCSedlPEGEP 1594
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlVPGRVAVPRFRVPQPAPSREAPASSTPP---LTGHS 3000

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960139137 1595 VK--SAGKDSTGQVEETDSTTVTDSQSEQSPTGSSEqvtnQERDESVVSEEHTTQGETSDQRTESP-SPEKH 1663
Cdd:PHA03247 3001 LSrvSSWASSLALHEETDPPPVSLKQTLWPPDDTED----SDADSLFDSDSERSDLEALDPLPPEPhDPFAH 3068
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1356-1572 6.00e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.39  E-value: 6.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1356 GVTKTSPTDTKQSQSKDEELRKAnSEGAILDKPEPPPTFMKPRTMSTSsDTRRPTRVTQSVTDFQRTERPQLPERPIGPL 1435
Cdd:pfam03154   43 GRNSPSAASTSSNDSKAESMKKS-SKKIKEEAPSPLKSAKRQREKGAS-DTEEPERATAKKSKTQEISRPNSPSEGEGES 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1436 PPKPTMKPILF--PTSETARTATATPKLPSPsQDGQpevSEAISVSQPQEKEKEPPTPSPRKEAPPAPSPRRILSTDIRE 1513
Cdd:pfam03154  121 SDGRSVNDEGSsdPKDIDQDNRSTSPSIPSP-QDNE---SDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAAT 196

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 960139137  1514 RAERAQSVTEETLPIPRPRMKPSPQRRAVSVHedSLLQHAAMLDPEELKAALPRRQKSP 1572
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAAPH--TLIQQTPTLHPQRLPSPHPPLQPMT 253
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 1290-1539 1.70e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1290 EKSRTPDGERRPKPirrsLREGKSQSLillSDVLPEQDGTAMHAKKHASESSSSFEQR-LHVMLHRMGVTKTSPTDTKQS 1368
Cdd:NF033839  170 QKPTTPAPDTKPSP----QPEGKKPSV---PDINQEKEKAKLAVATYMSKILDDIQKHhLQKEKHRQIVALIKELDELKK 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1369 QSKDE------ELRKANSEGAILDKPEPPPT-FMKPRTMSTSSDTRRPTRVTQSvTDFQRTERPQLPERPIGPLPPKPTM 1441
Cdd:NF033839  243 QALSEidnvntKVEIENTVHKIFADMDAVVTkFKKGLTQDTPKEPGNKKPSAPK-PGMQPSPQPEKKEVKPEPETPKPEV 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1442 KPIL-------FPTSETAR-TATATPKLPSPSQDGQPEVSEAISVSQPQEKEKE----PPTPSPR-KEAPPAPSPrrils 1508
Cdd:NF033839  322 KPQLekpkpevKPQPEKPKpEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEvkpqPETPKPEvKPQPEKPKP----- 396

                         250       260       270
                  ....*....|....*....|....*....|.
gi 960139137 1509 tDIRERAERAQSVTEETLPIPRPRMKPSPQR 1539
Cdd:NF033839  397 -EVKPQPEKPKPEVKPQPEKPKPEVKPQPEK 426
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 1452-1549 4.61e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 44.61  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1452 ARTATATPKLPSPSQDGQPEVSeAISVSQPQEKEKEPPTPSPRKEAPPAPSPRRILSTDIRERaERAQSVTEETLPI--P 1529
Cdd:NF041121   17 RAAAPPSPEGPAPTAASQPATP-PPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPP-GPAGAAPGAALPVrvP 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 960139137 1530 RPRMKPSP----------QRRAVSVHEDSL 1549
Cdd:NF041121   95 APPALPNPlelaralrplKRRVPSPRRVEL 124
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
569-594 1.30e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 1.30e-03
                            10        20
                    ....*....|....*....|....*.
gi 960139137    569 NASLSKIDISGNCIGDTGAKMLAKAL 594
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEAL 26
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 1377-1542 1.57e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 43.13  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1377 KANSEGAILDKP-EPPPTFMKPRTMSTSSDTRRPTRVTQSVTDFQrtERPQLPERPIGPLPPKPTMKPILFPTSETArta 1455
Cdd:COG5180   305 KGVASAPPATRPvRPPGGARDPGTPRPGQPTERPAGVPEAASDAG--QPPSAYPPAEEAVPGKPLEQGAPRPGSSGG--- 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1456 tatPKLPSPSQDGQPevseaisvsQPQEKEKEPPTPSPRKEAPPAPSPRRilstDIRERAERAQSVTEETLPIPRPRMKP 1535
Cdd:COG5180   380 ---DGAPFQPPNGAP---------QPGLGRRGAPGPPMGAGDLVQAALDG----GGRETASLGGAAGGAGQGPKADFVPG 443


                  ....*..
gi 960139137 1536 SPQRRAV 1542
Cdd:COG5180   444 DAESVSG 450
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 1386-1539 2.42e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1386 DKPEPPPTFMKPR-TMSTSSDTRRPTRVTQSVTdfQRTERPQLPERPIGPLPPKP-TMKPILFPTSETAR-TATATPKLP 1462
Cdd:NF033839  306 EKKEVKPEPETPKpEVKPQLEKPKPEVKPQPEK--PKPEVKPQLETPKPEVKPQPeKPKPEVKPQPEKPKpEVKPQPETP 383

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 960139137 1463 SPSQDGQPEVSEAISVSQPqEKEKEPPTPSPRKEAPPAPSPRRILSTDIRERAERAQSVTEETLPIPRPRMKPSPQR 1539
Cdd:NF033839  384 KPEVKPQPEKPKPEVKPQP-EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET 459
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1422-1541 5.79e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.91  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1422 TERPQLPERPIGPLPPKPTMKPILFPTSETARTATATPKLPSPSQDGQPEVSEAISVSQPQEKEKEPPTPSPRKEAPPAP 1501
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 960139137 1502 SPrrilstdirerAERAQSVTEETLPIPRPRMKPSPQRRA 1541
Cdd:NF040712  298 AP-----------AAPAAPAAPEAEEPARPEPPPAPKPKR 326
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1425-1503 6.82e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 39.39  E-value: 6.82e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960139137   1425 PQLPERPIGPLPPKPTMKPilfptsetarTATATPKLPSPSQdgQPEVSEAISVSQPQEKEKEPPTPSPRKEAPPAPSP 1503
Cdd:smart00818   66 PVVPQQPLMPVPGQHSMTP----------TQHHQPNLPQPAQ--QPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPL 132
 
Name Accession Description Interval E-value
Carm_PH pfam17888
Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain ...
 24-117 1.26e-27

Carmil pleckstrin homology domain; This is a non-canonical pleckstrin homology (PH) domain connected to a 16-leucine-rich repeat domain found in CARMIL (CP Arp2/3 complex myosin-I linker) proteins. The PH domain is interconnected with an N-terminal helix (N-helix), residues 10-20 and a C-terminal linker (Linker), residues 129-147 in Swiss:Q6EDY6. Structural and functional studies indicate that the PH domain involved in direct binding to the PM (plasma membrane) and a HD (helical domain) responsible for antiparallel dimerization and enhancement of CARMIL's membrane-binding activity. Furthermore, it appears that CARMIL's PH domain mediates non-specific binding to the membrane, in contrast to other PH domains that bind polyphosphorylated phosphatidylinositides, which are thought to function as signalling lipids.


