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Conserved domains on  [gi|341940533|sp|Q5DTK1|]
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RecName: Full=Chondroitin sulfate synthase 3; AltName: Full=Carbohydrate synthase 2; AltName: Full=Chondroitin glucuronyltransferase 3; AltName: Full=Chondroitin synthase 2; Short=ChSy-2; AltName: Full=Glucuronosyl-N-acetylgalactosaminyl-proteoglycan 4-beta-N-acetylgalactosaminyltransferase II; AltName: Full=N-acetylgalactosaminyl-proteoglycan 3-beta-glucuronosyltransferase 3; AltName: Full=N-acetylgalactosaminyltransferase 3

Protein Classification

chondroitin N-acetylgalactosaminyltransferase family protein( domain architecture ID 13451408)

chondroitin N-acetylgalactosaminyltransferase family protein such as chondroitin sulfate synthase 1, which has both beta-1,3-glucuronic acid and beta-1,4-N-acetylgalactosamine transferase activity

EC:  2.4.1.-
Gene Ontology:  GO:0008376
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
330-866 0e+00

Chondroitin N-acetylgalactosaminyltransferase;


:

Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 755.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  330 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHN 409
Cdd:pfam05679   1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYEGQRYFYFNYSSGKKGFIGNLKSKEFHSAITLHPVKDPADMYRLHK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  410 YMLSRKISELRYRTIQLHRESALMSKLSNSEVSKEDQQLGRTPSFNHfqPRERNEVMEWEFLTGKLLYSAAENQPpRQSI 489
Cdd:pfam05679  81 YFLSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNR--PKSRFDVLRWDYFTETHLYSADDGQP-RRRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  490 NSILRSALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVDPMHGVEYILDLLLLYKRHKGRklTVPVRRHAYLQQPF 569
Cdd:pfam05679 158 DGADKEDLDDVINTAMEEINRNYRPRGRVLEFKQLLNGYRRFDPLRGMEYILDLLLEYKKYRGR--TVPVRRRVYLQRPF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  570 SKPFFREVEELDvnrlvesinsgtqsfsvisnslkilsslqeakdigghNEKKVHILVPLVGRYDIFLRFMENFESTCLI 649
Cdd:pfam05679 236 SKVEIIPMPYVT-------------------------------------ESTRVHIILPLSGRYETFERFLENYERVCLE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  650 PKQNV-KLVIILFSRDAGQE--SIKHIELIQEYQSRYPSAEMMLIPMKGEFSRGLGLEMASSQFDNDTLLLFCDVDLIFR 726
Cdd:pfam05679 279 TGENVvLLLVVLYDPDEGQNdvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDSLLFFCDVDMVFT 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  727 GDFLQRCRDNTVQGQQVYYPIIFSQYDPKVTHMRNPPTEGD--FVFSKETGFWRDYGYGITCIYKSDLLGAGGFDTSIQG 804
Cdd:pfam05679 359 PEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDdnFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQG 438
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940533  805 WGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMQL 866
Cdd:pfam05679 439 WGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
Galactosyl_T super family cl21608
Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose: ...
170-400 1.24e-14

Galactosyltransferase; This family includes the galactosyltransferases UDP-galactose:2-acetamido-2-deoxy-D-glucose3beta-galactosyltransferase and UDP-Gal:beta-GlcNAc beta 1,3-galactosyltranferase. Specific galactosyltransferases transfer galactose to GlcNAc terminal chains in the synthesis of the lacto-series oligosaccharides types 1 and 2.


The actual alignment was detected with superfamily member pfam02434:

Pssm-ID: 473923  Cd Length: 248  Bit Score: 74.66  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  170 GDFLYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSsqQSPSAALgqPPPPLPVIALPGVDDSYPPQKKSFMM-IKYm 248
Cdd:pfam02434   3 LDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFT--DGEDEGL--PTRTGGHLINTNCSAGHCRKALSCKMaVEY- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  249 hDHYL-DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNTEELGKLGLEPGENFCMGGPGMIFSREVL 324
Cdd:pfam02434  78 -DRFLeSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  325 RRMVPHIGEClrEMYTT------HEDVEVGRCVRRFGGTQCVWSyemqQLFHENYEHnrkgyIQDLHNSKIHAAITL--- 395
Cdd:pfam02434 157 LKMSPWASGG--RFMSTsekirlPDDCTLGYIIENLLGVPLTHS----PLFHSHLEN-----LQDLPPETLHEQVTLsyg 225

                  ....*.
gi 341940533  396 -HPNKR 400
Cdd:pfam02434 226 kFWNKR 231
PRK07764 super family cl35613
DNA polymerase III subunits gamma and tau; Validated
49-238 7.64e-08

DNA polymerase III subunits gamma and tau; Validated


The actual alignment was detected with superfamily member PRK07764:

Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.15  E-value: 7.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  49 GRSATGPRADAQQLLPQPQSRPrlEQSPPPASHELPGPQQPEAAPGGPSFRSSPWQQPALLPQRRRGHTPEGATALPGAP 128
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARP--AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 129 AAKGEPEEEDGGAADPrkGGRPGSSHNGSGDGGAAVPTSGPgdflyvgvmtAQKYLGSRALAAQRTWArfipgrveffSS 208
Cdd:PRK07764 672 KAGGAAPAAPPPAPAP--AAPAAPAGAAPAQPAPAPAATPP----------AGQADDPAAQPPQAAQG----------AS 729
                        170       180       190
                 ....*....|....*....|....*....|
gi 341940533 209 QQSPSAALGQPPPPLPVIALPGVDDSYPPQ 238
Cdd:PRK07764 730 APSPAADDPVPLPPEPDDPPDPAGAPAQPP 759
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
330-866 0e+00

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 755.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  330 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHN 409
Cdd:pfam05679   1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYEGQRYFYFNYSSGKKGFIGNLKSKEFHSAITLHPVKDPADMYRLHK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  410 YMLSRKISELRYRTIQLHRESALMSKLSNSEVSKEDQQLGRTPSFNHfqPRERNEVMEWEFLTGKLLYSAAENQPpRQSI 489
Cdd:pfam05679  81 YFLSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNR--PKSRFDVLRWDYFTETHLYSADDGQP-RRRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  490 NSILRSALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVDPMHGVEYILDLLLLYKRHKGRklTVPVRRHAYLQQPF 569
Cdd:pfam05679 158 DGADKEDLDDVINTAMEEINRNYRPRGRVLEFKQLLNGYRRFDPLRGMEYILDLLLEYKKYRGR--TVPVRRRVYLQRPF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  570 SKPFFREVEELDvnrlvesinsgtqsfsvisnslkilsslqeakdigghNEKKVHILVPLVGRYDIFLRFMENFESTCLI 649
Cdd:pfam05679 236 SKVEIIPMPYVT-------------------------------------ESTRVHIILPLSGRYETFERFLENYERVCLE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  650 PKQNV-KLVIILFSRDAGQE--SIKHIELIQEYQSRYPSAEMMLIPMKGEFSRGLGLEMASSQFDNDTLLLFCDVDLIFR 726
Cdd:pfam05679 279 TGENVvLLLVVLYDPDEGQNdvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDSLLFFCDVDMVFT 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  727 GDFLQRCRDNTVQGQQVYYPIIFSQYDPKVTHMRNPPTEGD--FVFSKETGFWRDYGYGITCIYKSDLLGAGGFDTSIQG 804
Cdd:pfam05679 359 PEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDdnFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQG 438
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940533  805 WGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMQL 866
Cdd:pfam05679 439 WGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
170-400 1.24e-14

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 74.66  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  170 GDFLYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSsqQSPSAALgqPPPPLPVIALPGVDDSYPPQKKSFMM-IKYm 248
Cdd:pfam02434   3 LDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFT--DGEDEGL--PTRTGGHLINTNCSAGHCRKALSCKMaVEY- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  249 hDHYL-DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNTEELGKLGLEPGENFCMGGPGMIFSREVL 324
Cdd:pfam02434  78 -DRFLeSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  325 RRMVPHIGEClrEMYTT------HEDVEVGRCVRRFGGTQCVWSyemqQLFHENYEHnrkgyIQDLHNSKIHAAITL--- 395
Cdd:pfam02434 157 LKMSPWASGG--RFMSTsekirlPDDCTLGYIIENLLGVPLTHS----PLFHSHLEN-----LQDLPPETLHEQVTLsyg 225

                  ....*.
gi 341940533  396 -HPNKR 400
Cdd:pfam02434 226 kFWNKR 231
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
49-238 7.64e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.15  E-value: 7.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  49 GRSATGPRADAQQLLPQPQSRPrlEQSPPPASHELPGPQQPEAAPGGPSFRSSPWQQPALLPQRRRGHTPEGATALPGAP 128
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARP--AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 129 AAKGEPEEEDGGAADPrkGGRPGSSHNGSGDGGAAVPTSGPgdflyvgvmtAQKYLGSRALAAQRTWArfipgrveffSS 208
Cdd:PRK07764 672 KAGGAAPAAPPPAPAP--AAPAAPAGAAPAQPAPAPAATPP----------AGQADDPAAQPPQAAQG----------AS 729
                        170       180       190
                 ....*....|....*....|....*....|
gi 341940533 209 QQSPSAALGQPPPPLPVIALPGVDDSYPPQ 238
Cdd:PRK07764 730 APSPAADDPVPLPPEPDDPPDPAGAPAQPP 759
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
55-238 1.62e-04

