|
Name |
Accession |
Description |
Interval |
E-value |
| Ten_N |
pfam06484 |
Teneurin Intracellular Region; This family is found in the intracellular N-terminal region of ... |
192-351 |
6.40e-79 |
|
Teneurin Intracellular Region; This family is found in the intracellular N-terminal region of the Teneurin family of proteins. These proteins are 'pair-rule' genes and are involved in tissue patterning, specifically probably neural patterning. The intracellular domain is cleaved in response to homophilic interaction of the extracellular domain, and translocates to the nucleus. Here it probably carries out to some transcriptional regulatory activity. The length of this region and the conservation suggests that there may be two structural domains here (personal obs:C Yeats).
Pssm-ID: 461932 [Multi-domain] Cd Length: 367 Bit Score: 266.46 E-value: 6.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 192 DPGKLAAPGSAP--HGHGEGARRQEQPSNNPGQPTLQ----PLPPSHKQHpAQHHPSITSLNRNSLTNRRNQSPAPPAAL 265
Cdd:pfam06484 203 DPDEEFSPNSYLvrTGSGPQSAPSEQPPNFQNHSRLRtpppPLPPPHKQN-QHHHPSINSLNRSSLTNRRNPSPAPTASL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 266 PAELQTTPESVQLQDSWVLGSNVPLESRHFLFKTGTGTTPLFSTATPGYTMASGSVYSPPTRPLPRNTLSRSAFKFKKSS 345
Cdd:pfam06484 282 PAELQSTQESVQLQDSWVLNSNVPLETRHFLFKTGTGTTPLFCTASPGYPLTSGTVYSPPPRPLPRNTFSRPAFKLKKPY 361
|
....*.
gi 1907188991 346 KYCSWR 351
Cdd:pfam06484 362 KYCSWK 367
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
834-1193 |
9.57e-41 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 154.23 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 834 VSSIMGNGRRrsiscpscnGQADGNKLLA----PVALACGIDGSLYVGDF--NYVRRIFPSGNVTSVLELRNKDFRHSSN 907
Cdd:cd14953 1 VSTVAGSGTA---------GFSGGGGTAArfnsPSGVAVDAAGNLYVADRgnHRIRKITPDGVVTTVAGTGTAGFADGGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 908 PAHRYY----LATDPvTGDLYVSDTNTRRIYRpksLTGAKDLTknaeVVAGTGEqclpfdeARCGDGGKAVEATLMSPKG 983
Cdd:cd14953 72 AAAQFNtpsgVAVDA-AGNLYVADTGNHRIRK---ITPDGVVS----TLAGTGT-------AGFSDDGGATAAQFNYPTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 984 MAIDKNGLIYFVDGT--MIRKVDQNGIISTLLGSNDLTSAR--PLTcdtsmhisQVRLEWPTDLAINPMDNsIYVLD--N 1057
Cdd:cd14953 137 VAVDAAGNLYVADTGnhRIRKITPDGVVTTVAGTGGAGYAGdgPAT--------AAQFNNPTGVAVDAAGN-LYVADrgN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1058 NVVLQITENRQVRIAAGRPmhcqvpGVEYPVGKHAVQTTLESATAIAVSYSGVLYITETDEkkiNRIRQVTTDGEISLVA 1137
Cdd:cd14953 208 HRIRKITPDGVVTTVAGTG------TAGFSGDGGATAAQLNNPTGVAVDAAGNLYVADSGN---HRIRKITPAGVVTTVA 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907188991 1138 GIPSEcdckndancdcyQSGD-GYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAV 1193
Cdd:cd14953 279 GGGAG------------FSGDgGPATSAQFNNPTGVAVDAAGNLYVADTGNNRIRKI 323
|
|
| Tox-GHH |
pfam15636 |
GHH signature containing HNH/Endo VII superfamily nuclease toxin; A predicted toxin of the HNH ... |
2310-2387 |
6.84e-40 |
|
GHH signature containing HNH/Endo VII superfamily nuclease toxin; A predicted toxin of the HNH/Endonuclease VII fold present in bacterial polymorphic toxin systems with a characteriztic sG[HQ]H signature motif. In bacterial polymorphic toxin systems, the toxin is exported by the type 2, type 6, type 7 or TcdB/TcaC-type secretion system. The metazoan teneurin proteins possess an inactive of this domain at their C-terminus.
Pssm-ID: 464783 Cd Length: 78 Bit Score: 142.75 E-value: 6.84e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907188991 2310 EEKARILEQARQRALARAWAREQQRVRDGEEGARLWTEGEKRQLLSAGKVQGYDGYYVLSVEQYPELADSANNIQFLR 2387
Cdd:pfam15636 1 EERKRLLEHAKKRAVREAWHRERQLLRNGLPGSRDWTDEEKEELLSTGSVPGYDGEYIHPVEQYPELADDPSNIRFRK 78
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
1147-2087 |
8.21e-32 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 136.81 E-value: 8.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1147 NDANCDCYQSGDGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKNKPLLNSMNFYEVASPTDQELYIFDINGTHQ 1226
Cdd:COG3209 109 AAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPATGVGTGA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1227 YTVSLVTGDYLYNFSYSNDNDVTAVTDSNGNTLRIRRDPNRMPVRVVSPDNQVIWLTIGTNGCLKSMTAQGLELVLFTYH 1306
Cdd:COG3209 189 VTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAATTLGGTTGAGTG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1307 GNSGLLATK---SDETGWTTFFDYDSEGRLTNVTFPTGVVTNLHGDMDKAITVDIESSSREEDVSITSNLSSIDSFYTMV 1383
Cdd:COG3209 269 ASGAGLDAStgtGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1384 QDQLRNSYQIGYDGSLRIFYASGLDSHYQTEPHVLAGTANPTVAKRNMTLPGENGQNLVEWRFRKEQAQGKVNVFGRKLR 1463
Cdd:COG3209 349 VGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDGGPATAAGALTA 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1464 VNGRNLLSVDFDRTTKTEKIYDDHRKFLLRIAYDTSGHPTLWLPSSKLMAVNVTYSSTGQIASIQRGTTSEKVDYDSQGR 1543
Cdd:COG3209 429 GGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1544 IVSRVFADGKTWSYTYLEKSMVLLLHSQRQYIFEYDMWDRLSAITMPSVARHTMQTIRSIGYYRNIYNPPESNASIITDY 1623
Cdd:COG3209 509 TTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGT 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1624 NEEGLLLQTAFLGTSRRVLFKYRRQTRLSEILYDSTRVSFTYDETAGVLKTVNLQSDGFicTIRYRQIGPLIDRQIFRFS 1703
Cdd:COG3209 589 ATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGT--GVTTTGTTTTRATGTTGTG 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1704 EDGMVNARFDYSYDNSFRVTSMQGVINETPLPIDLYQFDDISGKVEQFGKFGVIYYDINQIISTAVMTYTKHFDAHGRIK 1783
Cdd:COG3209 667 TGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGTGGTTGTLTT 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1784 EIQYEifRSLMYWITIQYDNMGRVTKREIKIGPFANTTKYAYEYDVDGQLQTVYLNEKIMWRYNYDLNGNLHLLNPSSSA 1863
Cdd:COG3209 747 TSTTT--TTTAGALTYTYDALGRLTSETTPGGVTQGTYTTRYTYDALGRLTSVTYPDGETVTYTYDALGRLTSVITVGSG 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1864 RLTPL-----RYDLRDRITRLgdvqyrldEDGFLRQRGTEIFEYSSKGLLTRVYSKGSGWTviYRYDGLGRRVSSKTSLG 1938
Cdd:COG3209 825 GGTDLqdrtyTYDAAGNITSI--------TDALRAGTLTQTYTYDALGRLTSATDPGTTES--YTYDANGNLTSRTDGGT 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1939 QHLQFFYADLtyPTRITHvynhSSSEITSLYYDLQGHlfameissgdefyiaSDNTGTPLAVFSSNGLMLKQIQYTAYGE 2018
Cdd:COG3209 895 TTYTYDALGR--LVSVTK----PDGTTTTYTYDALGH---------------TDHLGSVRALTDASGQVVWRYDYDPFGN 953
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907188991 2019 IYFDSNVDFQLVIGFHGGLYDPLTKLIHFGERDYDILAGRWTTPDieiwkRIGKDPAPfNLYMFRNNNP 2087
Cdd:COG3209 954 LLAETSGAAANPLRFTGQEYDAETGLYYNGARYYDPALGRFLSPD-----PIGLAGGL-NLYAYVGNNP 1016
|
|
| Rhs_assc_core |
TIGR03696 |
RHS repeat-associated core domain; This model represents a conserved unique core sequence ... |
2013-2087 |
3.17e-09 |
|
RHS repeat-associated core domain; This model represents a conserved unique core sequence shared by large numbers of proteins. It is occasional in the Archaea Methanosarcina barkeri) but common in bacteria and eukaryotes. Most fall into two large classes. One class consists of long proteins in which two classes of repeats are abundant: an FG-GAP repeat (pfam01839) class, and an RHS repeat (pfam05593) or YD repeat (TIGR01643). This class includes secreted bacterial insecticidal toxins and intercellular signalling proteins such as the teneurins in animals. The other class consists of uncharacterized proteins shorter than 400 amino acids, where this core domain of about 75 amino acids tends to occur in the N-terminal half. Over twenty such proteins are found in Pseudomonas putida alone; little sequence similarity or repeat structure is found among these proteins outside the region modeled by this domain.