Pssm-ID: 436119  Cd Length: 94  Bit Score: 108.14  E-value: 1.26e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137    24 VQFMSLVHLNQGKGRADSRVLVISQWRAHVFYSKQPVKVESSFSYLEIYAITIDSIEQVVIETDRQIYSLGLMSVRDLEA 103
Cdd:pfam17888    1 IKLVKSVKLETKGDKVEDRILVLTPWRLFLLSAKVPTKVERTFHFLEIRAINSRNPNQVIVETDKSNYSLKLASEEDVDH 80

                           90
                   ....*....|....
gi 960139137   104 VVSHVTASLKKIFP 117
Cdd:pfam17888   81 VVGHILTALKKIFP 94
CARMIL_C pfam16000
CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich ...
 783-1139 3.18e-17

CARMIL C-terminus; This domain is found near to the C-terminus of leucine-rich repeat-containing proteins in the CARMIL family. In leucine-rich repeat-containing protein 16A (LRRC16A) it includes the region responsible for interaction with F-actin-capping protein subunit alpha-2 (CAPZA2).


Pssm-ID: 464966 [Multi-domain]  Cd Length: 299  Bit Score: 84.44  E-value: 3.18e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   783 CPRVVQRSSVNEQLADRVAKKTRQAAHFIQNTM-HEAENSIRNKLSELKLSVSVSLVESIINEVHQDLFVAQEKLDKHMR 861
Cdd:pfam16000    5 CPHVMQKAGVRQDLEKALSEKMTLPEEFVKSTLlEQAGVDIFNKLSEVKLSVASFLSDRIVDEVLEALSRSHHKLARHLS 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   862 EfsqsssikanvPQLRVMEHEFPTDDYVPviwRNSFHSRSIRPAPSIKSLLDVEgeqqaraaTHPQQEPEERGGGGGGGV 941
Cdd:pfam16000   85 Q-----------RGRTLLEPESLPDGDRP---ESSPLGPGKRHEGEIERLEELE--------TPMATLKSKRKSIHSRKL 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137   942 PQVSRVGTEERRRAQSLPLATGLSVTTAGQLKPGSPSywrreadaaaapaaaaaalSNREPRRSEPAPPQPPMDLPIEGH 1021
Cdd:pfam16000  143 RPVSVAFSVSELDLDKAPEEVPIHVEDASSGPPLPSS-------------------SPSEPELSASESLDSLSELPTEGQ 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1022 TLRHYTRSRPRPNRRNRQPPSKPQEQAAEiENEANENMGRVDEGVEEFFTKKIIPDDPLKHQREEPlikaqpaeptcvtt 1101
Cdd:pfam16000  204 KLQHLTKGRPKRNKTRAPTRPPGKVGPAQ-DGEQNGLSGRVDEGLEDFFSKKVIKLSTPTSPTSEP-------------- 268

                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 960139137  1102 appttstTTPIPTTAPSKNIKKKFGDFFAFKKVRAGRG 1139
Cdd:pfam16000  269 -------SSSSLFPDSPKKRKKRKSGFFNFIKPRSSKG 299
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 250-613 3.45e-17

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: 86.38  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  250 SLEASGLKMDFAIRMATALRESTasaVHIINLSVNAIEDKGVIALSQSLGKlSCCLSQLHLSKVSMSSKGLGCLVQVLHQ 329
Cdd:COG5238   159 LGLAARLGLLAAISMAKALQNNS---VETVYLGCNQIGDEGIEELAEALTQ-NTTVTTLWLKRNPIGDEGAEILAEALKG 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  330 STflcnTLTHLDLSGNtgCLATEEAMSLYRFLSAPNSVSHLDLSCTDCPLDTLfVSLS--LGCCTTLNYLNLSRNPfslr 407
Cdd:COG5238   235 NK----SLTTLDLSNN--QIGDEGVIALAEALKNNTTVETLYLSGNQIGAEGA-IALAkaLQGNTTLTSLDLSVNR---- 303

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  408 kvrevtrsvrdffskstvlkyVGFSGTklppealRLLLQGLATNTHLSELelDISSCELRSAGAQVIQEHIFEAKAISSL 487
Cdd:COG5238   304 ---------------------IGDEGA-------IALAEGLQGNKTLHTL--NLAYNGIGAQGAIALAKALQENTTLHSL 353

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  488 DLSDNgfesnmvtlilsigrshsikhlsigrnfamksrALTDvlhrlvqliqeeecpleslsvcdsklkTGTTILINSLG 567
Cdd:COG5238   354 DLSDN---------------------------------QIGD---------------------------EGAIALAKYLE 373

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 960139137  568 CNASLSKIDISGNCIGDTGAKMLAKALMMNtKLKTLVWDRNNVTAG 613
Cdd:COG5238   374 GNTTLRELNLGKNNIGKQGAEALIDALQTN-RLHTLILDGNLIGAE 418
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 397-648 7.80e-13

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: 71.62  E-value: 7.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  397 LNLSRNPFSLRKVREVTRSVRDffskstvLKYVGFSGTKLPPEALRLLLQGLATNTHLSELELdiSSCELRSAGAQVIQE 476
Cdd:cd00116     3 LSLKGELLKTERATELLPKLLC-------LQVLRLEGNTLGEEAAKALASALRPQPSLKELCL--SLNETGRIPRGLQSL 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  477 -HIFEAKA-ISSLDLSDNGFESNMVTLILSIGRSHSIKHLSIGRN------FAMKSRALTDVLHRLVQLIQEEeCPLESL 548
Cdd:cd00116    74 lQGLTKGCgLQELDLSDNALGPDGCGVLESLLRSSSLQELKLNNNglgdrgLRLLAKGLKDLPPALEKLVLGR-NRLEGA 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  549 SVCD--------SKLKT-----------GTTILINSLGCNASLSKIDISGNCIGDTGAKMLAKALMMNTKLKTLVWDRNN 609
Cdd:cd00116   153 SCEAlakalranRDLKElnlanngigdaGIRALAEGLKANCNLEVLDLNNNGLTDEGASALAETLASLKSLEVLNLGDNN 232

