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Conserved domains on  [gi|1907075186|ref|XP_036011682|]
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neuron navigator 3 isoform X6 [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 8.39e-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: 101.19  E-value: 8.39e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21285     70 MIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 67-445 1.26e-09

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: 63.78  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186   67 THTAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSnkAQGASNLNRRSQSFNSIDKNK 146
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVST--ADVTSPTPAGTTSGASPVTPS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  147 PPNYANGNEKDSPKGPQPSSGINgnTQPPSTSGQPPASAIPSPSASKPwrsksmnvkhsatsTMLTVKQPSPATSPTPSS 226
Cdd:pfam05109  492 PSPRDNGTESKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNATSP--------------TLGKTSPTSAVTTPTPNA 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  227 DRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQAPSSGPNDGGREDDAfsesgemegfNSGLNSGGSTNSSPKVS 306
Cdd:pfam05109  556 TSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPVVT 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  307 pklTPPKAGSKNFSNKKSLLQPKEKEEKTRdKNKACAEKSGKEEKDQVT------TEAAPKKTSKIASLIPKGSKTAAak 380
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSL-RPSSISETLSPSTSDNSTshmpllTSAHPTGGENITQVTPASTSTHH-- 693

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075186  381 keslIPSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFPKAITAEKASTPSLST 445
Cdd:pfam05109  694 ----VSTSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753
McrB super family cl34253
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1879-2144 2.00e-07

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: 55.93  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1879 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 1946
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1947 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 1997
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1998 GTMNQGVSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSFLEt 2074
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075186 2075 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2144
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 842-1157 1.45e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  842 KASLSVSQTGSWRRGMSAQGGTPATARQKTStsalktPGKTDDAKASEKGKTPLK-GSSLQRSPSDAGKSSGDEGKKPPS 920
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPPTPPPAS------PPPSPAPDLSEMLRPVGSpGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  921 GIGRSTASSSFGYKK--PSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTT 998
Cdd:PHA03307   169 SRQAALPLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  999 LQYRS---LPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDS 1075
Cdd:PHA03307   249 WGPENecpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1076 ESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLSPSTSLARQGSLE 1155
Cdd:PHA03307   329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408


                   ..
gi 1907075186 1156 SP 1157
Cdd:PHA03307   409 AG 410
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1435-1515 2.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


:

Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1435 EQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1514
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145


                   .
gi 1907075186 1515 Q 1515
Cdd:COG4372    146 A 146
 
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 8.39e-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: 101.19  E-value: 8.39e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21285     70 MIENIDACLSFLAAKGINIQGLSAEEIRNGNLKAILGLFFSLSRYK 115
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 67-445 1.26e-09

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: 63.78  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186   67 THTAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSnkAQGASNLNRRSQSFNSIDKNK 146
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVST--ADVTSPTPAGTTSGASPVTPS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  147 PPNYANGNEKDSPKGPQPSSGINgnTQPPSTSGQPPASAIPSPSASKPwrsksmnvkhsatsTMLTVKQPSPATSPTPSS 226
Cdd:pfam05109  492 PSPRDNGTESKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNATSP--------------TLGKTSPTSAVTTPTPNA 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  227 DRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQAPSSGPNDGGREDDAfsesgemegfNSGLNSGGSTNSSPKVS 306
Cdd:pfam05109  556 TSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPVVT 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  307 pklTPPKAGSKNFSNKKSLLQPKEKEEKTRdKNKACAEKSGKEEKDQVT------TEAAPKKTSKIASLIPKGSKTAAak 380
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSL-RPSSISETLSPSTSDNSTshmpllTSAHPTGGENITQVTPASTSTHH-- 693