Pssm-ID: 274730 [Multi-domain] Cd Length: 77 Bit Score: 55.58 E-value: 3.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907188991 2013 YTAYGEIYFDSNVDFQLvIGFHGGLYDPLTKLIHFGERDYDILAGRWTTPDieiwkRIGKDpAPFNLYMFRNNNP 2087
Cdd:TIGR03696 1 YDPYGEVLSESGAAPNP-LRFTGQYYDAETGLYYNGARYYDPELGRFLSPD-----PIGLG-GGLNLYAYVGNNP 68
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
863-1141 |
1.04e-08 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 58.88 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 863 PVALACGIDGSLYVGDF--NYVRRIFP-SGNVTsvlelrnkdfRHSSNPAHRYY-LATDPvTGDLYVSDTNTRRIYRpks 938
Cdd:COG4257 19 PRDVAVDPDGAVWFTDQggGRIGRLDPaTGEFT----------EYPLGGGSGPHgIAVDP-DGNLWFTDNGNNRIGR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 939 LTGAkdlTKNAEVVAGTGEQCLPFdearcgdggkaveatlmspkGMAIDKNGLIYFVDGT--MIRKVD-QNGIISTLLGS 1015
Cdd:COG4257 85 IDPK---TGEITTFALPGGGSNPH--------------------GIAFDPDGNLWFTDQGgnRIGRLDpATGEVTEFPLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1016 NDLTSARPLTCD--------------------TSMHISQVRLE----WPTDLAINPmDNSIYVLD--NNVVLQITEnrqv 1069
Cdd:COG4257 142 TGGAGPYGIAVDpdgnlwvtdfganaigridpDTGTLTEYALPtpgaGPRGLAVDP-DGNLWVADtgSGRIGRFDP---- 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907188991 1070 riAAGRpmhcqvpgveypVGKHAVQTTLESATAIAVSYSGVLYITETDekkINRIRQVTTDGEISLVAgIPS 1141
Cdd:COG4257 217 --KTGT------------VTEYPLPGGGARPYGVAVDGDGRVWFAESG---ANRIVRFDPDTELTEYV-LPS 270
|
|
| acid_disulf_rpt |
NF033662 |
acidic double-disulfide repeat; The acidic double-disulfide repeat is an Asp-rich repeat with ... |
464-494 |
1.44e-08 |
|
acidic double-disulfide repeat; The acidic double-disulfide repeat is an Asp-rich repeat with four nearly invariant Cys residues in a repeat length of about 35 amino acids.
Pssm-ID: 411265 [Multi-domain] Cd Length: 32 Bit Score: 52.13 E-value: 1.44e-08
10 20 30
....*....|....*....|....*....|.
gi 1907188991 464 AMETLCTDSKDNEGDGLIDCMDPDCCLQSSC 494
Cdd:NF033662 2 ATDTTCSDGIDNDGDGLTDCADPDCAGNPVC 32
|
|
| PLN02919 |
PLN02919 |
haloacid dehalogenase-like hydrolase family protein |
914-1197 |
3.36e-05 |
|
haloacid dehalogenase-like hydrolase family protein
Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 49.46 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 914 LATDPVTGDLYVSDTNTRRIYrpksltgAKDLTKNAEV-VAGTGEQCL---PFDEArcgdggkaveaTLMSPKGMAID-K 988
Cdd:PLN02919 573 LAIDLLNNRLFISDSNHNRIV-------VTDLDGNFIVqIGSTGEEGLrdgSFEDA-----------TFNRPQGLAYNaK 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 989 NGLIYFVD--GTMIRKVD-QNGIISTLLGS----NDLTSARPLTcdtsmhiSQVrLEWPTDLAINPMDNSIYV------- 1054
Cdd:PLN02919 635 KNLLYVADteNHALREIDfVNETVRTLAGNgtkgSDYQGGKKGT-------SQV-LNSPWDVCFEPVNEKVYIamagqhq 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1055 ------LD-------------------------------------NNVVLQITENRQVR-----------IAAGRPMhcq 1080
Cdd:PLN02919 707 iweyniSDgvtrvfsgdgyernlngssgtstsfaqpsgislspdlKELYIADSESSSIRaldlktggsrlLAGGDPT--- 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1081 VPGVEYPVGKH---AVQTTLESATAIAVSYSGVLYITETDEKKINRIRQVTtdGEISLVAGIPsecdckndancdcyQSG 1157
Cdd:PLN02919 784 FSDNLFKFGDHdgvGSEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLDPAT--KRVTTLAGTG--------------KAG 847
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907188991 1158 --DGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKNK 1197
Cdd:PLN02919 848 fkDGKALKAQLSEPAGLALGENGRLFVADTNNSLIRYLDLNK 889
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
1162-1288 |
7.20e-05 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 46.93 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1162 KDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKN-KPLLN-------SMNFYE---VASPTDQELYI----------FD 1220
Cdd:cd05819 3 GPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDgNFITSfgsfgsgDGQFNEpagVAVDSDGNLYVadtgnhriqkFD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907188991 1221 INGTHQYTVSlVTGDYLYNFSY------SNDNDVtAVTDSNGNtlRIrrdpnrmpvRVVSPDNQVIwLTIGTNG 1288
Cdd:cd05819 83 PDGNFLASFG-GSGDGDGEFNGprgiavDSSGNI-YVADTGNH--RI---------QKFDPDGEFL-TTFGSGG 142
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
432-461 |
5.20e-04 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 39.54 E-value: 5.20e-04
10 20 30
....*....|....*....|....*....|
gi 1907188991 432 PGLCNSNGRCTLDQNGWHCVCQPGWRGAGC 461
Cdd:cd00054 8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
|
|
| EGF |
pfam00008 |
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
435-458 |
1.17e-03 |
|
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.