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 960139137  610 VTAGGFMDVANALE------KNLTLQNISIPMSDVLQAHRSAPEK 648
Cdd:cd00116   233 LTDAGAAALASALLspnislLTLSLSCNDITDDGAKDLAEVLAEK 277
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 420-631 6.22e-11

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: 66.74  E-value: 6.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  420 FSKSTVLKYVGFSGTKLPPEALRLLLQGLATNTHLSELELdiSSCELRSAGAQVIQEHIFEAKAISSLDLSDNGF-ESNM 498
Cdd:COG5238   176 ALQNNSVETVYLGCNQIGDEGIEELAEALTQNTTVTTLWL--KRNPIGDEGAEILAEALKGNKSLTTLDLSNNQIgDEGV 253

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  499 VTLILSIGRSHSIKHLSIGRNF--AMKSRALTDVLHRLVQLiqeeecplESLSVCDSKLK-TGTTILINSLGCNASLSKI 575
Cdd:COG5238   254 IALAEALKNNTTVETLYLSGNQigAEGAIALAKALQGNTTL--------TSLDLSVNRIGdEGAIALAEGLQGNKTLHTL 325

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 960139137  576 DISGNCIGDTGAKMLAKALMMNTKLKTLVWDRNNVTAGGFMDVANALEKNLTLQNI 631
Cdd:COG5238   326 NLAYNGIGAQGAIALAKALQENTTLHSLDLSDNQIGDEGAIALAKYLEGNTTLREL 381
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 424-628 6.67e-11

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: 66.35  E-value: 6.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  424 TVLKYVGFSGTKLPPEALRLLLQGLATNTHLSELeLDISSCELRSAGAQVIQEHIFEAKAISSLDLSDNGF-ESNMVTLI 502
Cdd:COG5238   151 LGGNAVHLLGLAARLGLLAAISMAKALQNNSVET-VYLGCNQIGDEGIEELAEALTQNTTVTTLWLKRNPIgDEGAEILA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  503 LSIGRSHSIKHLSIGRNfamksrALTDvlhrlvqliqeeecpleslsvcdsklkTGTTILINSLGCNASLSKIDISGNCI 582
Cdd:COG5238   230 EALKGNKSLTTLDLSNN------QIGD---------------------------EGVIALAEALKNNTTVETLYLSGNQI 276

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 960139137  583 GDTGAKMLAKALMMNTKLKTLVWDRNNVTAGGFMDVANALEKNLTL 628
Cdd:COG5238   277 GAEGAIALAKALQGNTTLTSLDLSVNRIGDEGAIALAEGLQGNKTL 322
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
337-633 1.06e-10

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 65.73  E-value: 1.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  337 LTHLDLSGNTGclateeamslyrfLSAPNSVSHLDLSctDCPLDTLFVSLslGCCTTLNYLNLSRNPFSlrkvrevtrSV 416
Cdd:COG4886    98 LTELDLSGNEE-------------LSNLTNLESLDLS--GNQLTDLPEEL--ANLTNLKELDLSNNQLT---------DL 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  417 RDFFSKSTVLKYVGFSGTK---LPPEALRLllqglatnTHLSELelDISSCELRSagaqvIQEHIFEAKAISSLDLSDNG 493
Cdd:COG4886   152 PEPLGNLTNLKSLDLSNNQltdLPEELGNL--------TNLKEL--DLSNNQITD-----LPEPLGNLTNLEELDLSGNQ 216

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  494 FESnmvtLILSIGRSHSIKHLSIGRNfamksrALTDvLHRLVQLIQeeecpLESLSVCDSKLKTgttilINSLGCNASLS 573
Cdd:COG4886   217 LTD----LPEPLANLTNLETLDLSNN------QLTD-LPELGNLTN-----LEELDLSNNQLTD-----LPPLANLTNLK 275

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960139137  574 KIDISGNCIGDTGAKMLA--KALMMNTKLKTLVWDRNNVTAGGFMDVANALEKNLTLQNISI 633
Cdd:COG4886   276 TLDLSNNQLTDLKLKELEllLGLNSLLLLLLLLNLLELLILLLLLTTLLLLLLLLKGLLVTL 337
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1224-1663 8.72e-08

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 57.64  E-value: 8.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1224 DKMSPRAPSPVPTPALTPPASTPTPPASSPSKTEEVPALSPAAPPTKTPSPVPVVSPS---EREKSRTLEK--------S 1292
Cdd:PHA03247 2620 DTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASsppQRPRRRAARPtvgsltslA 2699

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1293 RTPDGERRPKPIRRSL------------REGKSQSLILLSDVLPEQDGTAMHAKKHASESSSSFEQRLHVMLHRMGVTKT 1360
Cdd:PHA03247 2700 DPPPPPPTPEPAPHALvsatplppgpaaARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGP 2779

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1361 SPTDTKQSQSKDEELRKA---NSEGAILDKPEPPPTFMKPRTMSTSSDTRRPTRVTqsvtdfqrterPQLPERPIGPLPP 1437
Cdd:PHA03247 2780 PRRLTRPAVASLSESRESlpsPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQ-----------PTAPPPPPGPPPP 2848

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1438 KPTMKPILFPTSETARTATATPKLPSPSQDGQPEVSE--AISVSQPQEKEKEPPTPSPRKEAPPAPSPRRilstdIRERA 1515
Cdd:PHA03247 2849 SLPLGGSVAPGGDVRRRPPSRSPAAKPAAPARPPVRRlaRPAVSRSTESFALPPDQPERPPQPQAPPPPQ-----PQPQP 2923

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1516 ERAQSVTEETLPIPRPRMKPSPQRRAVSVHEDSLLQHAAMLDP-EELKAALPRRQKSPGRKKGNVGELTTCSedlPEGEP 1594
Cdd:PHA03247 2924 PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGAlVPGRVAVPRFRVPQPAPSREAPASSTPP---LTGHS 3000

                         410       420       430       440       450       460       470
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960139137 1595 VK--SAGKDSTGQVEETDSTTVTDSQSEQSPTGSSEqvtnQERDESVVSEEHTTQGETSDQRTESP-SPEKH 1663
Cdd:PHA03247 3001 LSrvSSWASSLALHEETDPPPVSLKQTLWPPDDTED----SDADSLFDSDSERSDLEALDPLPPEPhDPFAH 3068
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 280-623 1.25e-07

