|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02919 |
PLN02919 |
haloacid dehalogenase-like hydrolase family protein |
30-724 |
0e+00 |
|
haloacid dehalogenase-like hydrolase family protein
Pssm-ID: 215497 [Multi-domain] Cd Length: 1057 Bit Score: 558.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 30 TQQEKDELVYQYLQKVDGWEQDLA---VPEFPEGLEWLNTEePLSIYKDLCGKVVVLDFFTYCCINCIHVLPDLHALERR 106
Cdd:PLN02919 370 AQNSGEGCVQQFVSYISDLESKKTatkVPEFPPKLDWLNTA-PLQFRRDLKGKVVILDFWTYCCINCMHVLPDLEFLEKK 448
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 107 FSDKDgLLIVGVHSAKFPNEKVLDNIKSAVLRYNITHPVVNDADASLWQELEVSCWPTLVILGPRGNLLFSLIGEGHRDK 186
Cdd:PLN02919 449 YKDQP-FTVVGVHSAKFDNEKDLEAIRNAVLRYNISHPVVNDGDMYLWRELGVSSWPTFAVVSPNGKLIAQLSGEGHRKD 527
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 187 LFSYTSIALKYYKDRGQIRDGKIGIKLFKESLP---PSPLLFPGKVAVDHATGRLVVADTGHHRILVIQKNGRIQSSIGG 263
Cdd:PLN02919 528 LDDLVEAALQYYGEKKLLDSTPLPLSLEKDNDPrllTSPLKFPGKLAIDLLNNRLFISDSNHNRIVVTDLDGNFIVQIGS 607
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 264 PN-PGRKDGMFSESSFNSPQGVA--IADNVIYVADTENHLIRKIDLEAEKVTTVAGVGIQGTDTEGGEEGDKQPISSPWD 340
Cdd:PLN02919 608 TGeEGLRDGSFEDATFNRPQGLAynAKKNLLYVADTENHALREIDFVNETVRTLAGNGTKGSDYQGGKKGTSQVLNSPWD 687
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 341 VALGTSgsevqrNDILWIAMAGTHQIWallldsgtlpkKSDLKKGTCIRFAGSGNEENRNNAYPHKAGFAQPSGLALASE 420
Cdd:PLN02919 688 VCFEPV------NEKVYIAMAGQHQIW-----------EYNISDGVTRVFSGDGYERNLNGSSGTSTSFAQPSGISLSPD 750
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 421 epWSCLFVADSESSTVRTVSLRDGAVKHLVGGerDPM---NLFAFGDVDGAGINAKLQHPLGVAWDEERQVlYVADSYNH 497
Cdd:PLN02919 751 --LKELYIADSESSSIRALDLKTGGSRLLAGG--DPTfsdNLFKFGDHDGVGSEVLLQHPLGVLCAKDGQI-YVADSYNH 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 498 KIKVVDPKTKGCTTLAGTGDASDASSSFAESAFNEPGGLCIGESGRlLYVADTNNHQIKVMDLEARTVSVLPVCKsdsav 577
Cdd:PLN02919 826 KIKKLDPATKRVTTLAGTGKAGFKDGKALKAQLSEPAGLALGENGR-LFVADTNNSLIRYLDLNKGEAAEILTLE----- 899
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 578 VDGSFPREKQKTVPKVPKSAAHIGLPPVTVHPGQALQ--LRLKLQLPPGAKLTEGAPSCWFLEAEGNEWLLQEqtPSGDI 655
Cdd:PLN02919 900 LKGVQPPRPKSKSLKRLRRRSSADTQVIKVDGVTSLEgdLQLKISLPPGYHFSKEARSKFEVEVEPENAVDID--PDEGT 977
|
650 660 670 680 690 700
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 29789158 656 ENISNQPAISLQIPTHCLSLEAVVSVVvflYYCSADsSACMMKGVVFRQPLQiTSTQPACAAPVELAYA 724
Cdd:PLN02919 978 LSPDGRASLHFKRSSASASTGRISCKV---YYCKED-EVCLYQSLVFEVPFE-EENGGESSSSITLKYT 1041
|
|
| NHL-2_like |
cd14951 |
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
261-623 |
0e+00 |
|
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. 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: 271321 [Multi-domain] Cd Length: 334 Bit Score: 529.84 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 261 IGGPNPGRKDGMFSESSFNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEKVTTVAGVGIQGTDTEGGEEGDKQPISSPW 339
Cdd:cd14951 1 IGSGERGLKDGSFAEASFNEPQGLALlPGNILYVADTENHALRKIDLETGTVTTLAGTGEQGRDGEGGGPGREQPLSSPW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 340 DVALGTSgsevqrNDILWIAMAGTHQIWALLLDSGTlpkksdlkkgtCIRFAGSGNEENRNNAYPHKAGFAQPSGLALAs 419
Cdd:cd14951 81 DVAWGPE------DDILYIAMAGTHQIWAYDLDTGT-----------CRVFAGSGNEGNRNGPYPHEAWFAQPSGLSLA- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 420 eePWSCLFVADSESSTVRTVSLRDGAVKHLVGGERDPMNLFAFGDVDGAGINAKLQHPLGVAWDEERQVlYVADSYNHKI 499
Cdd:cd14951 143 --GWGELFVADSESSAIRAVSLKDGGVKTLVGGTRVGTGLFDFGDRDGPGAEALLQHPLGVAALPDGSV-YVADTYNHKI 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 500 KVVDPKTKGCTTLAGTGDASDASssfAESAFNEPGGLCIGESGRlLYVADTNNHQIKVMDLEARTVSVLPVcksDSAVVD 579
Cdd:cd14951 220 KRVDPATGEVSTLAGTGKAGYKD---LEAQFSEPSGLVVDGDGR-LYVADTNNHRIRRLDLPTEALEVLTL---AHRTLR 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 29789158 580 GSFPREKQKTVPKVPKSAAHIGLPPVTvhPGQALQLRLKLQLPP 623
Cdd:cd14951 293 PATPPAPGPLRLRVRFTAPAGQKLDDR--WGPSTRLKLSISPPE 334
|
|
| TlpA_like_DipZ_like |
cd03012 |
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a ... |
55-182 |
8.35e-75 |
|
TlpA-like family, DipZ-like subfamily; composed uncharacterized proteins containing a TlpA-like TRX domain. Some members show domain architectures similar to that of E. coli DipZ protein (also known as DsbD). The only eukaryotic members of the TlpA family belong to this subfamily. TlpA is a disulfide reductase known to have a crucial role in the biogenesis of cytochrome aa3.
Pssm-ID: 239310 [Multi-domain] Cd Length: 126 Bit Score: 237.20 E-value: 8.35e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 55 PEFPEGLEWLNTEEPLSIYkDLCGKVVVLDFFTYCCINCIHVLPDLHALERRFSDkDGLLIVGVHSAKFPNEKVLDNIKS 134
Cdd:cd03012 1 PEFEGILQWLNTDKPLSLA-QLRGKVVLLDFWTYCCINCLHTLPYLTDLEQKYKD-DGLVVIGVHSPEFAFERDLANVKS 78
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 29789158 135 AVLRYNITHPVVNDADASLWQELEVSCWPTLVILGPRGNLLFSLIGEG 182
Cdd:cd03012 79 AVLRYGITYPVANDNDYATWRAYGNQYWPALYLIDPTGNVRHVHFGEG 126
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
226-555 |
1.32e-51 |
|
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: 182.34 E-value: 1.32e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 226 PGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRKDGMFSESSFNSPQGVAI--ADNvIYVADTENHLIRK 303
Cdd:cd14953 25 PSGVAVD-AAGNLYVADRGNHRIRKITPDGVVTTVAGTGTAGFADGGGAAAQFNTPSGVAVdaAGN-LYVADTGNHRIRK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 304 IDLeAEKVTTVAGVGIQGTDTEGGeeGDKQPISSPWDVALGTSGsevqrndILWIAMAGTHQIwallldsgtlpKKSDlK 383
Cdd:cd14953 103 ITP-DGVVSTLAGTGTAGFSDDGG--ATAAQFNYPTGVAVDAAG-------NLYVADTGNHRI-----------RKIT-P 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 384 KGTCIRFAGSGNEENRNNAYPHKAGFAQPSGLALASEEpwsCLFVADSESSTVRTVSLrDGAVKHLVGgerdpmNLFAFG 463
Cdd:cd14953 161 DGVVTTVAGTGGAGYAGDGPATAAQFNNPTGVAVDAAG---NLYVADRGNHRIRKITP-DGVVTTVAG------TGTAGF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 464 DVDGAGINAKLQHPLGVAWDeERQVLYVADSYNHKIKVVDPKTKGcTTLAG-----TGDASDASSsfaeSAFNEPGGLCI 538
Cdd:cd14953 231 SGDGGATAAQLNNPTGVAVD-AAGNLYVADSGNHRIRKITPAGVV-TTVAGggagfSGDGGPATS----AQFNNPTGVAV 304
|
330
....*....|....*..