Pssm-ID: 394967 Cd Length: 31 Bit Score: 38.13 E-value: 1.17e-03
|
| EGF |
smart00181 |
Epidermal growth factor-like domain; |
431-458 |
8.91e-03 |
|
Epidermal growth factor-like domain;
Pssm-ID: 214544 Cd Length: 35 Bit Score: 35.96 E-value: 8.91e-03
|
| RHS_repeat |
pfam05593 |
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
1310-1341 |
9.15e-03 |
|
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain.
Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 36.04 E-value: 9.15e-03
10 20 30
....*....|....*....|....*....|..
gi 1907188991 1310 GLLATKSDETGWTTFFDYDSEGRLTNVTFPTG 1341
Cdd:pfam05593 5 GRLTSVTDPDGRVTTYTYDAAGRLTAVTDPDG 36
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Ten_N |
pfam06484 |
Teneurin Intracellular Region; This family is found in the intracellular N-terminal region of ... |
192-351 |
6.40e-79 |
|
Teneurin Intracellular Region; This family is found in the intracellular N-terminal region of the Teneurin family of proteins. These proteins are 'pair-rule' genes and are involved in tissue patterning, specifically probably neural patterning. The intracellular domain is cleaved in response to homophilic interaction of the extracellular domain, and translocates to the nucleus. Here it probably carries out to some transcriptional regulatory activity. The length of this region and the conservation suggests that there may be two structural domains here (personal obs:C Yeats).
Pssm-ID: 461932 [Multi-domain] Cd Length: 367 Bit Score: 266.46 E-value: 6.40e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 192 DPGKLAAPGSAP--HGHGEGARRQEQPSNNPGQPTLQ----PLPPSHKQHpAQHHPSITSLNRNSLTNRRNQSPAPPAAL 265
Cdd:pfam06484 203 DPDEEFSPNSYLvrTGSGPQSAPSEQPPNFQNHSRLRtpppPLPPPHKQN-QHHHPSINSLNRSSLTNRRNPSPAPTASL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 266 PAELQTTPESVQLQDSWVLGSNVPLESRHFLFKTGTGTTPLFSTATPGYTMASGSVYSPPTRPLPRNTLSRSAFKFKKSS 345
Cdd:pfam06484 282 PAELQSTQESVQLQDSWVLNSNVPLETRHFLFKTGTGTTPLFCTASPGYPLTSGTVYSPPPRPLPRNTFSRPAFKLKKPY 361
|
....*.
gi 1907188991 346 KYCSWR 351
Cdd:pfam06484 362 KYCSWK 367
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
834-1193 |
9.57e-41 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 154.23 E-value: 9.57e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 834 VSSIMGNGRRrsiscpscnGQADGNKLLA----PVALACGIDGSLYVGDF--NYVRRIFPSGNVTSVLELRNKDFRHSSN 907
Cdd:cd14953 1 VSTVAGSGTA---------GFSGGGGTAArfnsPSGVAVDAAGNLYVADRgnHRIRKITPDGVVTTVAGTGTAGFADGGG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 908 PAHRYY----LATDPvTGDLYVSDTNTRRIYRpksLTGAKDLTknaeVVAGTGEqclpfdeARCGDGGKAVEATLMSPKG 983
Cdd:cd14953 72 AAAQFNtpsgVAVDA-AGNLYVADTGNHRIRK---ITPDGVVS----TLAGTGT-------AGFSDDGGATAAQFNYPTG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 984 MAIDKNGLIYFVDGT--MIRKVDQNGIISTLLGSNDLTSAR--PLTcdtsmhisQVRLEWPTDLAINPMDNsIYVLD--N 1057
Cdd:cd14953 137 VAVDAAGNLYVADTGnhRIRKITPDGVVTTVAGTGGAGYAGdgPAT--------AAQFNNPTGVAVDAAGN-LYVADrgN 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1058 NVVLQITENRQVRIAAGRPmhcqvpGVEYPVGKHAVQTTLESATAIAVSYSGVLYITETDEkkiNRIRQVTTDGEISLVA 1137
Cdd:cd14953 208 HRIRKITPDGVVTTVAGTG------TAGFSGDGGATAAQLNNPTGVAVDAAGNLYVADSGN---HRIRKITPAGVVTTVA 278
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1907188991 1138 GIPSEcdckndancdcyQSGD-GYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAV 1193
Cdd:cd14953 279 GGGAG------------FSGDgGPATSAQFNNPTGVAVDAAGNLYVADTGNNRIRKI 323
|
|
| Tox-GHH |
pfam15636 |
GHH signature containing HNH/Endo VII superfamily nuclease toxin; A predicted toxin of the HNH ... |
2310-2387 |
6.84e-40 |
|
GHH signature containing HNH/Endo VII superfamily nuclease toxin; A predicted toxin of the HNH/Endonuclease VII fold present in bacterial polymorphic toxin systems with a characteriztic sG[HQ]H signature motif. In bacterial polymorphic toxin systems, the toxin is exported by the type 2, type 6, type 7 or TcdB/TcaC-type secretion system. The metazoan teneurin proteins possess an inactive of this domain at their C-terminus.
