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Conserved domains on  [gi|1907185079|ref|XP_036009475|]
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neuron navigator 2 isoform X25 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CH_SF super family cl00030
calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding ...
1-46 1.04e-25

calponin homology (CH) domain superfamily; CH domains are actin filament (F-actin) binding motifs, which may be present as a single copy or in tandem repeats (which increase binding affinity). They either function as autonomous actin binding motifs or serve a regulatory function. CH domains are found in cytoskeletal and signal transduction proteins, including actin-binding proteins like spectrin, alpha-actinin, dystrophin, utrophin, and fimbrin, as well as proteins essential for regulation of cell shape (cortexillins), and signaling proteins (Vav).


The actual alignment was detected with superfamily member cd21285:

Pssm-ID: 469584  Cd Length: 121  Bit Score: 103.89  E-value: 1.04e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21285     70 MIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
1938-2175 5.48e-08

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


The actual alignment was detected with superfamily member COG1401:

Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1938 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2012
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 2013 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2063
Cdd:COG1401    284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 2064 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2140
Cdd:COG1401    364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907185079 2141 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2175
Cdd:COG1401    412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1489-1565 2.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907185079 1489 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1565
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1708-1763 7.44e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907185079 1708 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1763
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
168-562 1.02e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  168 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 246
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  247 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 326
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  327 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 405
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  406 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 469
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  470 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 549
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827
                          410
                   ....*....|...
gi 1907185079  550 NVTAESSSAGVSM 562
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
Mplasa_alph_rch super family cl37461
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1489-1761 2.47e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


The actual alignment was detected with superfamily member TIGR04523:

Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1489 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1568
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1569 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1637
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1638 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1703
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1704 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1761
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PRK07003 super family cl35530
DNA polymerase III subunit gamma/tau;
61-254 3.90e-03

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK07003:

Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079   61 LSSSPLPPAGSQVAGAPSQCQAGtpqhqglATPqAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAA 140
Cdd:PRK07003   356 LAFEPAVTGGGAPGGGVPARVAG-------AVP-APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  141 ANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMS---ENVPAPlENSPSVPVNCSSSAIPQPSMTSKP 217
Cdd:PRK07003   428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgsASAPAS-DAPPDAAFEPAPRAAAPSAATPAA 506
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907185079  218 WRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPA 254
Cdd:PRK07003   507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
809-1160 9.27e-03

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  809 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 888
Cdd:PHA03307    22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  889 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 967
Cdd:PHA03307    95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  968 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1046
Cdd:PHA03307   164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1047 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1120
Cdd:PHA03307   244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907185079 1121 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1160
Cdd:PHA03307   321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
1-46 1.04e-25

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 103.89  E-value: 1.04e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21285     70 MIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
1938-2175 5.48e-08