gi 29789158 539 GESGRlLYVADTNNHQI 555
Cdd:cd14953 305 DAAGN-LYVADTGNNRI 320
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
220-557 |
4.52e-44 |
|
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: 159.41 E-value: 4.52e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 220 PSPLLFPGKVAVDHaTGRLVVADTGHHRILVIQKNGRIQSSIGGpnPGRKDGMfsessFNSPQGVAI-ADNVIYVADTEN 298
Cdd:cd05819 4 PGELNNPQGIAVDS-SGNIYVADTGNNRIQVFDPDGNFITSFGS--FGSGDGQ-----FNEPAGVAVdSDGNLYVADTGN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 299 HLIRKIDLEAEKVTTVAGVGIQGTDteggeegdkqpISSPWDVALGTSGSevqrndiLWIAMAGTHQIWAllLDSGtlpk 378
Cdd:cd05819 76 HRIQKFDPDGNFLASFGGSGDGDGE-----------FNGPRGIAVDSSGN-------IYVADTGNHRIQK--FDPD---- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 379 ksdlkkGTCIRFAGSGNEENrnnayphkAGFAQPSGLALASEEPwscLFVADSESSTVRTVSLRDGAVkhlvggerdpmn 458
Cdd:cd05819 132 ------GEFLTTFGSGGSGP--------GQFNGPTGVAVDSDGN---IYVADTGNHRIQVFDPDGNFL------------ 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 459 lFAFGDvDGAGiNAKLQHPLGVAWDEERqVLYVADSYNHKIKVVDPktkGCTTLAGTGDASDASSSfaesaFNEPGGLCI 538
Cdd:cd05819 183 -TTFGS-TGTG-PGQFNYPTGIAVDSDG-NIYVADSGNNRVQVFDP---DGAGFGGNGNFLGSDGQ-----FNRPSGLAV 250
|
330
....*....|....*....
gi 29789158 539 GESGRlLYVADTNNHQIKV 557
Cdd:cd05819 251 DSDGN-LYVADTGNNRIQV 268
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
262-555 |
4.18e-43 |
|
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: 158.46 E-value: 4.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 262 GGPNPGRKDGMFSESSFNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEkVTTVAGVGIQGTDtegGEEGDKQPISSPWD 340
Cdd:cd14953 6 GSGTAGFSGGGGTAARFNSPSGVAVdAAGNLYVADRGNHRIRKITPDGV-VTTVAGTGTAGFA---DGGGAAAQFNTPSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 341 VALGTSGSevqrndiLWIAMAGTHQIwallldsgtlpKKSDLkKGTCIRFAGSGNEENRNNAYPHKAGFAQPSGLALase 420
Cdd:cd14953 82 VAVDAAGN-------LYVADTGNHRI-----------RKITP-DGVVSTLAGTGTAGFSDDGGATAAQFNYPTGVAV--- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 421 EPWSCLFVADSESSTVRTVSlRDGAVKHLVGGERdpmnlfAFGDVDGAGINAKLQHPLGVAWDEErQVLYVADSYNHKIK 500
Cdd:cd14953 140 DAAGNLYVADTGNHRIRKIT-PDGVVTTVAGTGG------AGYAGDGPATAAQFNNPTGVAVDAA-GNLYVADRGNHRIR 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 29789158 501 VVDPKTKGcTTLAGTGDASDASSSFAESA-FNEPGGLCIGESGRlLYVADTNNHQI 555
Cdd:cd14953 212 KITPDGVV-TTVAGTGTAGFSGDGGATAAqLNNPTGVAVDAAGN-LYVADSGNHRI 265
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
223-502 |
4.37e-30 |
|
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: 119.73 E-value: 4.37e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 223 LLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPnpGRKDGMFsessfNSPQGVAI-ADNVIYVADTENHLI 301
Cdd:cd05819 54 FNEPAGVAVD-SDGNLYVADTGNHRIQKFDPDGNFLASFGGS--GDGDGEF-----NGPRGIAVdSSGNIYVADTGNHRI 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 302 RKIDLEAEKVTTVagvgiqgtdteGGEEGDKQPISSPWDVALGTSGSevqrndiLWIAMAGTHQIwaLLLDSGtlpkksd 381
Cdd:cd05819 126 QKFDPDGEFLTTF-----------GSGGSGPGQFNGPTGVAVDSDGN-------IYVADTGNHRI--QVFDPD------- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 382 lkkGTCIRFAGSGNEENrnnayphkAGFAQPSGLALASEEPwscLFVADSESSTVRTVslrdgavkhlvggerDPMNLFA 461
Cdd:cd05819 179 ---GNFLTTFGSTGTGP--------GQFNYPTGIAVDSDGN---IYVADSGNNRVQVF---------------DPDGAGF 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 29789158 462 FGDVDGAGINAKLQHPLGVAWDEERQVlYVADSYNHKIKVV 502
Cdd:cd05819 230 GGNGNFLGSDGQFNRPSGLAVDSDGNL-YVADTGNNRIQVF 269
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
223-439 |
9.92e-29 |
|
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: 117.25 E-value: 9.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 223 LLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRK-DGMFSESSFNSPQGVAI-ADNVIYVADTENHL 300
Cdd:cd14953 131 FNYPTGVAVD-AAGNLYVADTGNHRIRKITPDGVVTTVAGTGGAGYAgDGPATAAQFNNPTGVAVdAAGNLYVADRGNHR 209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 301 IRKIDLeAEKVTTVAGVGIQGTDTEGGeeGDKQPISSPWDVALGTSGSevqrndiLWIAMAGTHQIwaLLLDSGtlpkks 380
Cdd:cd14953 210 IRKITP-DGVVTTVAGTGTAGFSGDGG--ATAAQLNNPTGVAVDAAGN-------LYVADSGNHRI--RKITPA------ 271
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789158 381 dlkkGTCIRFAGSGNEENRNNAYPHKAGFAQPSGLALASEepwSCLFVADSESSTVRTV 439
Cdd:cd14953 272 ----GVVTTVAGGGAGFSGDGGPATSAQFNNPTGVAVDAA---GNLYVADTGNNRIRKI 323
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
166-437 |
2.26e-28 |
|
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: 114.72 E-value: 2.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 166 VILGPRGNLLFSLIGEGHRDKLFSY-TSIALK---------YYKDRGQI--RDGKIGIKLFKESLPPSPLLFPGKVAVDH 233
Cdd:cd05819 32 QVFDPDGNFITSFGSFGSGDGQFNEpAGVAVDsdgnlyvadTGNHRIQKfdPDGNFLASFGGSGDGDGEFNGPRGIAVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 234 AtGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkdgmfsESSFNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEKVT 312
Cdd:cd05819 112 S-GNIYVADTGNHRIQKFDPDGEFLTTFGSGGSG-------PGQFNGPTGVAVdSDGNIYVADTGNHRIQVFDPDGNFLT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 313 TVAGVGIQGTDTeggeegdkqpiSSPWDVALGTSGSevqrndiLWIAMAGTHQIWallldsgtlpkksdlkkgtciRFAG 392
Cdd:cd05819 184 TFGSTGTGPGQF-----------NYPTGIAVDSDGN-------IYVADSGNNRVQ---------------------VFDP 224
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29789158 393 SGNEENRN-NAYPHKAGFAQPSGLALASEEpwsCLFVADSESSTVR 437
Cdd:cd05819 225 DGAGFGGNgNFLGSDGQFNRPSGLAVDSDG---NLYVADTGNNRIQ 267
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
278-582 |
1.92e-25 |
|
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: 106.25 E-value: 1.92e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 278 FNSPQGVAIA-DNVIYVADTENHLIRKIDLEAEKVTTVAGVGiqgtdteggeEGDKQpISSPWDVALGTSGSevqrndiL 356
Cdd:cd05819 7 LNNPQGIAVDsSGNIYVADTGNNRIQVFDPDGNFITSFGSFG----------SGDGQ-FNEPAGVAVDSDGN-------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 357 WIAMAGTHQIwallldsgtlpKKSDLKKGTCIRFAGSGNEENrnnayphkaGFAQPSGLAlaseepwsclfvadsesstv 436
Cdd:cd05819 69 YVADTGNHRI-----------QKFDPDGNFLASFGGSGDGDG---------EFNGPRGIA-------------------- 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 437 rtvslrdgavkhlvggerdpmnlfafgdVDGAGinaklqhplgvawdeerqVLYVADSYNHKIKVVDPKTKgCTTLAGTG 516
Cdd:cd05819 109 ----------------------------VDSSG------------------NIYVADTGNHRIQKFDPDGE-FLTTFGSG 141
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789158 517 DASDASssfaesaFNEPGGLCIGESGRLlYVADTNNHQIKVMDLEARTVSVLPvcksDSAVVDGSF 582
Cdd:cd05819 142 GSGPGQ-------FNGPTGVAVDSDGNI-YVADTGNHRIQVFDPDGNFLTTFG----STGTGPGQF 195
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
220-569 |
3.62e-25 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 105.49 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 220 PSPLLFPGKVAVDhATGRLVVADTGHHRILVIQ-KNGRIQSsiggpnpgrkdgmFSESSFNSPQGVAI-ADNVIYVADTE 297
Cdd:COG4257 13 PAPGSGPRDVAVD-PDGAVWFTDQGGGRIGRLDpATGEFTE-------------YPLGGGSGPHGIAVdPDGNLWFTDNG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 298 NHLIRKIDLEAEKVTTVAGVGiqgtdteggeegdkqPISSPWDVALGTSGSevqrndiLWIAMAGTHQIWALLLDSGTLp 377
Cdd:COG4257 79 NNRIGRIDPKTGEITTFALPG---------------GGSNPHGIAFDPDGN-------LWFTDQGGNRIGRLDPATGEV- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 378 kksdlkkgtcirfagsgneenrnNAYPHKAGFAQPSGLALASE-EPWsclfVADSESSTVRTVSLRDGAVKHLVGgerdp 456
Cdd:COG4257 136 -----------------------TEFPLPTGGAGPYGIAVDPDgNLW----VTDFGANAIGRIDPDTGTLTEYAL----- 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 457 mnlfafgdvdgagiNAKLQHPLGVAWDEErQVLYVADSYNHKIKVVDPKTKGCTTLAGTGDASdasssfaesafnEPGGL 536
Cdd:COG4257 184 --------------PTPGAGPRGLAVDPD-GNLWVADTGSGRIGRFDPKTGTVTEYPLPGGGA------------RPYGV 236
|
330 340 350
....*....|....*....|....*....|....
gi 29789158 537 CIGESGRlLYVADTNNHQIKVMDLEAR-TVSVLP 569
Cdd:COG4257 237 AVDGDGR-VWFAESGANRIVRFDPDTElTEYVLP 269
|
|
| TlpA_like_family |
cd02966 |
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ... |
75-180 |
3.63e-25 |
|
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.