Pssm-ID: 464783 Cd Length: 78 Bit Score: 142.75 E-value: 6.84e-40
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907188991 2310 EEKARILEQARQRALARAWAREQQRVRDGEEGARLWTEGEKRQLLSAGKVQGYDGYYVLSVEQYPELADSANNIQFLR 2387
Cdd:pfam15636 1 EERKRLLEHAKKRAVREAWHRERQLLRNGLPGSRDWTDEEKEELLSTGSVPGYDGEYIHPVEQYPELADDPSNIRFRK 78
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
914-1194 |
3.97e-38 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 146.91 E-value: 3.97e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 914 LATDPvTGDLYVSDTNTRRIYRpksltgakdLTKNAEV--VAGTGEqclpfdEARCGDGGKAveATLMSPKGMAIDKNGL 991
Cdd:cd14953 28 VAVDA-AGNLYVADRGNHRIRK---------ITPDGVVttVAGTGT------AGFADGGGAA--AQFNTPSGVAVDAAGN 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 992 IYFVDGT--MIRKVDQNGIISTLLGsndlTSARPLTCDTSMhiSQVRLEWPTDLAINPMDNsIYVLD--NNVVLQITENR 1067
Cdd:cd14953 90 LYVADTGnhRIRKITPDGVVSTLAG----TGTAGFSDDGGA--TAAQFNYPTGVAVDAAGN-LYVADtgNHRIRKITPDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1068 QVRIAAGRPmhcqVPGveYPVGKHAVQTTLESATAIAVSYSGVLYITETDEkkiNRIRQVTTDGEISLVAGIPSEcdckn 1147
Cdd:cd14953 163 VVTTVAGTG----GAG--YAGDGPATAAQFNNPTGVAVDAAGNLYVADRGN---HRIRKITPDGVVTTVAGTGTA----- 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907188991 1148 dancdcYQSGDGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAVS 1194
Cdd:cd14953 229 ------GFSGDGGATAAQLNNPTGVAVDAAGNLYVADSGNHRIRKIT 269
|
|
| RhsA |
COG3209 |
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction ... |
1147-2087 |
8.21e-32 |
|
Uncharacterized conserved protein RhaS, contains 28 RHS repeats [General function prediction only];
Pssm-ID: 442442 [Multi-domain] Cd Length: 1103 Bit Score: 136.81 E-value: 8.21e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1147 NDANCDCYQSGDGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKNKPLLNSMNFYEVASPTDQELYIFDINGTHQ 1226
Cdd:COG3209 109 AAATASAGRLVSTGAGAGGTVTAATGGTLGATAGSATTGSTDGGRGGVAVTGLAGGGASAYGLTLGGAAAGPATGVGTGA 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1227 YTVSLVTGDYLYNFSYSNDNDVTAVTDSNGNTLRIRRDPNRMPVRVVSPDNQVIWLTIGTNGCLKSMTAQGLELVLFTYH 1306
Cdd:COG3209 189 VTLATGLAGSALLALGSGAILGGLAGAYSGSATTATGTALGTPASVAATVTGSATGAAGAGAAVATAATTLGGTTGAGTG 268
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1307 GNSGLLATK---SDETGWTTFFDYDSEGRLTNVTFPTGVVTNLHGDMDKAITVDIESSSREEDVSITSNLSSIDSFYTMV 1383
Cdd:COG3209 269 ASGAGLDAStgtGGAGGSNAAATAGGLGGAGLGSGGAGGGGTAGGTTTAAGTTGTAAVSGAADAGTTTTTGTGTGGTTTT 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1384 QDQLRNSYQIGYDGSLRIFYASGLDSHYQTEPHVLAGTANPTVAKRNMTLPGENGQNLVEWRFRKEQAQGKVNVFGRKLR 1463
Cdd:COG3209 349 VGGGGSLTLGGYGAAGGLTTSVGAGGGGSTSGSTTTVGGGGTATGSGGGSSTTGVGAGTTTTSTTGGDGGPATAAGALTA 428
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1464 VNGRNLLSVDFDRTTKTEKIYDDHRKFLLRIAYDTSGHPTLWLPSSKLMAVNVTYSSTGQIASIQRGTTSEKVDYDSQGR 1543
Cdd:COG3209 429 GGTATGTGTGGGGTTAGTDATTTTGGAGASGTLTTTGGAATGATTGGGTEAGTGGGTLTSGSAGATTLGTDTTLDDTLGG 508
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1544 IVSRVFADGKTWSYTYLEKSMVLLLHSQRQYIFEYDMWDRLSAITMPSVARHTMQTIRSIGYYRNIYNPPESNASIITDY 1623
Cdd:COG3209 509 TTTTTAGARGLVVTTGTTLTLGTTTTATLSATDATGTGDTTTTGTVGTGTSTGTGGTGTVTTTGDGTGGASTTTGTTGGT 588
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1624 NEEGLLLQTAFLGTSRRVLFKYRRQTRLSEILYDSTRVSFTYDETAGVLKTVNLQSDGFicTIRYRQIGPLIDRQIFRFS 1703
Cdd:COG3209 589 ATTTTVTTTTTTSTAGTTTTTTSGYTRAGLTLTLGTGTASGLERATASTGSTTGGTTGT--GVTTTGTTTTRATGTTGTG 666
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1704 EDGMVNARFDYSYDNSFRVTSMQGVINETPLPIDLYQFDDISGKVEQFGKFGVIYYDINQIISTAVMTYTKHFDAHGRIK 1783
Cdd:COG3209 667 TGVTAGLTTLATGGTTVGGGTGTTSTATTGATTGGTETGTTVTTLAGGTTTRLGTTTTGGGGGTTTDGTGTGGTTGTLTT 746
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1784 EIQYEifRSLMYWITIQYDNMGRVTKREIKIGPFANTTKYAYEYDVDGQLQTVYLNEKIMWRYNYDLNGNLHLLNPSSSA 1863
Cdd:COG3209 747 TSTTT--TTTAGALTYTYDALGRLTSETTPGGVTQGTYTTRYTYDALGRLTSVTYPDGETVTYTYDALGRLTSVITVGSG 824
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1864 RLTPL-----RYDLRDRITRLgdvqyrldEDGFLRQRGTEIFEYSSKGLLTRVYSKGSGWTviYRYDGLGRRVSSKTSLG 1938
Cdd:COG3209 825 GGTDLqdrtyTYDAAGNITSI--------TDALRAGTLTQTYTYDALGRLTSATDPGTTES--YTYDANGNLTSRTDGGT 894
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1939 QHLQFFYADLtyPTRITHvynhSSSEITSLYYDLQGHlfameissgdefyiaSDNTGTPLAVFSSNGLMLKQIQYTAYGE 2018
Cdd:COG3209 895 TTYTYDALGR--LVSVTK----PDGTTTTYTYDALGH---------------TDHLGSVRALTDASGQVVWRYDYDPFGN 953
|
890 900 910 920 930 940
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907188991 2019 IYFDSNVDFQLVIGFHGGLYDPLTKLIHFGERDYDILAGRWTTPDieiwkRIGKDPAPfNLYMFRNNNP 2087
Cdd:COG3209 954 LLAETSGAAANPLRFTGQEYDAETGLYYNGARYYDPALGRFLSPD-----PIGLAGGL-NLYAYVGNNP 1016
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
951-1194 |
1.45e-31 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 127.65 E-value: 1.45e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 951 VVAGTGeqclpfdeARCGDGGKAVEATLMSPKGMAIDKNGLIYFVDGT--MIRKVDQNGIISTLLG------SNDLTSAr 1022
Cdd:cd14953 3 TVAGSG--------TAGFSGGGGTAARFNSPSGVAVDAAGNLYVADRGnhRIRKITPDGVVTTVAGtgtagfADGGGAA- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1023 pltcdtsmhisqVRLEWPTDLAINPMDNsIYVLD--NNVVLQITENRQVRIAAGrpmhcqVPGVEYPVGKHAVQTTLESA 1100
Cdd:cd14953 74 ------------AQFNTPSGVAVDAAGN-LYVADtgNHRIRKITPDGVVSTLAG------TGTAGFSDDGGATAAQFNYP 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1101 TAIAVSYSGVLYITETDEkkiNRIRQVTTDGEISLVAGIPSEcdckndancdcYQSGDGYAKDAKLNAPSSLAASPDGTL 1180
Cdd:cd14953 135 TGVAVDAAGNLYVADTGN---HRIRKITPDGVVTTVAGTGGA-----------GYAGDGPATAAQFNNPTGVAVDAAGNL 200
|
250
....*....|....