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: 55.44  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  280 NLSVNAIEDKG-VIALSQSLgkLSCCLSQLHLSkvsMSSKGLGCLVQVLHQstflCNTLTHLDLSGNtgCLATEEAMSLY 358
Cdd:cd00116    34 TLGEEAAKALAsALRPQPSL--KELCLSLNETG---RIPRGLQSLLQGLTK----GCGLQELDLSDN--ALGPDGCGVLE 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  359 RFLSAPnSVSHLDLscTDCPLDTL---FVSLSLG-CCTTLNYLNLSRNpfslRKVREVTRSVRDFFSKSTVLKYVGFSGT 434
Cdd:cd00116   103 SLLRSS-SLQELKL--NNNGLGDRglrLLAKGLKdLPPALEKLVLGRN----RLEGASCEALAKALRANRDLKELNLANN 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  435 KLPPEALRLLLQGLATNTHLSELelDISSCELRSAGAQVIQEHIFEAKAISSLDLSDNGfesnmvtlilsigrshsikhl 514
Cdd:cd00116   176 GIGDAGIRALAEGLKANCNLEVL--DLNNNGLTDEGASALAETLASLKSLEVLNLGDNN--------------------- 232

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  515 sigrnfamksraLTDVlhrlvqliqeeecpleslsvCDSKLKTGttilinSLGCNASLSKIDISGNCIGDTGAKMLAKAL 594
Cdd:cd00116   233 ------------LTDA--------------------GAAALASA------LLSPNISLLTLSLSCNDITDDGAKDLAEVL 274

                         330       340
                  ....*....|....*....|....*....
gi 960139137  595 MMNTKLKTLVWDRNNVTAGGFMDVANALE 623
Cdd:cd00116   275 AEKESLLELDLRGNKFGEEGAQLLAESLL 303
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
392-611 3.63e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 54.55  E-value: 3.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  392 TTLNYLNLSRNPFSLRKVREVTRSVRDFFSKSTVLKYVGFSGTKLPPEALRLLLQGLATNTHLSELE-LDISSCELRSag 470
Cdd:COG4886    50 TLLLSLLLRDLLLSSLLLLLSLLLLLLLSLLLLSLLLLGLTDLGDLTNLTELDLSGNEELSNLTNLEsLDLSGNQLTD-- 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  471 aqvIQEHIFEAKAISSLDLSDNGFESnmvtLILSIGRSHSIKHLSIGRNfamksrALTDVLHRLVQLIQeeecpLESLSV 550
Cdd:COG4886   128 ---LPEELANLTNLKELDLSNNQLTD----LPEPLGNLTNLKSLDLSNN------QLTDLPEELGNLTN-----LKELDL 189

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 960139137  551 CDSKLKTgttiLINSLGCNASLSKIDISGNCIGDtgakmLAKALMMNTKLKTLVWDRNNVT 611
Cdd:COG4886   190 SNNQITD----LPEPLGNLTNLEELDLSGNQLTD-----LPEPLANLTNLETLDLSNNQLT 241
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1356-1572 6.00e-07

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 54.39  E-value: 6.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1356 GVTKTSPTDTKQSQSKDEELRKAnSEGAILDKPEPPPTFMKPRTMSTSsDTRRPTRVTQSVTDFQRTERPQLPERPIGPL 1435
Cdd:pfam03154   43 GRNSPSAASTSSNDSKAESMKKS-SKKIKEEAPSPLKSAKRQREKGAS-DTEEPERATAKKSKTQEISRPNSPSEGEGES 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1436 PPKPTMKPILF--PTSETARTATATPKLPSPsQDGQpevSEAISVSQPQEKEKEPPTPSPRKEAPPAPSPRRILSTDIRE 1513
Cdd:pfam03154  121 SDGRSVNDEGSsdPKDIDQDNRSTSPSIPSP-QDNE---SDSDSSAQQQILQTQPPVLQAQSGAASPPSPPPPGTTQAAT 196

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 960139137  1514 RAERAQSVTEETLPIPRPRMKPSPQRRAVSVHedSLLQHAAMLDPEELKAALPRRQKSP 1572
Cdd:pfam03154  197 AGPTPSAPSVPPQGSPATSQPPNQTQSTAAPH--TLIQQTPTLHPQRLPSPHPPLQPMT 253
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1217-1554 6.78e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 54.56  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1217 DSTAVIQDKMSPRAPSPVPTPALTPPASTPTPPASSPSKTEEVPA--LSPAAPPTKTPSPvpvvspsereksrtleksrT 1294
Cdd:PHA03247 2690 PTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPAlpAAPAPPAVPAGPA-------------------T 2750

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1295 PDGERRPKpiRRSLREGKSQSLILLSDVLPEQDGTAMHAKKHASESSSSFEQRLHVMLHRMGVTKTSPT-DTKQSQSKDE 1373
Cdd:PHA03247 2751 PGGPARPA--RPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAAlPPAASPAGPL 2828

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1374 ELRKANSEGAILDKPEPPPTFMKPR-TMSTSSDTRR--PTRVTQSVTdfqrTERPQLPERPIGPLPPKPTMKPILFPTSE 1450
Cdd:PHA03247 2829 PPPTSAQPTAPPPPPGPPPPSLPLGgSVAPGGDVRRrpPSRSPAAKP----AAPARPPVRRLARPAVSRSTESFALPPDQ 2904

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1451 TARTATatPKLPSPSQDGQPEvseaisvsQPQEKEKEPPTPSPRKEAPPAPSPRRILSTDIRERAERAQ--SVTEETLPI 1528
Cdd:PHA03247 2905 PERPPQ--PQAPPPPQPQPQP--------PPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWlgALVPGRVAV 2974

                         330       340
                  ....*....|....*....|....*..
gi 960139137 1529 PRPRM-KPSPQRRAVSVHEDSLLQHAA 1554
Cdd:PHA03247 2975 PRFRVpQPAPSREAPASSTPPLTGHSL 3001
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
278-506 8.00e-07

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 53.40  E-value: 8.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  278 IINLSVNAIEDkgviaLSQSLGKLSCcLSQLHLS--KVSMSSKGLGCLVQvlhqstflcntLTHLDLSGNtgclateeam 355
Cdd:COG4886   117 SLDLSGNQLTD-----LPEELANLTN-LKELDLSnnQLTDLPEPLGNLTN-----------LKSLDLSNN---------- 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  356 slyRFLSAPNSVSHLD----LSCTDCPLDTLfvSLSLGCCTTLNYLNLSRNPFSlrkvrevtrSVRDFFSKSTVLKYVGF 431
Cdd:COG4886   170 ---QLTDLPEELGNLTnlkeLDLSNNQITDL--PEPLGNLTNLEELDLSGNQLT---------DLPEPLANLTNLETLDL 235