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075186  381 keslIPSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFPKAITAEKASTPSLST 445
Cdd:pfam05109  694 ----VSTSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1879-2144 2.00e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 55.93  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1879 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 1946
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1947 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 1997
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1998 GTMNQGVSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSFLEt 2074
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075186 2075 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2144
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 136-547 4.58e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.00  E-value: 4.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  136 SQSFNSIDKNKPPNYANGNEKDSPKGPQPSSGINGNTQPPSTSGQPPASAiPSPSASKPWRSKSMNVKHSATSTMLTVKQ 215
Cdd:PTZ00449   482 TQEIKKLIKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEE-GEHEDSKESDEPKEGGKPGETKEGEVGKK 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  216 PSPATSPTPSsdrlKPPVtegVKSAPSGQKSMLEKFKLVNARTALRP--PQAPSSGPNDGGREDDAFSESGEMEgfnsgl 293
Cdd:PTZ00449   561 PGPAKEHKPS----KIPT---LSKKPEFPKDPKHPKDPEEPKKPKRPrsAQRPTRPKSPKLPELLDIPKSPKRP------ 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  294 nsggSTNSSPKVSPKLTPPKA-----GSKNFSNKKSLLQPK-----EKEEKTRDKNKACAEKSGKEEKDQVTTEAAPKKT 363
Cdd:PTZ00449   628 ----ESPKSPKRPPPPQRPSSperpeGPKIIKSPKPPKSPKppfdpKFKEKFYDDYLDAAAKSKETKTTVVLDESFESIL 703

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  364 SKIASLIPKGSKTAAAKKESLIPSSSGIPKPGSKVPTPKQTISPGSAASKESEKFRTSKGSSSQAFPkAITAEKASTPSL 443
Cdd:PTZ00449   704 KETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLP-DILAEEFKEEDI 782

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  444 STPLDGREAGQASPSSScvmqvTHSSGQSPGNGAvQLPQQQQHSHPNTATVAPFiyrahsENEGTSLpPADSCTSPTKMD 523
Cdd:PTZ00449   783 HAETGEPDEAMKRPDSP-----SEHEDKPPGDHP-SLPKKRHRLDGLALSTTDL------ESDAGRI-AKDASGKIVKLK 849

                          410       420
                   ....*....|....*....|....
gi 1907075186  524 SSYSKTAKQCLEEISGEDPEARRM 547
Cdd:PTZ00449   850 RSKSFDDLTTVEEAEEMGAEARKI 873
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 842-1157 1.45e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  842 KASLSVSQTGSWRRGMSAQGGTPATARQKTStsalktPGKTDDAKASEKGKTPLK-GSSLQRSPSDAGKSSGDEGKKPPS 920
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPPTPPPAS------PPPSPAPDLSEMLRPVGSpGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  921 GIGRSTASSSFGYKK--PSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTT 998
Cdd:PHA03307   169 SRQAALPLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  999 LQYRS---LPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDS 1075
Cdd:PHA03307   249 WGPENecpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1076 ESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLSPSTSLARQGSLE 1155
Cdd:PHA03307   329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408


                   ..
gi 1907075186 1156 SP 1157
Cdd:PHA03307   409 AG 410
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1893-2013 4.00e-05

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: 45.83  E-value: 4.00e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  1893 HHRIILSGPSGTGKTYLANKLAEY-------VITKSGRKKTEDA------IATFNVDHKSSKELQQYLAN-LAEQCSADn 1958
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARElgppgggVIYIDGEDILEEVldqlllIIVGGKKASGSGELRLRLALaLARKLKPD- 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075186  1959 ngvelpvVIILDNLHH---------VGSLSDIFNGFLNCKYNKCPyIIGTMNQGVSSSPNLELH 2013
Cdd:smart00382   81 -------VLILDEITSlldaeqealLLLLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1896-1976 1.84e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 44.06  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1896 IILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGvelpvVIILDNLHHV 1975
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96


                   .
gi 1907075186 1976 G 1976
Cdd:cd00009     97 S 97
AAA_22 pfam13401
AAA domain;
1896-1983 5.27e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1896 IILSGPSGTGKTYLANKLAE----------YVITKSGRKKTE--DAIATF----NVDHKSSKELQQYLANLAEQCSAdnn 1959
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllRALLRAlglpLSGRLSKEELLAALQQLLLALAV--- 84

                           90       100
                   ....*....|....*....|....*....
gi 1907075186 1960 gvelPVVIILDNLHHVGS-----LSDIFN 1983
Cdd:pfam13401   85 ----AVVLIIDEAQHLSLealeeLRDLLN 109
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1435-1515 2.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1435 EQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1514
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145


                   .
gi 1907075186 1515 Q 1515
Cdd:COG4372    146 A 146
 
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 8.39e-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: 101.19  E-value: 8.39e-25
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 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 1.21e-24

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: 100.49  E-value: 1.21e-24
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 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 1.51e-21

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: 91.49  E-value: 1.51e-21
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSLSRYK 46
Cdd:cd21212     60 KLENIQACLQFLAALGVDVQGITAEDIVDGNLKAILGLFFSLSRYK 105
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 67-445 1.26e-09