gi 1907188991 1181 YIADLGNIRIRAVS 1194
Cdd:cd14953 201 YVADRGNHRIRKIT 214
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
853-1191 |
2.77e-19 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 90.07 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 853 GQADGnKLLAPVALACGIDGSLYVGDF--NYVRRIFPSGNVTSVLELRNKDFRHSSNPAHryyLATDPvTGDLYVSDTNT 930
Cdd:cd05819 1 GTGPG-ELNNPQGIAVDSSGNIYVADTgnNRIQVFDPDGNFITSFGSFGSGDGQFNEPAG---VAVDS-DGNLYVADTGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 931 RRIYRpksltgakdLTKNAEVVAGTGeqclpfdearcGDGGKAVEatLMSPKGMAIDKNGLIYFVDgTM---IRKVDQNG 1007
Cdd:cd05819 76 HRIQK---------FDPDGNFLASFG-----------GSGDGDGE--FNGPRGIAVDSSGNIYVAD-TGnhrIQKFDPDG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1008 IISTLLGSNDLTSARpltcdtsmhisqvrLEWPTDLAINPmDNSIYVLDnnvvlqiTENRQVRI--AAGRPMHcQVPGVE 1085
Cdd:cd05819 133 EFLTTFGSGGSGPGQ--------------FNGPTGVAVDS-DGNIYVAD-------TGNHRIQVfdPDGNFLT-TFGSTG 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1086 YPVGKhavqttLESATAIAVSYSGVLYITETDEkkiNRIRQVTTDGEISlvagipsecdckndancdcYQSGDGYAKDAK 1165
Cdd:cd05819 190 TGPGQ------FNYPTGIAVDSDGNIYVADSGN---NRVQVFDPDGAGF-------------------GGNGNFLGSDGQ 241
|
330 340
....*....|....*....|....*.
gi 1907188991 1166 LNAPSSLAASPDGTLYIADLGNIRIR 1191
Cdd:cd05819 242 FNRPSGLAVDSDGNLYVADTGNNRIQ 267
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
852-1124 |
7.27e-16 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 80.06 E-value: 7.27e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 852 NGQADGNkLLAPVALACGIDGSLYVGDF--NYVRRIFPSGNVTSVLELRNKDFRHSSNPahrYYLATDPvTGDLYVSDTN 929
Cdd:cd05819 47 FGSGDGQ-FNEPAGVAVDSDGNLYVADTgnHRIQKFDPDGNFLASFGGSGDGDGEFNGP---RGIAVDS-SGNIYVADTG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 930 TRRIYRpksltgakdLTKNAEVVAGTGeqclpfdearcgdGGKAVEATLMSPKGMAIDKNGLIYFVDGT--MIRKVDQNG 1007
Cdd:cd05819 122 NHRIQK---------FDPDGEFLTTFG-------------SGGSGPGQFNGPTGVAVDSDGNIYVADTGnhRIQVFDPDG 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1008 IISTLLGSNDLTSARpltcdtsmhisqvrLEWPTDLAINPMDNsIYVLD--NNVVLQITENRQVRIAAGRPMhCQVPGVE 1085
Cdd:cd05819 180 NFLTTFGSTGTGPGQ--------------FNYPTGIAVDSDGN-IYVADsgNNRVQVFDPDGAGFGGNGNFL-GSDGQFN 243
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907188991 1086 YPVGkhavqttlesataIAVSYSGVLYITETDEKKINRI 1124
Cdd:cd05819 244 RPSG-------------LAVDSDGNLYVADTGNNRIQVF 269
|
|
| Rhs_assc_core |
TIGR03696 |
RHS repeat-associated core domain; This model represents a conserved unique core sequence ... |
2013-2087 |
3.17e-09 |
|
RHS repeat-associated core domain; This model represents a conserved unique core sequence shared by large numbers of proteins. It is occasional in the Archaea Methanosarcina barkeri) but common in bacteria and eukaryotes. Most fall into two large classes. One class consists of long proteins in which two classes of repeats are abundant: an FG-GAP repeat (pfam01839) class, and an RHS repeat (pfam05593) or YD repeat (TIGR01643). This class includes secreted bacterial insecticidal toxins and intercellular signalling proteins such as the teneurins in animals. The other class consists of uncharacterized proteins shorter than 400 amino acids, where this core domain of about 75 amino acids tends to occur in the N-terminal half. Over twenty such proteins are found in Pseudomonas putida alone; little sequence similarity or repeat structure is found among these proteins outside the region modeled by this domain.
Pssm-ID: 274730 [Multi-domain] Cd Length: 77 Bit Score: 55.58 E-value: 3.17e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907188991 2013 YTAYGEIYFDSNVDFQLvIGFHGGLYDPLTKLIHFGERDYDILAGRWTTPDieiwkRIGKDpAPFNLYMFRNNNP 2087
Cdd:TIGR03696 1 YDPYGEVLSESGAAPNP-LRFTGQYYDAETGLYYNGARYYDPELGRFLSPD-----PIGLG-GGLNLYAYVGNNP 68
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
863-1141 |
1.04e-08 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 58.88 E-value: 1.04e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 863 PVALACGIDGSLYVGDF--NYVRRIFP-SGNVTsvlelrnkdfRHSSNPAHRYY-LATDPvTGDLYVSDTNTRRIYRpks 938
Cdd:COG4257 19 PRDVAVDPDGAVWFTDQggGRIGRLDPaTGEFT----------EYPLGGGSGPHgIAVDP-DGNLWFTDNGNNRIGR--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 939 LTGAkdlTKNAEVVAGTGEQCLPFdearcgdggkaveatlmspkGMAIDKNGLIYFVDGT--MIRKVD-QNGIISTLLGS 1015
Cdd:COG4257 85 IDPK---TGEITTFALPGGGSNPH--------------------GIAFDPDGNLWFTDQGgnRIGRLDpATGEVTEFPLP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1016 NDLTSARPLTCD--------------------TSMHISQVRLE----WPTDLAINPmDNSIYVLD--NNVVLQITEnrqv 1069
Cdd:COG4257 142 TGGAGPYGIAVDpdgnlwvtdfganaigridpDTGTLTEYALPtpgaGPRGLAVDP-DGNLWVADtgSGRIGRFDP---- 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907188991 1070 riAAGRpmhcqvpgveypVGKHAVQTTLESATAIAVSYSGVLYITETDekkINRIRQVTTDGEISLVAgIPS 1141
Cdd:COG4257 217 --KTGT------------VTEYPLPGGGARPYGVAVDGDGRVWFAESG---ANRIVRFDPDTELTEYV-LPS 270
|
|
| acid_disulf_rpt |
NF033662 |
acidic double-disulfide repeat; The acidic double-disulfide repeat is an Asp-rich repeat with ... |
464-494 |
1.44e-08 |
|
acidic double-disulfide repeat; The acidic double-disulfide repeat is an Asp-rich repeat with four nearly invariant Cys residues in a repeat length of about 35 amino acids.
Pssm-ID: 411265 [Multi-domain] Cd Length: 32 Bit Score: 52.13 E-value: 1.44e-08
10 20 30
....*....|....*....|....*....|.