Pssm-ID: 239264 [Multi-domain] Cd Length: 116 Bit Score: 100.77 E-value: 3.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 75 DLCGKVVVLDFFTYCCINCIHVLPDLHALERRFSDkDGLLIVGVHSAKFPNEKVldniKSAVLRYNITHPVVNDADASLW 154
Cdd:cd02966 16 DLKGKVVLVNFWASWCPPCRAEMPELEALAKEYKD-DGVEVVGVNVDDDDPAAV----KAFLKKYGITFPVLLDPDGELA 90
|
90 100
....*....|....*....|....*.
gi 29789158 155 QELEVSCWPTLVILGPRGNLLFSLIG 180
Cdd:cd02966 91 KAYGVRGLPTTFLIDRDGRIRARHVG 116
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
407-559 |
2.66e-24 |
|
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: 104.53 E-value: 2.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 407 AGFAQPSGLALASEepwSCLFVADSESSTVRTVSlRDGAVKHLVGGErdpmnlfAFGDVDGAGINAKLQHPLGVAWDEER 486
Cdd:cd14953 20 ARFNSPSGVAVDAA---GNLYVADRGNHRIRKIT-PDGVVTTVAGTG-------TAGFADGGGAAAQFNTPSGVAVDAAG 88
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789158 487 QvLYVADSYNHKIKVVDPKTkGCTTLAGTGDASDASSSFAESA-FNEPGGLCIGESGRLlYVADTNNHQIKVMD 559
Cdd:cd14953 89 N-LYVADTGNHRIRKITPDG-VVSTLAGTGTAGFSDDGGATAAqFNYPTGVAVDAAGNL-YVADTGNHRIRKIT 159
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
226-557 |
3.02e-24 |
|
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: 103.13 E-value: 3.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 226 PGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRkdgmfseSSFNSPQGVAIA-DNVIYVADTENHLIRKI 304
Cdd:cd14956 15 PRGIAVDAD-DNVYVADARNGRIQVFDKDGTFLRRFGTTGDGP-------GQFGRPRGLAVDkDGWLYVADYWGDRIQVF 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 305 DLEAEKVTTvagvgiqgtdteGGEEGDKQP-ISSPWDVALGTSGSevqrndiLWIAMAGTHQIWALLLDsgtlpkksdlk 383
Cdd:cd14956 87 TLTGELQTI------------GGSSGSGPGqFNAPRGVAVDADGN-------LYVADFGNQRIQKFDPD----------- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 384 kGTCIRFAGSgneenrnnaYPHKAG-FAQPSGLALAseePWSCLFVADSESSTVRTVSlRDGAVKHLVGGErdpmnlfaf 462
Cdd:cd14956 137 -GSFLRQWGG---------TGIEPGsFNYPRGVAVD---PDGTLYVADTYNDRIQVFD-NDGAFLRKWGGR--------- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 463 gdvdGAGiNAKLQHPLGVAWDEERQVlYVADSYNHKIKVVdpkTKGCTTLAGTGDASDASssfaeSAFNEPGGLCIGESG 542
Cdd:cd14956 194 ----GTG-PGQFNYPYGIAIDPDGNV-FVADFGNNRIQKF---TADGTFLTSWGSPGTGP-----GQFKNPWGVVVDADG 259
|
330
....*....|....*
gi 29789158 543 RlLYVADTNNHQIKV 557
Cdd:cd14956 260 T-VYVADSNNNRVQR 273
|
|
| NHL_like_2 |
cd14957 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
225-557 |
9.42e-24 |
|
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: 101.57 E-value: 9.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 225 FPGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkdgmfsESSFNSPQGVAIADN-VIYVADTENHLIRk 303
Cdd:cd14957 19 TPRGIAVDSA-GNIYVADTGNNRIQVFTSSGVYSYSIGSGGTG-------SGQFNSPYGIAVDSNgNIYVADTDNNRIQ- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 304 idleaekVTTVAGV---GIQGTDTEGGeegdkqPISSPWDVALGTSGSevqrndiLWIAMAGTH--QIWAllldsgtlpk 378
Cdd:cd14957 90 -------VFNSSGVyqySIGTGGSGDG------QFNGPYGIAVDSNGN-------IYVADTGNHriQVFT---------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 379 ksdlKKGTCIRFAGSGNEENRNnayphkagFAQPSGLALASEepwSCLFVADSESSTVRTVSlRDGAVKHLVGGErdpmn 458
Cdd:cd14957 140 ----SSGTFSYSIGSGGTGPGQ--------FNGPQGIAVDSD---GNIYVADTGNHRIQVFT-SSGTFQYTFGSS----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 459 lfafgdvdGAGiNAKLQHPLGVAWDEERQVlYVADSYNHKIKVVDPktkgcttlAGTGDASDASSSFAESAFNEPGGLCI 538
Cdd:cd14957 199 --------GSG-PGQFSDPYGIAVDSDGNI-YVADTGNHRIQVFTS--------SGAYQYSIGTSGSGNGQFNYPYGIAV 260
|
330
....*....|....*....
gi 29789158 539 GESGRlLYVADTNNHQIKV 557
Cdd:cd14957 261 DNDGK-IYVADSNNNRIQV 278
|
|
| TrxA |
COG0526 |
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ... |
53-187 |
1.92e-22 |
|
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440292 [Multi-domain] Cd Length: 139 Bit Score: 93.60 E-value: 1.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 53 AVPEFPegLEWLNtEEPLSIyKDLCGKVVVLDFFTYCCINCIHVLPDLHALERRFsdkDGLLIVGVHSAKFPnekvlDNI 132
Cdd:COG0526 7 PAPDFT--LTDLD-GKPLSL-ADLKGKPVLVNFWATWCPPCRAEMPVLKELAEEY---GGVVFVGVDVDENP-----EAV 74
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 29789158 133 KSAVLRYNITHPVVNDADASLWQELEVSCWPTLVILGPRGNLLFSLIGEGHRDKL 187
Cdd:COG0526 75 KAFLKELGLPYPVLLDPDGELAKAYGVRGIPTTVLIDKDGKIVARHVGPLSPEEL 129
|
|
| NHL_like_4 |
cd14955 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
225-555 |
3.43e-20 |
|
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: 271325 [Multi-domain] Cd Length: 279 Bit Score: 91.10 E-value: 3.43e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 225 FPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkDGMFsessfNSPQGVAI--ADNViYVADTENHLIR 302
Cdd:cd14955 17 SPSGIAVD-SAGNVYVADTGNNRIQKFDSTGTFLTKWGSSGSG--DGQF-----YSPTGIAVdsDGNV-YVADTGNHRIQ 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 303 KIDLEAEKVTTvagVGIQGTdteggeeGDKQpISSPWDVAlgtsgseVQRNDILWIAMAGTHQIwaLLLDS-GTLpkksD 381
Cdd:cd14955 88 KFDSTGTFLTK---WGSSGS-------GDGQ-FNSPSGIA-------VDSAGNVYVTDSGNNRI--QKFDSsGTF----I 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 382 LKKGTcirfAGSGNEEnrnnayphkagFAQPSGLALASEepwSCLFVADSESSTVRTVSlRDGAVkhlvggerdpmnLFA 461
Cdd:cd14955 144 TKWGS----FGSGDGQ-----------FNSPTGIAVDSA---GNVYVADTGNNRIQKFT-STGTF------------LTK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 462 FGdVDGAGiNAKLQHPLGVAWDEERQVlYVADSYNHKIKVVDPktkgcttlAGTGDASDASSSFAESAFNEPGGLCIGES 541
Cdd:cd14955 193 WG-SEGSG-DGQFNAPYGIAVDSAGNV-YVADTGNNRIQKFDS--------SGTFITKWGSEGSGDGQFNSPSGIAVDSA 261
|
330
....*....|....