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.44  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  55 PRADAQQLLPQPQSRPRLEQSPPPAS----HELPGPQQPE----AAPGGPSFRSSPWQQPALLPQ-----RRRGHTPEGA 121
Cdd:COG5180  266 RAAIGDTPAAEPPGLPVLEAGSEPQSdapeAETARPIDVKgvasAPPATRPVRPPGGARDPGTPRpgqptERPAGVPEAA 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 122 TALPGAPAAKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAVPTSGPGDFLYVGVMTAQKYLGSRALAAQRTWARFIpg 201
Cdd:COG5180  346 SDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETA-- 423
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 341940533 202 rveffsSQQSPSAALGQPPPPLPViALPGVDDSYPPQ 238
Cdd:COG5180  424 ------SLGGAAGGAGQGPKADFV-PGDAESVSGPAG 453
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
674-836 3.01e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 42.56  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 674 ELIQEYQSRYPsaemmlIPMK-------GeF----SRGLGLEMASSQFdndtlLLFCDVDLIFRGDFLQRCRDNT----- 737
Cdd:cd06420   42 ELIEEFKSQFP------IPIKhvwqedeG-FrkakIRNKAIAAAKGDY-----LIFIDGDCIPHPDFIADHIELAepgvf 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 738 VQGQQVYYPIIFSQYDPKVTHMrnpptegdfvfsketGFWrdygygitciyKSDLLGAGGFDTSIQGWGLEDVDLYNKVI 817
Cdd:cd06420  110 LSGSRVLLNEKLTERGIRGCNM---------------SFW-----------KKDLLAVNGFDEEFTGWGGEDSELVARLL 163
                        170
                 ....*....|....*....
gi 341940533 818 LSGLRPFRSQEVGVVhiFH 836
Cdd:cd06420  164 NSGIKFRKLKFAAIV--FH 180
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
71-205 1.05e-03

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 42.68  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  71 RLEQSPPPASHELPGPQQPEAAPGGPSfrsspwqqpallpqrrrghtPEGATALPGAPAAKGEPEEEDGGAADPRKGGRP 150
Cdd:NF041121  14 QMGRAAAPPSPEGPAPTAASQPATPPP--------------------PAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940533 151 GSSHNGSgdggaavPTSGPGDFLYVGVMTAQKYLGSRALA-AQRTWARFIPGRVEF 205
Cdd:NF041121  74 PPPPPGP-------AGAAPGAALPVRVPAPPALPNPLELArALRPLKRRVPSPRRV 122
 
Name Accession Description Interval E-value
CHGN pfam05679
Chondroitin N-acetylgalactosaminyltransferase;
330-866 0e+00

Chondroitin N-acetylgalactosaminyltransferase;


Pssm-ID: 461712 [Multi-domain]  Cd Length: 500  Bit Score: 755.64  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  330 HIGECLREMYTTHEDVEVGRCVRRFGGTQCVWSYEMQQLFHENYEHNRKGYIQDLHNSKIHAAITLHPNKRPAYQYRLHN 409
Cdd:pfam05679   1 HLDWCLKNLYSTHEDVELGRCIQKFAGIPCTWSYEGQRYFYFNYSSGKKGFIGNLKSKEFHSAITLHPVKDPADMYRLHK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  410 YMLSRKISELRYRTIQLHRESALMSKLSNSEVSKEDQQLGRTPSFNHfqPRERNEVMEWEFLTGKLLYSAAENQPpRQSI 489
Cdd:pfam05679  81 YFLSLELQKLRQEIIKLQREIKNMSELLPEGIDSLSWPLGIPPPLNR--PKSRFDVLRWDYFTETHLYSADDGQP-RRRL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  490 NSILRSALDDTVLQVMEMINENAKSRGRLIDFKEIQYGYRRVDPMHGVEYILDLLLLYKRHKGRklTVPVRRHAYLQQPF 569
Cdd:pfam05679 158 DGADKEDLDDVINTAMEEINRNYRPRGRVLEFKQLLNGYRRFDPLRGMEYILDLLLEYKKYRGR--TVPVRRRVYLQRPF 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  570 SKPFFREVEELDvnrlvesinsgtqsfsvisnslkilsslqeakdigghNEKKVHILVPLVGRYDIFLRFMENFESTCLI 649
Cdd:pfam05679 236 SKVEIIPMPYVT-------------------------------------ESTRVHIILPLSGRYETFERFLENYERVCLE 278
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  650 PKQNV-KLVIILFSRDAGQE--SIKHIELIQEYQSRYPSAEMMLIPMKGEFSRGLGLEMASSQFDNDTLLLFCDVDLIFR 726
Cdd:pfam05679 279 TGENVvLLLVVLYDPDEGQNdvFAEIKELIEELEKKYPKAKIPWISVKGEFSRGKALDLGAKKFPPDSLLFFCDVDMVFT 358
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  727 GDFLQRCRDNTVQGQQVYYPIIFSQYDPKVTHMRNPPTEGD--FVFSKETGFWRDYGYGITCIYKSDLLGAGGFDTSIQG 804
Cdd:pfam05679 359 PEFLNRCRMNTIQGKQVYFPIVFSQYDPEVVYYDKPVPTSDdnFDISKDTGHWRRYGFGIVCFYKSDYMAVGGFRTSIQG 438
                         490       500       510       520       530       540
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 341940533  805 WGLEDVDLYNKVILSGLRPFRSQEVGVVHIFHPVHCDPNLDPKQYKMCLGSKASTFASTMQL 866
Cdd:pfam05679 439 WGLEDVDLYDKFVKSGLHVFRAVEPGLVHRYHPRHCDPRLSEKQYHMCLGSKAEGLASRTQL 500
Fringe pfam02434
Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls ...
170-400 1.24e-14