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: 63.78  E-value: 1.26e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186   67 THTAPQSEASQAKTQQDMQSslTARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSnkAQGASNLNRRSQSFNSIDKNK 146
Cdd:pfam05109  416 THKVIFSKAPESTTTSPTLN--TTGFAAPNTTTGLPSSTHVPTNLTAPASTGPTVST--ADVTSPTPAGTTSGASPVTPS 491

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  147 PPNYANGNEKDSPKGPQPSSGINgnTQPPSTSGQPPASAIPSPSASKPwrsksmnvkhsatsTMLTVKQPSPATSPTPSS 226
Cdd:pfam05109  492 PSPRDNGTESKAPDMTSPTSAVT--TPTPNATSPTPAVTTPTPNATSP--------------TLGKTSPTSAVTTPTPNA 555

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  227 DRLKPPVTegvKSAPSGQKSMLEKfklVNARTALRPPQAPSSGPNDGGREDDAfsesgemegfNSGLNSGGSTNSSPKVS 306
Cdd:pfam05109  556 TSPTPAVT---TPTPNATIPTLGK---TSPTSAVTTPTPNATSPTVGETSPQA----------NTTNHTLGGTSSTPVVT 619

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  307 pklTPPKAGSKNFSNKKSLLQPKEKEEKTRdKNKACAEKSGKEEKDQVT------TEAAPKKTSKIASLIPKGSKTAAak 380
Cdd:pfam05109  620 ---SPPKNATSAVTTGQHNITSSSTSSMSL-RPSSISETLSPSTSDNSTshmpllTSAHPTGGENITQVTPASTSTHH-- 693

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907075186  381 keslIPSSSGIPKPGskvpTPKQTISPG-SAASKESEKFRTSKGSSSQ--AFPKAITAEKASTPSLST 445
Cdd:pfam05109  694 ----VSTSSPAPRPG----TTSQASGPGnSSTSTKPGEVNVTKGTPPKnaTSPQAPSGQKTAVPTVTS 753
CH_ACTN_rpt1 cd21214
first calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) ...
 2-42 1.75e-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: 51.24  E-value: 1.75e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907075186    2 IENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21214     63 IANVNKALDFIASKGVKLVSIGAEEIVDGNLKMTLGMIWTI 103
McrB COG1401
5-methylcytosine-specific restriction endonuclease McrBC, GTP-binding regulatory subunit McrB ...
 1879-2144 2.00e-07

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


Pssm-ID: 441011 [Multi-domain]  Cd Length: 477  Bit Score: 55.93  E-value: 2.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1879 PKPITQRYFNLLMEHHRIILSGPSGTGKTYLANKLAEYVI-TKSGRKKtedaIATFNVDHKSSKELQQY----------- 1946
Cdd:COG1401    207 FEETLEAFLAALKTKKNVILAGPPGTGKTYLARRLAEALGgEDNGRIE----FVQFHPSWSYEDFLLGYrpsldegkyep 282

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1947 ----LANLAEQCSADNNGvelPVVIILD--NLHHVgslSDIFNGFL--------------NCKYNKCP---------YII 1997
Cdd:COG1401    283 tpgiFLRFCLKAEKNPDK---PYVLIIDeiNRANV---EKYFGELLsllesdkrgeelsiELPYSGEGeefsippnlYII 356

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1998 GTMNQGVSSspnlelhhnfrwvlcanhtepvKGFLGRYLRRK--LIEMEIERN-IRNNDLVKIIDwipktwhHLNSFLEt 2074
Cdd:COG1401    357 GTMNTDDRS----------------------LALSDKALRRRftFEFLDPDLDkLSNEEVVDLLE-------ELNEILE- 406

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907075186 2075 hsSSDVTIGPRLFLPCPMDVEGSRVWFMDLWNYSLVPYVLEA-VREGLQMYGKRAPWEDPSKWVLDTYPWS 2144
Cdd:COG1401    407 --KRDFQIGHRALLLLDGLLSGDLDLLLLLLLLLLELLLLLLdKLDLLGMAEFEDRLELSEYLPLLLRASL 475
CH_SpAIN1-like_rpt1 cd21215
first calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ...
 1-42 1.18e-06