gi 29789158 542 GRlLYVADTNNHQI 555
Cdd:cd14955 262 GN-VYVADSGNNRI 274
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
222-557 |
3.67e-20 |
|
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: 90.81 E-value: 3.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 222 PLLFPGKVAVDhaTGRLVVADTGHHRILVIQKNGRIQSSIGGpnPGRKDGmfsesSFNSPQGVAI-ADNVIYVADTENHL 300
Cdd:cd14963 8 PLNKPMGVAVS--DGRIYVADTNNHRVQVFDYEGKFKKSFGG--PGTGPG-----EFKYPYGIAVdSDGNIYVADLYNGR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 301 IRKIDLEAEKVTTVAgvgiqgtdteggEEGDKQPISSPwdVALGTSGsevqrnDILWIAMAGTHQIWALLLDSgtlpkKS 380
Cdd:cd14963 79 IQVFDPDGKFLKYFP------------EKKDRVKLISP--AGLAIDD------GKLYVSDVKKHKVIVFDLEG-----KL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 381 DLKKGTcirfAGSGNEEnrnnayphkagFAQPSGLALASEepwSCLFVADSESSTVRTVSLRDGAVKHLVGGERDPMNLF 460
Cdd:cd14963 134 LLEFGK----PGSEPGE-----------LSYPNGIAVDED---GNIYVADSGNGRIQVFDKNGKFIKELNGSPDGKSGFV 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 461 AfgdvdgaginaklqhPLGVAWDeERQVLYVADSYNHKIKVVDPKTKGCTTLAGTGDASDasssfaesAFNEPGGLCIGE 540
Cdd:cd14963 196 N---------------PRGIAVD-PDGNLYVVDNLSHRVYVFDEQGKELFTFGGRGKDDG--------QFNLPNGLFIDD 251
|
330
....*....|....*..
gi 29789158 541 SGRlLYVADTNNHQIKV 557
Cdd:cd14963 252 DGR-LYVTDRENNRVAV 267
|
|
| Thioredoxin_8 |
pfam13905 |
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the ... |
78-173 |
4.51e-19 |
|
Thioredoxin-like; Thioredoxins are small enzymes that participate in redox reactions, via the reversible oxidation of an active centre disulfide bond.
Pssm-ID: 464033 [Multi-domain] Cd Length: 95 Bit Score: 82.74 E-value: 4.51e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 78 GKVVVLDFFTYCCINCIHVLPDLHALERRFSDKDGLLIVGVHSAKFPNEkvLDNIKSAVLRYNITHPVVNDADASLWQEL 157
Cdd:pfam13905 1 GKVVLLYFGASWCKPCRRFTPLLKELYEKLKKKKNVEIVFVSLDRDLEE--FKDYLKKMPKDWLSVPFDDDERNELKRKY 78
|
90
....*....|....*.
gi 29789158 158 EVSCWPTLVILGPRGN 173
Cdd:pfam13905 79 GVNAIPTLVLLDPNGE 94
|
|
| NHL_like_6 |
cd14962 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
213-557 |
9.41e-18 |
|
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: 83.79 E-value: 9.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 213 LFKESLPPSPLLFPGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRkdgmfsessFNSPQGVAI-ADNVI 291
Cdd:cd14962 1 VTGEERPKEALTRPYGVAADGR-GRIYVADTGRGAVFVFDLPNGKVFVIGNAGPNR---------FVSPIGVAIdANGNL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 292 YVADTENHLIRKIDLEAEKVTTVagvgiqgtdteGGEEGDKQPIsspwDVALGTSGsevqrnDILWIAMAGTHQIWALLL 371
Cdd:cd14962 71 YVSDAELGKVFVFDRDGKFLRAI-----------GAGALFKRPT----GIAVDPAG------KRLYVVDTLAHKVKVFDL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 372 DSGTLpkkSDLKKgtcirfAGSGNEEnrnnayphkagFAQPSGLALASEepwSCLFVADSESSTVRTVSLRDGAVKHLvg 451
Cdd:cd14962 130 DGRLL---FDIGK------RGSGPGE-----------FNLPTDLAVDRD---GNLYVTDTMNFRVQIFDADGKFLRSF-- 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 452 GERdpmnlfafGDVDGAginakLQHPLGVAWDEERQVlYVADSYNHKIKVVDPKTKGCTTLAGTGDASDasssfaesAFN 531
Cdd:cd14962 185 GER--------GDGPGS-----FARPKGIAVDSEGNI-YVVDAAFDNVQIFNPEGELLLTVGGPGSGPG--------EFY 242
|
330 340
....*....|....*....|....*.
gi 29789158 532 EPGGLCIGESGRlLYVADTNNHQIKV 557
Cdd:cd14962 243 LPSGIAIDKDDR-IYVVDQFNRRIQV 267
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
461-568 |
1.26e-17 |
|
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: 84.50 E-value: 1.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 461 AFGDVDGAGINAKLQHPLGVAWDEErQVLYVADSYNHKIKVVDPKTKgCTTLAGTGDASDASSSFAESAFNEPGGLCIGE 540
Cdd:cd14953 9 TAGFSGGGGTAARFNSPSGVAVDAA-GNLYVADRGNHRIRKITPDGV-VTTVAGTGTAGFADGGGAAAQFNTPSGVAVDA 86
|
90 100
....*....|....*....|....*...
gi 29789158 541 SGRlLYVADTNNHQIKVMDLeARTVSVL 568
Cdd:cd14953 87 AGN-LYVADTGNHRIRKITP-DGVVSTL 112
|
|
| NHL_TRIM71_like |
cd14954 |
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
229-557 |
2.72e-16 |
|
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain] Cd Length: 285 Bit Score: 79.90 E-value: 2.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 229 VAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGpnPGRKDGmfsesSFNSPQGVAI-ADNVIYVADTENHLIRKIDLE 307
Cdd:cd14954 29 VAVD-KDGRIIVADRSNNRVQVFDPDGKFLRKFGS--YGSRDG-----QFDRPAGVAVnSRGRIIVADKDNHRIQVFDLN 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 308 aekvttvaGVGIQGTDTEGGEEGDKQpisSPWDVAlgtsgseVQRNDILWIAMAGTHQIWALLLDsgtlpkksdlkkGTC 387
Cdd:cd14954 101 --------GRFLLKFGERGTKNGQFN---YPWGVA-------VDSEGRIYVSDTRNHRVQVFDSD------------GQF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 388 IR-FAGSGNEEnrnnayphkAGFAQPSGLALASEEPwscLFVADSESSTVRTVSlRDGAVKHLVGGErdpmnlfafGDVD 466
Cdd:cd14954 151 IRkFGFEGAGP---------GQLDSPRGVAVNPDGN---IVVSDFNNHRLQVFD-PDGQFLRFFGSE---------GSGN 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 467 GaginaKLQHPLGVAWDEERQVLyVADSYNHKIKVVDPKTKGCTTLAGTGDasdasssfAESAFNEPGGLCIGESGRLLy 546
Cdd:cd14954 209 G-----QFKRPRGVAVDDEGNII-VADSGNHRVQVFSPDGEFLCSFGTEGN--------GEGQFDRPSGVAVTPDGRIV- 273
|
330
....*....|.
gi 29789158 547 VADTNNHQIKV 557
Cdd:cd14954 274 VVDRGNHRIQV 284
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
274-559 |
4.86e-16 |
|
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: 78.87 E-value: 4.86e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 274 SESSFNSPQGVAIADNVIYVADTENHLIRKIDLEAEKVTTVagvgiqgtdteGGEEGDKQPISSPWDVALGTSGSevqrn 353
Cdd:cd14963 5 FGDPLNKPMGVAVSDGRIYVADTNNHRVQVFDYEGKFKKSF-----------GGPGTGPGEFKYPYGIAVDSDGN----- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 354 diLWIAMAGTHQIWalLLDSgtlpkksdlkKGTCIRFAGSGneENRNNAyphkagfAQPSGLALASEEpwscLFVADSES 433
Cdd:cd14963 69 --IYVADLYNGRIQ--VFDP----------DGKFLKYFPEK--KDRVKL-------ISPAGLAIDDGK----LYVSDVKK 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 434 STVrTVSLRDGAVKHLVGGErdpmnlfafGDVDGaginaKLQHPLGVAWDEERQvLYVADSYNHKIKVVDPKTKGCTTLA 513
Cdd:cd14963 122 HKV-IVFDLEGKLLLEFGKP---------GSEPG-----ELSYPNGIAVDEDGN-IYVADSGNGRIQVFDKNGKFIKELN 185
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 29789158 514 GTGDASdasssfaeSAFNEPGGLCIGESGRlLYVADTNNHQIKVMD 559
Cdd:cd14963 186 GSPDGK--------SGFVNPRGIAVDPDGN-LYVVDNLSHRVYVFD 222
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
277-570 |
9.09e-16 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 78.14 E-value: 9.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 277 SFNSPQGVAIA-DNVIYVADTENHLIRKIDLEAEKVTTVagvgiqgtdteggeegDKQPISSPWDVALGTSGSevqrndi 355
Cdd:COG4257 15 PGSGPRDVAVDpDGAVWFTDQGGGRIGRLDPATGEFTEY----------------PLGGGSGPHGIAVDPDGN------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 356 LWIAMAGTHQIWALlldsgtlpkksDLKKGTCIRFAGSGNEenrnnAYPHKAGFAqPSGLalaseepwscLFVADSESST 435
Cdd:COG4257 72 LWFTDNGNNRIGRI-----------DPKTGEITTFALPGGG-----SNPHGIAFD-PDGN----------LWFTDQGGNR 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 436 VRTVSLRDGAVKhlvggerdpmnLFAFGdVDGAGinaklqhPLGVAWDEERQVlYVADSYNHKIKVVDPKTKGCTTLAGt 515
Cdd:COG4257 125 IGRLDPATGEVT-----------EFPLP-TGGAG-------PYGIAVDPDGNL-WVTDFGANAIGRIDPDTGTLTEYAL- 183
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 29789158 516 gdasdasssfaESAFNEPGGLCIGESGRLlYVADTNNHQIKVMDLEARTVSVLPV 570
Cdd:COG4257 184 -----------PTPGAGPRGLAVDPDGNL-WVADTGSGRIGRFDPKTGTVTEYPL 226
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
225-436 |
7.72e-15 |
|
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: 75.40 E-value: 7.72e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 225 FPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkdgmfsESSFNSPQGVAI-ADNVIYVADTENHLIRK 303
Cdd:cd14956 108 APRGVAVD-ADGNLYVADFGNQRIQKFDPDGSFLRQWGGTGIE-------PGSFNYPRGVAVdPDGTLYVADTYNDRIQV 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 304 IDLEAEKVTTVAGVGiqgtdTEGGEegdkqpISSPWDVALGTSGSevqrndiLWIAMAGTHQIWALLLDsgtlpkksdlk 383
Cdd:cd14956 180 FDNDGAFLRKWGGRG-----TGPGQ------FNYPYGIAIDPDGN-------VFVADFGNNRIQKFTAD----------- 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 29789158 384 kGTCIRFAGSgneenrnnaYPHKAG-FAQPSGLALASEepwSCLFVADSESSTV 436
Cdd:cd14956 231 -GTFLTSWGS---------PGTGPGqFKNPWGVVVDAD---GTVYVADSNNNRV 271
|
|
| Bcp |
COG1225 |
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones]; |
75-181 |
1.32e-14 |
|
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
Pssm-ID: 440838 [Multi-domain] Cd Length: 136 Bit Score: 71.05 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 75 DLCGKVVVLDFFTYCCINCIHVLPDLHALERRFSDKdGLLIVGVHSAKfpnekvLDNIKSAVLRYNITHPVVNDADASLW 154
Cdd:COG1225 18 DLRGKPVVLYFYATWCPGCTAELPELRDLYEEFKDK-GVEVLGVSSDS------DEAHKKFAEKYGLPFPLLSDPDGEVA 90
|
90 100
....*....|....*....|....*..