Fringe-like; The drosophila protein fringe (FNG) is a glucosaminyltransferase that controls the response of the Notch receptor to specific ligands. FNG is localized to the Golgi apparatus (not secreted as previously thought). Modification of Notch occurs through glycosylation by FNG. The xenopus homolog, lunatic fringe, has been implicated in a variety of functions.


Pssm-ID: 367085  Cd Length: 248  Bit Score: 74.66  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  170 GDFLYVGVMTAQKYLGSRALAAQRTWARFIPGRVEFFSsqQSPSAALgqPPPPLPVIALPGVDDSYPPQKKSFMM-IKYm 248
Cdd:pfam02434   3 LDDIFIAVKTTKKFHKTRLPLLLKTWISRAKHQTYIFT--DGEDEGL--PTRTGGHLINTNCSAGHCRKALSCKMaVEY- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  249 hDHYL-DKYEWFMRADDDVYIKGDKLEEFLRSLNSSKPLYLGQT---GLGNTEELGKLGLEPGENFCMGGPGMIFSREVL 324
Cdd:pfam02434  78 -DRFLeSGKKWFCHVDDDNYVNVPRLVRLLSCYNHTQDVYLGKPslyRPIEATERVKGNRKVGFWFATGGAGFCISRGLA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  325 RRMVPHIGEClrEMYTT------HEDVEVGRCVRRFGGTQCVWSyemqQLFHENYEHnrkgyIQDLHNSKIHAAITL--- 395
Cdd:pfam02434 157 LKMSPWASGG--RFMSTsekirlPDDCTLGYIIENLLGVPLTHS----PLFHSHLEN-----LQDLPPETLHEQVTLsyg 225

                  ....*.
gi 341940533  396 -HPNKR 400
Cdd:pfam02434 226 kFWNKR 231
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
49-238 7.64e-08

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 56.15  E-value: 7.64e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  49 GRSATGPRADAQQLLPQPQSRPrlEQSPPPASHELPGPQQPEAAPGGPSFRSSPWQQPALLPQRRRGHTPEGATALPGAP 128
Cdd:PRK07764 594 AAGGEGPPAPASSGPPEEAARP--AAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPA 671
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 129 AAKGEPEEEDGGAADPrkGGRPGSSHNGSGDGGAAVPTSGPgdflyvgvmtAQKYLGSRALAAQRTWArfipgrveffSS 208
Cdd:PRK07764 672 KAGGAAPAAPPPAPAP--AAPAAPAGAAPAQPAPAPAATPP----------AGQADDPAAQPPQAAQG----------AS 729
                        170       180       190
                 ....*....|....*....|....*....|
gi 341940533 209 QQSPSAALGQPPPPLPVIALPGVDDSYPPQ 238
Cdd:PRK07764 730 APSPAADDPVPLPPEPDDPPDPAGAPAQPP 759
PRK14959 PRK14959
DNA polymerase III subunits gamma and tau; Provisional
6-158 2.82e-07

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 184923 [Multi-domain]  Cd Length: 624  Bit Score: 54.30  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   6 RRPWVSVALGLVLGFTAASWLIAPRVAELSEKRRRGSSLCSYYGRSATGPRADAQQLLPQP-QSRPrleQSPPPA----- 79
Cdd:PRK14959 340 RRVLTSLEPAMALELLLLNLAMLPRLMPVESLRPSGGGASAPSGSAAEGPASGGAATIPTPgTQGP---QGTAPAagmtp 416
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  80 SHELPGPQQPEAAPGgPSFrssPWQQPALLPQRRrGHTPEGATALPGAPAAKGEPEEEDGGAADPRKGGRPGSS--HNGS 157
Cdd:PRK14959 417 SSAAPATPAPSAAPS-PRV---PWDDAPPAPPRS-GIPPRPAPRMPEASPVPGAPDSVASASDAPPTLGDPSDTaeHTPS 491