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1938 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2012
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 2013 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2063
Cdd:COG1401    284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 2064 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2140
Cdd:COG1401    364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907185079 2141 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2175
Cdd:COG1401    412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
AAA_22 pfam13401
AAA domain;
1949-2042 2.03e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1949 LTEHRRII-LSGPSGTGKTYLANRLSE----------YVVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCN 2014
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLL 80
                           90       100
                   ....*....|....*....|....*...
gi 1907185079 2015 SENNAVdmplVIILDNLHHVSslGEIFN 2042
Cdd:pfam13401   81 ALAVAV----VLIIDEAQHLS--LEALE 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1489-1565 2.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907185079 1489 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1565
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1952-2060 5.29e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 5.29e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  1952 HRRIILSGPSGTGKTYLANRLSEYVVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2025
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1907185079  2026 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2060
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1708-1763 7.44e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907185079 1708 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1763
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
1700-1758 9.05e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 40.24  E-value: 9.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907185079 1700 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1758
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
168-562 1.02e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  168 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 246
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  247 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 326
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  327 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 405
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  406 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 469
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  470 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 549
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827
                          410
                   ....*....|...
gi 1907185079  550 NVTAESSSAGVSM 562
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1489-1761 2.47e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1489 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1568
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1569 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1637
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1638 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1703
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1704 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1761
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
61-254 3.90e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079   61 LSSSPLPPAGSQVAGAPSQCQAGtpqhqglATPqAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAA 140
Cdd:PRK07003   356 LAFEPAVTGGGAPGGGVPARVAG-------AVP-APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  141 ANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMS---ENVPAPlENSPSVPVNCSSSAIPQPSMTSKP 217
Cdd:PRK07003   428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgsASAPAS-DAPPDAAFEPAPRAAAPSAATPAA 506
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907185079  218 WRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPA 254
Cdd:PRK07003   507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
809-1160 9.27e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  809 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 888
Cdd:PHA03307    22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  889 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 967
Cdd:PHA03307    95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  968 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1046
Cdd:PHA03307   164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1047 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1120
Cdd:PHA03307   244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907185079 1121 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1160
Cdd:PHA03307   321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
PHA03247 PHA03247
large tegument protein UL36; Provisional
89-566 9.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079   89 GLATPQAPCQLLQPVSHQQGKTqvemqsrlPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPS 168
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSVPP--------PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD 2620
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  169 NHEKEPLASSASSHPgmseNVPAPLENSPSVPVNCSSSAiPQPSMTSKPWRSKSLSVKHTATSAMLSVKP---------- 238
Cdd:PHA03247  2621 THAPDPPPPSPSPAA----NEPDPHPPPTVPPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRraarptvgsl 2695
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  239 ---AGPEAPRPTPEamkPAPNNQKSMLEklklfnSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGP 315
Cdd:PHA03247  2696 tslADPPPPPPTPE---PAPHALVSATP------LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  316 ASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDlkeetkadlSGVAVT 395
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQPT 2837
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  396 EMPKKSSKIASFIPKGGKL------------NSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLP 463
Cdd:PHA03247  2838 APPPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  464 PQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTvSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRS 543
Cdd:PHA03247  2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
                          490       500
                   ....*....|....*....|...
gi 1907185079  544 QTDTEGNVTAESSSAGVSMEPSH 566
Cdd:PHA03247  2997 TGHSLSRVSSWASSLALHEETDP 3019
 
Name Accession Description Interval E-value
CH_NAV2 cd21285
calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also ...
1-46 1.04e-25

calponin homology (CH) domain found in neuron navigator 2; Neuron navigator 2 (NAV2), also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV2 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409134  Cd Length: 121  Bit Score: 103.89  E-value: 1.04e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21285     70 MIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
CH_NAV3 cd21286
calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also ...
1-46 2.55e-22

calponin homology (CH) domain found in neuron navigator 3; Neuron navigator 3 (NAV3), also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration. NAV3 contains a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409135  Cd Length: 105  Bit Score: 93.56  E-value: 2.55e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21286     60 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 105
CH_NAV2-like cd21212
calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; ...
1-46 3.75e-22

calponin homology (CH) domain found in neuron navigator (NAV) 2, NAV3, and similar proteins; This family includes neuron navigator 2 (NAV2) and NAV3, both of which contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs. NAV2, also called helicase APC down-regulated 1 (HELAD1), pore membrane and/or filament-interacting-like protein 2 (POMFIL2), retinoic acid inducible in neuroblastoma 1 (RAINB1), Steerin-2 (STEERIN2), or Unc-53 homolog 2 (unc53H2), possesses 3' to 5' helicase activity and exonuclease activity. It is involved in neuronal development, specifically in the development of different sensory organs. NAV3, also called pore membrane and/or filament-interacting-like protein 1 (POMFIL1), Steerin-3 (STEERIN3), or Unc-53 homolog 3 (unc53H3), may regulate IL2 production by T-cells. It may be involved in neuron regeneration.