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: 48.94  E-value: 1.18e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21215     62 KLENVNKALEFIKSRGVKLTNIGAEDIVDGNLKLILGLLWTL 103
CH_DIXDC1 cd21213
calponin homology (CH) domain found in Dixin and similar proteins; Dixin, also called ...
 1-46 4.20e-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: 47.29  E-value: 4.20e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL-SRYK 46
Cdd:cd21213     60 RKENVEKVLQFMASKRIRMHQTSAKDIVDGNLKAIMRLILALaAHFK 106
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 136-547 4.58e-06

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 52.00  E-value: 4.58e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  136 SQSFNSIDKNKPPNYANGNEKDSPKGPQPSSGINGNTQPPSTSGQPPASAiPSPSASKPWRSKSMNVKHSATSTMLTVKQ 215
Cdd:PTZ00449   482 TQEIKKLIKKSKKKLAPIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEE-GEHEDSKESDEPKEGGKPGETKEGEVGKK 560

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  216 PSPATSPTPSsdrlKPPVtegVKSAPSGQKSMLEKFKLVNARTALRP--PQAPSSGPNDGGREDDAFSESGEMEgfnsgl 293
Cdd:PTZ00449   561 PGPAKEHKPS----KIPT---LSKKPEFPKDPKHPKDPEEPKKPKRPrsAQRPTRPKSPKLPELLDIPKSPKRP------ 627

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  294 nsggSTNSSPKVSPKLTPPKA-----GSKNFSNKKSLLQPK-----EKEEKTRDKNKACAEKSGKEEKDQVTTEAAPKKT 363
Cdd:PTZ00449   628 ----ESPKSPKRPPPPQRPSSperpeGPKIIKSPKPPKSPKppfdpKFKEKFYDDYLDAAAKSKETKTTVVLDESFESIL 703

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  364 SKIASLIPKGSKTAAAKKESLIPSSSGIPKPGSKVPTPKQTISPGSAASKESEKFRTSKGSSSQAFPkAITAEKASTPSL 443
Cdd:PTZ00449   704 KETLPETPGTPFTTPRPLPPKLPRDEEFPFEPIGDPDAEQPDDIEFFTPPEEERTFFHETPADTPLP-DILAEEFKEEDI 782

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  444 STPLDGREAGQASPSSScvmqvTHSSGQSPGNGAvQLPQQQQHSHPNTATVAPFiyrahsENEGTSLpPADSCTSPTKMD 523
Cdd:PTZ00449   783 HAETGEPDEAMKRPDSP-----SEHEDKPPGDHP-SLPKKRHRLDGLALSTTDL------ESDAGRI-AKDASGKIVKLK 849

                          410       420
                   ....*....|....*....|....
gi 1907075186  524 SSYSKTAKQCLEEISGEDPEARRM 547
Cdd:PTZ00449   850 RSKSFDDLTTVEEAEEMGAEARKI 873
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 842-1157 1.45e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 1.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  842 KASLSVSQTGSWRRGMSAQGGTPATARQKTStsalktPGKTDDAKASEKGKTPLK-GSSLQRSPSDAGKSSGDEGKKPPS 920
Cdd:PHA03307    95 LAPASPAREGSPTPPGPSSPDPPPPTPPPAS------PPPSPAPDLSEMLRPVGSpGPPPAASPPAAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  921 GIGRSTASSSFGYKK--PSGVGASTMITSSGATITSGSATLGKIPKSAAIGGKSNAGRKTSLDGSQNQDDVVLHVSSKTT 998
Cdd:PHA03307   169 SRQAALPLSSPEETAraPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCG 248

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  999 LQYRS---LPRPSKSSTSGIPGRGGHRSSTSSIDSNVSSKSAGATTSKLREPTKIGSGRSSPVTVNQTDKEKEKVAVSDS 1075
Cdd:PHA03307   249 WGPENecpLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSS 328

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1076 ESVSLSGSPKSSPTSASACGTQGLRQPGSKYPDIASPTFRRLFGAKAGGKSASAPNTEGAKSSSVVLSPSTSLARQGSLE 1155
Cdd:PHA03307   329 TSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRFP 408


                   ..
gi 1907075186 1156 SP 1157
Cdd:PHA03307   409 AG 410
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 1893-2013 4.00e-05