                 .
gi 341940533 158 G 158
Cdd:PRK14959 492 G 492
PHA03247 PHA03247
large tegument protein UL36; Provisional
64-224 9.11e-07

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 53.02  E-value: 9.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   64 PQPQSRPRLeqsPPPASHELPGPQQPEAAPGGPSFRSSPwQQPALLPQRRRGHTPEGATALPGAPAAKGEPEEEDGGAAD 143
Cdd:PHA03247 2551 PPPPLPPAA---PPAAPDRSVPPPRPAPRPSEPAVTSRA-RRPDAPPQSARPRAPVDDRGDPRGPAPPSPLPPDTHAPDP 2626
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  144 PRKGGRPGSSHNGSGDGGAAVPTSGPGDFLYVGVMTAQKYLGSRALAA------QRTWARFIPGRVeffssqqSPSAALG 217
Cdd:PHA03247 2627 PPPSPSPAANEPDPHPPPTVPPPERPRDDPAPGRVSRPRRARRLGRAAqassppQRPRRRAARPTV-------GSLTSLA 2699

                  ....*..
gi 341940533  218 QPPPPLP 224
Cdd:PHA03247 2700 DPPPPPP 2706
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
777-837 3.01e-06

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 45.68  E-value: 3.01e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940533  777 WRDYGYGITCIYKSDLLGAGGFDTSIQGWGLEDVDLYNKVILSGLRPFR-SQEVG-VVHIFHP 837
Cdd:pfam02709  16 YKTYFGGVLALSREDFERINGFSNGFWGWGGEDDDLYNRLLLAGLEIERpPGDIGrYYMLYHK 78
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
49-170 4.44e-06

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.55  E-value: 4.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   49 GRSATGPRADAQQLLPQPqSRPRLEQSPPPASHELPGPQQPEAAPGGPSFRSSPWQQPALLPQRRRGHTPEG------AT 122
Cdd:PHA03307  160 AAVASDAASSRQAALPLS-SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADdagassSD 238
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 341940533  123 ALPGAPAAKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAvPTSGPG 170
Cdd:PHA03307  239 SSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPS-SRPGPA 285
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
52-145 5.24e-06

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 50.37  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  52 ATGPRADAQQLLPQPQSRPRLEQSPPPASHELPGPQQPEAAPGG-PSFRSSPWQQPALLPQRRRGHTPEGATALPGAPAA 130
Cdd:PRK07764 417 PAAAAAPAPAAAPQPAPAPAPAPAPPSPAGNAPAGGAPSPPPAAaPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAA 496
                         90
                 ....*....|....*..
gi 341940533 131 KGEPEEEDGG--AADPR 145
Cdd:PRK07764 497 PAAPAAPAGAddAATLR 513
PHA03247 PHA03247
large tegument protein UL36; Provisional
49-237 3.11e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 48.01  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   49 GRSATGPRADAQQLLPQPQSRPRLEQSP--PPASHELPGPQQPEAAPGGPSFRSSPWQQPALLPQRrrghTPEGATALPG 126
Cdd:PHA03247 2659 GRVSRPRRARRLGRAAQASSPPQRPRRRaaRPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPG----PAAARQASPA 2734
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  127 APAAKGEPEEEDGGAAD--PRKGGRPGSSHNGSGDGGAAVPTSGPGDFLYVgvmTAQKYLGSRALAAQRTW-----ARFI 199
Cdd:PHA03247 2735 LPAAPAPPAVPAGPATPggPARPARPPTTAGPPAPAPPAAPAAGPPRRLTR---PAVASLSESRESLPSPWdpadpPAAV 2811
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 341940533  200 PGRVEFFSSQQSPSAALgqPPPPLPVIALPGVDDSYPP 237
Cdd:PHA03247 2812 LAPAAALPPAASPAGPL--PPPTSAQPTAPPPPPGPPP 2847
PHA03378 PHA03378
EBNA-3B; Provisional
48-169 5.43e-05

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 46.98  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  48 YGRSATGPRAdaqqLLPqPQSRPRLEQSPPPAshelPGPQQPEAAPGGPSFRSSPWQQPALLPQRrrghTPEGATALPGA 127
Cdd:PHA03378 674 YQPSPTGANT----MLP-IQWAPGTMQPPPRA----PTPMRPPAAPPGRAQRPAAATGRARPPAA----APGRARPPAAA 740
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 341940533 128 PAAKGEPEEEDGGAADPRkgGRPGSSHNGSGDGGAAVPTSGP 169
Cdd:PHA03378 741 PGRARPPAAAPGRARPPA--AAPGRARPPAAAPGAPTPQPPP 780
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
19-171 6.75e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 6.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  19 GFTAASWLIAPRVAELSEKRRRGSSLCSYYGRSATGPRADAQQLL---PQPQSRPRLEQSPPPASHELPGPQQPEAAPGG 95
Cdd:PRK07764 635 APAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAKAGGAAPAappPAPAPAAPAAPAGAAPAQPAPAPAATPPAGQA 714
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 341940533  96 PSfrssPWQQPALLPQRRRGHTPEGATALPGAPaakgEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAVPTSGPGD 171
Cdd:PRK07764 715 DD----PAAQPPQAAQGASAPSPAADDPVPLPP----EPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEE 782
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
27-164 8.21e-05