gi 29789158 155 QELEVSCWPTLVILGPRGNLLFSLIGE 181
Cdd:COG1225 91 KAYGVRGTPTTFLIDPDGKIRYVWVGP 117
|
|
| NHL_like_3 |
cd14956 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
260-564 |
3.50e-14 |
|
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: 73.47 E-value: 3.50e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 260 SIGGPnpGRKDGmfsesSFNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEKVTTVagvGIQGTDTEGGEEGdkqpissp 338
Cdd:cd14956 1 SWGGR--GSGPG-----QFKDPRGIAVdADDNVYVADARNGRIQVFDKDGTFLRRF---GTTGDGPGQFGRP-------- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 339 wdvalgtSGSEVQRNDILWIAMAGTHQIwallldsgtlpKKSDLKkGTCIRFAGSgneenrnnaYPHKAG-FAQPSGLAL 417
Cdd:cd14956 63 -------RGLAVDKDGWLYVADYWGDRI-----------QVFTLT-GELQTIGGS---------SGSGPGqFNAPRGVAV 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 418 ASEepwSCLFVADSESStvRTVSLR-DGAVkhlvggerdpmnLFAFGDVDGAGInaKLQHPLGVAWDEErQVLYVADSYN 496
Cdd:cd14956 115 DAD---GNLYVADFGNQ--RIQKFDpDGSF------------LRQWGGTGIEPG--SFNYPRGVAVDPD-GTLYVADTYN 174
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789158 497 HKIKVVDPKTKGCTTLAGTGdasdassSFaESAFNEPGGLCIGESGRlLYVADTNNHQIKVMDLEART 564
Cdd:cd14956 175 DRIQVFDNDGAFLRKWGGRG-------TG-PGQFNYPYGIAIDPDGN-VFVADFGNNRIQKFTADGTF 233
|
|
| NHL_like_2 |
cd14957 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
217-347 |
1.18e-11 |
|
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: 66.14 E-value: 1.18e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 217 SLPPSPLLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGgpnpgrkDGMFSESSFNSPQGVAI-ADNVIYVAD 295
Cdd:cd14957 105 GSGDGQFNGPYGIAVD-SNGNIYVADTGNHRIQVFTSSGTFSYSIG-------SGGTGPGQFNGPQGIAVdSDGNIYVAD 176
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 29789158 296 TENHLIRKIDLEAEKVTTVagvgiqGTDTEGGEEgdkqpISSPWDVALGTSG 347
Cdd:cd14957 177 TGNHRIQVFTSSGTFQYTF------GSSGSGPGQ-----FSDPYGIAVDSDG 217
|
|
| NHL_like_2 |
cd14957 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
217-366 |
1.45e-11 |
|
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: 65.75 E-value: 1.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 217 SLPPSPLLFPGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkDGmfsesSFNSPQGVAIaDNV--IYVA 294
Cdd:cd14957 152 GTGPGQFNGPQGIAVDSD-GNIYVADTGNHRIQVFTSSGTFQYTFGSSGSG--PG-----QFSDPYGIAV-DSDgnIYVA 222
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 29789158 295 DTENHLIrkidleaeKVTTVAGV-----GIQGTDTEGgeegdkqpISSPWDVAlgtsgseVQRNDILWIAMAGTHQI 366
Cdd:cd14957 223 DTGNHRI--------QVFTSSGAyqysiGTSGSGNGQ--------FNYPYGIA-------VDNDGKIYVADSNNNRI 276
|
|
| NHL_like_6 |
cd14962 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
327-561 |
2.23e-11 |
|
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: 64.92 E-value: 2.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 327 GEEGDKQPISSPWDVAlgtsgseVQRNDILWIAMAGTHQIWALlldsgtlpkksDLKKGtciRFAGSGNEENRNnayphk 406
Cdd:cd14962 3 GEERPKEALTRPYGVA-------ADGRGRIYVADTGRGAVFVF-----------DLPNG---KVFVIGNAGPNR------ 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 407 agFAQPSGLALASEEPwscLFVADSESstvrtvslrdGAVKHLVGGERdPMNLFafgdvdgaGINAKLQHPLGVAWDEER 486
Cdd:cd14962 56 --FVSPIGVAIDANGN---LYVSDAEL----------GKVFVFDRDGK-FLRAI--------GAGALFKRPTGIAVDPAG 111
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789158 487 QVLYVADSYNHKIKVVDPKTKGCTTLAGTGDasdasssfAESAFNEPGGLCIGESGRlLYVADTNNHQIKVMDLE 561
Cdd:cd14962 112 KRLYVVDTLAHKVKVFDLDGRLLFDIGKRGS--------GPGEFNLPTDLAVDRDGN-LYVTDTMNFRVQIFDAD 177
|
|
| NHL-2_like |
cd14951 |
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL ... |
229-338 |
6.49e-11 |
|
NHL repeat domain of NHL repeat-containing protein 2 and similar proteins; NHL repeat-containing protein 2 (NHLRC2) and related bacterial proteins; members of this eukaryotic and bacterial family are uncharacterized, the NHL repeat domain is found C-terminally of a thioredoxin domain. 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: 271321 [Multi-domain] Cd Length: 334 Bit Score: 64.52 E-value: 6.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 229 VAVDhATGRLVVADTGHHRILVIQ-KNGRIQSSIGGPNPGRKDgmfSESSFNSPQGVAIADN-VIYVADTENHLIRKIDL 306
Cdd:cd14951 201 VAAL-PDGSVYVADTYNHKIKRVDpATGEVSTLAGTGKAGYKD---LEAQFSEPSGLVVDGDgRLYVADTNNHRIRRLDL 276
|
90 100 110
....*....|....*....|....*....|....*
gi 29789158 307 EAE--KVTTVAGVGIQG-TDTEGGEEGDKQPISSP 338
Cdd:cd14951 277 PTEalEVLTLAHRTLRPaTPPAPGPLRLRVRFTAP 311
|
|
| NHL_TRIM71_like |
cd14954 |
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
223-305 |
6.87e-11 |
|
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain] Cd Length: 285 Bit Score: 63.72 E-value: 6.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 223 LLFPGKVAVDHaTGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRKDgmfsessFNSPQGVAI-ADNVIYVADTENHLI 301
Cdd:cd14954 117 FNYPWGVAVDS-EGRIYVSDTRNHRVQVFDSDGQFIRKFGFEGAGPGQ-------LDSPRGVAVnPDGNIVVSDFNNHRL 188
|
....
gi 29789158 302 RKID 305
Cdd:cd14954 189 QVFD 192
|
|
| NHL_like_4 |
cd14955 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
225-305 |
8.47e-11 |
|
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: 271325 [Multi-domain] Cd Length: 279 Bit Score: 63.36 E-value: 8.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 225 FPGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGgpNPGRKDGMFsessfNSPQGVAI-ADNVIYVADTENHLIRK 303
Cdd:cd14955 205 APYGIAVDSA-GNVYVADTGNNRIQKFDSSGTFITKWG--SEGSGDGQF-----NSPSGIAVdSAGNVYVADSGNNRIQK 276
|
..
