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Conserved domains on  [gi|568915500|ref|XP_006498843|]
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protein GNAS isoform X7 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
780-1112 0e+00

Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins contains the guanine nucleotide binding site. The heterotrimeric GNP-binding proteins are signal transducers that communicate signals from many hormones, neurotransmitters, chemokines, and autocrine and paracrine factors. Extracellular signals are received by receptors, which activate the G proteins, which in turn route the signals to several distinct intracellular signaling pathways. The alpha subunit of G proteins is a weak GTPase. In the resting state, heterotrimeric G proteins are associated at the cytosolic face of the plasma membrane and the alpha subunit binds to GDP. Upon activation by a receptor GDP is replaced with GTP, and the G-alpha/GTP complex dissociates from the beta and gamma subunits. This results in activation of downstream signaling pathways, such as cAMP synthesis by adenylyl cyclase, which is terminated when GTP is hydrolized and the heterotrimers reconstitute.


:

Pssm-ID: 206639 [Multi-domain]  Cd Length: 315  Bit Score: 535.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  780 HRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLVPPveLANPENQFRVDYILSVM 859
Cdd:cd00066     1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIP--YGDPENEKDAKKILSLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  860 N-VPNFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQV 938
Cdd:cd00066    79 PrAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIETDFSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  939 DKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQ 1018
Cdd:cd00066   159 KNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILFLNKK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500 1019 DLLAEKVLagKSKIEDYFPEFaryttpedatpePGEDPRVTRAKYFIRDEFLRISTasgDGRHYCYPHFTCAVDTENIRR 1098
Cdd:cd00066   239 DLFEEKIK--KSPLTDYFPDY------------TGPPNDYEEAAKYIKKKFLDLNR---NPNKEIYPHFTCATDTENIRF 301
                         330
                  ....*....|....
gi 568915500 1099 VFNDCRDIIQRMHL 1112
Cdd:cd00066   302 VFDAVKDIILQNNL 315
PRK12323 super family cl46901
DNA polymerase III subunit gamma/tau;
330-531 2.36e-06

DNA polymerase III subunit gamma/tau;


The actual alignment was detected with superfamily member PRK12323:

Pssm-ID: 481241 [Multi-domain]  Cd Length: 700  Bit Score: 51.80  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  330 SPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGS 409
Cdd:PRK12323  390 AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  410 DAGAPTDSAMlTDSQSDAGEDGTAPGTPSDLQSDPEELEEAPAVRADPdggaapvapaTPAESESEGSRDPAAEPASEAV 489
Cdd:PRK12323  470 RPVAAAAAAA-PARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA----------APAGWVAESIPDPATADPDDAF 538
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915500  490 PATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPITPKE 531
Cdd:PRK12323  539 ETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580
PHA03247 super family cl33720
large tegument protein UL36; Provisional
50-496 4.61e-06

large tegument protein UL36; Provisional


The actual alignment was detected with superfamily member PHA03247:

Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   50 ATEPDSEPSNNEPVPDETGS--EISGPPEDSKSDIQSPCQAFEEVRVGGDYSPPPEEAMPFETQQP-------SLGDFW- 119
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPhpPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgSLTSLAd 2700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  120 PTLEQPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAY--TPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVP 197
Cdd:PHA03247 2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApaPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  198 RALPAEPG---NIRFENAGFREDYSPPPEESVPfqVGGEEFGGDSPPPGLPRvipqigiggefPTVAVPSALCLAPAENA 274
Cdd:PHA03247 2781 RRLTRPAVaslSESRESLPSPWDPADPPAAVLA--PAAALPPAASPAGPLPP-----------PTSAQPTAPPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  275 PPLWVRGAI----DRPFREAVRSPPNFACDS---PPMEITRPLLEIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPD 347
Cdd:PHA03247 2848 PSLPLGGSVapggDVRRRPPSRSPAAKPAAParpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  348 KSECAERPPvEREAAEMEGSPTTATAVE--GKVPSPERG---DGSSTQPEAMDAKPAPA--AQAVSTGSDAGAPtDSAML 420
Cdd:PHA03247 2928 QPQPPPPPP-PRPQPPLAPTTDPAGAGEpsGAVPQPWLGalvPGRVAVPRFRVPQPAPSreAPASSTPPLTGHS-LSRVS 3005
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  421 TDSQSDAGEDGTAPGTPSDLQ------------------SDPEELEEAPAVRADPDGGAAPVAPATPAESESEGSRDPAA 482
Cdd:PHA03247 3006 SWASSLALHEETDPPPVSLKQtlwppddtedsdadslfdSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSS 3085
                         490
                  ....*....|....
gi 568915500  483 EPASEAVPATTAES 496
Cdd:PHA03247 3086 QFGPPPLSANAALS 3099
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
730-772 1.17e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


:

Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 38.40  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568915500  730 PGKAKdpmEERRKQMRKEAIEMREQKRADKKRSKLIDKQLEEE 772
Cdd:cd22249     4 PGEIR---EEYEAQLKKLEEERRKEREEEEKASEELIRKLQEE 43
 
Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
780-1112 0e+00

Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins contains the guanine nucleotide binding site. The heterotrimeric GNP-binding proteins are signal transducers that communicate signals from many hormones, neurotransmitters, chemokines, and autocrine and paracrine factors. Extracellular signals are received by receptors, which activate the G proteins, which in turn route the signals to several distinct intracellular signaling pathways. The alpha subunit of G proteins is a weak GTPase. In the resting state, heterotrimeric G proteins are associated at the cytosolic face of the plasma membrane and the alpha subunit binds to GDP. Upon activation by a receptor GDP is replaced with GTP, and the G-alpha/GTP complex dissociates from the beta and gamma subunits. This results in activation of downstream signaling pathways, such as cAMP synthesis by adenylyl cyclase, which is terminated when GTP is hydrolized and the heterotrimers reconstitute.


Pssm-ID: 206639 [Multi-domain]  Cd Length: 315  Bit Score: 535.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  780 HRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLVPPveLANPENQFRVDYILSVM 859
Cdd:cd00066     1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIP--YGDPENEKDAKKILSLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  860 N-VPNFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQV 938
Cdd:cd00066    79 PrAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIETDFSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  939 DKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQ 1018
Cdd:cd00066   159 KNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILFLNKK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500 1019 DLLAEKVLagKSKIEDYFPEFaryttpedatpePGEDPRVTRAKYFIRDEFLRISTasgDGRHYCYPHFTCAVDTENIRR 1098
Cdd:cd00066   239 DLFEEKIK--KSPLTDYFPDY------------TGPPNDYEEAAKYIKKKFLDLNR---NPNKEIYPHFTCATDTENIRF 301
                         330
                  ....*....|....
gi 568915500 1099 VFNDCRDIIQRMHL 1112
Cdd:cd00066   302 VFDAVKDIILQNNL 315
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
759-1115 5.39e-171

G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding site


Pssm-ID: 214595 [Multi-domain]  Cd Length: 342  Bit Score: 505.96  E-value: 5.39e-171
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    759 KKRSKLIDKQLEEEKMDYMCTHRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLV 838
Cdd:smart00275    1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    839 PPVElaNPENQFRVDYILSVMNVPN---FDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYV 915
Cdd:smart00275   81 IPFE--DPESILDIRIITEQFNKTDeteNVLPKEIAKAIKALWKDEGIQECYRRRNEFQLNDSASYFLDNIDRIGDPDYV 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    916 PSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALN 995
Cdd:smart00275  159 PTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESLN 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    996 LFKSIWNNRWLRTISVILFLNKQDLLAEKVLagKSKIEDYFPEFaryttpedatpepGEDPRVTRAKYFIRDEFLRISTa 1075
Cdd:smart00275  239 LFESICNSRWFANTSIILFLNKIDLFEEKIK--KVPLVDYFPDY-------------KGPNDYEAAAKFIKQKFLRLNR- 302
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|
gi 568915500   1076 sGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQY 1115
Cdd:smart00275  303 -NSSRKSIYHHFTCATDTRNIRVVFDAVKDIILQRNLKDA 341
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
779-1107 1.95e-142

G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular signaling pathways. The G protein alpha subunit binds guanyl nucleotide and is a weak GTPase. A set of residues that are unique to G-alpha as compared to its ancestor the Arf-like family form a ring of residues centered on the nucleotide binding site. A Ggamma is found fused to an inactive Galpha in the Dictyostelium protein gbqA.


Pssm-ID: 459835 [Multi-domain]  Cd Length: 316  Bit Score: 430.86  E-value: 1.95e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   779 THRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLvpPVELANPENQFRVDYILSV 858
Cdd:pfam00503    5 EVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERL--GIELSNPENKERLDDLLSL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   859 MNVPNFD--FPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKF 936
Cdd:pfam00503   83 DSSLKNEteFTPELAEDIKRLWNDPGIQECYERRNEFQLPDSAEYFLDNLDRIASPDYVPTDQDILRARVKTTGIIETKF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   937 QVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLN 1016
Cdd:pfam00503  163 EFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDQVLYEDDSTNRMEESLKLFEEICNSPWFKNTPIILFLN 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  1017 KQDLLAEKVlaGKSKIEDYFPEFAryttpedatpepGEDPRVTRAKYFIRDEFLRISTasgDGRHYCYPHFTCAVDTENI 1096
Cdd:pfam00503  243 KKDLFEEKL--KKSPLSDYFPDYT------------GNPNDYEEALKYIRNKFLDLNK---NPNRKIYTHFTCATDTENI 305
                          330
                   ....*....|.
gi 568915500  1097 RRVFNDCRDII 1107
Cdd:pfam00503  306 RFVFDAVKDII 316
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
330-531 2.36e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.80  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  330 SPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGS 409
Cdd:PRK12323  390 AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  410 DAGAPTDSAMlTDSQSDAGEDGTAPGTPSDLQSDPEELEEAPAVRADPdggaapvapaTPAESESEGSRDPAAEPASEAV 489
Cdd:PRK12323  470 RPVAAAAAAA-PARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA----------APAGWVAESIPDPATADPDDAF 538
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915500  490 PATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPITPKE 531
Cdd:PRK12323  539 ETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
931-1038 2.72e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 48.82  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  931 IFETKFQVD--KVNFHMFDVGGQ---RDERRKWIQCFNDVTAIIFVVASSsynmviREDNqTNRLQEALNLFKSIwnnrw 1005
Cdd:COG1100    41 IDKKELKLDglDVDLVIWDTPGQdefRETRQFYARQLTGASLYLFVVDGT------REET-LQSLYELLESLRRL----- 108
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915500 1006 LRTISVILFLNKQDLLAEKVLAGKSKIEDYFPE 1038
Cdd:COG1100   109 GKKSPIILVLNKIDLYDEEEIEDEERLKEALSE 141
PHA03247 PHA03247
large tegument protein UL36; Provisional
50-496 4.61e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   50 ATEPDSEPSNNEPVPDETGS--EISGPPEDSKSDIQSPCQAFEEVRVGGDYSPPPEEAMPFETQQP-------SLGDFW- 119
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPhpPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgSLTSLAd 2700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  120 PTLEQPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAY--TPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVP 197
Cdd:PHA03247 2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApaPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  198 RALPAEPG---NIRFENAGFREDYSPPPEESVPfqVGGEEFGGDSPPPGLPRvipqigiggefPTVAVPSALCLAPAENA 274
Cdd:PHA03247 2781 RRLTRPAVaslSESRESLPSPWDPADPPAAVLA--PAAALPPAASPAGPLPP-----------PTSAQPTAPPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  275 PPLWVRGAI----DRPFREAVRSPPNFACDS---PPMEITRPLLEIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPD 347
Cdd:PHA03247 2848 PSLPLGGSVapggDVRRRPPSRSPAAKPAAParpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  348 KSECAERPPvEREAAEMEGSPTTATAVE--GKVPSPERG---DGSSTQPEAMDAKPAPA--AQAVSTGSDAGAPtDSAML 420
Cdd:PHA03247 2928 QPQPPPPPP-PRPQPPLAPTTDPAGAGEpsGAVPQPWLGalvPGRVAVPRFRVPQPAPSreAPASSTPPLTGHS-LSRVS 3005
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  421 TDSQSDAGEDGTAPGTPSDLQ------------------SDPEELEEAPAVRADPDGGAAPVAPATPAESESEGSRDPAA 482
Cdd:PHA03247 3006 SWASSLALHEETDPPPVSLKQtlwppddtedsdadslfdSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSS 3085
                         490
                  ....*....|....
gi 568915500  483 EPASEAVPATTAES 496
Cdd:PHA03247 3086 QFGPPPLSANAALS 3099
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
941-1020 5.09e-06