Pssm-ID: 409061  Cd Length: 105  Bit Score: 93.03  E-value: 3.75e-22
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21212     60 KLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
1938-2175 5.48e-08

5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB [Defense mechanisms];


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 57.86  E-value: 5.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1938 PKPILQRYVSLLTEHRRIILSGPSGTGKTYLANRLSEYVVlreGRELTDGVIATFNVDHKSSKELRQYLSNLADQ----- 2012
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALG---GEDNGRIEFVQFHPSWSYEDFLLGYRPSLDEGkyept 283
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 2013 -------CNSENNAVDMPLVIILD--NLHHVSS-LGEIFNGL------------LNCKYHKCP-------YIIGTMNQAT 2063
Cdd:COG1401    284 pgiflrfCLKAEKNPDKPYVLIIDeiNRANVEKyFGELLSLLesdkrgeelsieLPYSGEGEEfsippnlYIIGTMNTDD 363
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 2064 SStpnlqlhhnfrwvlcanhtepvKGFLGRFLRRK--LMETEIS-GRVRNAELVKIInwipkvwHHLNRFLEahsSSDVT 2140
Cdd:COG1401    364 RS----------------------LALSDKALRRRftFEFLDPDlDKLSNEEVVDLL-------EELNEILE---KRDFQ 411
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1907185079 2141 IGPRLFLSCPIDVDGSRVWFTDLWNYSIIPYLLEA 2175
Cdd:COG1401    412 IGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLL 446
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
2-42 3.56e-07

first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409063  Cd Length: 105  Bit Score: 50.47  E-value: 3.56e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907185079    2 IENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21214     63 IANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTI 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
1-46 1.21e-06

calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called coiled-coil protein DIX1, coiled-coil-DIX1, or DIX domain-containing protein 1, is a positive effector of the Wnt signaling pathway. It activates WNT3A signaling via DVL2 and regulates JNK activation by AXIN1 and DVL2. Members of this family contain a single copy of the CH domain at the N-terminus. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409062  Cd Length: 107  Bit Score: 49.22  E-value: 1.21e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL-SRYK 46
Cdd:cd21213     60 RKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALaAHFK 106
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
1-42 1.85e-05

first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409064  Cd Length: 107  Bit Score: 45.85  E-value: 1.85e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21215     62 KLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTL 103
AAA_22 pfam13401
AAA domain;
1949-2042 2.03e-05

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 46.18  E-value: 2.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1949 LTEHRRII-LSGPSGTGKTYLANRLSE----------YVVLREGRELTD---GVIATFNVDHKSSKELRQYLSNLADQCN 2014
Cdd:pfam13401    1 IRFGAGILvLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllrALLRALGLPLSGRLSKEELLAALQQLLL 80
                           90       100
                   ....*....|....*....|....*...
gi 1907185079 2015 SENNAVdmplVIILDNLHHVSslGEIFN 2042
Cdd:pfam13401   81 ALAVAV----VLIIDEAQHLS--LEALE 102
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1489-1565 2.75e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 45.66  E-value: 2.75e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907185079 1489 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQslgnmtiRLQSLTMTAEQKDSELNELRKTIELLKKQN 1565
Cdd:COG4372     62 EQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQE-------ELESLQEEAEELQEELEELQKERQDLEQQR 131
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
1-42 3.68e-04

first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and similar proteins; Protein jitterbug (Jbug) is an actin-meshwork organizing protein. It is required to maintain the shape and cell orientation of the Drosophila notum epithelium during flight muscle attachment to tendon cells. Jbug contains three copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409076  Cd Length: 109  Bit Score: 41.89  E-value: 3.68e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21227     62 KLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHL 103
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
1952-2060 5.29e-04

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 42.75  E-value: 5.29e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  1952 HRRIILSGPSGTGKTYLANRLSEYVVLREGRELT-DGVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDM-----PLV 2025
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARELGPPGGGVIYiDGEDILEEVLDQLLLIIVGGKKASGSGELRLRLALALarklkPDV 81
                            90       100       110       120
                    ....*....|....*....|....*....|....*....|...
gi 1907185079  2026 IILDNLHHVSS--------LGEIFNGLLNCKYHKCPYIIGTMN 2060
Cdd:smart00382   82 LILDEITSLLDaeqealllLLEELRLLLLLKSEKNLTVILTTN 124
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1708-1763 7.44e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 44.51  E-value: 7.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907185079 1708 QLRNELRDKEMKLTDIRLEALSSAHQLDQLREAMNRMQSEIEKLKAENDRLKSESQ 1763
Cdd:COG4372     77 QLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRK 132
Atg16_CCD cd22887
Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family ...
1700-1758 9.05e-04