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 960139137  432 SGTKLPPealrllLQGLATNTHLSelELDISSCELRSAGaqviqeHIFEAKAISSLDLSDNGFESNMVTLILSIG 506
Cdd:COG4886   236 SNNQLTD------LPELGNLTNLE--ELDLSNNQLTDLP------PLANLTNLKTLDLSNNQLTDLKLKELELLL 296
LRR COG4886
Leucine-rich repeat (LRR) protein [Transcription];
363-611 3.14e-06

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


Pssm-ID: 443914 [Multi-domain]  Cd Length: 414  Bit Score: 51.47  E-value: 3.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  363 APNSVSHLDLSCTDCPLDTLFVSLSLGCCTTLNYLNLSRNPFSLRKVREVTRSVRDFFSKSTVLKYVGFSGTKLPPEALR 442
Cdd:COG4886     1 LLLLLLSLTLKLLLLLLLELLTTLILLLLLLLLLLALLLLSLLSLLLLLTLLLSLLLRDLLLSSLLLLLSLLLLLLLSLL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  443 LLLQGLATNTHLSEL----ELDISSCElrsagaqviqeHIFEAKAISSLDLSDNGFESnmvtLILSIGRSHSIKHLSIGR 518
Cdd:COG4886    81 LLSLLLLGLTDLGDLtnltELDLSGNE-----------ELSNLTNLESLDLSGNQLTD----LPEELANLTNLKELDLSN 145

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  519 NfamksrALTDVLHRLVQLIQeeecpLESLSVCDSKLKTgttiLINSLGCNASLSKIDISGNCIGDtgakmLAKALMMNT 598
Cdd:COG4886   146 N------QLTDLPEPLGNLTN-----LKSLDLSNNQLTD----LPEELGNLTNLKELDLSNNQITD-----LPEPLGNLT 205

                         250
                  ....*....|...
gi 960139137  599 KLKTLVWDRNNVT 611
Cdd:COG4886   206 NLEELDLSGNQLT 218
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 1364-1626 1.58e-05

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 50.07  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1364 DTKQSQSKDEELR-KANSEGAILDKPEPP--------PTFMK-PRTMSTSSDTRRPTRVTQSvtdfQRTERPQLPERPig 1433
Cdd:PTZ00449  536 DSKESDEPKEGGKpGETKEGEVGKKPGPAkehkpskiPTLSKkPEFPKDPKHPKDPEEPKKP----KRPRSAQRPTRP-- 609

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1434 PLPPKPTMKPIlfPTSETARTATATPKLP----SPSQDGQPEVSEAISVSQPQEKEKEPPTPSPRKE-----APPAPSPR 1504
Cdd:PTZ00449  610 KSPKLPELLDI--PKSPKRPESPKSPKRPpppqRPSSPERPEGPKIIKSPKPPKSPKPPFDPKFKEKfyddyLDAAAKSK 687

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1505 RILSTDIREraERAQSVTEETLP----IPRPRMKPSPQRRAvsvhEDSLLQHAAMLDPEELKAALPRRQKSPGRKKGNVG 1580
Cdd:PTZ00449  688 ETKTTVVLD--ESFESILKETLPetpgTPFTTPRPLPPKLP----RDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFH 761

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 960139137 1581 ElTTCSEDLPE--GEPVKSAGKDS-TGQVEETDSTTVTDSQSEQSPTGS 1626
Cdd:PTZ00449  762 E-TPADTPLPDilAEEFKEEDIHAeTGEPDEAMKRPDSPSEHEDKPPGD 809
RNA1 COG5238
Ran GTPase-activating protein (RanGAP) involved in mRNA processing and transport [Translation, ...
 513-638 2.78e-05

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: 48.63  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  513 HLSIGRNFAMKSRALTDVLHRLVQLiqeeecPLESLSVCDSKLKTGTTILINSLGCNASLSKIDISGNCIGDTGAKMLAK 592
Cdd:COG5238   129 DSLILYLALPRRINLIQVLKDPLGG------NAVHLLGLAARLGLLAAISMAKALQNNSVETVYLGCNQIGDEGIEELAE 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 960139137  593 ALMMNTKLKTLVWDRNNVTAGGFMDVANALEKNLTLQNISIPMSDV 638
Cdd:COG5238   203 ALTQNTTVTTLWLKRNPIGDEGAEILAEALKGNKSLTTLDLSNNQI 248
Granin pfam01271
Granin (chromogranin or secretogranin);
1455-1662 6.13e-05

Granin (chromogranin or secretogranin);


Pssm-ID: 279595 [Multi-domain]  Cd Length: 584  Bit Score: 47.72  E-value: 6.13e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1455 ATATPKLPSPSQDGQPEVSEAISVSQPQEKEKEPPTpSPRKEAPPAPSPRRILSTDIRERAERAQSVTEETLPIPRPRMK 1534
Cdd:pfam01271   67 QSEASHLSSRSRDGLSDEDMQIITEALRQAENEPGG-HSRENQPYALQVEKEFKTDHSDDYETQQWEEEKLKHMRFPLRY 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1535 PSPQRRAVSVHEDSLlqhaamldPEELKAalPRRQKSPGRKKGNVGELTTCSEDLPEgePVKSAGKDSTGQVEETDSTTV 1614
Cdd:pfam01271  146 EENSEEKHSEREGEL--------SEVFEN--PRSQATLKKVFEEVSRLDTPSKQKRE--KSDEREKSSQESGEDTYRQEN 213

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*...
gi 960139137  1615 TDSQSEQSPTGSSEQvtnQERDESVVSEEHTTQGETSDQRTESPSPEK 1662
Cdd:pfam01271  214 IPQEDQVGPEDQEPS---EEGEEDATQEEVKRSRPRTHHGRSLPDESS 258
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 1385-1515 1.15e-04

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 46.70  E-value: 1.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1385 LDKPEPPPTFMKPRTMSTSSDTRRPTRVTQSV-TDFQRTERPQLPerpigplppKPTMKPILFPTSETARTATATPKLPS 1463
Cdd:pfam13254  208 LMRSPAPGGHSKSPSVSGISADSSPTKEEPSEeADTLSTDKEQSP---------APTSASEPPPKTKELPKDSEEPAAPS 278

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 960139137  1464 PSQDGQPEVSEAISVSQPQEKEKE------PPTPSPRKEAPPAPSPRRILSTDIRERA 1515
Cdd:pfam13254  279 KSAEASTEKKEPDTESSPETSSEKsapsllSPVSKASIDKPLSSPDRDPLSPKPKPQS 336
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 1290-1539 1.70e-04