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 48.04  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  941 VNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASssynmviredNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDL 1020
Cdd:PLN00223   61 ISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDS----------NDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDL 130
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
308-542 1.64e-04

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 45.61  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  308 RPLLEIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPErgdgs 387
Cdd:COG3266   149 LTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVAAA----- 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  388 stqPEAMDAKPAPAAQAVSTGSDAGAPTDSAMLTDSQSDAGEDGTAPGTPSDLQsdPEELEEAPAVRADPdggaapvapa 467
Cdd:COG3266   224 ---AELAALALLAAGAAEVLTARLVLLLLIIGSALKAPSQASSASAPATTSLGE--QQEVSLPPAVAAQP---------- 288
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915500  468 tpaesesegSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPiTPKEPTTRAVPSARA 542
Cdd:COG3266   289 ---------AAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAP-APEAAAAAAAPAAPA 353
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
933-1041 1.15e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 40.82  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   933 ETKFQVD--KVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYnmVIR-EDNQTNRLQEALNLFKSiwnnrwlrTI 1009
Cdd:TIGR00231   41 TTVIEEDgkTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVIL--VLDvEEILEKQTKEIIHHADS--------GV 110
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568915500  1010 SVILFLNKQDLLAEKV------LAGKSKIEDYFPEFAR 1041
Cdd:TIGR00231  111 PIILVGNKIDLKDADLkthvasEFAKLNGEPIIPLSAE 148
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
730-772 1.17e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 38.40  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568915500  730 PGKAKdpmEERRKQMRKEAIEMREQKRADKKRSKLIDKQLEEE 772
Cdd:cd22249     4 PGEIR---EEYEAQLKKLEEERRKEREEEEKASEELIRKLQEE 43
 
Name Accession Description Interval E-value
G-alpha cd00066
Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins ...
780-1112 0e+00

Alpha subunit of G proteins (guanine nucleotide binding); The alpha subunit of G proteins contains the guanine nucleotide binding site. The heterotrimeric GNP-binding proteins are signal transducers that communicate signals from many hormones, neurotransmitters, chemokines, and autocrine and paracrine factors. Extracellular signals are received by receptors, which activate the G proteins, which in turn route the signals to several distinct intracellular signaling pathways. The alpha subunit of G proteins is a weak GTPase. In the resting state, heterotrimeric G proteins are associated at the cytosolic face of the plasma membrane and the alpha subunit binds to GDP. Upon activation by a receptor GDP is replaced with GTP, and the G-alpha/GTP complex dissociates from the beta and gamma subunits. This results in activation of downstream signaling pathways, such as cAMP synthesis by adenylyl cyclase, which is terminated when GTP is hydrolized and the heterotrimers reconstitute.


Pssm-ID: 206639 [Multi-domain]  Cd Length: 315  Bit Score: 535.57  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  780 HRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLVPPveLANPENQFRVDYILSVM 859
Cdd:cd00066     1 VKLLLLGAGESGKSTILKQMKILHGNGFSDEERREFRPVIYSNILQSMKALLRAMETLNIP--YGDPENEKDAKKILSLA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  860 N-VPNFDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKFQV 938
Cdd:cd00066    79 PrAEEGPLPPELAEAIKRLWKDPGIQACYDRRNEYQLNDSAKYFLDNLDRISDPDYIPTEQDILRSRVKTTGIIETDFSI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  939 DKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQ 1018
Cdd:cd00066   159 KNLKFRMFDVGGQRSERKKWIHCFEDVTAIIFVVALSEYDQVLVEDESVNRMQESLKLFDSICNSRWFANTSIILFLNKK 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500 1019 DLLAEKVLagKSKIEDYFPEFaryttpedatpePGEDPRVTRAKYFIRDEFLRISTasgDGRHYCYPHFTCAVDTENIRR 1098
Cdd:cd00066   239 DLFEEKIK--KSPLTDYFPDY------------TGPPNDYEEAAKYIKKKFLDLNR---NPNKEIYPHFTCATDTENIRF 301
                         330
                  ....*....|....
gi 568915500 1099 VFNDCRDIIQRMHL 1112
Cdd:cd00066   302 VFDAVKDIILQNNL 315
G_alpha smart00275
G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding ...
759-1115 5.39e-171

G protein alpha subunit; Subunit of G proteins that contains the guanine nucleotide binding site


Pssm-ID: 214595 [Multi-domain]  Cd Length: 342  Bit Score: 505.96  E-value: 5.39e-171
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    759 KKRSKLIDKQLEEEKMDYMCTHRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLV 838
Cdd:smart00275    1 IRRNKEIEKQLEEERKKKKREVKLLLLGAGESGKSTILKQMRILHGDGFSQEERREYRPLIYSNILESMKALVDAMEELN 80
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    839 PPVElaNPENQFRVDYILSVMNVPN---FDFPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYV 915
Cdd:smart00275   81 IPFE--DPESILDIRIITEQFNKTDeteNVLPKEIAKAIKALWKDEGIQECYRRRNEFQLNDSASYFLDNIDRIGDPDYV 158
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    916 PSDQDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALN 995
Cdd:smart00275  159 PTEQDILRSRVPTTGIQETAFIVKKLFFRMFDVGGQRSERKKWIHCFDNVTAIIFCVALSEYDQVLEEDESTNRMQESLN 238
                           250       260       270       280       290       300       310       320
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    996 LFKSIWNNRWLRTISVILFLNKQDLLAEKVLagKSKIEDYFPEFaryttpedatpepGEDPRVTRAKYFIRDEFLRISTa 1075
Cdd:smart00275  239 LFESICNSRWFANTSIILFLNKIDLFEEKIK--KVPLVDYFPDY-------------KGPNDYEAAAKFIKQKFLRLNR- 302
                           330       340       350       360
                    ....*....|....*....|....*....|....*....|
gi 568915500   1076 sGDGRHYCYPHFTCAVDTENIRRVFNDCRDIIQRMHLRQY 1115
Cdd:smart00275  303 -NSSRKSIYHHFTCATDTRNIRVVFDAVKDIILQRNLKDA 341
G-alpha pfam00503
G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular ...
779-1107 1.95e-142

G-protein alpha subunit; G proteins couple receptors of extracellular signals to intracellular signaling pathways. The G protein alpha subunit binds guanyl nucleotide and is a weak GTPase. A set of residues that are unique to G-alpha as compared to its ancestor the Arf-like family form a ring of residues centered on the nucleotide binding site. A Ggamma is found fused to an inactive Galpha in the Dictyostelium protein gbqA.


Pssm-ID: 459835 [Multi-domain]  Cd Length: 316  Bit Score: 430.86  E-value: 1.95e-142
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   779 THRLLLLGAGESGKSTIVKQMRILHVNGFNGDEKATKVQDIKNNLKEAIETIVAAMSNLvpPVELANPENQFRVDYILSV 858
Cdd:pfam00503    5 EVKLLLLGAGESGKSTILKQMKIIHGGGFSEEERKQYRPVIYSNILRSLKTLIEAMERL--GIELSNPENKERLDDLLSL 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   859 MNVPNFD--FPPEFYEHAKALWEDEGVRACYERSNEYQLIDCAQYFLDKIDVIKQADYVPSDQDLLRCRVLTSGIFETKF 936
Cdd:pfam00503   83 DSSLKNEteFTPELAEDIKRLWNDPGIQECYERRNEFQLPDSAEYFLDNLDRIASPDYVPTDQDILRARVKTTGIIETKF 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   937 QVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYNMVIREDNQTNRLQEALNLFKSIWNNRWLRTISVILFLN 1016
Cdd:pfam00503  163 EFKGLKFRLFDVGGQRSERKKWIHCFEDVTAIIFVVSLSEYDQVLYEDDSTNRMEESLKLFEEICNSPWFKNTPIILFLN 242
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  1017 KQDLLAEKVlaGKSKIEDYFPEFAryttpedatpepGEDPRVTRAKYFIRDEFLRISTasgDGRHYCYPHFTCAVDTENI 1096
Cdd:pfam00503  243 KKDLFEEKL--KKSPLSDYFPDYT------------GNPNDYEEALKYIRNKFLDLNK---NPNRKIYTHFTCATDTENI 305
                          330
                   ....*....|.
gi 568915500  1097 RRVFNDCRDII 1107
Cdd:pfam00503  306 RFVFDAVKDII 316
Arf_Arl cd00878
ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl ...
928-1022 1.31e-12

ADP-ribosylation factor(Arf)/Arf-like (Arl) small GTPases; Arf (ADP-ribosylation factor)/Arl (Arf-like) small GTPases. Arf proteins are activators of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. Arfs are N-terminally myristoylated. Members of the Arf family are regulators of vesicle formation in intracellular traffic that interact reversibly with membranes of the secretory and endocytic compartments in a GTP-dependent manner. They depart from other small GTP-binding proteins by a unique structural device, interswitch toggle, that implements front-back communication from N-terminus to the nucleotide binding site. Arf-like (Arl) proteins are close relatives of the Arf, but only Arl1 has been shown to function in membrane traffic like the Arf proteins. Arl2 has an unrelated function in the folding of native tubulin, and Arl4 may function in the nucleus. Most other Arf family proteins are so far relatively poorly characterized. Thus, despite their significant sequence homologies, Arf family proteins may regulate unrelated functions.