Coiled-coiled domain of autophagy-related 16 (Atg16) family proteins; The Atg16 family includes Saccharomyces cerevisiae Atg16 (also called cytoplasm to vacuole targeting protein 11, CVT11, or SAP18), human autophagy-related protein 16-1 (also called APG16-like 1, ATG16L1, or APG16L) and autophagy-related protein 16-2 (also called APG16-like 2, ATG16L2, WD repeat-containing protein 80 or WDR80), and similar proteins. Atg16 stabilizes the Atg5-Atg12 conjugate and mediates the formation of the 350 kDa complex, which is necessary for autophagy. The Atg5-Atg12/Atg16 complex is required for efficient promotion of Atg8-conjugation to phosphatidylethanolamine and Atg8 localization to the pre-autophagosomal structure (PAS). Similarly, human ATG16L1 plays an essential role in autophagy and acts as a molecular scaffold which mediates protein-protein interactions essential for autophagosome formation. ATG16L2, though structurally similar to ATG16L1 and able to form a complex with the autophagy proteins Atg5 and Atg12, is not essential for autophagy. Single-nucleotide polymorphisms in ATG16L1 is associated with an increased risk of developing Crohn disease. Saccharomyces cerevisiae Atg16 contains an N-terminal domain (NTD) that interacts with the Atg5-Atg12 protein conjugate and a coiled-coil domain (CCD) that dimerizes and mediates self-assembly. Human ATG16L1 and ATG16L2 also contains an N-terminal region that binds Atg5, a CCD homologous to the yeast CCD, and a WD40 domain that represents approximately 50% of the full-length protein. This model corresponds to the CCD of Atg16 family proteins.


Pssm-ID: 439196 [Multi-domain]  Cd Length: 91  Bit Score: 40.24  E-value: 9.05e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907185079 1700 DSEAETVMQLRNELRDKEMKLTDIR--LEALSSAHQ-----LDQLREAMNRMQSEIEKLKAENDRL 1758
Cdd:cd22887      7 QELEKRLAELEAELASLEEEIKDLEeeLKEKNKANEilndeLIALQIENNLLEEKLRKLQEENDEL 72
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
168-562 1.02e-03

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 44.52  E-value: 1.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  168 SNHEKEPLASSASSHPGMSE-NVPAPlenSPSVPVNCSSSAIPQPSMTSKPWRSKSLSVkhtaTSAMLSVKPAGPEAPRP 246
Cdd:pfam05109  451 STHVPTNLTAPASTGPTVSTaDVTSP---TPAGTTSGASPVTPSPSPRDNGTESKAPDM----TSPTSAVTTPTPNATSP 523
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  247 TPEAMKPAPNNQKSMLEKLKLFNSKGGSKAGEGSASRDTSCERleilPSFEETEELEATANRALSTVGPASSSPKIALKG 326
Cdd:pfam05109  524 TPAVTTPTPNATSPTLGKTSPTSAVTTPTPNATSPTPAVTTPT----PNATIPTLGKTSPTSAVTTPTPNATSPTVGETS 599
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  327 IAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKgkdlTKRVSVTDRPDLKEET-KADLSGVAVTEMPkkssKIA 405
Cdd:pfam05109  600 PQANTTNHTLGGTSSTPVVTSPPKNATSAVTTGQHNITS----SSTSSMSLRPSSISETlSPSTSDNSTSHMP----LLT 671
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  406 SFIPKGGKLNSTKKEATAPSH-----SGIPKPGMKNVSAKSPSAPIPPKEGERSrgkLSSGLPP-----------QKAQL 469
Cdd:pfam05109  672 SAHPTGGENITQVTPASTSTHhvstsSPAPRPGTTSQASGPGNSSTSTKPGEVN---VTKGTPPknatspqapsgQKTAV 748
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  470 DSRHSSSSSSLASSEGKGPGGTSLNPSISSQTVSGSVGTTQTTGSNTVSVqLPQPQQQYNHPNTATVAPFLYRSQTDTEG 549
Cdd:pfam05109  749 PTVTSTGGKANSTTGGKHTTGHGARTSTEPTTDYGGDSTTPRTRYNATTY-LPPSTSSKLRPRWTFTSPPVTTAQATVPV 827
                          410
                   ....*....|...
gi 1907185079  550 NVTAESSSAGVSM 562
Cdd:pfam05109  828 PPTSQPRFSNLSM 840
AAA_18 pfam13238
AAA domain;
1955-2032 1.68e-03