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 46.52  E-value: 8.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  27 IAPRVAELsEKRRRGSSLCSYYGRSATGPR-ADAQQLLPQPQSRPRLEQSPPPASHELPGPQ-QPEAAPGGPSFRSSPWQ 104
Cdd:PRK07764 374 LLARLERL-ERRLGVAGGAGAPAAAAPSAAaAAPAAAPAPAAAAPAAAAAPAPAAAPQPAPApAPAPAPPSPAGNAPAGG 452
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 105 QPALLPQRRRGHTPEGATALPGAPAAKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAV 164
Cdd:PRK07764 453 APSPPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAPAAPAGADDAATL 512
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
29-227 9.01e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 46.32  E-value: 9.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   29 PRVAELSEKRRRGSSLCSYYGRSATGPRADAQQLLPQPQSRPRLEQSPPPASHELPGPqQPEAAPGGPSFRSSPwqqpal 108
Cdd:PHA03307  225 GRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRP-GPASSSSSPRERSPS------ 297
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  109 lPQRRRGHTPEGATALPGAPAAKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAVPTSGPGDFlyVGVMTAQKYLGSRA 188
Cdd:PHA03307  298 -PSPSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPA--DPSSPRKRPRPSRA 374
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 341940533  189 LAAQRTWARFIPGR------VEFFSSQQSPSAALGQPPPPLPVIA 227
Cdd:PHA03307  375 PSSPAASAGRPTRRraraavAGRARRRDATGRFPAGRPRPSPLDA 419
PHA03247 PHA03247
large tegument protein UL36; Provisional
38-147 1.34e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   38 RRRGSSLcSYYGRSATGPRADAQQLL-PQPQSRPRLEQSPPPASHELPGPQQPEAAPGGPSFRSSPWQQPALLPQRRrgh 116
Cdd:PHA03247 2863 RRRPPSR-SPAAKPAAPARPPVRRLArPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQPPPPPPPR--- 2938
                          90       100       110
                  ....*....|....*....|....*....|.
gi 341940533  117 tPEGATALPGAPAAKGEPEeedGGAADPRKG 147
Cdd:PHA03247 2939 -PQPPLAPTTDPAGAGEPS---GAVPQPWLG 2965
PBP1 COG5180
PAB1-binding protein, interacts with poly(A)-binding protein [RNA processing and modification]; ...
55-238 1.62e-04

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


Pssm-ID: 444064 [Multi-domain]  Cd Length: 548  Bit Score: 45.44  E-value: 1.62e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  55 PRADAQQLLPQPQSRPRLEQSPPPAS----HELPGPQQPE----AAPGGPSFRSSPWQQPALLPQ-----RRRGHTPEGA 121
Cdd:COG5180  266 RAAIGDTPAAEPPGLPVLEAGSEPQSdapeAETARPIDVKgvasAPPATRPVRPPGGARDPGTPRpgqptERPAGVPEAA 345
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 122 TALPGAPAAKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAVPTSGPGDFLYVGVMTAQKYLGSRALAAQRTWARFIpg 201
Cdd:COG5180  346 SDAGQPPSAYPPAEEAVPGKPLEQGAPRPGSSGGDGAPFQPPNGAPQPGLGRRGAPGPPMGAGDLVQAALDGGGRETA-- 423
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 341940533 202 rveffsSQQSPSAALGQPPPPLPViALPGVDDSYPPQ 238
Cdd:COG5180  424 ------SLGGAAGGAGQGPKADFV-PGDAESVSGPAG 453
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
674-836 3.01e-04

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 42.56  E-value: 3.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 674 ELIQEYQSRYPsaemmlIPMK-------GeF----SRGLGLEMASSQFdndtlLLFCDVDLIFRGDFLQRCRDNT----- 737
Cdd:cd06420   42 ELIEEFKSQFP------IPIKhvwqedeG-FrkakIRNKAIAAAKGDY-----LIFIDGDCIPHPDFIADHIELAepgvf 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 738 VQGQQVYYPIIFSQYDPKVTHMrnpptegdfvfsketGFWrdygygitciyKSDLLGAGGFDTSIQGWGLEDVDLYNKVI 817
Cdd:cd06420  110 LSGSRVLLNEKLTERGIRGCNM---------------SFW-----------KKDLLAVNGFDEEFTGWGGEDSELVARLL 163
                        170
                 ....*....|....*....
gi 341940533 818 LSGLRPFRSQEVGVVhiFH 836
Cdd:cd06420  164 NSGIKFRKLKFAAIV--FH 180
PHA03269 PHA03269
envelope glycoprotein C; Provisional
64-213 6.75e-04