Pssm-ID: 206644 [Multi-domain]  Cd Length: 158  Bit Score: 66.83  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  928 TSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSynmviREdnqtnRLQEALNLFKSIWNNRWLR 1007
Cdd:cd00878    30 TIGFNVETVEYKNVKFTVWDVGGQDKIRPLWKHYYENTDGLIFVVDSSD-----RE-----RIEEAKNELHKLLNEEELK 99
                          90
                  ....*....|....*
gi 568915500 1008 TISVILFLNKQDLLA 1022
Cdd:cd00878   100 GAPLLILANKQDLPG 114
Arf pfam00025
ADP-ribosylation factor family; Pfam combines a number of different Prosite families together
937-1020 3.05e-11

ADP-ribosylation factor family; Pfam combines a number of different Prosite families together


Pssm-ID: 459636 [Multi-domain]  Cd Length: 160  Bit Score: 63.01  E-value: 3.05e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   937 QVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSynmvirednqTNRLQEALNLFKSIWNNRWLRTISVILFLN 1016
Cdd:pfam00025   40 TYKNVKFTVWDVGGQESLRPLWRNYFPNTDAVIFVVDSAD----------RDRIEEAKEELHALLNEEELADAPLLILAN 109

                   ....
gi 568915500  1017 KQDL 1020
Cdd:pfam00025  110 KQDL 113
Arfrp1 cd04160
Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a ...
937-1020 3.56e-08

Arf-related protein 1 (Arfrp1); Arfrp1 (Arf-related protein 1), formerly known as ARP, is a membrane-associated Arf family member that lacks the N-terminal myristoylation motif. Arfrp1 is mainly associated with the trans-Golgi compartment and the trans-Golgi network, where it regulates the targeting of Arl1 and the GRIP domain-containing proteins, golgin-97 and golgin-245, onto Golgi membranes. It is also involved in the anterograde transport of the vesicular stomatitis virus G protein from the Golgi to the plasma membrane, and in the retrograde transport of TGN38 and Shiga toxin from endosomes to the trans-Golgi network. Arfrp1 also inhibits Arf/Sec7-dependent activation of phospholipase D. Deletion of Arfrp1 in mice causes embryonic lethality at the gastrulation stage and apoptosis of mesodermal cells, indicating its importance in development.


Pssm-ID: 206725 [Multi-domain]  Cd Length: 168  Bit Score: 54.27  E-value: 3.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  937 QVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSsynmviREDnqtnRLQEALNLFKSIWNNRWLRTISVILFLN 1016
Cdd:cd04160    47 EVGKARLMFWDLGGQEELRSLWDKYYAESHGVIYVIDST------DRE----RFNESKSAFEKVINNEALEGVPLLVLAN 116

                  ....
gi 568915500 1017 KQDL 1020
Cdd:cd04160   117 KQDL 120
Arf6 cd04149
ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins ...
941-1020 5.84e-08

ADP ribosylation factor 6 (Arf6); Arf6 subfamily. Arf6 (ADP ribosylation factor 6) proteins localize to the plasma membrane, where they perform a wide variety of functions. In its active, GTP-bound form, Arf6 is involved in cell spreading, Rac-induced formation of plasma membrane ruffles, cell migration, wound healing, and Fc-mediated phagocytosis. Arf6 appears to change the actin structure at the plasma membrane by activating Rac, a Rho family protein involved in membrane ruffling. Arf6 is required for and enhances Rac formation of ruffles. Arf6 can regulate dendritic branching in hippocampal neurons, and in yeast it localizes to the growing bud, where it plays a role in polarized growth and bud site selection. In leukocytes, Arf6 is required for chemokine-stimulated migration across endothelial cells. Arf6 also plays a role in down-regulation of beta2-adrenergic receptors and luteinizing hormone receptors by facilitating the release of sequestered arrestin to allow endocytosis. Arf6 is believed to function at multiple sites on the plasma membrane through interaction with a specific set of GEFs, GAPs, and effectors. Arf6 has been implicated in breast cancer and melanoma cell invasion, and in actin remodelling at the invasion site of Chlamydia infection.


Pssm-ID: 206716  Cd Length: 168  Bit Score: 53.62  E-value: 5.84e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  941 VNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYnmvirednqtNRLQEALNLFKSIWNNRWLRTISVILFLNKQDL 1020
Cdd:cd04149    53 VKFNVWDVGGQDKIRPLWRHYYTGTQGLIFVVDSADR----------DRIDEARQELHRIINDREMRDALLLVFANKQDL 122
Arf1_5_like cd04150
ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like ...
936-1020 1.11e-07

ADP-ribosylation factor-1 (Arf1) and ADP-ribosylation factor-5 (Arf5); The Arf1-Arf5-like subfamily contains Arf1, Arf2, Arf3, Arf4, Arf5, and related proteins. Arfs1-5 are soluble proteins that are crucial for assembling coat proteins during vesicle formation. Each contains an N-terminal myristoylated amphipathic helix that is folded into the protein in the GDP-bound state. GDP/GTP exchange exposes the helix, which anchors to the membrane. Following GTP hydrolysis, the helix dissociates from the membrane and folds back into the protein. A general feature of Arf1-5 signaling may be the cooperation of two Arfs at the same site. Arfs1-5 are generally considered to be interchangeable in function and location, but some specific functions have been assigned. Arf1 localizes to the early/cis-Golgi, where it is activated by GBF1 and recruits the coat protein COPI. It also localizes to the trans-Golgi network (TGN), where it is activated by BIG1/BIG2 and recruits the AP1, AP3, AP4, and GGA proteins. Humans, but not rodents and other lower eukaryotes, lack Arf2. Human Arf3 shares 96% sequence identity with Arf1 and is believed to generally function interchangeably with Arf1. Human Arf4 in the activated (GTP-bound) state has been shown to interact with the cytoplasmic domain of epidermal growth factor receptor (EGFR) and mediate the EGF-dependent activation of phospholipase D2 (PLD2), leading to activation of the activator protein 1 (AP-1) transcription factor. Arf4 has also been shown to recognize the C-terminal sorting signal of rhodopsin and regulate its incorporation into specialized post-Golgi rhodopsin transport carriers (RTCs). There is some evidence that Arf5 functions at the early-Golgi and the trans-Golgi to affect Golgi-associated alpha-adaptin homology Arf-binding proteins (GGAs).


Pssm-ID: 206717 [Multi-domain]  Cd Length: 159  Bit Score: 52.41  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  936 FQVDKV-----NFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASssynmviredNQTNRLQEALNLFKSIWNNRWLRTIS 1010
Cdd:cd04150    34 FNVETVeykniSFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDS----------NDRERIGEAREELQRMLNEDELRDAV 103
                          90
                  ....*....|
gi 568915500 1011 VILFLNKQDL 1020
Cdd:cd04150   104 LLVFANKQDL 113
ARLTS1 cd04156
Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), ...
940-1020 2.79e-07

Arf-like tumor suppressor gene 1 (ARLTS1 or Arl11); ARLTS1 (Arf-like tumor suppressor gene 1), also known as Arl11, is a member of the Arf family of small GTPases that is believed to play a major role in apoptotic signaling. ARLTS1 is widely expressed and functions as a tumor suppressor gene in several human cancers. ARLTS1 is a low-penetrance suppressor that accounts for a small percentage of familial melanoma or familial chronic lymphocytic leukemia (CLL). ARLTS1 inactivation seems to occur most frequently through biallelic down-regulation by hypermethylation of the promoter. In breast cancer, ARLTS1 alterations were typically a combination of a hypomorphic polymorphism plus loss of heterozygosity. In a case of thyroid adenoma, ARLTS1 alterations were polymorphism plus promoter hypermethylation. The nonsense polymorphism Trp149Stop occurs with significantly greater frequency in familial cancer cases than in sporadic cancer cases, and the Cys148Arg polymorphism is associated with an increase in high-risk familial breast cancer.


Pssm-ID: 133356 [Multi-domain]  Cd Length: 160  Bit Score: 51.26  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  940 KVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYnmvirednqtNRLQEALNLFKSIWNNRWLRTISVILFLNKQD 1019
Cdd:cd04156    43 HLSLTVWDVGGQEKMRTVWKCYLENTDGLVYVVDSSDE----------ARLDESQKELKHILKNEHIKGVPVVLLANKQD 112

                  .
gi 568915500 1020 L 1020
Cdd:cd04156   113 L 113
Arl3 cd04155
Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most ...
929-1021 4.80e-07

Arf-like 3 (Arl3) GTPase; Arl3 (Arf-like 3) is an Arf family protein that differs from most Arf family members in the N-terminal extension. In is inactive, GDP-bound form, the N-terminal extension forms an elongated loop that is hydrophobically anchored into the membrane surface; however, it has been proposed that this region might form a helix in the GTP-bound form. The delta subunit of the rod-specific cyclic GMP phosphodiesterase type 6 (PDEdelta) is an Arl3 effector. Arl3 binds microtubules in a regulated manner to alter specific aspects of cytokinesis via interactions with retinitis pigmentosa 2 (RP2). It has been proposed that RP2 functions in concert with Arl3 to link the cell membrane and the cytoskeleton in photoreceptors as part of the cell signaling or vesicular transport machinery. In mice, the absence of Arl3 is associated with abnormal epithelial cell proliferation and cyst formation.


Pssm-ID: 206721 [Multi-domain]  Cd Length: 174  Bit Score: 50.86  E-value: 4.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  929 SGIFETK-FQVDKVN-----FHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSynmvirednqTNRLQEALNLFKSIWN 1002
Cdd:cd04155    41 SHITPTQgFNIKNVQadgfkLNVWDIGGQRKIRPYWRNYFENTDVLIYVIDSAD----------RKRFEEAGQELVELLE 110
                          90
                  ....*....|....*....
gi 568915500 1003 NRWLRTISVILFLNKQDLL 1021
Cdd:cd04155   111 EEKLAGVPVLVFANKQDLL 129
Arl2l1_Arl13_like cd04161
Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a ...
928-1038 8.12e-07

Arl2-like protein 1 (Arl2l1) and Arl13; Arl2l1 (Arl2-like protein 1) and Arl13 form a subfamily of the Arf family of small GTPases. Arl2l1 was identified in human cells during a search for the gene(s) responsible for Bardet-Biedl syndrome (BBS). Like Arl6, the identified BBS gene, Arl2l1 is proposed to have cilia-specific functions. Arl13 is found on the X chromosome, but its expression has not been confirmed; it may be a pseudogene.


Pssm-ID: 133361 [Multi-domain]  Cd Length: 167  Bit Score: 50.08  E-value: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  928 TSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSsynmvireDNQtnRLQEALNLFKSIWNNRWLR 1007
Cdd:cd04161    30 TVGFTPTKLRLDKYEVCIFDLGGGANFRGIWVNYYAEAHGLVFVVDSS--------DDD--RVQEVKEILRELLQHPRVS 99
                          90       100       110
                  ....*....|....*....|....*....|.
gi 568915500 1008 TISVILFLNKQDLlaEKVLAGKSKIEDYFPE 1038
Cdd:cd04161   100 GKPILVLANKQDK--KNALLGADVIEYLSLE 128
ARF smart00177
ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular ...
937-1020 1.16e-06

ARF-like small GTPases; ARF, ADP-ribosylation factor; Ras homologues involved in vesicular transport. Activator of phospholipase D isoforms. Unlike Ras proteins they lack cysteine residues at their C-termini and therefore are unlikely to be prenylated. ARFs are N-terminally myristoylated. Contains ATP/GTP-binding motif (P-loop).