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 46.30  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1290 EKSRTPDGERRPKPirrsLREGKSQSLillSDVLPEQDGTAMHAKKHASESSSSFEQR-LHVMLHRMGVTKTSPTDTKQS 1368
Cdd:NF033839  170 QKPTTPAPDTKPSP----QPEGKKPSV---PDINQEKEKAKLAVATYMSKILDDIQKHhLQKEKHRQIVALIKELDELKK 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1369 QSKDE------ELRKANSEGAILDKPEPPPT-FMKPRTMSTSSDTRRPTRVTQSvTDFQRTERPQLPERPIGPLPPKPTM 1441
Cdd:NF033839  243 QALSEidnvntKVEIENTVHKIFADMDAVVTkFKKGLTQDTPKEPGNKKPSAPK-PGMQPSPQPEKKEVKPEPETPKPEV 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1442 KPIL-------FPTSETAR-TATATPKLPSPSQDGQPEVSEAISVSQPQEKEKE----PPTPSPR-KEAPPAPSPrrils 1508
Cdd:NF033839  322 KPQLekpkpevKPQPEKPKpEVKPQLETPKPEVKPQPEKPKPEVKPQPEKPKPEvkpqPETPKPEvKPQPEKPKP----- 396

                         250       260       270
                  ....*....|....*....|....*....|.
gi 960139137 1509 tDIRERAERAQSVTEETLPIPRPRMKPSPQR 1539
Cdd:NF033839  397 -EVKPQPEKPKPEVKPQPEKPKPEVKPQPEK 426
LRR_RI cd00116
Leucine-rich repeats (LRRs), ribonuclease inhibitor (RI)-like subfamily. LRRs are 20-29 ...
 198-466 2.16e-04

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: 45.42  E-value: 2.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  198 SHLDSRDLALAVGALSFNQWFTKICS-KDFKLSPD-VQEQVLYMIARS-----SALEEVSLEASGLKMDFAIRMATALRE 270
Cdd:cd00116    84 QELDLSDNALGPDGCGVLESLLRSSSlQELKLNNNgLGDRGLRLLAKGlkdlpPALEKLVLGRNRLEGASCEALAKALRA 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  271 STAsaVHIINLSVNAIEDKGVIALSQSLgKLSCCLSQLHLSKvsmsskglgclvqvlhqstflcNTLTHldlsgnTGCLA 350
Cdd:cd00116   164 NRD--LKELNLANNGIGDAGIRALAEGL-KANCNLEVLDLNN----------------------NGLTD------EGASA 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  351 TEEAmslyrfLSAPNSVSHLDLSctDCPLDTL----FVSLSLGCCTTLNYLNLSRNPFSLRKVREVTRSVRDFFSkstvL 426
Cdd:cd00116   213 LAET------LASLKSLEVLNLG--DNNLTDAgaaaLASALLSPNISLLTLSLSCNDITDDGAKDLAEVLAEKES----L 280

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 960139137  427 KYVGFSGTKLPPEALRLLLQGLATNTHlSELELDISSCEL 466
Cdd:cd00116   281 LELDLRGNKFGEEGAQLLAESLLEPGN-ELESLWVKDDSF 319
PRK14950 PRK14950
DNA polymerase III subunits gamma and tau; Provisional
 1440-1566 2.76e-04

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237864 [Multi-domain]  Cd Length: 585  Bit Score: 45.57  E-value: 2.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1440 TMKPILFPTSETARTATATPKLPSPSQDGQPEVSEAISVSQ--PQEKEKEPPTPSPRKEAPPAPSPRRILSTDIREraer 1517
Cdd:PRK14950  359 LLVPVPAPQPAKPTAAAPSPVRPTPAPSTRPKAAAAANIPPkePVRETATPPPVPPRPVAPPVPHTPESAPKLTRA---- 434

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 960139137 1518 aqSVTEETLPIPRPRMKPSPQRRAVSVHEDSLlqhaamldpEELKAALP 1566
Cdd:PRK14950  435 --AIPVDEKPKYTPPAPPKEEEKALIADGDVL---------EQLEAIWK 472
PHA03378 PHA03378
EBNA-3B; Provisional
 1388-1504 3.19e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 45.44  E-value: 3.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1388 PEPPPTFMKPRTMStssdtrrPTRVTQSVTDFQRTERPQLPERPIGPLPPKPTMKPILFPTSETARTATATPKLPSPSQd 1467
Cdd:PHA03378  707 PAAPPGRAQRPAAA-------TGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQP- 778

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 960139137 1468 gQPEVSEAisvsqPQEKEKEPPTPSPRKEAPPAP---SPR 1504
Cdd:PHA03378  779 -PPQAPPA-----PQQRPRGAPTPQPPPQAGPTSmqlMPR 812
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 1383-1557 3.65e-04

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 45.46  E-value: 3.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1383 AILDKPEPPPTFMkPRTMSTSSDTRRPTRVTQSVTDFQRTERPQLPERPIGPLPPKPTMKPILFPTSetartatATPKLP 1462
Cdd:PRK10263  734 ALLDDGPHEPLFT-PIVEPVQQPQQPVAPQQQYQQPQQPVAPQPQYQQPQQPVAPQPQYQQPQQPVA-------PQPQYQ 805

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1463 SPSQDGQPEVseaiSVSQPQEKEKEPPtPSPRKEAPPAPSPRRILSTDIRERAERAQSVTEETLPIPRPRMKPSPQRRAV 1542
Cdd:PRK10263  806 QPQQPVAPQP----QYQQPQQPVAPQP-QYQQPQQPVAPQPQDTLLHPLLMRNGDSRPLHKPTTPLPSLDLLTPPPSEVE 880

                         170
                  ....*....|....*
gi 960139137 1543 SVHEDSLLQHAAMLD 1557
Cdd:PRK10263  881 PVDTFALEQMARLVE 895
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
 1452-1549 4.61e-04

SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 (BAC70047.1) whose C-terminal region suggests restriction enzyme activity (PMID: 18456708), and with other proteins with unrelated C-terminal regions. A member protein was also identified in a kanamycin biosynthetic gene cluster (PMID:16766657), while N-terminal regions of two other member proteins were named Trypco1 in a bioinformatic study (PMID:32101166) of predicted bacterial conflict systems.