AAA domain;


Pssm-ID: 433052 [Multi-domain]  Cd Length: 128  Bit Score: 40.49  E-value: 1.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1955 IILSGPSGTGKTYLANRLSEyvVLREGRELTD-----GVIATFNVDHKSSKELRQYLSNLADQCNSENNAVDMPLVIILD 2029
Cdd:pfam13238    1 ILITGTPGVGKTTLAKELSK--RLGFGDNVRDlalenGLVLGDDPETRESKRLDEDKLDRLLDLLEENAALEEGGNLIID 78

                   ...
gi 1907185079 2030 NLH 2032
Cdd:pfam13238   79 GHL 81
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
1489-1761 2.47e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 43.09  E-value: 2.47e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1489 EKCQSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQNAAA 1568
Cdd:TIGR04523  303 QKEQDWNKELKSELKNQEKKLEEIQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEKLKKENQSY 382
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1569 QAAINGVIN-TPELNCK---GNGSAQATDLRIRRQHSSDSVS-------SINSATSHSSVGSNIESDSKKKKRKNWVNEL 1637
Cdd:TIGR04523  383 KQEIKNLESqINDLESKiqnQEKLNQQKDEQIKKLQQEKELLekeierlKETIIKNNSEIKDLTNQDSVKELIIKNLDNT 462
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1638 RSSFKQafgkkkspksasshsDIEEMTDsslpSSPKLPHNGSTGSTPL-LRNAHSNSLISECMDSEA------------- 1703
Cdd:TIGR04523  463 RESLET---------------QLKVLSR----SINKIKQNLEQKQKELkSKEKELKKLNEEKKELEEkvkdltkkisslk 523
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1704 ETVMQLRNELRDKEMKLTDIRLEALSSAHQL--DQLREAMNRMQSEIEKLKAENDRLKSE 1761
Cdd:TIGR04523  524 EKIEKLESEKKEKESKISDLEDELNKDDFELkkENLEKEIDEKNKEIEELKQTQKSLKKK 583
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
2-42 3.23e-03

first calponin homology (CH) domain found in the filamin family; The filamin family includes filamin-A (FLN-A), filamin-B (FLN-B) and filamin-C (FLN-C). Filamins function to anchor various transmembrane proteins to the actin cytoskeleton. FLN-A is also called actin-binding protein 280 (ABP-280), alpha-filamin, endothelial actin-binding protein, filamin-1, or non-muscle filamin. It promotes orthogonal branching of actin filaments and links actin filaments to membrane glycoproteins. It also serves as a scaffold for a wide range of cytoplasmic signaling proteins. FLN-B is also called ABP-278, ABP-280 homolog, actin-binding-like protein, beta-filamin, filamin homolog 1 (Fh1), filamin-3, thyroid autoantigen, truncated actin-binding protein, or truncated ABP. It connects cell membrane constituents to the actin cytoskeleton and may also promote orthogonal branching of actin filaments as well as link actin filaments to membrane glycoproteins. FLN-C, also called FLNc, ABP-280-like protein, ABP-L, actin-binding-like protein, filamin-2, or gamma-filamin, is a muscle-specific filamin that plays a central role in muscle cells, probably by functioning as a large actin-cross-linking protein. It may be involved in reorganizing the actin cytoskeleton in response to signaling events, and may also display structural functions at the Z lines in muscle cells. FLN-C is critical for normal myogenesis and for maintaining the structural integrity of the muscle fibers. This family also includes Drosophila melanogaster protein jitterbug (Jbug), which is an actin-meshwork organizing protein containing three copies of the CH domain. Other members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409032  Cd Length: 108  Bit Score: 39.39  E-value: 3.23e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907185079    2 IENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21183     64 LENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTL 104
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
61-254 3.90e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 42.53  E-value: 3.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079   61 LSSSPLPPAGSQVAGAPSQCQAGtpqhqglATPqAPCQLLQPVSHQQGKTQVEMQSRLPGPTARVAAAGSEAKTRGGSAA 140
Cdd:PRK07003   356 LAFEPAVTGGGAPGGGVPARVAG-------AVP-APGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPP 427
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  141 ANNRRSQSFNNYDKSKPVTSPPPPAPPSNHEKEPLASSASSHPGMS---ENVPAPlENSPSVPVNCSSSAIPQPSMTSKP 217
Cdd:PRK07003   428 AAPAPPATADRGDDAADGDAPVPAKANARASADSRCDERDAQPPADsgsASAPAS-DAPPDAAFEPAPRAAAPSAATPAA 506
                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1907185079  218 WRSKSLSVKHTATSAMLSVKPAGPEAPRPTPEAMKPA 254
Cdd:PRK07003   507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPA 543
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
2-38 4.93e-03