Pssm-ID: 128474 [Multi-domain]  Cd Length: 175  Bit Score: 49.92  E-value: 1.16e-06
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500    937 QVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASssynmviredNQTNRLQEALNLFKSIWNNRWLRTISVILFLN 1016
Cdd:smart00177   53 TYKNISFTVWDVGGQDKIRPLWRHYYTNTQGLIFVVDS----------NDRDRIDEAREELHRMLNEDELRDAVILVFAN 122

                    ....
gi 568915500   1017 KQDL 1020
Cdd:smart00177  123 KQDL 126
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
330-531 2.36e-06

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 51.80  E-value: 2.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  330 SPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGS 409
Cdd:PRK12323  390 AAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAAARQASARGPGGAPAPAPAPAAAPAAAARPAAAGP 469
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  410 DAGAPTDSAMlTDSQSDAGEDGTAPGTPSDLQSDPEELEEAPAVRADPdggaapvapaTPAESESEGSRDPAAEPASEAV 489
Cdd:PRK12323  470 RPVAAAAAAA-PARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDA----------APAGWVAESIPDPATADPDDAF 538
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 568915500  490 PATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPITPKE 531
Cdd:PRK12323  539 ETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPDMFDGD 580
Gem1 COG1100
GTPase SAR1 family domain [General function prediction only];
931-1038 2.72e-06

GTPase SAR1 family domain [General function prediction only];


Pssm-ID: 440717 [Multi-domain]  Cd Length: 177  Bit Score: 48.82  E-value: 2.72e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  931 IFETKFQVD--KVNFHMFDVGGQ---RDERRKWIQCFNDVTAIIFVVASSsynmviREDNqTNRLQEALNLFKSIwnnrw 1005
Cdd:COG1100    41 IDKKELKLDglDVDLVIWDTPGQdefRETRQFYARQLTGASLYLFVVDGT------REET-LQSLYELLESLRRL----- 108
                          90       100       110
                  ....*....|....*....|....*....|...
gi 568915500 1006 LRTISVILFLNKQDLLAEKVLAGKSKIEDYFPE 1038
Cdd:COG1100   109 GKKSPIILVLNKIDLYDEEEIEDEERLKEALSE 141
PHA03247 PHA03247
large tegument protein UL36; Provisional
50-496 4.61e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   50 ATEPDSEPSNNEPVPDETGS--EISGPPEDSKSDIQSPCQAFEEVRVGGDYSPPPEEAMPFETQQP-------SLGDFW- 119
Cdd:PHA03247 2621 THAPDPPPPSPSPAANEPDPhpPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAQASSPPQRPRRRaarptvgSLTSLAd 2700
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  120 PTLEQPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAY--TPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVP 197
Cdd:PHA03247 2701 PPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAApaPPAVPAGPATPGGPARPARPPTTAGPPAPAPPAAPAAGPP 2780
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  198 RALPAEPG---NIRFENAGFREDYSPPPEESVPfqVGGEEFGGDSPPPGLPRvipqigiggefPTVAVPSALCLAPAENA 274
Cdd:PHA03247 2781 RRLTRPAVaslSESRESLPSPWDPADPPAAVLA--PAAALPPAASPAGPLPP-----------PTSAQPTAPPPPPGPPP 2847
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  275 PPLWVRGAI----DRPFREAVRSPPNFACDS---PPMEITRPLLEIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPD 347
Cdd:PHA03247 2848 PSLPLGGSVapggDVRRRPPSRSPAAKPAAParpPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPP 2927
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  348 KSECAERPPvEREAAEMEGSPTTATAVE--GKVPSPERG---DGSSTQPEAMDAKPAPA--AQAVSTGSDAGAPtDSAML 420
Cdd:PHA03247 2928 QPQPPPPPP-PRPQPPLAPTTDPAGAGEpsGAVPQPWLGalvPGRVAVPRFRVPQPAPSreAPASSTPPLTGHS-LSRVS 3005
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  421 TDSQSDAGEDGTAPGTPSDLQ------------------SDPEELEEAPAVRADPDGGAAPVAPATPAESESEGSRDPAA 482
Cdd:PHA03247 3006 SWASSLALHEETDPPPVSLKQtlwppddtedsdadslfdSDSERSDLEALDPLPPEPHDPFAHEPDPATPEAGARESPSS 3085
                         490
                  ....*....|....
gi 568915500  483 EPASEAVPATTAES 496
Cdd:PHA03247 3086 QFGPPPLSANAALS 3099
PLN00223 PLN00223
ADP-ribosylation factor; Provisional
941-1020 5.09e-06

ADP-ribosylation factor; Provisional


Pssm-ID: 165788  Cd Length: 181  Bit Score: 48.04  E-value: 5.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  941 VNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASssynmviredNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDL 1020
Cdd:PLN00223   61 ISFTVWDVGGQDKIRPLWRHYFQNTQGLIFVVDS----------NDRDRVVEARDELHRMLNEDELRDAVLLVFANKQDL 130
PHA03247 PHA03247
large tegument protein UL36; Provisional
152-654 5.42e-06

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 51.09  E-value: 5.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  152 PGLGAYTPPPEEAMPFEFNePAQGDHSQPPlQVPDlAPGGPEALVPRALPAEPgnirfenagfredysppPEESVPFQV- 230
Cdd:PHA03247 2475 PGAPVYRRPAEARFPFAAG-AAPDPGGGGP-PDPD-APPAPSRLAPAILPDEP-----------------VGEPVHPRMl 2534
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  231 ----GGEEFGGDS---PPPGLPrvipqigiggefptvavPSALCLAPAENAPPlwVRGAiDRPFREAVRSPPNFAcDSPP 303
Cdd:PHA03247 2535 twirGLEELASDDagdPPPPLP-----------------PAAPPAAPDRSVPP--PRPA-PRPSEPAVTSRARRP-DAPP 2593
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  304 mEITRPlleigRASIGVDDDTAVNMDSPPIASDGPPIEvSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPER 383
Cdd:PHA03247 2594 -QSARP-----RAPVDDRGDPRGPAPPSPLPPDTHAPD-PPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRR 2666
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  384 GD--GSSTQPEAMDAKPAPAA--QAVSTGSDAGAPTDSAMLTDSQSDAGEDGT--APGTPSDLQSDPEeLEEAPAVRADP 457
Cdd:PHA03247 2667 ARrlGRAAQASSPPQRPRRRAarPTVGSLTSLADPPPPPPTPEPAPHALVSATplPPGPAAARQASPA-LPAAPAPPAVP 2745
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  458 DGGA---APVAPATPAESESEGSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAavsatlaEPAARAAPITPKEPTT 534
Cdd:PHA03247 2746 AGPAtpgGPARPARPPTTAGPPAPAPPAAPAAGPPRRLTRPAVASLSESRESLPSPW-------DPADPPAAVLAPAAAL 2818
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  535 RAVPSARAHPAAGAVPGAPAMSASARAAAARAAYAGPLVWGAR-SLSATPAARASLPARAAAAARAASAARAVAAGRSAS 613
Cdd:PHA03247 2819 PPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGGSVAPGGDvRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESF 2898
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|.
gi 568915500  614 AAPSRAHLRPPSPEIQVADPPTPRPPPRPTAWPDKYERGRS 654
Cdd:PHA03247 2899 ALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRP 2939
Arl6 cd04157
Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small ...
926-1020 5.71e-06

Arf-like 6 (Arl6) GTPase; Arl6 (Arf-like 6) forms a subfamily of the Arf family of small GTPases. Arl6 expression is limited to the brain and kidney in adult mice, but it is expressed in the neural plate and somites during embryogenesis, suggesting a possible role for Arl6 in early development. Arl6 is also believed to have a role in cilia or flagella function. Several proteins have been identified that bind Arl6, including Arl6 interacting protein (Arl6ip), and SEC61beta, a subunit of the heterotrimeric conducting channel SEC61p. Based on Arl6 binding to these effectors, Arl6 is also proposed to play a role in protein transport, membrane trafficking, or cell signaling during hematopoietic maturation. At least three specific homozygous Arl6 mutations in humans have been found to cause Bardet-Biedl syndrome, a disorder characterized by obesity, retinopathy, polydactyly, renal and cardiac malformations, learning disabilities, and hypogenitalism. Older literature suggests that Arl6 is a part of the Arl4/Arl7 subfamily, but analyses based on more recent sequence data place Arl6 in its own subfamily.


Pssm-ID: 206722 [Multi-domain]  Cd Length: 162  Bit Score: 47.81  E-value: 5.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  926 VLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASS-SYNMVIREDNQTNRLQEAlnLFKSiwnnr 1004
Cdd:cd04157    30 VPTVGFNVESFKKGNLSFTAFDMSGQGKYRGLWEHYYKNIQGIIFVIDSSdRLRMVVAKDELELLLNHP--DIKH----- 102
                          90
                  ....*....|....*.
gi 568915500 1005 wlRTISVILFLNKQDL 1020
Cdd:cd04157   103 --RRIPILFYANKMDL 116
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
100-458 6.79e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 6.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  100 PPPEEAMPFETQQPSLGDFWPTLEQPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAYTPPPeeampfefnePAQGDHSQ 179
Cdd:PRK07764  435 PAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA----------PAAPAAPA 504
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  180 PPLQVPDLAPGGPE--------------ALVPRALPAEP-GN---IRFENAGFREDYSPPPEESVPFQVGGEEFGGD--- 238
Cdd:PRK07764  505 GADDAATLRERWPEilaavpkrsrktwaILLPEATVLGVrGDtlvLGFSTGGLARRFASPGNAEVLVTALAEELGGDwqv 584
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  239 ----SPPPGLPRvipqiGIGGEFPTVAVPSALCLAPAENAPPlwvrGAIDRPFREAVRSPP-----NFACDSPPMEITRP 309
Cdd:PRK07764  585 eavvGPAPGAAG-----GEGPPAPASSGPPEEAARPAAPAAP----AAPAAPAPAGAAAAPaeasaAPAPGVAAPEHHPK 655
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  310 LLEIGRASIGVDDDTAVNMDSPPIASDGPPIEV-----SGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERG 384
Cdd:PRK07764  656 HVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAapaapAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAA 735
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 568915500  385 DGSSTQPEAMDAKPAPAAQAVSTGSDAGAPtdsamltdsqsdAGEDGTAPGTPSDLQSDPEELEEAPAVRADPD 458
Cdd:PRK07764  736 DDPVPLPPEPDDPPDPAGAPAQPPPPPAPA------------PAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
Ras_like_GTPase cd00882
Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like ...
937-1025 8.69e-06

Rat sarcoma (Ras)-like superfamily of small guanosine triphosphatases (GTPases); Ras-like GTPase superfamily. The Ras-like superfamily of small GTPases consists of several families with an extremely high degree of structural and functional similarity. The Ras superfamily is divided into at least four families in eukaryotes: the Ras, Rho, Rab, and Sar1/Arf families. This superfamily also includes proteins like the GTP translation factors, Era-like GTPases, and G-alpha chain of the heterotrimeric G proteins. Members of the Ras superfamily regulate a wide variety of cellular functions: the Ras family regulates gene expression, the Rho family regulates cytoskeletal reorganization and gene expression, the Rab and Sar1/Arf families regulate vesicle trafficking, and the Ran family regulates nucleocytoplasmic transport and microtubule organization. The GTP translation factor family regulates initiation, elongation, termination, and release in translation, and the Era-like GTPase family regulates cell division, sporulation, and DNA replication. Members of the Ras superfamily are identified by the GTP binding site, which is made up of five characteristic sequence motifs, and the switch I and switch II regions.