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 44.61  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1452 ARTATATPKLPSPSQDGQPEVSeAISVSQPQEKEKEPPTPSPRKEAPPAPSPRRILSTDIRERaERAQSVTEETLPI--P 1529
Cdd:NF041121   17 RAAAPPSPEGPAPTAASQPATP-PPPAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPPPPPPP-GPAGAAPGAALPVrvP 94

                          90       100       110
                  ....*....|....*....|....*....|
gi 960139137 1530 RPRMKPSP----------QRRAVSVHEDSL 1549
Cdd:NF041121   95 APPALPNPlelaralrplKRRVPSPRRVEL 124
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1223-1594 6.96e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1223 QDKMSPRAPSPVPTPALTPPASTPTPPASSPSKTEEVPALSPAAPPTKTPSPVPVVSPSEREKSRTLEKSRTPDGERRPK 1302
Cdd:PHA03307   82 NESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1303 PirRSLREGKSQSLILLSdvLPEQDGTAMHAKKHASESSSSFEQRLHVMlHRMGVTKTSPTDTKQSQSKDEELRKANSEG 1382
Cdd:PHA03307  162 V--ASDAASSRQAALPLS--SPEETARAPSSPPAEPPPSTPPAAASPRP-PRRSSPISASASSPAPAPGRSAADDAGASS 236

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1383 AILDKPEPPPTFMKPRTM---STSSDTRRPTRVTQSVTDFQRTERPQLPERPIGPLPPKPTMKPILFPTSETARTATATP 1459
Cdd:PHA03307  237 SDSSSSESSGCGWGPENEcplPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASS 316

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1460 KLPSPSQDG------QPEVSEAISVSQPQEkEKEPPTPSPRKEAPPAPSPRRilstdiRERAERAQSVTeetlPIPRPRm 1533
Cdd:PHA03307  317 SSSSSRESSssstssSSESSRGAAVSPGPS-PSRSPSPSRPPPPADPSSPRK------RPRPSRAPSSP----AASAGR- 384

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 960139137 1534 kPSPQRRAVSVHEDSLLQHAamldPEELKAALPRRqkSPGRKKGNVGELTTCSEDL-PEGEP 1594
Cdd:PHA03307  385 -PTRRRARAAVAGRARRRDA----TGRFPAGRPRP--SPLDAGAASGAFYARYPLLtPSGEP 439
DUF4045 pfam13254
Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. ...
 1385-1576 7.87e-04

Domain of unknown function (DUF4045); This presumed domain is functionally uncharacterized. This domain family is found in bacteria and eukaryotes, and is typically between 384 and 430 amino acids in length.


Pssm-ID: 433066 [Multi-domain]  Cd Length: 415  Bit Score: 44.00  E-value: 7.87e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1385 LDKPEPPPTFMKPRTMSTSSDTRRPTRVTQSVT--DFQRTERPQ--LPERPIGPLPPKPTMKPilfpTSETARTATATPK 1460
Cdd:pfam13254  158 LNRPESPKPKAQPSQPAQPAWMKELNKIRQSRAsvDLGRPNSFKevTPVGLMRSPAPGGHSKS----PSVSGISADSSPT 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1461 LPSPSQDGQPEVSE------AISVSQPQEKEKEPPTPSprkEAPPAPSPRRILSTDIRERAERAQSVTEETLPIPR---P 1531
Cdd:pfam13254  234 KEEPSEEADTLSTDkeqspaPTSASEPPPKTKELPKDS---EEPAAPSKSAEASTEKKEPDTESSPETSSEKSAPSllsP 310

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 960139137  1532 RMKPSPQRRAVSVHEDSLLQHAAMLDP-EELKAALPRRQKSPGRKK 1576
Cdd:pfam13254  311 VSKASIDKPLSSPDRDPLSPKPKPQSPpKDFRANLRSREVPKDKSK 356
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1386-1623 9.73e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 44.16  E-value: 9.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1386 DKPEPPPTfMKPRTMSTSSDTRRPTrvtqsvtdfqrterPQLPERPIGPLPPKPTMKPILFPTSETARtataTPKLPSPS 1465
Cdd:PHA03247 2547 DAGDPPPP-LPPAAPPAAPDRSVPP--------------PRPAPRPSEPAVTSRARRPDAPPQSARPR----APVDDRGD 2607

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1466 QDGQPEVSEAisvsqpqekekePPTPSPRKEAPPAPSPRrilstdireRAERAQSVTEETLPIPRPRMKPSPQRraVSVH 1545
Cdd:PHA03247 2608 PRGPAPPSPL------------PPDTHAPDPPPPSPSPA---------ANEPDPHPPPTVPPPERPRDDPAPGR--VSRP 2664

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 960139137 1546 edsllQHAAMLDPEELKAALPRRQKSPGRKKgNVGELTTCSEDLPEGEPVKSAgkdSTGQVEETDSTTVTDSQSEQSP 1623
Cdd:PHA03247 2665 -----RRARRLGRAAQASSPPQRPRRRAARP-TVGSLTSLADPPPPPPTPEPA---PHALVSATPLPPGPAAARQASP 2733
PRK14960 PRK14960
DNA polymerase III subunit gamma/tau;
1424-1612 1.10e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237868 [Multi-domain]  Cd Length: 702  Bit Score: 43.88  E-value: 1.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1424 RPQLPERPIGPLPPKPTMKPI--LFPTSETARTATATPKLPSPSQDGQPEVSEAISVSQPQEKEKEPPTPSPRKEAPPAP 1501
Cdd:PRK14960  359 RPLAPNEILVSEPVQQNGQAEvgLNSQAQTAQEITPVSAVQPVEVISQPAMVEPEPEPEPEPEPEPEPEPEPEPEPEPEP 438

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1502 SPRRILSTDI-------RERAERAQSVTEETLPIPRPRMKPSPQRRAVSVHEDSllqHAAMLDPEELKAALPRRQKSPGR 1574
Cdd:PRK14960  439 EPEPQPNQDLmvfdpnhHELIGLESAVVQETVSVLEEDFIPVPEQKLVQVQAET---QVKQIEPEPASTAEPIGLFEASS 515

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 960139137 1575 KKGNVGELTTC----SEDLPEGEPVKSAGKDST-GQVEETDST 1612
Cdd:PRK14960  516 AEFSLAQDTSAydlvSEPVIEQQSLVQAEIVETvAVVKEPNAT 558
LRR_RI smart00368
Leucine rich repeat, ribonuclease inhibitor type;
569-594 1.30e-03

Leucine rich repeat, ribonuclease inhibitor type;


Pssm-ID: 197686 [Multi-domain]  Cd Length: 28  Bit Score: 37.77  E-value: 1.30e-03
                            10        20
                    ....*....|....*....|....*.
gi 960139137    569 NASLSKIDISGNCIGDTGAKMLAKAL 594
Cdd:smart00368    1 NPSLRELDLSNNKLGDEGARALAEAL 26
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
 1377-1542 1.57e-03

PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification];


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 43.13  E-value: 1.57e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1377 KANSEGAILDKP-EPPPTFMKPRTMSTSSDTRRPTRVTQSVTDFQrtERPQLPERPIGPLPPKPTMKPILFPTSETArta 1455
Cdd:COG5180   305 KGVASAPPATRPvRPPGGARDPGTPRPGQPTERPAGVPEAASDAG--QPPSAYPPAEEAVPGKPLEQGAPRPGSSGG--- 379