envelope glycoprotein C; Provisional


Pssm-ID: 165527 [Multi-domain]  Cd Length: 566  Bit Score: 43.18  E-value: 6.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  64 PQPQSRPRLEQSPPPASHELPGPQ---QPEAAPgGPSFRSSPWQQPALLPQRRRGHTPEGATALPGAPAAKgePEEEDGG 140
Cdd:PHA03269  54 PDPAVAPTSAASRKPDLAQAPTPAaseKFDPAP-APHQAASRAPDPAVAPQLAAAPKPDAAEAFTSAAQAH--EAPADAG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 141 AADPRKGGRPgsshngsgdggAAVPTSGPGDFLYVGVM--TAQKYLGSRALAAQRT-----WARFIPGRVEFFSSQQSPS 213
Cdd:PHA03269 131 TSAASKKPDP-----------AAHTQHSPPPFAYTRSMehIACTHGGIQFIPYFHKfilpcYLQIFTGQGAAFKQHELPK 199
PRK07003 PRK07003
DNA polymerase III subunit gamma/tau;
55-237 8.18e-04

DNA polymerase III subunit gamma/tau;


Pssm-ID: 235906 [Multi-domain]  Cd Length: 830  Bit Score: 43.30  E-value: 8.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  55 PRADAQQLLPQPQSRPRLEQSPPPASHElPGPQQPEAAPGGPSFRSSPWQQPALLPQ-RRRGHTPEGAT-----ALPGAP 128
Cdd:PRK07003 459 ADSRCDERDAQPPADSGSASAPASDAPP-DAAFEPAPRAAAPSAATPAAVPDARAPAaASREDAPAAAAppapeARPPTP 537
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 129 AAkGEPEEEDGGAADP----RKGGRPGSSHNGSGDGGAAVPTSGPGdflyvgvmTAQKYLGSR-ALAAQRTWARFIPGRV 203
Cdd:PRK07003 538 AA-AAPAARAGGAAAAldvlRNAGMRVSSDRGARAAAAAKPAAAPA--------AAPKPAAPRvAVQVPTPRARAATGDA 608
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 341940533 204 EFFSSQQSPSAA-LGQPPPP---------LPVIA---LPGVDDSYPP 237
Cdd:PRK07003 609 PPNGAARAEQAAeSRGAPPPwedippddyVPLSAdegFGGPDDGFVP 655
SAV_2336_NTERM NF041121
SAV_2336 family N-terminal domain; This HMM describes an N-terminal domain shared by SAV_2336 ...
71-205 1.05e-03

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


Pssm-ID: 469044 [Multi-domain]  Cd Length: 473  Bit Score: 42.68  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  71 RLEQSPPPASHELPGPQQPEAAPGGPSfrsspwqqpallpqrrrghtPEGATALPGAPAAKGEPEEEDGGAADPRKGGRP 150
Cdd:NF041121  14 QMGRAAAPPSPEGPAPTAASQPATPPP--------------------PAAPPSPPGDPPEPPAPEPAPLPAPYPGSLAPP 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 341940533 151 GSSHNGSgdggaavPTSGPGDFLYVGVMTAQKYLGSRALA-AQRTWARFIPGRVEF 205
Cdd:NF041121  74 PPPPPGP-------AGAAPGAALPVRVPAPPALPNPLELArALRPLKRRVPSPRRV 122
PRK12323 PRK12323
DNA polymerase III subunit gamma/tau;
49-237 1.65e-03

DNA polymerase III subunit gamma/tau;


Pssm-ID: 237057 [Multi-domain]  Cd Length: 700  Bit Score: 42.17  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  49 GRSATGPRADAQQLLPQPQSRPRLEQSPPPASHELPGPQQPEAAPGGPSFRSSPWQ-QPALLP----QRRRGHTPEGATA 123
Cdd:PRK12323 370 GGAGPATAAAAPVAQPAPAAAAPAAAAPAPAAPPAAPAAAPAAAAAARAVAAAPARrSPAPEAlaaaRQASARGPGGAPA 449
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 124 LPGAPA---AKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAVPTSGPGDFLYVGVMTAQKYLGSRALAAQRTWARFIP 200
Cdd:PRK12323 450 PAPAPAaapAAAARPAAAGPRPVAAAAAAAPARAAPAAAPAPADDDPPPWEELPPEFASPAPAQPDAAPAGWVAESIPDP 529
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 341940533 201 GRVEFFSSQQSPSAALGQPPPPLPVIALPGVDDSYPP 237
Cdd:PRK12323 530 ATADPDDAFETLAPAPAAAPAPRAAAATEPVVAPRPP 566
dnaA PRK14086
chromosomal replication initiator protein DnaA;
28-171 3.12e-03

chromosomal replication initiator protein DnaA;