Pssm-ID: 206648 [Multi-domain]  Cd Length: 161  Bit Score: 47.07  E-value: 8.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  937 QVDKVNFHMFDVGGQRDERRKWI-----QCFNDVTAIIFVVASSSYNMvirEDNQTNrlqealnlfkSIWNNRWLRTISV 1011
Cdd:cd00882    43 DKGKVKLVLVDTPGLDEFGGLGReelarLLLRGADLILLVVDSTDRES---EEDAKL----------LILRRLRKEGIPI 109
                          90
                  ....*....|....
gi 568915500 1012 ILFLNKQDLLAEKV 1025
Cdd:cd00882   110 ILVGNKIDLLEERE 123
Sar1 cd00879
Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII ...
940-1020 1.48e-05

Sar1 is an essential component of COPII vesicle coats; Sar1 is an essential component of COPII vesicle coats involved in export of cargo from the ER. The GTPase activity of Sar1 functions as a molecular switch to control protein-protein and protein-lipid interactions that direct vesicle budding from the ER. Activation of the GDP to the GTP-bound form of Sar1 involves the membrane-associated guanine nucleotide exchange factor (GEF) Sec12. Sar1 is unlike all Ras superfamily GTPases that use either myristoyl or prenyl groups to direct membrane association and function, in that Sar1 lacks such modification. Instead, Sar1 contains a unique nine-amino-acid N-terminal extension. This extension contains an evolutionarily conserved cluster of bulky hydrophobic amino acids, referred to as the Sar1-N-terminal activation recruitment (STAR) motif. The STAR motif mediates the recruitment of Sar1 to ER membranes and facilitates its interaction with mammalian Sec12 GEF leading to activation.


Pssm-ID: 206645 [Multi-domain]  Cd Length: 191  Bit Score: 46.89  E-value: 1.48e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  940 KVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYnmvirednqtNRLQEALNLFKSIWNNRWLRTISVILFLNKQD 1019
Cdd:cd00879    62 NVKFTTFDLGGHEQARRVWKDYFPEVDGIVFLVDAADP----------ERFQESKEELDSLLNDEELANVPILILGNKID 131

                  .
gi 568915500 1020 L 1020
Cdd:cd00879   132 K 132
PHA03247 PHA03247
large tegument protein UL36; Provisional
98-646 2.75e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.78  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   98 YSPPPEEAMPFetqqpslgdfwptleQPGPSGTPSGLQAFNPAilEPGTPTGASPGLGAYTPPPEEAMP------FEFNE 171
Cdd:PHA03247 2480 YRRPAEARFPF---------------AAGAAPDPGGGGPPDPD--APPAPSRLAPAILPDEPVGEPVHPrmltwiRGLEE 2542
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  172 PAQGDHSQP-PLQVPDLAPGGPEALVPRALPA-EPGNIRFENAGFREDysPPPEESVPFQVGGEEfgGDSPPPGLPRVIP 249
Cdd:PHA03247 2543 LASDDAGDPpPPLPPAAPPAAPDRSVPPPRPApRPSEPAVTSRARRPD--APPQSARPRAPVDDR--GDPRGPAPPSPLP 2618
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  250 qigiggefPTVAVPSALCLAPAENAPPLWVRGAIDRPFREAVRSPPNFACDSPPMEITRPlleiGRASigvdddtavNMD 329
Cdd:PHA03247 2619 --------PDTHAPDPPPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRL----GRAA---------QAS 2677
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  330 SPPIASDGPPIEVSGAPDKSeCAERPPVEREAaemEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGS 409
Cdd:PHA03247 2678 SPPQRPRRRAARPTVGSLTS-LADPPPPPPTP---EPAPHALVSATPLPPGPAAARQASPALPAAPAPPAVPAGPATPGG 2753
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  410 DAGAPTDSAMLTDSQSdagedgTAPGTPSdlqsdpeeleEAPAVRADPDGGAAPVAPATPAESESEGSRDPAAEPASEAV 489
Cdd:PHA03247 2754 PARPARPPTTAGPPAP------APPAAPA----------AGPPRRLTRPAVASLSESRESLPSPWDPADPPAAVLAPAAA 2817
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  490 PATTAESASGAAPVTQVEPAAAAVSATLAEPA------------------ARAAPITPKEPTTRAVPSARAHPAAGAVPG 551
Cdd:PHA03247 2818 LPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSlplggsvapggdvrrrppSRSPAAKPAAPARPPVRRLARPAVSRSTES 2897
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  552 APAMSASARAAAARAAYAGPLVWGARSLSATPAARASLPARAAAAARAASAARAVAAGRSASAAPSRAHLRP-------- 623
Cdd:PHA03247 2898 FALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPgrvavprf 2977
                         570       580
                  ....*....|....*....|....*
gi 568915500  624 --PSPEIQVADPPTPRPPPRPTAWP 646
Cdd:PHA03247 2978 rvPQPAPSREAPASSTPPLTGHSLS 3002
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
360-542 3.27e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 48.31  E-value: 3.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  360 EAAEMEGSPTtATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGSDAGAPTDSAMLTDSQSDAGEDGTAPGTPSD 439
Cdd:PRK07003  359 EPAVTGGGAP-GGGVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATAD 437
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  440 LQSDPEELEEAPAVRADpdggaapvAPATPAESESEGSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAVSATLAE 519
Cdd:PRK07003  438 RGDDAADGDAPVPAKAN--------ARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPD 509
                         170       180
                  ....*....|....*....|...
gi 568915500  520 PAARAAPITPKEPTTRAVPSARA 542
Cdd:PRK07003  510 ARAPAAASREDAPAAAAPPAPEA 532
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
124-508 4.15e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 47.67  E-value: 4.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  124 QPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAYTPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVPRALPAE 203
Cdd:PRK07764  395 AAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAAPSAQPAPAPAAAP 474
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  204 PGNIRfENAGFREDYSPPPEESVPFQVGGEefGGDSPPPGLPRVIPQI------------GIGGEFPTVAVPSALCLAPA 271
Cdd:PRK07764  475 EPTAA-PAPAPPAAPAPAAAPAAPAAPAAP--AGADDAATLRERWPEIlaavpkrsrktwAILLPEATVLGVRGDTLVLG 551
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  272 ENAPPLwvRGAIDRP-----FREAVRSPPNFACdsppmeitRPLLEIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAP 346
Cdd:PRK07764  552 FSTGGL--ARRFASPgnaevLVTALAEELGGDW--------QVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAP 621
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  347 DKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGSDA-GAPTDSAMLTDSQS 425
Cdd:PRK07764  622 AAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPApAAPAAPAGAAPAQP 701
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  426 DAGEDGTAPGTPSdlQSDPEELEEAPAVRADPDGGAAPVAPATPAESESEGSRDPAAEPASEAVPATTAESASGAAPVTQ 505
Cdd:PRK07764  702 APAPAATPPAGQA--DDPAAQPPQAAQGASAPSPAADDPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPP 779

                  ...
gi 568915500  506 VEP 508
Cdd:PRK07764  780 SEE 782
Arl5_Arl8 cd04153
Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like ...
936-1020 4.42e-05

Arf-like 5 (Arl5) and 8 (Arl8) GTPases; Arl5/Arl8 subfamily. Arl5 (Arf-like 5) and Arl8, like Arl4 and Arl7, are localized to the nucleus and nucleolus. Arl5 is developmentally regulated during embryogenesis in mice. Human Arl5 interacts with the heterochromatin protein 1-alpha (HP1alpha), a nonhistone chromosomal protein that is associated with heterochromatin and telomeres, and prevents telomere fusion. Arl5 may also play a role in embryonic nuclear dynamics and/or signaling cascades. Arl8 was identified from a fetal cartilage cDNA library. It is found in brain, heart, lung, cartilage, and kidney. No function has been assigned for Arl8 to date.


Pssm-ID: 133353 [Multi-domain]  Cd Length: 174  Bit Score: 45.42  E-value: 4.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  936 FQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSynmviREdnqtnRLQEALNLFKSIWNNRWLRTISVILFL 1015
Cdd:cd04153    54 IVYKNIRFLMWDIGGQESLRSSWNTYYTNTDAVILVIDSTD-----RE-----RLPLTKEELYKMLAHEDLRKAVLLVLA 123

                  ....*
gi 568915500 1016 NKQDL 1020
Cdd:cd04153   124 NKQDL 128
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
88-310 5.02e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 47.56  E-value: 5.02e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   88 AFEEVRVGGDYSPPPEEAMPFETQQPslgdfwPTLEQPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAYTPPPEEAMPF 167
Cdd:PRK12323  362 AFRPGQSGGGAGPATAAAAPVAQPAP------AAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAA 435
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  168 EFNEPAQGDHSQP-----PLQVPDLAPGGPEA-LVPRALPAEPGNIRFENAGFR--EDYSPPPEESVP--FQVGGEEFGG 237
Cdd:PRK12323  436 ARQASARGPGGAPapapaPAAAPAAAARPAAAgPRPVAAAAAAAPARAAPAAAPapADDDPPPWEELPpeFASPAPAQPD 515
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915500  238 DSPPPGLPRVIPQIGIG---GEFPTVAVPSALCLAPAENAPPLWVRGAIdRPFREAVRSPPNFACDSPPMEITRPL 310
Cdd:PRK12323  516 AAPAGWVAESIPDPATAdpdDAFETLAPAPAAAPAPRAAAATEPVVAPR-PPRASASGLPDMFDGDWPALAARLPV 590
PTZ00133 PTZ00133
ADP-ribosylation factor; Provisional
941-1020 5.87e-05

ADP-ribosylation factor; Provisional


Pssm-ID: 173423  Cd Length: 182  Bit Score: 45.22  E-value: 5.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  941 VNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASssynmviredNQTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDL 1020
Cdd:PTZ00133   61 LKFTMWDVGGQDKLRPLWRHYYQNTNGLIFVVDS----------NDRERIGDAREELERMLSEDELRDAVLLVFANKQDL 130
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
373-542 6.13e-05

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 47.15  E-value: 6.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  373 AVEGKVPSP-ERGDGSSTQPEAMDAKPAPAAQAVSTGSDAGAPTDSAMLT-----DSQSDAGEDGTAPGTPSDLQSDPEE 446
Cdd:PRK07003  375 RVAGAVPAPgARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEappaaPAPPATADRGDDAADGDAPVPAKAN 454
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  447 LEEAPAVRADPDGGAAPVAPATPAESESEGSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAP 526
Cdd:PRK07003  455 ARASADSRCDERDAQPPADSGSASAPASDAPPDAAFEPAPRAAAPSAATPAAVPDARAPAAASREDAPAAAAPPAPEARP 534
                         170
                  ....*....|....*.
gi 568915500  527 ITPKEpttrAVPSARA 542
Cdd:PRK07003  535 PTPAA----AAPAARA 546
Arl2 cd04154
Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind ...
936-1020 8.89e-05

Arf-like 2 (Arl2) GTPase; Arl2 (Arf-like 2) GTPases are members of the Arf family that bind GDP and GTP with very low affinity. Unlike most Arf family proteins, Arl2 is not myristoylated at its N-terminal helix. The protein PDE-delta, first identified in photoreceptor rod cells, binds specifically to Arl2 and is structurally very similar to RhoGDI. Despite the high structural similarity between Arl2 and Rho proteins and between PDE-delta and RhoGDI, the interactions between the GTPases and their effectors are very different. In its GTP bound form, Arl2 interacts with the protein Binder of Arl2 (BART), and the complex is believed to play a role in mitochondrial adenine nucleotide transport. In its GDP bound form, Arl2 interacts with tubulin- folding Cofactor D; this interaction is believed to play a role in regulation of microtubule dynamics that impact the cytoskeleton, cell division, and cytokinesis.