first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409042  Cd Length: 116  Bit Score: 38.82  E-value: 4.93e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907185079    2 IENIDACLNFLAAKgINTQGLSAEEIRNGNLKAILGL 38
Cdd:cd21193     74 IENVNKALAFLKTK-VRLENIGAEDIVDGNPRLILGL 109
AAA_28 pfam13521
AAA domain;
1954-1986 5.56e-03

AAA domain;


Pssm-ID: 433278 [Multi-domain]  Cd Length: 164  Bit Score: 39.94  E-value: 5.56e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907185079 1954 RIILSGPSGTGKTYLANRLSE---YVVLRE-GRELTD 1986
Cdd:pfam13521    1 RIVITGGPSTGKTTLAEALAArfgYPVVPEaAREILE 37
ExeA COG3267
Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, ...
1949-2035 5.77e-03

Type II secretory pathway ATPase component GspA/ExeA/MshM [Intracellular trafficking, secretion, and vesicular transport, Extracellular structures];


Pssm-ID: 442498 [Multi-domain]  Cd Length: 261  Bit Score: 40.93  E-value: 5.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1949 LTEHRRII-LSGPSGTGKTYLANRL-----SEYVVLR------EGRELTDGVIATFNVDHKSS------KELRQYLSNLA 2010
Cdd:COG3267     39 LAQGGGFVvLTGEVGTGKTTLLRRLlerlpDDVKVAYipnpqlSPAELLRAIADELGLEPKGAskadllRQLQEFLLELA 118
                           90       100
                   ....*....|....*....|....*
gi 1907185079 2011 DQcnsennavDMPLVIILDNLHHVS 2035
Cdd:COG3267    119 AA--------GRRVVLIIDEAQNLP 135
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
1492-1564 5.91e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 41.29  E-value: 5.91e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907185079 1492 QSEIRKLRRELDASQEKVSALTTQLTANAHLVAAFEQSLGNMTIRLQSLTMTAEQKDSELNELRKTIELLKKQ 1564
Cdd:COG4942     26 EAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAE 98
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
1-42 6.14e-03