gi 1907188991 464 AMETLCTDSKDNEGDGLIDCMDPDCCLQSSC 494
Cdd:NF033662 2 ATDTTCSDGIDNDGDGLTDCADPDCAGNPVC 32
|
|
| NHL_like_2 |
cd14957 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
978-1288 |
1.99e-08 |
|
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271327 [Multi-domain] Cd Length: 280 Bit Score: 58.05 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 978 LMSPKGMAIDKNGLIYFVD--GTMIRKVDQNGIISTLLGSNDltsarpltcdtsmhISQVRLEWPTDLAINPMDNsIYVL 1055
Cdd:cd14957 17 FNTPRGIAVDSAGNIYVADtgNNRIQVFTSSGVYSYSIGSGG--------------TGSGQFNSPYGIAVDSNGN-IYVA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1056 DNNvvlqitENR-QVRIAAGrpmhcqvpGVEYPVGKHAVQTT-LESATAIAVSYSGVLYITETDEkkiNRIRQVTTDGEI 1133
Cdd:cd14957 82 DTD------NNRiQVFNSSG--------VYQYSIGTGGSGDGqFNGPYGIAVDSNGNIYVADTGN---HRIQVFTSSGTF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1134 slvagipsecdckndancdCYQSGDGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRavsknkpllnsmnfyevasptd 1213
Cdd:cd14957 145 -------------------SYSIGSGGTGPGQFNGPQGIAVDSDGNIYVADTGNHRIQ---------------------- 183
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907188991 1214 qelyIFDINGTHQYTV-SLVTGDYLynFSYSNDNDVtavtDSNGNTLRIRRDPNRmpVRVVSPDNqVIWLTIGTNG 1288
Cdd:cd14957 184 ----VFTSSGTFQYTFgSSGSGPGQ--FSDPYGIAV----DSDGNIYVADTGNHR--IQVFTSSG-AYQYSIGTSG 246
|
|
| NHL_PKND_like |
cd14952 |
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ... |
914-1190 |
2.02e-08 |
|
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271322 [Multi-domain] Cd Length: 247 Bit Score: 57.60 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 914 LATDPvTGDLYVSDTNTRRIYRpksltgakdltknaeVVAGTGEQ-CLPFDEarcgdggkaveatLMSPKGMAIDKNGLI 992
Cdd:cd14952 15 VAVDA-AGNVYVADSGNNRVLK---------------LAAGSTTQtVLPFTG-------------LYQPQGVAVDAAGTV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 993 YFVDGtmirkvDQNGIISTLLGSNDLTsARPLTcdtsmhisqvRLEWPTDLAINPMDNsIYVLDNnvvlqiTENRQVRIA 1072
Cdd:cd14952 66 YVTDF------GNNRVLKLAAGSTTQT-VLPFT----------GLNDPTGVAVDAAGN-VYVADT------GNNRVLKLA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1073 AGRPMHCQVPgveypvgkhavQTTLESATAIAVSYSGVLYITETDEkkiNRIRQvttdgeisLVAGipsecdckndANCD 1152
Cdd:cd14952 122 AGSNTQTVLP-----------FTGLSNPDGVAVDGAGNVYVTDTGN---NRVLK--------LAAG----------STTQ 169
|
250 260 270
....*....|....*....|....*....|....*...
gi 1907188991 1153 CYQSGDGyakdakLNAPSSLAASPDGTLYIADLGNIRI 1190
Cdd:cd14952 170 TVLPFTG------LNSPSGVAVDTAGNVYVTDHGNNRV 201
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
921-1195 |
1.35e-06 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271326 [Multi-domain] Cd Length: 274 Bit Score: 52.28 E-value: 1.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 921 GDLYVSDTNTRRIyrpksltgakdltknaEVVAGTGEQCLPFDEARCGDGGkaveatLMSPKGMAIDKNGLIYFVDGT-- 998
Cdd:cd14956 24 DNVYVADARNGRI----------------QVFDKDGTFLRRFGTTGDGPGQ------FGRPRGLAVDKDGWLYVADYWgd 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 999 MIRKVDQNGIISTLLGSNdltSARPLTCDTsmhisqvrlewPTDLAINPmDNSIYVLD--NNVVLQITENRQVRIAAGRP 1076
Cdd:cd14956 82 RIQVFTLTGELQTIGGSS---GSGPGQFNA-----------PRGVAVDA-DGNLYVADfgNQRIQKFDPDGSFLRQWGGT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1077 mhcqvpgvEYPVGKhavqttLESATAIAVSYSGVLYITETdekKINRIRQVTTDGEISLVAGIPSecdckndancdcyqS 1156
Cdd:cd14956 147 --------GIEPGS------FNYPRGVAVDPDGTLYVADT---YNDRIQVFDNDGAFLRKWGGRG--------------T 195
|
250 260 270
....*....|....*....|....*....|....*....
gi 1907188991 1157 GDGyakdaKLNAPSSLAASPDGTLYIADLGNIRIRAVSK 1195
Cdd:cd14956 196 GPG-----QFNYPYGIAIDPDGNVFVADFGNNRIQKFTA 229
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
912-1191 |
4.64e-06 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 50.79 E-value: 4.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 912 YYLATDPvTGDLYVSDTNTRRIYRpksltgakdltknaeVVAGTGEqclpFDEARCGDGGkaveatlmSPKGMAIDKNGL 991
Cdd:COG4257 20 RDVAVDP-DGAVWFTDQGGGRIGR---------------LDPATGE----FTEYPLGGGS--------GPHGIAVDPDGN 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 992 IYFVDGT--MIRKVD-QNGIISTLLGSNDLTSarpltcdtsmhisqvrlewPTDLAINPmDNSIYVLD--NNVVLQIT-E 1065
Cdd:COG4257 72 LWFTDNGnnRIGRIDpKTGEITTFALPGGGSN-------------------PHGIAFDP-DGNLWFTDqgGNRIGRLDpA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1066 NRQVRiaagrpmhcqvpgvEYPVGKHAVQTTlesatAIAVSYSGVLYITETdekKINRIRQVTTD-GEISLvagipsecd 1144
Cdd:COG4257 132 TGEVT--------------EFPLPTGGAGPY-----GIAVDPDGNLWVTDF---GANAIGRIDPDtGTLTE--------- 180
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1907188991 1145 ckndancdcyqsgdgYAKDAKLNAPSSLAASPDGTLYIADLGNIRIR 1191
Cdd:COG4257 181 ---------------YALPTPGAGPRGLAVDPDGNLWVADTGSGRIG 212
|
|
| NHL_PKND_like |
cd14952 |
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ... |
860-1121 |
1.70e-05 |
|
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein with a cytosolic kinase domain and an extracellular sensor domain that contains NHL repeats. It plays a key role in the development of central nervous system tuberculosis, by mediating the invasion of host brain endothelia. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271322 [Multi-domain] Cd Length: 247 Bit Score: 48.74 E-value: 1.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 860 LLAPVALACGIDGSLYVGDF--NYVRRIFPSGNVTSVLElrnkdFRHSSNPAHryyLATDPVtGDLYVSDTNTRRIyrpk 937
Cdd:cd14952 51 LYQPQGVAVDAAGTVYVTDFgnNRVLKLAAGSTTQTVLP-----FTGLNDPTG---VAVDAA-GNVYVADTGNNRV---- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 938 sltgakdltknAEVVAGTGEQC-LPFdearcgdggkaveATLMSPKGMAIDKNGLIYFVDGtmirkvDQNGIISTLLGSN 1016
Cdd:cd14952 118 -----------LKLAAGSNTQTvLPF-------------TGLSNPDGVAVDGAGNVYVTDT------GNNRVLKLAAGST 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1017 DLTsARPLTCDTSmhisqvrlewPTDLAINPMDNsIYVLDNNvvlqitENRQVRIAAGRPMHCQVP--GVEYPVGkhavq 1094
Cdd:cd14952 168 TQT-VLPFTGLNS----------PSGVAVDTAGN-VYVTDHG------NNRVLKLAAGSTTPTVLPftGLNGPLG----- 224
|
250 260
....*....|....*....|....*..