Pssm-ID: 206720 [Multi-domain]  Cd Length: 173  Bit Score: 44.24  E-value: 8.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  936 FQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSynmvirednqTNRLQEALNLFKSIWNNRWLRTISVILFL 1015
Cdd:cd04154    53 LEYNGYKLNIWDVGGQKSLRSYWRNYFESTDALIWVVDSSD----------RARLEDCKRELQKLLVEERLAGATLLIFA 122

                  ....*
gi 568915500 1016 NKQDL 1020
Cdd:cd04154   123 NKQDL 127
DamX COG3266
Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell ...
308-542 1.64e-04

Cell division protein DamX, binds to the septal ring, contains C-terminal SPOR domain [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 442497 [Multi-domain]  Cd Length: 455  Bit Score: 45.61  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  308 RPLLEIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPErgdgs 387
Cdd:COG3266   149 LTLLIVLPLLEEQLLLLALQDIQGTLQALGAVAALLGLRKAEEALALRAGSAAADALALLLLLLASALGEAVAAA----- 223
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  388 stqPEAMDAKPAPAAQAVSTGSDAGAPTDSAMLTDSQSDAGEDGTAPGTPSDLQsdPEELEEAPAVRADPdggaapvapa 467
Cdd:COG3266   224 ---AELAALALLAAGAAEVLTARLVLLLLIIGSALKAPSQASSASAPATTSLGE--QQEVSLPPAVAAQP---------- 288
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 568915500  468 tpaesesegSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPiTPKEPTTRAVPSARA 542
Cdd:COG3266   289 ---------AAAAAAQPSAVALPAAPAAAAAAAAPAEAAAPQPTAAKPVVTETAAPAAP-APEAAAAAAAPAAPA 353
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
172-542 2.38e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 45.55  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  172 PAQGDHSQPPLQVPDLAPGGPEALVPRALPAEPGNIRFenagfredysPPPEESVPFQVGGEEFGGDSPPPGLPRVIPQI 251
Cdd:PHA03307   55 VVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPTWSL----------STLAPASPAREGSPTPPGPSSPDPPPPTPPPA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  252 GIGgefPTVAVPSAlclAPAENAPPLWVRGAIDRPFREAVRSPPNFACDSPPmeitrplleigrasigvddDTAVNMDSP 331
Cdd:PHA03307  125 SPP---PSPAPDLS---EMLRPVGSPGPPPAASPPAAGASPAAVASDAASSR-------------------QAALPLSSP 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  332 PIASDGPPievsgAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGSDA 411
Cdd:PHA03307  180 EETARAPS-----SPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENE 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  412 ---GAPTDSAMLTDSQSDAGEDGTAPGTPSDLQSDPEELEEAPAVRADPDGGAAPVAPATPAESESEGSRDPAAEPASEA 488
Cdd:PHA03307  255 cplPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSE 334
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 568915500  489 VPATTAeSASGAAPVTQVEPAAAAVSATLAEPAARAAPITPkePTTRAVPSARA 542
Cdd:PHA03307  335 SSRGAA-VSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRA--PSSPAASAGRP 385
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
175-439 3.98e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 44.48  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  175 GDHSQPPLQVPDLAPGGPEALVPRALPAEPGNIRFENAgfredysPPPEESVPFQVGGEEFGGDSPPPGLPRVIPQIGIG 254
Cdd:PRK12323  370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPA-------AAPAAAAAARAVAAAPARRSPAPEALAAARQASAR 442
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  255 GEFPTVAVPSALCLAPAENAPPLwvrgaidrpfREAVRSPPNFACDSPPMEitrpllEIGRASIGVDDDtavnmdsPPIA 334
Cdd:PRK12323  443 GPGGAPAPAPAPAAAPAAAARPA----------AAGPRPVAAAAAAAPARA------APAAAPAPADDD-------PPPW 499
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  335 SDGPPIEVSGAPDKSECAERPpvereaAEMEGSPTTATAVegkvPSPERgdgsSTQPEAMDAKPAPAAQAVSTGSDAGAP 414
Cdd:PRK12323  500 EELPPEFASPAPAQPDAAPAG------WVAESIPDPATAD----PDDAF----ETLAPAPAAAPAPRAAAATEPVVAPRP 565
                         250       260
                  ....*....|....*....|....*
gi 568915500  415 tdsamltdsqSDAGEDGTAPGTPSD 439
Cdd:PRK12323  566 ----------PRASASGLPDMFDGD 580
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
330-626 4.92e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 4.92e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  330 SPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAmDAKPAPAAQAVSTGS 409
Cdd:PRK07764  397 AAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAA-APSAQPAPAPAAAPE 475
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  410 DAGAPTDSAMLTDSQSDAGEDGTAPGTPSDlQSDPEELEEA-PAVR--------------------ADPDGGAAPVAPat 468
Cdd:PRK07764  476 PTAAPAPAPPAAPAPAAAPAAPAAPAAPAG-ADDAATLRERwPEILaavpkrsrktwaillpeatvLGVRGDTLVLGF-- 552
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  469 paesESEGSRDPAAEPASE---------------AVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPITPKEPT 533
Cdd:PRK07764  553 ----STGGLARRFASPGNAevlvtalaeelggdwQVEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPA 628
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  534 TRAVPSARAHPAAGAVPGAPAMSASARAAAARAAYAGPLVWGARSLSATPAARASLPARAAAAARAASAARAVAAGRSAS 613
Cdd:PRK07764  629 PAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAAT 708
                         330
                  ....*....|...
gi 568915500  614 AAPSRAHLRPPSP 626
Cdd:PRK07764  709 PPAGQADDPAAQP 721
Arl1 cd04151
ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi ...
941-1020 5.82e-04

ADP ribosylation factor 1 (Arf1); Arl1 subfamily. Arl1 (Arf-like 1) localizes to the Golgi complex, where it is believed to recruit effector proteins to the trans-Golgi network. Like most members of the Arf family, Arl1 is myristoylated at its N-terminal helix and mutation of the myristoylation site disrupts Golgi targeting. In humans, the Golgi-localized proteins golgin-97 and golgin-245 have been identified as Arl1 effectors. Golgins are large coiled-coil proteins found in the Golgi, and these golgins contain a C-terminal GRIP domain, which is the site of Arl1 binding. Additional Arl1 effectors include the GARP (Golgi-associated retrograde protein)/VFT (Vps53) vesicle-tethering complex and Arfaptin 2. Arl1 is not required for exocytosis, but appears necessary for trafficking from the endosomes to the Golgi. In Drosophila zygotes, mutation of Arl1 is lethal, and in the host-bloodstream form of Trypanosoma brucei, Arl1 is essential for viability.


Pssm-ID: 206718 [Multi-domain]  Cd Length: 158  Bit Score: 41.63  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  941 VNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSynmvirednqTNRLQEALNLFKSIWNNRWLRTISVILFLNKQDL 1020
Cdd:cd04151    43 LKFQVWDLGGQTSIRPYWRCYYSNTDAIIYVVDSTD----------RDRLGISKSELHAMLEEEELKDAVLLVFANKQDM 112
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
325-524 6.08e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 44.07  E-value: 6.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  325 AVNMDSPPIAsdGPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQA 404
Cdd:PRK07003  361 AVTGGGAPGG--GVPARVAGAVPAPGARAAAAVGASAVPAVTAVTGAAGAALAPKAAAAAAATRAEAPPAAPAPPATADR 438
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  405 VSTGSDAGAPTDSAMLTDSQSDAGEDGTAPGTPSDlqsdpEELEEAPAVRADPDggaapvaPATPAESESEGSRDPAAEP 484
Cdd:PRK07003  439 GDDAADGDAPVPAKANARASADSRCDERDAQPPAD-----SGSASAPASDAPPD-------AAFEPAPRAAAPSAATPAA 506
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 568915500  485 ASEAVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARA 524
Cdd:PRK07003  507 VPDARAPAAASREDAPAAAAPPAPEARPPTPAAAAPAARA 546
PRK13108 PRK13108
prolipoprotein diacylglyceryl transferase; Reviewed
341-532 8.09e-04

prolipoprotein diacylglyceryl transferase; Reviewed


Pssm-ID: 237284 [Multi-domain]  Cd Length: 460  Bit Score: 43.43  E-value: 8.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  341 EVSGAPDKSECAERPPVEREAAEmegSPTTATAVEGKVPSPErGDGSSTQPEAMdakpapAAQAVSTGSDAGAPTDSAML 420
Cdd:PRK13108  280 EAPGALRGSEYVVDEALEREPAE---LAAAAVASAASAVGPV-GPGEPNQPDDV------AEAVKAEVAEVTDEVAAESV 349
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  421 TDSQSDAGEDGTApgtpsdlqsdPEELEEAPAVRADPdgGAAPVAPATPAESESEGSRDPAAEPASEAvpattAESASGA 500
Cdd:PRK13108  350 VQVADRDGESTPA----------VEETSEADIEREQP--GDLAGQAPAAHQVDAEAASAAPEEPAALA-----SEAHDET 412
                         170       180       190
                  ....*....|....*....|....*....|..
gi 568915500  501 APVTQVEPAAAAVSATLAEPAARAAPITPKEP 532
Cdd:PRK13108  413 EPEVPEKAAPIPDPAKPDELAVAGPGDDPAEP 444
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
295-663 1.04e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.24  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  295 PNFACDSPPMEITRPLLEIGRASIGVDDDtAVNMDSPPIASDG--PPIEVSGAPDKSECAERPPVEREAAEMEGSPTTAT 372
Cdd:PHA03307   19 EFFPRPPATPGDAADDLLSGSQGQLVSDS-AELAAVTVVAGAAacDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAP 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  373 AVEGKVPSPERGDGSST-------QPEAMDAKPAPAAQAVSTGSDAGAPTDSAML---TDSQSDAGEDGTAPGTPSDLQS 442
Cdd:PHA03307   98 ASPAREGSPTPPGPSSPdpppptpPPASPPPSPAPDLSEMLRPVGSPGPPPAASPpaaGASPAAVASDAASSRQAALPLS 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  443 DPEELEEAP-----AVRADPDGGAAPVAPATPAESESEGSRDPAAEPASEAVPATTAESASGAAPvtqvEPAAAAVSATL 517
Cdd:PHA03307  178 SPEETARAPssppaEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSS----ESSGCGWGPEN 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  518 AEPAARAAPITPKEPTTRAVPSARAHPAAGAVPGAPAMSASARAAAARAAYAGPLVWGARSLSATpAARASLPARAAAAA 597
Cdd:PHA03307  254 ECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSS-SSSRESSSSSTSSS 332
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915500  598 RAASAARAVAAGRSASAAPSRAHLRPPSPEIQVADPPTPRPPPRPTAWPDKYERGRSCCRYEASSG 663
Cdd:PHA03307  333 SESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRA 398
small_GTP TIGR00231
small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this ...
933-1041 1.15e-03

small GTP-binding protein domain; Proteins with a small GTP-binding domain recognized by this model include Ras, RhoA, Rab11, translation elongation factor G, translation initiation factor IF-2, tetratcycline resistance protein TetM, CDC42, Era, ADP-ribosylation factors, tdhF, and many others. In some proteins the domain occurs more than once.This model recognizes a large number of small GTP-binding proteins and related domains in larger proteins. Note that the alpha chains of heterotrimeric G proteins are larger proteins in which the NKXD motif is separated from the GxxxxGK[ST] motif (P-loop) by a long insert and are not easily detected by this model. [Unknown function, General]