first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family includes plectin, dystonin and microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1). Plectin, also called PCN, PLTN, hemidesmosomal protein 1 (HD1), or plectin-1, is a structural component of muscle. It interlinks intermediate filaments with microtubules and microfilaments, and anchors intermediate filaments to desmosomes or hemidesmosomes. It could also bind muscle proteins such as actin to membrane complexes in muscle. Dystonin, also called 230 kDa bullous pemphigoid antigen, 230/240 kDa bullous pemphigoid antigen, bullous pemphigoid antigen 1 (BPA or BPAG1), dystonia musculorum protein, or hemidesmosomal plaque protein, is a cytoskeletal linker protein that acts as an integrator of intermediate filaments, actin, and microtubule cytoskeleton networks. It is required for anchoring either intermediate filaments to the actin cytoskeleton in neural and muscle cells, or keratin-containing intermediate filaments to hemidesmosomes in epithelial cells. MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. Members of this family contain two copies of the CH domain. This model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409037  Cd Length: 105  Bit Score: 38.54  E-value: 6.14e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907185079    1 MIENIDACLNFLAAKGINTQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21188     59 RLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTI 100
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
809-1160 9.27e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  809 INTSSSISSYANTPASSRRNLDVQTDAEKHSQVernslwsGDDIKKSDGGSDSGVKMEPGSKWRRNPSDMSDESDKSVSG 888
Cdd:PHA03307    22 PRPPATPGDAADDLLSGSQGQLVSDSAELAAVT-------VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSLST 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  889 KKNPVLSQTGSWRRGMtaevgitmpRTKPSAPTGTLKTPGTGKTDDAKVSEKGRLSPKASQV-KRSPSDAGRSSGDESkk 967
Cdd:PHA03307    95 LAPASPAREGSPTPPG---------PSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPpAASPPAAGASPAAVA-- 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  968 TLPSSSRTPTVNANSFGFKKQSGSAAGLAM-ITASGATVTSRSATLGKIPKSSALVGRPTGRKTSMDGAPNQDDGYLSLS 1046
Cdd:PHA03307   164 SDAASSRQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSE 243
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079 1047 SR------TNLQYRSLPRPSKSNSRNGAGNRCSTSSIDSNMSSKSAGlpvPKLREPSKASLGSSLPGLVNQTDKEKGISS 1120
Cdd:PHA03307   244 SSgcgwgpENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSS---PRERSPSPSPSSPGSGPAPSSPRASSSSSS 320
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1907185079 1121 DSESVASCNS-VKVNPATQPVSSSAQ----ATLQPGTKYADVASP 1160
Cdd:PHA03307   321 SRESSSSSTSsSSESSRGAAVSPGPSpsrsPSPSRPPPPADPSSP 365
PHA03247 PHA03247
large tegument protein UL36; Provisional
89-566 9.27e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 9.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079   89 GLATPQAPCQLLQPVSHQQGKTqvemqsrlPGPTARVAAAGSEAKTRGGSAAANNRRSQSFNNYDKSKPVTSPPPPAPPS 168
Cdd:PHA03247  2549 GDPPPPLPPAAPPAAPDRSVPP--------PRPAPRPSEPAVTSRARRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPD 2620
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  169 NHEKEPLASSASSHPgmseNVPAPLENSPSVPVNCSSSAiPQPSMTSKPWRSKSLSVKHTATSAMLSVKP---------- 238
Cdd:PHA03247  2621 THAPDPPPPSPSPAA----NEPDPHPPPTVPPPERPRDD-PAPGRVSRPRRARRLGRAAQASSPPQRPRRraarptvgsl 2695
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  239 ---AGPEAPRPTPEamkPAPNNQKSMLEklklfnSKGGSKAGEGSASRDTSCERLEILPSFEETEELEATANRALSTVGP 315
Cdd:PHA03247  2696 tslADPPPPPPTPE---PAPHALVSATP------LPPGPAAARQASPALPAAPAPPAVPAGPATPGGPARPARPPTTAGP 2766
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  316 ASSSPKIALKGIAQRTFSRALTNKKSSPKGNEKEKEKQQREKEKEKEKEKGKDLTKRVSVTDRPDlkeetkadlSGVAVT 395
Cdd:PHA03247  2767 PAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPP---------TSAQPT 2837
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  396 EMPKKSSKIASFIPKGGKL------------NSTKKEATAPSHSGIPKPGMKNVSAKSPSAPIPPKEGERSRGKLSSGLP 463
Cdd:PHA03247  2838 APPPPPGPPPPSLPLGGSVapggdvrrrppsRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPP 2917
                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907185079  464 PQKAQLDSRHSSSSSSLASSEGKGPGGTSLNPSISSQTvSGSVGTTQTTGSNTVSVQLPQPQQQYNHPNTATVAPFLYRS 543
Cdd:PHA03247  2918 QPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEP-SGAVPQPWLGALVPGRVAVPRFRVPQPAPSREAPASSTPPL 2996
                          490       500
                   ....*....|....*....|...
gi 1907185079  544 QTDTEGNVTAESSSAGVSMEPSH 566
Cdd:PHA03247  2997 TGHSLSRVSSWASSLALHEETDP 3019
 
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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