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: 45.83  E-value: 4.00e-05
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  1893 HHRIILSGPSGTGKTYLANKLAEY-------VITKSGRKKTEDA------IATFNVDHKSSKELQQYLAN-LAEQCSADn 1958
Cdd:smart00382    2 GEVILIVGPPGSGKTTLARALARElgppgggVIYIDGEDILEEVldqlllIIVGGKKASGSGELRLRLALaLARKLKPD- 80

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907075186  1959 ngvelpvVIILDNLHH---------VGSLSDIFNGFLNCKYNKCPyIIGTMNQGVSSSPNLELH 2013
Cdd:smart00382   81 -------VLILDEITSlldaeqealLLLLEELRLLLLLKSEKNLT-VILTTNDEKDLGPALLRR 136
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 1896-1976 1.84e-04

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 44.06  E-value: 1.84e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1896 IILSGPSGTGKTYLANKLAEYVITKSGRKKTEDAIATFNVDHKSSKELQQYLANLAEQCSADNNGvelpvVIILDNLHHV 1975
Cdd:cd00009     22 LLLYGPPGTGKTTLARAIANELFRPGAPFLYLNASDLLEGLVVAELFGHFLVRLLFELAEKAKPG-----VLFIDEIDSL 96


                   .
gi 1907075186 1976 G 1976
Cdd:cd00009     97 S 97
AAA_22 pfam13401
AAA domain;
1896-1983 5.27e-04

AAA domain;


Pssm-ID: 379165 [Multi-domain]  Cd Length: 129  Bit Score: 41.94  E-value: 5.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1896 IILSGPSGTGKTYLANKLAE----------YVITKSGRKKTE--DAIATF----NVDHKSSKELQQYLANLAEQCSAdnn 1959
Cdd:pfam13401    8 LVLTGESGTGKTTLLRRLLEqlpevrdsvvFVDLPSGTSPKDllRALLRAlglpLSGRLSKEELLAALQQLLLALAV--- 84

                           90       100
                   ....*....|....*....|....*....
gi 1907075186 1960 gvelPVVIILDNLHHVGS-----LSDIFN 1983
Cdd:pfam13401   85 ----AVVLIIDEAQHLSLealeeLRDLLN 109
CH_jitterbug-like_rpt1 cd21227
first calponin homology (CH) domain found in Drosophila melanogaster protein jitterbug and ...
 1-42 7.00e-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: 41.12  E-value: 7.00e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21227     62 KLENVTLALKAMAEDGIKLVNIGNEDIVNGNLKLILGLIWHL 103
PHA03378 PHA03378
EBNA-3B; Provisional
 89-272 8.27e-04

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 44.67  E-value: 8.27e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186   89 TARYAAQSKHSGIATSQKKPTRLPGPSRVPAASSSNKAQGASNLNRRSQSFNSIDKNKPPNYANGNEKD---SPKGPQPS 165
Cdd:PHA03378   678 PTGANTMLPIQWAPGTMQPPPRAPTPMRPPAAPPGRAQRPAAATGRARPPAAAPGRARPPAAAPGRARPpaaAPGRARPP 757

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  166 SGINGNTQPPSTSG-----QPPASAIPSPSaSKPWRSKSMNVKHSATSTMLTVKQPSPATSPTPSSDRLKPPVTEGVKSA 240
Cdd:PHA03378   758 AAAPGRARPPAAAPgaptpQPPPQAPPAPQ-QRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQGPTKQILRQLLTGGVKRG 836

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1907075186  241 -PSGQK-SMLEKfklvnaRTALRPPQAPSSGPND 272
Cdd:PHA03378   837 rPSLKKpAALER------QAAAGPTPSPGSGTSD 864
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 86-459 8.52e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 44.78  E-value: 8.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186   86 SSLTARYAAQSKHSGIATSQKKPTrlPGPSRVPAASSSNKAQGASNLNRRSQSFNSIDKNKPPnyANGNEKDSPKGPQPS 165
Cdd:PHA03307    93 STLAPASPAREGSPTPPGPSSPDP--PPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPP--AAGASPAAVASDAAS 168

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  166 SGingNTQPPSTSGQPPASAIPSPSASKPWRSKSmnvkHSATSTMLTVKQPSPATSPTPSSDRLKPPVTEGVKSAPSGQK 245
Cdd:PHA03307   169 SR---QAALPLSSPEETARAPSSPPAEPPPSTPP----AAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSS 241