Pssm-ID: 272973 [Multi-domain]  Cd Length: 162  Bit Score: 40.82  E-value: 1.15e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   933 ETKFQVD--KVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSSYnmVIR-EDNQTNRLQEALNLFKSiwnnrwlrTI 1009
Cdd:TIGR00231   41 TTVIEEDgkTYKFNLLDTAGQEDYDAIRRLYYPQVERSLRVFDIVIL--VLDvEEILEKQTKEIIHHADS--------GV 110
                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 568915500  1010 SVILFLNKQDLLAEKV------LAGKSKIEDYFPEFAR 1041
Cdd:TIGR00231  111 PIILVGNKIDLKDADLkthvasEFAKLNGEPIIPLSAE 148
UDM1_RNF168_RNF169-like cd22249
UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, ...
730-772 1.17e-03

UDM1 (ubiquitin-dependent DSB recruitment module 1) found in RING finger proteins RNF168, RNF169 and similar proteins; This model represents the UDM1 (ubiquitin-dependent double-strand break [DSB] recruitment module 1) found in RING finger proteins, RNF168 and RNF169. RNF168 is an E3 ubiquitin-protein ligase that promotes non-canonical K27 ubiquitination to signal DNA damage. It functions, together with RNF8, as a DNA damage response (DDR) factor that promotes a series of ubiquitylation events on substrates such as H2A and H2AX. With H2AK13/15 ubiquitylation, it facilitates recruitment of repair factors p53-binding protein 1 (53BP1) or the RAP80-BRCA1 complex to sites of double-strand breaks (DSBs), and inhibits homologous recombination (HR) in cells deficient in the tumor suppressor BRCA1. RNF168 also promotes H2A neddylation, which antagonizes ubiquitylation of H2A and regulates DNA damage repair. In addition, RNF168 forms a functional complex with RAD6A or RAD6B during the DNA damage response. RNF169 is an uncharacterized E3 ubiquitin-protein ligase paralogous to RNF168. It functions as a negative regulator of the DNA damage signaling cascade. RNF169 recognizes polyubiquitin structures but does not itself contribute to double-strand break (DSB)-induced chromatin ubiquitylation. It contributes to the regulation of DSB repair pathway utilization via functionally competing with recruiting repair factors, 53BP1 and RAP80-BRCA1, for association with RNF168-modified chromatin, independent of its catalytic activity, limiting the magnitude of the RNF8/RNF168-dependent signaling response to DSBs. The UDM1 domain comprises LRM1 (LR motif 1), UMI (ubiquitin-interacting motif [UIM]- and MIU-related UBD) and MIU1 (motif interacting with ubiquitin 1). Mutations of Ub-interacting residues in UDM1 have little effect on the accumulation of RNF168 to DSB sites, suggesting that it may not be the main site of binding ubiquitylated and polyubiquitylated targets.


Pssm-ID: 409016 [Multi-domain]  Cd Length: 66  Bit Score: 38.40  E-value: 1.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 568915500  730 PGKAKdpmEERRKQMRKEAIEMREQKRADKKRSKLIDKQLEEE 772
Cdd:cd22249     4 PGEIR---EEYEAQLKKLEEERRKEREEEEKASEELIRKLQEE 43
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
49-417 1.92e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 1.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   49 MATEPDSEPsnnepvpdetgseisGPPEDSKSDIQSPCQAFeevrvggdysPPPEEAMPFETQQPslgdfwptlEQPGPS 128
Cdd:PHA03307   67 PPTGPPPGP---------------GTEAPANESRSTPTWSL----------STLAPASPAREGSP---------TPPGPS 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  129 GTPSGLQAFNPAILEPGTPTGASPGL---GAYTPPPEEAMPFEFNEPAQG-DHSQPPLQVPDLAPGGPEALVPRALPAEP 204
Cdd:PHA03307  113 SPDPPPPTPPPASPPPSPAPDLSEMLrpvGSPGPPPAASPPAAGASPAAVaSDAASSRQAALPLSSPEETARAPSSPPAE 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  205 GNIRFENAGFRedySPPPEESVPFQVggeefGGDSPPPGLPRVIPQIGIGGEFPTVAVPSALCLAPAENAPPLWVRGAID 284
Cdd:PHA03307  193 PPPSTPPAAAS---PRPPRRSSPISA-----SASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPIT 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  285 RPFREAVRSPPNfacdsppMEITRPLLEIGRASIGVDDDtavnmDSPPIASDGPPieVSGAPDKSECAERPPVEREAAEM 364
Cdd:PHA03307  265 LPTRIWEASGWN-------GPSSRPGPASSSSSPRERSP-----SPSPSSPGSGP--APSSPRASSSSSSSRESSSSSTS 330
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 568915500  365 EGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGSDAGAPTDS 417
Cdd:PHA03307  331 SSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAG 383
PRK08691 PRK08691
DNA polymerase III subunits gamma and tau; Validated
50-276 2.07e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236333 [Multi-domain]  Cd Length: 709  Bit Score: 42.39  E-value: 2.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   50 ATEPDSEPSNNEPV-PDETGSEISGPPEDsksdiqspcQAFEEVRVGGDYSPPPEEAMPFETQQPSlgdfwptleqpGPS 128
Cdd:PRK08691  391 AKKPQPRPEAETAQtPVQTASAAAMPSEG---------KTAGPVSNQENNDVPPWEDAPDEAQTAA-----------GTA 450
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  129 GTPSglqAFNPAILEPGTPtgaspglgaytPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVPRALPAEPGNIR 208
Cdd:PRK08691  451 QTSA---KSIQTASEAETP-----------PENQVSKNKAADNETDAPLSEVPSENPIQATPNDEAVETETFAHEAPAEP 516
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915500  209 FENAGFREDYSPPpeesvpfqvggeEFGGDSPPPGLPRVIPQIGIGGEFPTVAVPSALCLAPAENAPP 276
Cdd:PRK08691  517 FYGYGFPDNDCPP------------EDGAEIPPPDWEHAAPADTAGGGADEEAEAGGIGGNNTPSAPP 572
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
340-542 2.08e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 42.28  E-value: 2.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  340 IEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGSDAGAPTDSAM 419
Cdd:PRK07764  584 VEAVVGPAPGAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDAS 663
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  420 LTDSQSDAGEDGTAPGTPSDLQSDPEELEEAPAVRADPDGGAAPVAPAtpaesesEGSRDPAAEPASEAVPATT-AESAS 498
Cdd:PRK07764  664 DGGDGWPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAATPPA-------GQADDPAAQPPQAAQGASApSPAAD 736
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 568915500  499 GAAPVTQVEPAAAAVSATLAEPAARAAPITPKEPTTRAVPSARA 542
Cdd:PRK07764  737 DPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPS 780
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
231-579 2.14e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 42.47  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  231 GGEEFGGDSPPPGLPRVIPQIGIGGEFPTVAvpsalclAPAENAPPLWVRGAIDRPFREAVRSPPNFACDSPPMEITRPL 310
Cdd:PHA03307   17 GGEFFPRPPATPGDAADDLLSGSQGQLVSDS-------AELAAVTVVAGAAACDRFEPPTGPPPGPGTEAPANESRSTPT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  311 L-------EIGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPDKSECA--ERPPVEREAAEMEGSPTTATAV-EGKVPS 380
Cdd:PHA03307   90 WslstlapASPAREGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLrpVGSPGPPPAASPPAAGASPAAVaSDAASS 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  381 PERGDGSSTQPEAMDAKPAPAAQA-VSTGSDAGAPTDSAMLTDSQSDAGEDGTAPG---------------TPSDLQSDP 444
Cdd:PHA03307  170 RQAALPLSSPEETARAPSSPPAEPpPSTPPAAASPRPPRRSSPISASASSPAPAPGrsaaddagasssdssSSESSGCGW 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  445 EELEEAPAVRADPD-----------GGAAPVAPATPAESESEGSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAV 513
Cdd:PHA03307  250 GPENECPLPRPAPItlptriweasgWNGPSSRPGPASSSSSPRERSPSPSPSSPGSGPAPSSPRASSSSSSSRESSSSST 329
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 568915500  514 SATLAEPAARAAPITPkePTTRAVPSARAHPAAGAVPGAPAMSASARAAAARAAYAGPLVWGARSL 579
Cdd:PHA03307  330 SSSSESSRGAAVSPGP--SPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPAASAGRPTRRRARAA 393
ARD1 cd04158
(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein ...
919-1020 3.49e-03

(ADP-ribosylation factor domain protein 1 (ARD1); ARD1 (ADP-ribosylation factor domain protein 1) is an unusual member of the Arf family. In addition to the C-terminal Arf domain, ARD1 has an additional 46-kDa N-terminal domain that contains a RING finger domain, two predicted B-Boxes, and a coiled-coil protein interaction motif. This domain belongs to the TRIM (tripartite motif) or RBCC (RING, B-Box, coiled-coil) family. Like most Arfs, the ARD1 Arf domain lacks detectable GTPase activity. However, unlike most Arfs, the full-length ARD1 protein has significant GTPase activity due to the GAP (GTPase-activating protein) activity exhibited by the 46-kDa N-terminal domain. The GAP domain of ARD1 is specific for its own Arf domain and does not bind other Arfs. The rate of GDP dissociation from the ARD1 Arf domain is slowed by the adjacent 15 amino acids, which act as a GDI (GDP-dissociation inhibitor) domain. ARD1 is ubiquitously expressed in cells and localizes to the Golgi and to the lysosomal membrane. Two Tyr-based motifs in the Arf domain are responsible for Golgi localization, while the GAP domain controls lysosomal localization.