gi 1907188991 1095 ttlesataIAVSYSGVLYITETDEKKI 1121
Cdd:cd14952 225 --------VAVDAAGNVYVADRGNDRV 243
|
|
| PLN02919 |
PLN02919 |
haloacid dehalogenase-like hydrolase family protein |
914-1197 |
3.36e-05 |
|
haloacid dehalogenase-like hydrolase family protein
Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 49.46 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 914 LATDPVTGDLYVSDTNTRRIYrpksltgAKDLTKNAEV-VAGTGEQCL---PFDEArcgdggkaveaTLMSPKGMAID-K 988
Cdd:PLN02919 573 LAIDLLNNRLFISDSNHNRIV-------VTDLDGNFIVqIGSTGEEGLrdgSFEDA-----------TFNRPQGLAYNaK 634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 989 NGLIYFVD--GTMIRKVD-QNGIISTLLGS----NDLTSARPLTcdtsmhiSQVrLEWPTDLAINPMDNSIYV------- 1054
Cdd:PLN02919 635 KNLLYVADteNHALREIDfVNETVRTLAGNgtkgSDYQGGKKGT-------SQV-LNSPWDVCFEPVNEKVYIamagqhq 706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1055 ------LD-------------------------------------NNVVLQITENRQVR-----------IAAGRPMhcq 1080
Cdd:PLN02919 707 iweyniSDgvtrvfsgdgyernlngssgtstsfaqpsgislspdlKELYIADSESSSIRaldlktggsrlLAGGDPT--- 783
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1081 VPGVEYPVGKH---AVQTTLESATAIAVSYSGVLYITETDEKKINRIRQVTtdGEISLVAGIPsecdckndancdcyQSG 1157
Cdd:PLN02919 784 FSDNLFKFGDHdgvGSEVLLQHPLGVLCAKDGQIYVADSYNHKIKKLDPAT--KRVTTLAGTG--------------KAG 847
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1907188991 1158 --DGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKNK 1197
Cdd:PLN02919 848 fkDGKALKAQLSEPAGLALGENGRLFVADTNNSLIRYLDLNK 889
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
1162-1288 |
7.20e-05 |
|
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures. The repeats have a catalytic activity in Peptidyl-glycine alpha-amidating monooxygenase; proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Tripartite motif-containing protein 32 interacts with the activation domain of Tat. This interaction is mediated by the NHL repeats.
Pssm-ID: 271320 [Multi-domain] Cd Length: 269 Bit Score: 46.93 E-value: 7.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1162 KDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKN-KPLLN-------SMNFYE---VASPTDQELYI----------FD 1220
Cdd:cd05819 3 GPGELNNPQGIAVDSSGNIYVADTGNNRIQVFDPDgNFITSfgsfgsgDGQFNEpagVAVDSDGNLYVadtgnhriqkFD 82
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907188991 1221 INGTHQYTVSlVTGDYLYNFSY------SNDNDVtAVTDSNGNtlRIrrdpnrmpvRVVSPDNQVIwLTIGTNG 1288
Cdd:cd05819 83 PDGNFLASFG-GSGDGDGEFNGprgiavDSSGNI-YVADTGNH--RI---------QKFDPDGEFL-TTFGSGG 142
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
1156-1196 |
8.82e-05 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat domains is found in a variety of domain architectures. The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271323 [Multi-domain] Cd Length: 323 Bit Score: 47.14 E-value: 8.82e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 1907188991 1156 SGDGYAKDAKLNAPSSLAASPDGTLYIADLGNIRIRAVSKN 1196
Cdd:cd14953 12 FSGGGGTAARFNSPSGVAVDAAGNLYVADRGNHRIRKITPD 52
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
859-1116 |
2.51e-04 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 45.36 E-value: 2.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 859 KLLAPVALACGIDGSLYVGDFnYVRRI--F-PSGNVTSVLElRNKDFRHSSNPAHryyLATDpvTGDLYVSDTNTRRIYr 935
Cdd:cd14963 54 EFKYPYGIAVDSDGNIYVADL-YNGRIqvFdPDGKFLKYFP-EKKDRVKLISPAG---LAID--DGKLYVSDVKKHKVI- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 936 pksltgakdltknaeVVAGTGEQCLPFdearcGDGGKAvEATLMSPKGMAIDKNGLIYFVD--GTMIRKVDQNG-IISTL 1012
Cdd:cd14963 126 ---------------VFDLEGKLLLEF-----GKPGSE-PGELSYPNGIAVDEDGNIYVADsgNGRIQVFDKNGkFIKEL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1013 LGSNDLTSArpltcdtsmhisqvrLEWPTDLAINPmDNSIYVLDN--NVVLQITENRQVRIAAGRpmhcqvPGVEypvgk 1090
Cdd:cd14963 185 NGSPDGKSG---------------FVNPRGIAVDP-DGNLYVVDNlsHRVYVFDEQGKELFTFGG------RGKD----- 237
|
250 260
....*....|....*....|....*.
gi 1907188991 1091 havQTTLESATAIAVSYSGVLYITET 1116
Cdd:cd14963 238 ---DGQFNLPNGLFIDDDGRLYVTDR 260
|
|
| EGF_CA |
cd00054 |
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular ... |
432-461 |
5.20e-04 |
|
Calcium-binding EGF-like domain, present in a large number of membrane-bound and extracellular (mostly animal) proteins. Many of these proteins require calcium for their biological function and calcium-binding sites have been found to be located at the N-terminus of particular EGF-like domains; calcium-binding may be crucial for numerous protein-protein interactions. Six conserved core cysteines form three disulfide bridges as in non calcium-binding EGF domains, whose structures are very similar. EGF_CA can be found in tandem repeat arrangements.
Pssm-ID: 238011 Cd Length: 38 Bit Score: 39.54 E-value: 5.20e-04
10 20 30
....*....|....*....|....*....|
gi 1907188991 432 PGLCNSNGRCTLDQNGWHCVCQPGWRGAGC 461
Cdd:cd00054 8 GNPCQNGGTCVNTVGSYRCSCPPGYTGRNC 37
|
|
| EGF |
pfam00008 |
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very ... |
435-458 |
1.17e-03 |
|
EGF-like domain; There is no clear separation between noise and signal. pfam00053 is very similar, but has 8 instead of 6 conserved cysteines. Includes some cytokine receptors. The EGF domain misses the N-terminus regions of the Ca2+ binding EGF domains (this is the main reason of discrepancy between swiss-prot domain start/end and Pfam). The family is hard to model due to many similar but different sub-types of EGF domains. Pfam certainly misses a number of EGF domains.
Pssm-ID: 394967 Cd Length: 31 Bit Score: 38.13 E-value: 1.17e-03
|
| EGF |
cd00053 |
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large ... |
432-460 |
1.41e-03 |
|
Epidermal growth factor domain, found in epidermal growth factor (EGF) presents in a large number of proteins, mostly animal; the list of proteins currently known to contain one or more copies of an EGF-like pattern is large and varied; the functional significance of EGF-like domains in what appear to be unrelated proteins is not yet clear; a common feature is that these repeats are found in the extracellular domain of membrane-bound proteins or in proteins known to be secreted (exception: prostaglandin G/H synthase); the domain includes six cysteine residues which have been shown to be involved in disulfide bonds; the main structure is a two-stranded beta-sheet followed by a loop to a C-terminal short two-stranded sheet; Subdomains between the conserved cysteines vary in length; the region between the 5th and 6th cysteine contains two conserved glycines of which at least one is present in most EGF-like domains; a subset of these bind calcium.