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  246 SMLEKFKLVNARTALRPPQAPSSGPndgGREDDAFSESGEMEGFNSGLNSGGSTNSSPKVSPKltPPKAGSKNFSNKKSl 325
Cdd:PHA03307   242 SESSGCGWGPENECPLPRPAPITLP---TRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPS--SPGSGPAPSSPRAS- 315

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186  326 lqpkEKEEKTRDKNKACAEKSGKEEKDQVTTEAAPKKTSkiasliPKGSKtaaakkesliPSSSGIPKPGSKVPTPKQTI 405
Cdd:PHA03307   316 ----SSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRS------PSPSR----------PPPPADPSSPRKRPRPSRAP 375

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907075186  406 SPGSAASKESEKFRTSKGSSSQAFPKAITAEKASTPSLSTPLDGREAGQASPSS 459
Cdd:PHA03307   376 SSPAASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAASGAFYAR 429
CH_beta_spectrin_rpt1 cd21193
first calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ...
 2-38 1.20e-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: 40.74  E-value: 1.20e-03
                           10        20        30
                   ....*....|....*....|....*....|....*..
gi 1907075186    2 IENVDVCLSFLAARgVNVQGLSAEEIRNGNLKAILGL 38
Cdd:cd21193     74 IENVNKALAFLKTK-VRLENIGAEDIVDGNPRLILGL 109
CH_PLEC-like_rpt1 cd21188
first calponin homology (CH) domain found in the plectin/dystonin/MACF1 family; This family ...
 1-42 1.90e-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: 39.69  E-value: 1.90e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21188     59 RLQNVQTALDFLKYRKIKLVNIRAEDIVDGNPKLTLGLIWTI 100
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
1435-1515 2.81e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1435 EQIHKLRRELVASQEKVATLTSQLSANAHLVAAFEKSLGNMTGRLQSLTMTAEQKESELIELRETIEMLKAQNSAAQAAI 1514
Cdd:COG4372     66 EELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEI 145


                   .
gi 1907075186 1515 Q 1515
Cdd:COG4372    146 A 146
CH_FLN-like_rpt1 cd21183
first calponin homology (CH) domain found in the filamin family; The filamin family includes ...
 2-42 3.24e-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: 3.24e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907075186    2 IENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21183     64 LENVSTALKFIEADHIKLVNIGSGDIVNGNIKLILGLIWTL 104
DEXHc_RE cd17926
DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family ...
 1894-1998 6.80e-03

DEXH-box helicase domain of DEAD-like helicase restriction enzyme family proteins; This family is composed of helicase restriction enzymes and similar proteins such as TFIIH basal transcription factor complex helicase XPB subunit. These proteins are part of the DEAD-like helicase superfamily, a diverse family of proteins involved in ATP-dependent RNA or DNA unwinding. This domain contains the ATP-binding region.


Pssm-ID: 350684 [Multi-domain]  Cd Length: 146  Bit Score: 39.21  E-value: 6.80e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1894 HRIILSGPSGTGKTYLANKLAEY---------VITKSGRKKTEDAIATFNVDHKS------SKELQ----------QYLA 1948
Cdd:cd17926     19 RRGILVLPTGSGKTLTALALIAYlkelrtlivVPTDALLDQWKERFEDFLGDSSIgligggKKKDFddanvvvatyQSLS 98

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1949 NLAEQCSADNNgveLPVVIILDNLHHVGSLSdiFNGFLncKYNKCPYIIG 1998
Cdd:cd17926     99 NLAEEEKDLFD---QFGLLIVDEAHHLPAKT--FSEIL--KELNAKYRLG 141
CH_PARV_rpt2 cd21222
second calponin homology (CH) domain found in the parvin family; The parvin family includes ...
 1-45 7.93e-03

second calponin homology (CH) domain found in the parvin family; The parvin family includes alpha-parvin, beta-parvin, and gamma-parvin. Alpha-parvin, also called actopaxin, calponin-like integrin-linked kinase-binding protein (CH-ILKBP), or matrix-remodeling-associated protein 2, plays a role in sarcomere organization and in smooth muscle cell contraction. It is required for normal development of the embryonic cardiovascular system, and for normal septation of the heart outflow tract. Beta-parvin, also called affixin, is an adapter protein that plays a role in integrin signaling via ILK and in activation of the GTPases Cdc42 and Rac1 by guanine exchange factors, such as ARHGEF6. Both alpha-parvin and beta-parvin are involved in the reorganization of the actin cytoskeleton and the formation of lamellipodia, and both play roles in cell adhesion, cell spreading, establishment or maintenance of cell polarity, and cell migration. Gamma-parvin probably plays a role in the regulation of cell adhesion and cytoskeleton organization. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409071  Cd Length: 121  Bit Score: 38.34  E-value: 7.93e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1907075186    1 MIENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL-SRY 45
Cdd:cd21222     76 KLHNVKLALELMEDAGISTPKIRPEDIVNGDLKSILRVLYSLfSKY 121
AAA_7 pfam12775
P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 ...
 1873-1913 8.08e-03