gi 29789158 304 ID 305
Cdd:cd14955 277 FA 278
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
327-561 |
1.56e-10 |
|
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: 62.31 E-value: 1.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 327 GEEGDkqPISSPWDVAlgtsgseVQRNDIlWIAMAGTHQIwaLLLDSGTLPKKSdlkkgtcirFAGSGNEENRnnayphk 406
Cdd:cd14963 3 GPFGD--PLNKPMGVA-------VSDGRI-YVADTNNHRV--QVFDYEGKFKKS---------FGGPGTGPGE------- 54
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 407 agFAQPSGLALASEEPwscLFVADSESSTVRTVSlRDGAVKHLVGGERDpmnlfafgdvdgagiNAKLQHPLGVAWDEER 486
Cdd:cd14963 55 --FKYPYGIAVDSDGN---IYVADLYNGRIQVFD-PDGKFLKYFPEKKD---------------RVKLISPAGLAIDDGK 113
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789158 487 qvLYVADSYNHKIKVVDPKTKGCTTLAGTGDAsdasssfaESAFNEPGGLCIGESGRLlYVADTNNHQIKVMDLE 561
Cdd:cd14963 114 --LYVSDVKKHKVIVFDLEGKLLLEFGKPGSE--------PGELSYPNGIAVDEDGNI-YVADSGNGRIQVFDKN 177
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
218-436 |
1.89e-10 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 61.63 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 218 LPPSPLLFPGKVAVDHATGRLVVADTGHHRILVI-QKNGRIQSSIGGPNpgrkdgmfsessfnSPQGVAI--ADNVIYVA 294
Cdd:COG3391 62 LGAAAVADADGADAGADGRRLYVANSGSGRVSVIdLATGKVVATIPVGG--------------GPRGLAVdpDGGRLYVA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 295 DTENHLIRKIDLEAEKVTTVAGVGiqgtdteggeegdkqpiSSPWDVALGTSGSEvqrndiLWIAMAGTHQIWALLLdsg 374
Cdd:COG3391 128 DSGNGRVSVIDTATGKVVATIPVG-----------------AGPHGIAVDPDGKR------LYVANSGSNTVSVIVS--- 181
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 29789158 375 tlpkKSDLKKGTCIRFAGSGNeenrnnayphkagfaQPSGLALASEEPWscLFVADSESSTV 436
Cdd:COG3391 182 ----VIDTATGKVVATIPVGG---------------GPVGVAVSPDGRR--LYVANRGSNTS 222
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
163-369 |
2.25e-10 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 61.96 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 163 PTLVILGPRGNLLFSLIGeGHRdklfsytsIAlKYYKDRGQIRDGKIgiklfkeslpPSPLLFPGKVAVDHAtGRLVVAD 242
Cdd:COG4257 104 PHGIAFDPDGNLWFTDQG-GNR--------IG-RLDPATGEVTEFPL----------PTGGAGPYGIAVDPD-GNLWVTD 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 243 TGHHRILVI-QKNGRIqSSIGGPNPgrkdgmfsessFNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEKVTTVAGVGiq 320
Cdd:COG4257 163 FGANAIGRIdPDTGTL-TEYALPTP-----------GAGPRGLAVdPDGNLWVADTGSGRIGRFDPKTGTVTEYPLPG-- 228
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 29789158 321 gtdteggeegdkqPISSPWDVAlgtsgseVQRNDILWIAMAGTHQIWAL 369
Cdd:COG4257 229 -------------GGARPYGVA-------VDGDGRVWFAESGANRIVRF 257
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
167-325 |
2.27e-10 |
|
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: 61.92 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 167 ILGPRGNLLFSLIGEGHRDKLFSYTSIALK----YYKDRGQIR------DGKIGIKLFKESLPPSPLLFPGKVAVDHAtG 236
Cdd:cd14963 81 VFDPDGKFLKYFPEKKDRVKLISPAGLAIDdgklYVSDVKKHKvivfdlEGKLLLEFGKPGSEPGELSYPNGIAVDED-G 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 237 RLVVADTGHHRILVIQKNGRIQSSIGgpnpGRKDGmfsESSFNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEKVTTva 315
Cdd:cd14963 160 NIYVADSGNGRIQVFDKNGKFIKELN----GSPDG---KSGFVNPRGIAVdPDGNLYVVDNLSHRVYVFDEQGKELFT-- 230
|
170
....*....|
gi 29789158 316 gVGIQGTDTE 325
Cdd:cd14963 231 -FGGRGKDDG 239
|
|
| NHL_TRIM71_like |
cd14954 |
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
223-301 |
2.46e-10 |
|
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain] Cd Length: 285 Bit Score: 62.18 E-value: 2.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 223 LLFPGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGGpnPGRKDGMFSessfnSPQGVAI-ADNVIYVADTENHLI 301
Cdd:cd14954 211 FKRPRGVAVDDE-GNIIVADSGNHRVQVFSPDGEFLCSFGT--EGNGEGQFD-----RPSGVAVtPDGRIVVVDRGNHRI 282
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
426-565 |
2.82e-10 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 61.25 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 426 LFVADSESSTVRTVSLRDGAVKHLVGGERDPMnlfafgdvdgaginaklqhplGVAWDEERQVLYVADSYNHKIKVVDPK 505
Cdd:COG3391 82 LYVANSGSGRVSVIDLATGKVVATIPVGGGPR---------------------GLAVDPDGGRLYVADSGNGRVSVIDTA 140
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 29789158 506 TKGCTTLAGTGdasdasssfaesafNEPGGLCIGESGRLLYVADTNNHQI----KVMDLEARTV 565
Cdd:COG3391 141 TGKVVATIPVG--------------AGPHGIAVDPDGKRLYVANSGSNTVsvivSVIDTATGKV 190
|
|
| NHL_TRIM71_like |
cd14954 |
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
459-568 |
3.12e-10 |
|
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain] Cd Length: 285 Bit Score: 61.79 E-value: 3.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 459 LFAFGDvDGAGiNAKLQHPLGVAWDEERQVlYVADSYNHKIKVVDPKTKGCTTLAGTGDAsdasssfaESAFNEPGGLCI 538
Cdd:cd14954 104 LLKFGE-RGTK-NGQFNYPWGVAVDSEGRI-YVSDTRNHRVQVFDSDGQFIRKFGFEGAG--------PGQLDSPRGVAV 172
|
90 100 110
....*....|....*....|....*....|
gi 29789158 539 GESGRLlYVADTNNHQIKVMDLEARTVSVL 568
Cdd:cd14954 173 NPDGNI-VVSDFNNHRLQVFDPDGQFLRFF 201
|
|
| NHL_TRIM71_like |
cd14954 |
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
220-301 |
6.97e-10 |
|
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain] Cd Length: 285 Bit Score: 60.64 E-value: 6.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 220 PSPLLFPGKVAVDHaTGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkDGMfsessFNSPQGVAIAD-NVIYVADTEN 298
Cdd:cd14954 161 PGQLDSPRGVAVNP-DGNIVVSDFNNHRLQVFDPDGQFLRFFGSEGSG--NGQ-----FKRPRGVAVDDeGNIIVADSGN 232
|
...
gi 29789158 299 HLI 301
Cdd:cd14954 233 HRV 235
|
|
| Vgb |
COG4257 |
Streptogramin lyase [Defense mechanisms]; |
161-506 |
3.95e-09 |
|
Streptogramin lyase [Defense mechanisms];
Pssm-ID: 443399 [Multi-domain] Cd Length: 270 Bit Score: 58.11 E-value: 3.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 161 CWPTLVILGPRGNLLFsligeghrdklfsytsialkyykdrgqirdgkigiklfkeslppspllfpgkvavdhatgrlvv 240
Cdd:COG4257 59 SGPHGIAVDPDGNLWF---------------------------------------------------------------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 241 ADTGHHRILVI-QKNGRIqSSIGGPNPGrkdgmfsessfNSPQGVAI-ADNVIYVADTENHLIRKIDLEAEKVTTVAGvg 318
Cdd:COG4257 75 TDNGNNRIGRIdPKTGEI-TTFALPGGG-----------SNPHGIAFdPDGNLWFTDQGGNRIGRLDPATGEVTEFPL-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 319 iqgtdteggeegdKQPISSPWDVALGTSGSevqrndiLWIAMAGTHQIWALLLDSGTLpkksdlkkgtcirfagsgneen 398
Cdd:COG4257 141 -------------PTGGAGPYGIAVDPDGN-------LWVTDFGANAIGRIDPDTGTL---------------------- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 399 rnNAYPHKAGFAQPSGLALASEEPwscLFVADSESSTVRTVSLRDGAVKHLVggerdpmnlfafgdvdgagINAKLQHPL 478
Cdd:COG4257 179 --TEYALPTPGAGPRGLAVDPDGN---LWVADTGSGRIGRFDPKTGTVTEYP-------------------LPGGGARPY 234
|
330 340
....*....|....*....|....*...