Pssm-ID: 206723 [Multi-domain]  Cd Length: 169  Bit Score: 39.63  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  919 QDLLRCRVLTSGIFETKFQVDKVNFHMFDVGGQRDERRKWIQCFNDVTAIIFVVASSsynmvirednQTNRLQEALNLFK 998
Cdd:cd04158    21 QDEFMQPIPTIGFNVETVEYKNLKFTIWDVGGKHKLRPLWKHYYLNTQAVVFVIDSS----------HRDRVSEAHSELA 90
                          90       100
                  ....*....|....*....|..
gi 568915500  999 SIWNNRWLRTISVILFLNKQDL 1020
Cdd:cd04158    91 KLLTEKELRDALLLIFANKQDV 112
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
19-438 3.78e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.70  E-value: 3.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   19 PPEVGEQPEQEPLEAPGAAAPGAGAGPAEEMATEPDSEPSNNEPVPDETGSEIS-----GPPEDSKSDIQSPcqafeeVR 93
Cdd:PHA03307   66 EPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPtpppaSPPPSPAPDLSEM------LR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   94 VGGDYSPPPEEAMPFETQQPSlgdfwptleqPGPSGTPSGLQAFNP-AILEPGTPTGASPGlgaytpppeeampfefnEP 172
Cdd:PHA03307  140 PVGSPGPPPAASPPAAGASPA----------AVASDAASSRQAALPlSSPEETARAPSSPP-----------------AE 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  173 AQGDHSQPPLQVPDLAPGGPEALVPRALPAEPGNIRFENAGFREDYSPPPEESVPFQVGGEEFGGDSPPPGLPRVIPQIG 252
Cdd:PHA03307  193 PPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEA 272
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  253 IGGEfptvaVPSALCLAPAENAPPlwvRGAIDRPFREAVRSPPnfaCDSPPmeitRPLLEIGRASIGVDDDT--AVNMDS 330
Cdd:PHA03307  273 SGWN-----GPSSRPGPASSSSSP---RERSPSPSPSSPGSGP---APSSP----RASSSSSSSRESSSSSTssSSESSR 337
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  331 PPIASDGPPIEVSGAPDKSECAERPPvereaaemegSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVSTGS- 409
Cdd:PHA03307  338 GAAVSPGPSPSRSPSPSRPPPPADPS----------SPRKRPRPSRAPSSPAASAGRPTRRRARAAVAGRARRRDATGRf 407
                         410       420
                  ....*....|....*....|....*....
gi 568915500  410 DAGAPTDSAMLTDSQSDAGEDGTAPGTPS 438
Cdd:PHA03307  408 PAGRPRPSPLDAGAASGAFYARYPLLTPS 436
PHA03247 PHA03247
large tegument protein UL36; Provisional
96-634 3.81e-03

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 41.46  E-value: 3.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   96 GDYSPPPEEAMPFETQQPSLGdfwPTLEQPGPSGTPSGLQAFNPAI-------LEPGTPTGASPGLGAYTPPPEEAMPfe 168
Cdd:PHA03247 2549 GDPPPPLPPAAPPAAPDRSVP---PPRPAPRPSEPAVTSRARRPDAppqsarpRAPVDDRGDPRGPAPPSPLPPDTHA-- 2623
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  169 fnepaqgdhsqPPLQVPDLAPGGPEALVPRALPAEPGNIRfenagfrEDYSPPPEESVPFQVG--GEEFGGDSPPPG-LP 245
Cdd:PHA03247 2624 -----------PDPPPPSPSPAANEPDPHPPPTVPPPERP-------RDDPAPGRVSRPRRARrlGRAAQASSPPQRpRR 2685
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  246 RVIPqigiggefPTVAVPSALCLAPA-----ENAPPLWVRGAIDRPFREAVR--SPPNFACDSPPMEITRPLLEIGRASI 318
Cdd:PHA03247 2686 RAAR--------PTVGSLTSLADPPPppptpEPAPHALVSATPLPPGPAAARqaSPALPAAPAPPAVPAGPATPGGPARP 2757
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  319 GVDDDTAVnmdspPIASDGPPIEVSGAPDKsecAERPPVEREAAEMEGSPTTATAVEGKVPSPERgdgssTQPEAMDAKP 398
Cdd:PHA03247 2758 ARPPTTAG-----PPAPAPPAAPAAGPPRR---LTRPAVASLSESRESLPSPWDPADPPAAVLAP-----AAALPPAASP 2824
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  399 APAAQAVSTGSDAGAPTDSAMLTDSQSDAGedGTAPGTPSDLQSDPEELEEAPAVRADPDGG-------AAPVAPATPAE 471
Cdd:PHA03247 2825 AGPLPPPTSAQPTAPPPPPGPPPPSLPLGG--SVAPGGDVRRRPPSRSPAAKPAAPARPPVRrlarpavSRSTESFALPP 2902
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  472 SESEGSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPITPKEPTTRAVPSARAHPAAGAVPG 551
Cdd:PHA03247 2903 DQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSGAVPQPWLGALVPGRVAVPRFRVPQP 2982
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  552 APAMSASARAAAARAAYAGPLV--WgARSLS----ATPAARASLPARAAAAARAASAARAVAAGRSASAAPSRAHLRPPS 625
Cdd:PHA03247 2983 APSREAPASSTPPLTGHSLSRVssW-ASSLAlheeTDPPPVSLKQTLWPPDDTEDSDADSLFDSDSERSDLEALDPLPPE 3061

                  ....*....
gi 568915500  626 PEIQVADPP 634
Cdd:PHA03247 3062 PHDPFAHEP 3070
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
50-204 5.44e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.74  E-value: 5.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   50 ATEPDSEPSNNEPVPDETGSEISGPPEDSKSDIQSPcqafeEVRVGGDYSPPPEEAMPFETQQPSLGDFWPTLEQPGPSG 129
Cdd:PRK07764  633 AAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDG-----WPAKAGGAAPAAPPPAPAPAAPAAPAGAAPAQPAPAPAA 707
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 568915500  130 TPSGLQAFNPAILEPGTPTGASPGLGA---YTPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVPRALPAEP 204
Cdd:PRK07764  708 TPPAGQADDPAAQPPQAAQGASAPSPAaddPVPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEM 785
PHA03378 PHA03378
EBNA-3B; Provisional
75-369 6.46e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 40.82  E-value: 6.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500   75 PEDSKSDIQSPCQAFEEVRVGGDYSPPPEEAMPFETQQPSLGdfwPTLEQPGPSGTPSGLQAFNPAilEPGTPTGASPGL 154
Cdd:PHA03378  529 PPQPRAGRRAPCVYTEDLDIESDEPASTEPVHDQLLPAPGLG---PLQIQPLTSPTTSQLASSAPS--YAQTPWPVPHPS 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  155 GAYTPPPEEAMPFEFNEPAQGDHSQPPLqvpdlaPGGPEALVPralpaepgnIRFENAGFREDYSPPPEESVPFQVGGEE 234
Cdd:PHA03378  604 QTPEPPTTQSHIPETSAPRQWPMPLRPI------PMRPLRMQP---------ITFNVLVFPTPHQPPQVEITPYKPTWTQ 668
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  235 FGGD--SPPPGLPRVIPQIGIGgefPTVAVPSALclAPAENAPPLWVRGAIDRPFREAVRSPPNFAcdsPPMEITRPLLE 312
Cdd:PHA03378  669 IGHIpyQPSPTGANTMLPIQWA---PGTMQPPPR--APTPMRPPAAPPGRAQRPAAATGRARPPAA---APGRARPPAAA 740
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 568915500  313 IGRASIGVDDDTAVNMDSPPIASDGPPIEVSGAPDKSECAERPPVEREAAEMEGSPT 369
Cdd:PHA03378  741 PGRARPPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAPQQRPRGAPTPQ 797
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
122-540 7.26e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 40.35  E-value: 7.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  122 LEQPGPSGTPSGLQAFNPAILEPGTPTGASPGLGAYTPPPEEAMPFEFNEPAQGDHSQPPLQVPDLAPGGPEALVPRALP 201
Cdd:PRK07764  381 LERRLGVAGGAGAPAAAAPSAAAAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAA 460
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  202 AepgnirfenagfredyspPPEESVPFQVGGEEFGGDSPPPGLPRVIPQigiggefPTVAVPSAlclaPAENAPPLWVRG 281
Cdd:PRK07764  461 A------------------PSAQPAPAPAAAPEPTAAPAPAPPAAPAPA-------AAPAAPAA----PAAPAGADDAAT 511
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  282 aIDRPF---REAVRsppnfacdsppmEITRPLLEIGRASI---GVDDDTAV-NMDSPPIAsdgppiEVSGAPDKSEcaer 354
Cdd:PRK07764  512 -LRERWpeiLAAVP------------KRSRKTWAILLPEAtvlGVRGDTLVlGFSTGGLA------RRFASPGNAE---- 568
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  355 ppVEREA-AEMEGSPTTATAVEGKVPSPERGDGS--STQPEAMDAKPAPAAQAVSTGSDAGAPTDSAMLTDSQSDAGEDG 431
Cdd:PRK07764  569 --VLVTAlAEELGGDWQVEAVVGPAPGAAGGEGPpaPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPG 646
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  432 TAPGTPSDLQSDPEELEEAPAVRADPDGGAAPVAPATPaeSESEGSRDPAAEPASEAVPATTAESASGAAPVTQVEPAAA 511
Cdd:PRK07764  647 VAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAAPPPA--PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQA 724
                         410       420
                  ....*....|....*....|....*....
gi 568915500  512 AVSATLAEPAARAAPITPKEPTTRAVPSA 540
Cdd:PRK07764  725 AQGASAPSPAADDPVPLPPEPDDPPDPAG 753
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
376-528 7.58e-03

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 40.48  E-value: 7.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  376 GKVPSPERgdGSSTQPEAMDAKPAPAAQAVSTGSDAGAPTDSAMLTDSQSDAGEDGTAPGTPS----DLQSDPEE---LE 448
Cdd:PRK14949  636 GKKSSADR--KPKTPPSRAPPASLSKPASSPDASQTSASFDLDPDFELATHQSVPEAALASGSapapPPVPDPYDrppWE 713
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  449 EAPAVRADPDGGAAPVAPATPAESESEG-SRDPAAEPASEAVPATTAESASGAAPVTQVEPAAAAVSATLAEPAARAAPI 527
Cdd:PRK14949  714 EAPEVASANDGPNNAAEGNLSESVEDASnSELQAVEQQATHQPQVQAEAQSPASTTALTQTSSEVQDTELNLVLLSSGSI 793

                  .
gi 568915500  528 T 528
Cdd:PRK14949  794 T 794
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
337-538 8.45e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 40.24  E-value: 8.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  337 GPPIEVSGAPDKSECAERPPVEREAAEMEGSPTTATAVEGKVPSPERGDGSSTQPEAMDAKPApAAQAVSTGSDAGAPTD 416
Cdd:PRK12323  373 GPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARRSPAPEALAA-ARQASARGPGGAPAPA 451
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  417 SAMLTDSQSDAGEDGTAPGTPSDLQSDPEELEeAPAVRADPDGGAAPVAPATPAESESEGSRDPAAEPA---SEAVPATT 493
Cdd:PRK12323  452 PAPAAAPAAAARPAAAGPRPVAAAAAAAPARA-APAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAgwvAESIPDPA 530
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 568915500  494 AESASGAAPVTQVEPAAAAVSATLAEPAARAAPITPKEPTTRAVP 538
Cdd:PRK12323  531 TADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPPRASASGLPD 575
fliD PRK08724
flagellar filament capping protein FliD;
330-458 9.37e-03

flagellar filament capping protein FliD;


Pssm-ID: 236335 [Multi-domain]  Cd Length: 673  Bit Score: 40.24  E-value: 9.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 568915500  330 SPPIASDGPPIEVSGAPDKSECAERP--PVEREAAEmegsptTATAVEGKVPSPERGDGSSTQPEAMDAKPAPAAQAVST 407
Cdd:PRK08724  220 AQQVIAPLTPEEQKVAPELSDEEGNAipPADQEVAE------EIQDAAQIAQQQEATAALAALEEPISAGGATAAAAGQA 293
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 568915500  408 GSDAGAPTDSAMLTDSQSdaGEDGTAPGTPSDLQSDPE-ELEEAPAVRAdPD 458
Cdd:PRK08724  294 AIDAAEAKAYLRPEDRIP--GWTETASGTLLDSYPEPEeELDEAAIAKA-PD 342
 
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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