P-loop containing dynein motor region; This domain is found in human cytoplasmic dynein-2 proteins. Cytoplasmic dynein-2 (dynein-2) performs intraflagellar transport and is associated with human skeletal ciliopathies. Dyneins share a conserved motor domain that couples cycles of ATP hydrolysis with conformational changes to produce movement. Structural analysis reveal that the motor's ring consists of six AAA+ domains (ATPases associated with various cellular activities (AAA1-AAA6). This is the third nucleotide binding sites in the dynein motor. However, AAA3 has lost the catalytic residues necessary for ATP hydrolysis (the Walker B glutamate, the arginine finger, sensor-I and sensor-II motifs).


Pssm-ID: 463698 [Multi-domain]  Cd Length: 179  Bit Score: 39.68  E-value: 8.08e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907075186 1873 VFDTLIPKPITQRY---FNLLMEHHR-IILSGPSGTGKTYLANKL 1913
Cdd:pfam12775    7 FSEILVPTVDTVRYtylLDLLLKNGKpVLLVGPTGTGKTVIIQNL 51
CH_CTX_rpt1 cd21225
first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling ...
 1-44 9.31e-03

first calponin homology (CH) domain found in cortexillin; Cortexillins are actin-bundling proteins that play a critical role in regulating cell morphology and actin cytoskeleton reorganization. They play a major role in cytokinesis and 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: 409074  Cd Length: 111  Bit Score: 37.90  E-value: 9.31e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1907075186    1 MIENVDVCLSFLAAR-GVNVQGLSAEEIRNGNLKAILGLFFSLSR 44
Cdd:cd21225     64 MIQNLHLAMLFIEEDlKIRVQGIGAEDFVDNNKKLILGLLWTLYR 108
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 1896-1988 9.38e-03

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 39.19  E-value: 9.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907075186 1896 IILSGPSGTGKTYLANKLAEY----VITKSGRKKTEDAIAtfnvdhKSSKELQQyLANLAEQCSadnngvelPVVIILD- 1970
Cdd:cd19481     29 ILLYGPPGTGKTLLAKALAGElglpLIVVKLSSLLSKYVG------ESEKNLRK-IFERARRLA--------PCILFIDe 93

                           90       100
                   ....*....|....*....|....*..
gi 1907075186 1971 ---------NLHHVGSLSDIFNGFLNC 1988
Cdd:cd19481     94 idaigrkrdSSGESGELRRVLNQLLTE 120
DnaC COG1484
DNA replication protein DnaC [Replication, recombination and repair];
1868-1910 9.69e-03

DNA replication protein DnaC [Replication, recombination and repair];


Pssm-ID: 441093 [Multi-domain]  Cd Length: 242  Bit Score: 40.15  E-value: 9.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907075186 1868 SLDSFVFDTliPKPITQRYFNLL-----MEHHR-IILSGPSGTGKTYLA 1910
Cdd:COG1484     70 TLEDFDFDA--QPGLDRRQILELatldfIERGEnLILLGPPGTGKTHLA 116
CH_FLN_rpt1 cd21228
first calponin homology (CH) domain found in filamins; The filamin family includes filamin-A ...
 2-42 9.93e-03

first calponin homology (CH) domain found in filamins; 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. Members of this family contain two copies of the CH domain. The model corresponds to the first CH domain. CH domains are actin filament (F-actin) binding motifs.


Pssm-ID: 409077  Cd Length: 108  Bit Score: 37.85  E-value: 9.93e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1907075186    2 IENVDVCLSFLAARGVNVQGLSAEEIRNGNLKAILGLFFSL 42
Cdd:cd21228     64 LENVSVALEFLERESIKLVSIDSSAIVDGNLKLILGLIWTL 104
 
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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