gi 29789158 479 GVAWDEERQVlYVADSYNHKIKVVDPKT 506
Cdd:COG4257 235 GVAVDGDGRV-WFAESGANRIVRFDPDT 261
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
69-298 |
5.62e-09 |
|
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: 57.69 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 69 PLSIYKDLCGKVVVLDFFTycciNCIHVLpdlhalerrfsDKDGLLIvgvhsAKFPNEKVLDNIKS-AVLRYNITHPVVN 147
Cdd:cd14963 58 PYGIAVDSDGNIYVADLYN----GRIQVF-----------DPDGKFL-----KYFPEKKDRVKLISpAGLAIDDGKLYVS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 148 DADASlwqelevscwpTLVILGPRGNLLFSLIGEGHRDKLFSY-TSIALK-----YYKDRGQIR------DGKIGIKLFK 215
Cdd:cd14963 118 DVKKH-----------KVIVFDLEGKLLLEFGKPGSEPGELSYpNGIAVDedgniYVADSGNGRiqvfdkNGKFIKELNG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 216 ESLPPSPLLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPnpGRKDGmfsesSFNSPQGVAIADN-VIYVA 294
Cdd:cd14963 187 SPDGKSGFVNPRGIAVD-PDGNLYVVDNLSHRVYVFDEQGKELFTFGGR--GKDDG-----QFNLPNGLFIDDDgRLYVT 258
|
....
gi 29789158 295 DTEN 298
Cdd:cd14963 259 DREN 262
|
|
| NHL_like_2 |
cd14957 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
460-559 |
1.61e-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: 56.51 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 460 FAFGDVdGAGINAkLQHPLGVAWDEERQvLYVADSYNHKIKVVDPKTKGCTTLaGTGDASDasssfaeSAFNEPGGLCIG 539
Cdd:cd14957 5 YAFGSN-GSGNGQ-FNTPRGIAVDSAGN-IYVADTGNNRIQVFTSSGVYSYSI-GSGGTGS-------GQFNSPYGIAVD 73
|
90 100
....*....|....*....|
gi 29789158 540 ESGRlLYVADTNNHQIKVMD 559
Cdd:cd14957 74 SNGN-IYVADTDNNRIQVFN 92
|
|
| NHL_like_2 |
cd14957 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
477-559 |
4.10e-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: 55.35 E-value: 4.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 477 PLGVAWDEERQVlYVADSYNHKIKVVDPKTKGCTTLAGTGDASdasssfaeSAFNEPGGLCIGESGRlLYVADTNNHQIK 556
Cdd:cd14957 67 PYGIAVDSNGNI-YVADTDNNRIQVFNSSGVYQYSIGTGGSGD--------GQFNGPYGIAVDSNGN-IYVADTGNHRIQ 136
|
...
gi 29789158 557 VMD 559
Cdd:cd14957 137 VFT 139
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
218-506 |
5.77e-08 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 54.31 E-value: 5.77e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 218 LPPSPLLFPGKVAVDHATGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRKDGMFSESSFNSPQGVAIAD-NVIYVADT 296
Cdd:COG3391 8 LVAVLLAVLALAALAVAVAALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADgRRLYVANS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 297 ENHLIRKIDLEAEKVTTVAGVGiqgtdteggeegdkqpiSSPWDVALGTSGSEvqrndiLWIAMAGTHQIWALlldsgtl 376
Cdd:COG3391 88 GSGRVSVIDLATGKVVATIPVG-----------------GGPRGLAVDPDGGR------LYVADSGNGRVSVI------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 377 pkksDLKKGTCIRFAGSGNeenrnnayphkagfaQPSGLALASEEPWscLFVADSESSTVRTV----SLRDGAVKHLVgg 452
Cdd:COG3391 138 ----DTATGKVVATIPVGA---------------GPHGIAVDPDGKR--LYVANSGSNTVSVIvsviDTATGKVVATI-- 194
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789158 453 erdpmnlfAFGdvdgaginaklQHPLGVAWDEERQVLYVADSYN-------HKIKVVDPKT 506
Cdd:COG3391 195 --------PVG-----------GGPVGVAVSPDGRRLYVANRGSntsnggsNTVSVIDLAT 236
|
|
| NHL_TRIM71_like |
cd14954 |
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; ... |
405-563 |
9.14e-08 |
|
NHL repeat domain of the tripartite motif-containing protein 71 (TRIM71) and related proteins; The E3 ubiquitin-protein ligase TRIM71 (LIN-41) is a RING-finger domain containing protein that has been associated with a variety of activities. The NHL repeat domain appears responsible for targeting TRIM71 to mRNAs, and TRIM71 appears responsible for translational repression and mRNA decay. Together with BRAT, TRIM71 may be part of a family of mRNA repressors that regulate proliferation and differentiation. TRIM has been shown to negatively regulate stability of Lin28B, which inhibits the pre-let-7 miRNA precursor from maturing by recruiting the terminal uriyltransferase TUT4. This family also contains the Caenorhabditis elegans NHL repeat containing 1 (NHL-1), a RING-finger-containing protein that was shown to interact with E2 ubiquitin conjugating enzymes in two-hybrid screens. Its domain architecture resembles that of the E3 ubiquitin protein ligases TRIM2, TRIM32, and TRIM71. 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: 271324 [Multi-domain] Cd Length: 285 Bit Score: 54.09 E-value: 9.14e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 405 HKAG-FAQPSGLALASEEPwscLFVADSESSTVRtVSLRDGAVKHLVGGErdpmnlfafGDVDGaginaKLQHPLGVAWD 483
Cdd:cd14954 18 SKDGeLCRPWGVAVDKDGR---IIVADRSNNRVQ-VFDPDGKFLRKFGSY---------GSRDG-----QFDRPAGVAVN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 484 EERQVlYVADSYNHKIKVVDPktKGCTTLA----GTGDASdasssfaesaFNEPGGLCIGESGRlLYVADTNNHQIKVMD 559
Cdd:cd14954 80 SRGRI-IVADKDNHRIQVFDL--NGRFLLKfgerGTKNGQ----------FNYPWGVAVDSEGR-IYVSDTRNHRVQVFD 145
|
....
gi 29789158 560 LEAR 563
Cdd:cd14954 146 SDGQ 149
|
|
| NHL_like_4 |
cd14955 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
467-559 |
1.43e-07 |
|
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: 271325 [Multi-domain] Cd Length: 279 Bit Score: 53.73 E-value: 1.43e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 467 GAGiNAKLQHPLGVAWDEERQVlYVADSYNHKIKVVDpktkgcttlaGTGD--ASDASSSFAESAFNEPGGLCIGESGRL 544
Cdd:cd14955 56 GSG-DGQFYSPTGIAVDSDGNV-YVADTGNHRIQKFD----------STGTflTKWGSSGSGDGQFNSPSGIAVDSAGNV 123
|
90
....*....|....*
gi 29789158 545 lYVADTNNHQIKVMD 559
Cdd:cd14955 124 -YVTDSGNNRIQKFD 137
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
434-573 |
2.14e-07 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 52.39 E-value: 2.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 434 STVRTVSLRDGAVKHLVGGERDPMNLFAFGDVDGAGINAKLQHPLGVAWDEERQVLYVADSYNHKIKVVDPKTKgctTLA 513
Cdd:COG3391 27 ALGLGGGGPLLAAASGGVVGAAVGGGGVALLAGLGLGAAAVADADGADAGADGRRLYVANSGSGRVSVIDLATG---KVV 103
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 29789158 514 GTGDASDasssfaesafnEPGGLCIGESGRLLYVADTNNHQIKVMDLEARTV-SVLPVCKS 573
Cdd:COG3391 104 ATIPVGG-----------GPRGLAVDPDGGRLYVADSGNGRVSVIDTATGKVvATIPVGAG 153
|
|
| NHL_like_6 |
cd14962 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
163-296 |
1.15e-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: 271332 [Multi-domain] Cd Length: 271 Bit Score: 50.66 E-value: 1.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 163 PTLVILGPRGNLLFSLIGEGHRDKLFSytsialkyyKDRGQIRD-GKIGIKlfkeslpPSPLLFPGKVAVDHAtGRLVVA 241
Cdd:cd14962 102 PTGIAVDPAGKRLYVVDTLAHKVKVFD---------LDGRLLFDiGKRGSG-------PGEFNLPTDLAVDRD-GNLYVT 164
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 29789158 242 DTGHHRILVIQKNGRIQSSIG--GPNPGrkdgmfsesSFNSPQGVAI-ADNVIYVADT 296
Cdd:cd14962 165 DTMNFRVQIFDADGKFLRSFGerGDGPG---------SFARPKGIAVdSEGNIYVVDA 213
|
|
| NHL_like_5 |
cd14963 |
Uncharacterized NHL-repeat domain in bacterial proteins; The NHL (NCL-1, HT2A and LIN-41) ... |
471-569 |
1.34e-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: 271333 [Multi-domain] Cd Length: 268 Bit Score: 50.37 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 471 NAKLQHPLGVAWDEERqvLYVADSYNHKIKVVDPKTKGCTTLAGTGDAsdasssfaESAFNEPGGLCIGESGRLlYVADT 550
Cdd:cd14963 6 GDPLNKPMGVAVSDGR--IYVADTNNHRVQVFDYEGKFKKSFGGPGTG--------PGEFKYPYGIAVDSDGNI-YVADL 74
|
90
....*....|....*....