Pssm-ID: 238010 Cd Length: 36 Bit Score: 38.23 E-value: 1.41e-03
10 20
....*....|....*....|....*....
gi 1907188991 432 PGLCNSNGRCTLDQNGWHCVCQPGWRGAG 460
Cdd:cd00053 5 SNPCSNGGTCVNTPGSYRCVCPPGYTGDR 33
|
|
| NHL_like_6 |
cd14962 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
971-1190 |
1.57e-03 |
|
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271332 [Multi-domain] Cd Length: 271 Bit Score: 42.96 E-value: 1.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 971 GKAVEATLMSPKGMAIDKNGLIYFVDGT--MIRKVDQNGIISTLLGSNDLtsarpltcdtsmhisQVRlewPTDLAINPM 1048
Cdd:cd14962 49 GNAGPNRFVSPIGVAIDANGNLYVSDAElgKVFVFDRDGKFLRAIGAGAL---------------FKR---PTGIAVDPA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1049 DNSIYVLDnnvvlqiTENRQVRI--AAGRPMHcQVPgveyPVGKHAVQttLESATAIAVSYSGVLYITETDEKKINRI-- 1124
Cdd:cd14962 111 GKRLYVVD-------TLAHKVKVfdLDGRLLF-DIG----KRGSGPGE--FNLPTDLAVDRDGNLYVTDTMNFRVQIFda 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1125 --RQVTTDGEISLVAG---IPSECDCKNDAN---CDCYQS---------------GDGYAKDAKLNAPSSLAASPDGTLY 1181
Cdd:cd14962 177 dgKFLRSFGERGDGPGsfaRPKGIAVDSEGNiyvVDAAFDnvqifnpegellltvGGPGSGPGEFYLPSGIAIDKDDRIY 256
|
....*....
gi 1907188991 1182 IADLGNIRI 1190
Cdd:cd14962 257 VVDQFNRRI 265
|
|
| YD_repeat_2x |
TIGR01643 |
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular ... |
1518-1558 |
2.29e-03 |
|
YD repeat (two copies); This model describes two tandem copies of a 21-residue extracellular repeat found in Gram-negative, Gram-positive, and animal proteins. The repeat is named for a YD dipeptide, the most strongly conserved motif of the repeat. These repeats appear in general to be involved in binding carbohydrate; the chicken teneurin-1 YD-repeat region has been shown to bind heparin.
Pssm-ID: 273728 [Multi-domain] Cd Length: 42 Bit Score: 37.57 E-value: 2.29e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 1907188991 1518 YSSTGQ-IASIQRGTTSEKVDYDSQGRIVSRVFADGKTWSYT 1558
Cdd:TIGR01643 1 YDAAGRlTGSTDADGTTTRYTYDAAGRLVEITDADGGSTRYE 42
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
866-1009 |
2.33e-03 |
|
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase YvrE is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 442613 [Multi-domain] Cd Length: 266 Bit Score: 42.19 E-value: 2.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 866 LACGIDGSLYVGDFNYVR------RIFPSGNVTSVLElrnkDFrHSSN-----PAHRYylatdpvtgdLYVSDTNTRRIY 934
Cdd:COG3386 98 GVVDPDGRLYFTDMGEYLptgalyRVDPDGSLRVLAD----GL-TFPNgiafsPDGRT----------LYVADTGAGRIY 162
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907188991 935 R-PKSLTGAkdLTkNAEVVAgtgeqclpfdEARCGDGGkaveatlmsPKGMAIDKNGLIY--FVDGTMIRKVDQNGII 1009
Cdd:COG3386 163 RfDLDADGT--LG-NRRVFA----------DLPDGPGG---------PDGLAVDADGNLWvaLWGGGGVVRFDPDGEL 218
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
858-935 |
3.71e-03 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 41.54 E-value: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 858 NKLLAPVALACGIDGSLYVGDF--NYVRRIFP-SGNVTSvlelrnkdFRHSSNPAHRYYLATDPvTGDLYVSDTNTRRIY 934
Cdd:COG4257 185 TPGAGPRGLAVDPDGNLWVADTgsGRIGRFDPkTGTVTE--------YPLPGGGARPYGVAVDG-DGRVWFAESGANRIV 255
|
.
gi 1907188991 935 R 935
Cdd:COG4257 256 R 256
|
|
| hEGF |
pfam12661 |
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six ... |
435-456 |
4.59e-03 |
|
Human growth factor-like EGF; hEGF, or human growth factor-like EGF, domains have six conserved residues disulfide-bonded into the characteriztic 'ababcc' pattern. They are involved in growth and proliferation of cells, in proteins of the Notch/Delta pathway, neurogulin and selectins. hEGFs are also found in mosaic proteins with four-disulfide laminin EGFs such as aggrecan and perlecan. The core fold of the EGF domain consists of two small beta-hairpins packed against each other. Two major structural variants have been identified based on the structural context of the C-terminal Cys residue of disulfide 'c' in the C-terminal hairpin: hEGFs and cEGFs. In hEGFs the C-terminal thiol resides in the beta-turn, resulting in shorter loop-lengths between the Cys residues of disulfide 'c', typically C[8-9]XC. These shorter loop-lengths are also typical of the four-disulfide EGF domains, laminin ad integrin. Tandem hEGF domains have six linking residues between terminal cysteines of adjacent domains. hEGF domains may or may not bind calcium in the linker region. hEGF domains with the consensus motif CXD4X[F,Y]XCXC are hydroxylated exclusively in the Asp residue.
Pssm-ID: 463660 Cd Length: 22 Bit Score: 36.54 E-value: 4.59e-03
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| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
1165-1261 |
4.66e-03 |
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Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies, typically as 6 instances. It is about 40 residues long and resembles the WD repeat and other beta-propeller structures.
Pssm-ID: 271333 [Multi-domain] Cd Length: 268 Bit Score: 41.51 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907188991 1165 KLNAPSSLAASPDGTLYIADLGNIRIRAVSKN----------KPLLNSM----------NFYeVASPTDQELYIFDINGT 1224
Cdd:cd14963 54 EFKYPYGIAVDSDGNIYVADLYNGRIQVFDPDgkflkyfpekKDRVKLIspaglaiddgKLY-VSDVKKHKVIVFDLEGK 132
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90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1907188991 1225 HQYTVSLVtGDYLYNFSYSN----DNDVT-AVTDSNGNtlRI 1261
Cdd:cd14963 133 LLLEFGKP-GSEPGELSYPNgiavDEDGNiYVADSGNG--RI 171
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| EGF |
smart00181 |
Epidermal growth factor-like domain; |
431-458 |
8.91e-03 |
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Epidermal growth factor-like domain;
Pssm-ID: 214544 Cd Length: 35 Bit Score: 35.96 E-value: 8.91e-03
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| RHS_repeat |
pfam05593 |
RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be ... |
1310-1341 |
9.15e-03 |
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RHS Repeat; RHS proteins contain extended repeat regions. These repeats often appear to be involved in ligand binding. Note that this model may not find all the repeats in a protein and that it covers two RHS repeats. The 3D structure of an RHS-repeat-containing protein (the B and C components of an ABC toxin complex) has been determined. The RHS repeats form an extended strip of beta-sheet that spirals around to form a hollow shell, encapsulating the variable C-terminal domain.
Pssm-ID: 461685 [Multi-domain] Cd Length: 37 Bit Score: 36.04 E-value: 9.15e-03
10 20 30
....*....|....*....|....*....|..
gi 1907188991 1310 GLLATKSDETGWTTFFDYDSEGRLTNVTFPTG 1341
Cdd:pfam05593 5 GRLTSVTDPDGRVTTYTYDAAGRLTAVTDPDG 36
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