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1456 tatPKLPSPSQDGQPevseaisvsQPQEKEKEPPTPSPRKEAPPAPSPRRilstDIRERAERAQSVTEETLPIPRPRMKP 1535
Cdd:COG5180   380 ---DGAPFQPPNGAP---------QPGLGRRGAPGPPMGAGDLVQAALDG----GGRETASLGGAAGGAGQGPKADFVPG 443


                  ....*..
gi 960139137 1536 SPQRRAV 1542
Cdd:COG5180   444 DAESVSG 450
Atrophin-1 pfam03154
Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian ...
 1388-1504 1.77e-03

Atrophin-1 family; Atrophin-1 is the protein product of the dentatorubral-pallidoluysian atrophy (DRPLA) gene. DRPLA OMIM:125370 is a progressive neurodegenerative disorder. It is caused by the expansion of a CAG repeat in the DRPLA gene on chromosome 12p. This results in an extended polyglutamine region in atrophin-1, that is thought to confer toxicity to the protein, possibly through altering its interactions with other proteins. The expansion of a CAG repeat is also the underlying defect in six other neurodegenerative disorders, including Huntington's disease. One interaction of expanded polyglutamine repeats that is thought to be pathogenic is that with the short glutamine repeat in the transcriptional coactivator CREB binding protein, CBP. This interaction draws CBP away from its usual nuclear location to the expanded polyglutamine repeat protein aggregates that are characteriztic of the polyglutamine neurodegenerative disorders. This interferes with CBP-mediated transcription and causes cytotoxicity.


Pssm-ID: 460830 [Multi-domain]  Cd Length: 991  Bit Score: 43.22  E-value: 1.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137  1388 PEPPPTFMKPRTMSTSSDTRRPTRVTQSVTdfqrtERPQLPERPIGPLPPKPTMKPILFPTSETARTATATPKLPSPSQD 1467
Cdd:pfam03154  428 PAQPPVLTQSQSLPPPAASHPPTSGLHQVP-----SQSPFPQHPFVPGGPPPITPPSGPPTSTSSAMPGIQPPSSASVSS 502

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 960139137  1468 GQPEVSEAISVSQPQEKEKEPPTPSPRKEAPPaPSPR 1504
Cdd:pfam03154  503 SGPVPAAVSCPLPPVQIKEEALDEAEEPESPP-PPPR 538
PspC_subgroup_2 NF033839
pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, ...
 1386-1539 2.42e-03

pneumococcal surface protein PspC, LPXTG-anchored form; The pneumococcal surface protein PspC, as described in Streptococcus pneumoniae, is a repetitive and highly variable protein, recognized by a conserved N-terminal domain and also by genomic location. This form, subgroup 2, is anchored covalently after cleavage by sortase at a C-terminal LPXTG site. The other form, subgroup 1, has variable numbers of a choline-binding repeat in the C-terminal region, and is also known as choline-binding protein A.


Pssm-ID: 468202 [Multi-domain]  Cd Length: 557  Bit Score: 42.45  E-value: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1386 DKPEPPPTFMKPR-TMSTSSDTRRPTRVTQSVTdfQRTERPQLPERPIGPLPPKP-TMKPILFPTSETAR-TATATPKLP 1462
Cdd:NF033839  306 EKKEVKPEPETPKpEVKPQLEKPKPEVKPQPEK--PKPEVKPQLETPKPEVKPQPeKPKPEVKPQPEKPKpEVKPQPETP 383

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 960139137 1463 SPSQDGQPEVSEAISVSQPqEKEKEPPTPSPRKEAPPAPSPRRILSTDIRERAERAQSVTEETLPIPRPRMKPSPQR 1539
Cdd:NF033839  384 KPEVKPQPEKPKPEVKPQP-EKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPEKPKPEVKPQPET 459
SepH NF040712
septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces ...
 1422-1541 5.79e-03

septation protein SepH; Septation protein H (SepH) was firstly characterized in Streptomyces venezuelae, and homologs were identified in Mycobacterium smegmatis. SepH contains a N-terminal DUF3071 domain and a conserved C-terminal region. It binds directly to cell division protein FtsZ to stimulate the assembly of FtsZ protofilaments.


Pssm-ID: 468676 [Multi-domain]  Cd Length: 346  Bit Score: 40.91  E-value: 5.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 960139137 1422 TERPQLPERPIGPLPPKPTMKPILFPTSETARTATATPKLPSPSQDGQPEVSEAISVSQPQEKEKEPPTPSPRKEAPPAP 1501
Cdd:NF040712  218 EPAPAAEGAPATDSDPAEAGTPDDLASARRRRAGVEQPEDEPVGPGAAPAAEPDEATRDAGEPPAPGAAETPEAAEPPAP 297

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 960139137 1502 SPrrilstdirerAERAQSVTEETLPIPRPRMKPSPQRRA 1541
Cdd:NF040712  298 AP-----------AAPAAPAAPEAEEPARPEPPPAPKPKR 326
Amelogenin smart00818
Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem ...
 1425-1503 6.82e-03

Amelogenins, cell adhesion proteins, play a role in the biomineralisation of teeth; They seem to regulate formation of crystallites during the secretory stage of tooth enamel development and are thought to play a major role in the structural organisation and mineralisation of developing enamel. The extracellular matrix of the developing enamel comprises two major classes of protein: the hydrophobic amelogenins and the acidic enamelins. Circular dichroism studies of porcine amelogenin have shown that the protein consists of 3 discrete folding units: the N-terminal region appears to contain beta-strand structures, while the C-terminal region displays characteristics of a random coil conformation. Subsequent studies on the bovine protein have indicated the amelogenin structure to contain a repetitive beta-turn segment and a "beta-spiral" between Gln112 and Leu138, which sequester a (Pro, Leu, Gln) rich region. The beta-spiral offers a probable site for interactions with Ca2+ ions. Muatations in the human amelogenin gene (AMGX) cause X-linked hypoplastic amelogenesis imperfecta, a disease characterised by defective enamel. A 9bp deletion in exon 2 of AMGX results in the loss of codons for Ile5, Leu6, Phe7 and Ala8, and replacement by a new threonine codon, disrupting the 16-residue (Met1-Ala16) amelogenin signal peptide.


Pssm-ID: 197891 [Multi-domain]  Cd Length: 165  Bit Score: 39.39  E-value: 6.82e-03
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 960139137   1425 PQLPERPIGPLPPKPTMKPilfptsetarTATATPKLPSPSQdgQPEVSEAISVSQPQEKEKEPPTPSPRKEAPPAPSP 1503
Cdd:smart00818   66 PVVPQQPLMPVPGQHSMTP----------TQHHQPNLPQPAQ--QPFQPQPLQPPQPQQPMQPQPPVHPIPPLPPQPPL 132
 
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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