Pssm-ID: 237605 [Multi-domain]  Cd Length: 617  Bit Score: 41.35  E-value: 3.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  28 APRVAELSEKRRRGSSLCSYYGRSATGPRADAQQLLPQ--------PQSRPRLEQSPPPASHELPGPQQPEAA------- 92
Cdd:PRK14086 101 HARRTSEPELPRPGRRPYEGYGGPRADDRPPGLPRQDQlptarpayPAYQQRPEPGAWPRAADDYGWQQQRLGfpprapy 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  93 --PGGPSFRSSPWQQPALL------PQRRRGHTPEGATALPG---------APAAKGEPEEEDGGAADPRKGGRPGSSHN 155
Cdd:PRK14086 181 asPASYAPEQERDREPYDAgrpeydQRRRDYDHPRPDWDRPRrdrtdrpepPPGAGHVHRGGPGPPERDDAPVVPIRPSA 260
                        170
                 ....*....|....*.
gi 341940533 156 GSGDGGAAVPTSGPGD 171
Cdd:PRK14086 261 PGPLAAQPAPAPGPGE 276
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
65-241 3.56e-03

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 41.31  E-value: 3.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533   65 QPQSRPRLEQSPPPASHELPGPQQPEAAPGGPSfrssPWQQPALLPQRRRGhTPEGATALPGAPAAKGEPEEEDGGAADP 144
Cdd:PHA03307   60 AACDRFEPPTGPPPGPGTEAPANESRSTPTWSL----STLAPASPAREGSP-TPPGPSSPDPPPPTPPPASPPPSPAPDL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  145 RKGGRPGSSHNGSGDGGAAVPTSGPGDflyvgVMTAQKYLGSRALAAqrtwarfipgrveffSSQQSPSAALGQPPPPLP 224
Cdd:PHA03307  135 SEMLRPVGSPGPPPAASPPAAGASPAA-----VASDAASSRQAALPL---------------SSPEETARAPSSPPAEPP 194
                         170
                  ....*....|....*..
gi 341940533  225 VIALPGVDDSYPPQKKS 241
Cdd:PHA03307  195 PSTPPAAASPRPPRRSS 211
GINS_A_psf1 cd11710
Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric ...
364-441 7.11e-03

Alpha-helical domain of GINS complex protein Psf1; Psf1 is a component of the GINS tetrameric protein complex. Psf1 is mainly expressed in highly proliferative tissues, such as blastocysts, adult bone marrow, and testis, in which the stem cell system is active. Loss of Psf1 causes embryonic lethality. GINS is a complex of four subunits (Sld5, Psf1, Psf2 and Psf3) that is involved in both initiation and elongation stages of eukaryotic chromosome replication. Besides being essential for the maintenance of genomic integrity, GINS plays a central role in coordinating DNA replication with cell cycle checkpoints and is involved in cell growth. The eukaryotic GINS subunits are homologous and homologs are also found in the archaea; the complex is not found in bacteria. The four subunits of the complex consist of two domains each, termed the alpha-helical (A) and beta-strand (B) domains. The A and B domains of Sld5/Psf1 are permuted with respect to Psf1/Psf3.


Pssm-ID: 212548  Cd Length: 129  Bit Score: 37.62  E-value: 7.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533 364 EMQQLFHENYEHNRKGYIQDLHNS-----KIHAAITLHpNKRP--AYQY-RLhnymlsRKISELRYRTIQlHRESALMSK 435
Cdd:cd11710   33 EIRDLYEENQALLEEAQEEEEDPGlipglLVRHLSILR-NKRCllAYLYeRL------DRIRELRWENGS-VLPEDIKEN 104

                 ....*.
gi 341940533 436 LSNSEV 441
Cdd:cd11710  105 LSPAEK 110
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
49-170 8.50e-03

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 39.97  E-value: 8.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 341940533  49 GRSATGPRADAQQLlpqpqsrPRLE-------------QSPPPASHELPGPQQPEAAPGGPS---FRSSPWQQPALLPQR 112
Cdd:PRK07764 365 PSASDDERGLLARL-------ERLErrlgvaggagapaAAAPSAAAAAPAAAPAPAAAAPAAaaaPAPAAAPQPAPAPAP 437
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 341940533 113 RRGHTPEGATALPG-----APAAKGEPEEEDGGAADPRKGGRPGSSHNGSGDGGAAVPTSGPG 170
Cdd:PRK07764 438 APAPPSPAGNAPAGgapspPPAAAPSAQPAPAPAAAPEPTAAPAPAPPAAPAPAAAPAAPAAP 500
 
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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