gi 29789158 551 NNHQIKVMDLEARTVSVLP 569
Cdd:cd14963 75 YNGRIQVFDPDGKFLKYFP 93
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
380-570 |
1.90e-06 |
|
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: 49.89 E-value: 1.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 380 SDLKKGTCIRFAGSGNEENRnnaYPHKAGFaqPSGLALASEepwSCLFVADSESSTVRtVSLRDGAVKHLVGGERDPMNL 459
Cdd:COG3386 24 VDIPGGRIHRYDPDGGAVEV---FAEPSGR--PNGLAFDPD---GRLLVADHGRGLVR-FDPADGEVTVLADEYGKPLNR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 460 FAFGDVDGAG------------------INAKLQ-HPL--------GVAWDEERQVLYVADSYNHKIKVVDpktkgcttL 512
Cdd:COG3386 95 PNDGVVDPDGrlyftdmgeylptgalyrVDPDGSlRVLadgltfpnGIAFSPDGRTLYVADTGAGRIYRFD--------L 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 513 AGTGDASDAsSSFAESAFNE--PGGLCIGESGRlLYVADTNNHQIKVMDLEARTVSVLPV 570
Cdd:COG3386 167 DADGTLGNR-RVFADLPDGPggPDGLAVDADGN-LWVALWGGGGVVRFDPDGELLGRIEL 224
|
|
| YncE |
COG3391 |
DNA-binding beta-propeller fold protein YncE [General function prediction only]; |
411-570 |
4.48e-06 |
|
DNA-binding beta-propeller fold protein YncE [General function prediction only];
Pssm-ID: 442618 [Multi-domain] Cd Length: 237 Bit Score: 48.54 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 411 QPSGLALASEEpwSCLFVADSESSTVRTVSLRDGAVKHLVGGERDPMnlfafgdvdgaginaklqhplGVAWDEERQVLY 490
Cdd:COG3391 111 GPRGLAVDPDG--GRLYVADSGNGRVSVIDTATGKVVATIPVGAGPH---------------------GIAVDPDGKRLY 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 491 VADSYNHKI----KVVDPKTKGCTTLAGTGDAsdasssfaesafnePGGLCIGESGRLLYVADTNNHQIkvmDLEARTVS 566
Cdd:COG3391 168 VANSGSNTVsvivSVIDTATGKVVATIPVGGG--------------PVGVAVSPDGRRLYVANRGSNTS---NGGSNTVS 230
|
....
gi 29789158 567 VLPV 570
Cdd:COG3391 231 VIDL 234
|
|
| NHL_like_4 |
cd14955 |
Uncharacterized NHL-repeat domain in bacterial and archaeal proteins; The NHL (NCL-1, HT2A and ... |
477-559 |
4.99e-06 |
|
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: 271325 [Multi-domain] Cd Length: 279 Bit Score: 48.73 E-value: 4.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 477 PLGVAWDEERQVlYVADSYNHKIKVVDPK----TKGCTTlaGTGDAsdasssfaesAFNEPGGLCIGESGRLlYVADTNN 552
Cdd:cd14955 18 PSGIAVDSAGNV-YVADTGNNRIQKFDSTgtflTKWGSS--GSGDG----------QFYSPTGIAVDSDGNV-YVADTGN 83
|
....*..
gi 29789158 553 HQIKVMD 559
Cdd:cd14955 84 HRIQKFD 90
|
|
| NHL_PAL_like |
cd14958 |
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
229-301 |
5.21e-06 |
|
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. 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: 271328 [Multi-domain] Cd Length: 300 Bit Score: 48.80 E-value: 5.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789158 229 VAVDhATGRLVVADtGH--HRILVIQKNGRIQSSIGGPNPGrkdgmfsESSFNSPQGVAI-ADNVIYVADTENHLI 301
Cdd:cd14958 133 VAVA-PDGDIFVAD-GYcnSRIVKFSPDGKLLKSWGEPGSG-------PGQFNLPHSIALdEDGRVYVADRENGRI 199
|
|
| NHL_TRIM32_like |
cd14961 |
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
226-501 |
6.60e-06 |
|
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). 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: 271331 [Multi-domain] Cd Length: 273 Bit Score: 48.43 E-value: 6.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 226 PGKVAVDHaTGRLVVADTGHHRILVIQKNGRIQSSIggpnpgrkdGMFSESSFN--SPQGVAI-ADNVIYVADTENHLIR 302
Cdd:cd14961 13 PTGVAVTP-TGRVVVADDGNKRIQVFDSDGNCLQQF---------GPKGDAGQDirYPLDVAVtPDGHIVVTDAGDRSVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 303 KIDLEAEKVTTVagvgiqgtdteggeegdKQPISSPWDVALgTSGSEVqrndILWIAMAGThqIWALLLDS--GTLPKKS 380
Cdd:cd14961 83 VFSFDGRLKLFV-----------------RKSFSLPWGVAV-NPSGEI----LVTDSEAGK--LFVLTVDFklGILKKGQ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 381 DLKKG-TCIRF------------AGSGNEENRNNAYPHKAGFAQ---------------------PSGLALASEepwSCL 426
Cdd:cd14961 139 KLCSQlCRPRFvavsrlgavavtEHLFANGTRSSSTRVKVFSSGgqllgqidsfglnlvfpslicASGVAFDSE---GNV 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 29789158 427 FVADSESstvrtvslrdGAVKHLvgGERDPMNLFAFGDVDGaginakLQHPLGVAWDEERQVLyVADSYNHKIKV 501
Cdd:cd14961 216 IVADTGS----------GAILCL--GKPEGFPILKPIVTQG------LSRPVGLAVTPDGSLV-VLDSGNHCVKI 271
|
|
| NHL_PKND_like |
cd14952 |
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ... |
279-569 |
8.06e-06 |
|
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: 47.97 E-value: 8.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 279 NSPQGVAI--ADNViYVADTENHLIRKIDLEAEKVTTVagvgiqgtdteggeegdkqPIS---SPWDVALGTSGSevqrn 353
Cdd:cd14952 10 DGPGGVAVdaAGNV-YVADSGNNRVLKLAAGSTTQTVL-------------------PFTglyQPQGVAVDAAGT----- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 354 diLWIAMAGTHQIWALLLDSGT---LPkksdlkkgtcirFAGSGNeenrnnayphkagfaqPSGLALASEepwSCLFVAD 430
Cdd:cd14952 65 --VYVTDFGNNRVLKLAAGSTTqtvLP------------FTGLND----------------PTGVAVDAA---GNVYVAD 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 431 SESSTVrtVSLRDGAVkhlvggerdpmnlfAFGDVDGAGinakLQHPLGVAWDEERQVlYVADSYNHKIKVVDPKTKGCT 510
Cdd:cd14952 112 TGNNRV--LKLAAGSN--------------TQTVLPFTG----LSNPDGVAVDGAGNV-YVTDTGNNRVLKLAAGSTTQT 170
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 29789158 511 TLAGTGDASdasssfaesafnePGGLCIGESGRLlYVADTNNHQIKVMDLEARTVSVLP 569
Cdd:cd14952 171 VLPFTGLNS-------------PSGVAVDTAGNV-YVTDHGNNRVLKLAAGSTTPTVLP 215
|
|
| NHL_like_1 |
cd14953 |
Uncharacterized NHL-repeat domain in bacterial proteins; This bacterial family of NHL-repeat ... |
510-555 |
1.90e-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: 1.90e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 29789158 510 TTLAGTGDASDASSSFAESAFNEPGGLCIGESGRlLYVADTNNHQI 555
Cdd:cd14953 2 STVAGSGTAGFSGGGGTAARFNSPSGVAVDAAGN-LYVADRGNHRI 46
|
|
| NHL_PKND_like |
cd14952 |
NHL repeat domain of the protein kinase PknD; PknD is a mycobacterial transmembrane protein ... |
218-555 |
2.04e-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: 46.82 E-value: 2.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 218 LPPSPLLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIggPnpgrkdgmFSEssFNSPQGVAI-ADNVIYVADT 296
Cdd:cd14952 4 LPFTGLDGPGGVAVD-AAGNVYVADSGNNRVLKLAAGSTTQTVL--P--------FTG--LYQPQGVAVdAAGTVYVTDF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 297 ENHLIRKIDLEAEKVTTVAGVGiqgtdteggeegdkqpISSPWDVALGTSGSevqrndiLWIAMAGTHQIWALLLDSGT- 375
Cdd:cd14952 71 GNNRVLKLAAGSTTQTVLPFTG----------------LNDPTGVAVDAAGN-------VYVADTGNNRVLKLAAGSNTq 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 376 --LPkksdlkkgtcirFAGSGNeenrnnayphkagfaqPSGLALASEepwSCLFVADSESSTVrtvslrdgaVKhLVGGE 453
Cdd:cd14952 128 tvLP------------FTGLSN----------------PDGVAVDGA---GNVYVTDTGNNRV---------LK-LAAGS 166
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 454 RDPMNLfAFGDvdgaginakLQHPLGVAWDEERQVlYVADSYNHKIKVVDPKTKGCTTLAGTGdasdasssfaesaFNEP 533
Cdd:cd14952 167 TTQTVL-PFTG---------LNSPSGVAVDTAGNV-YVTDHGNNRVLKLAAGSTTPTVLPFTG-------------LNGP 222
|
330 340
....*....|....*....|..
gi 29789158 534 GGLCIGESGRlLYVADTNNHQI 555
Cdd:cd14952 223 LGVAVDAAGN-VYVADRGNDRV 243
|
|
| NHL_brat_like |
cd14959 |
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ... |
527-584 |
2.69e-05 |
|
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. 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: 271329 [Multi-domain] Cd Length: 274 Bit Score: 46.49 E-value: 2.69e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 527 ESAFNEPGGLCIGESGRLLyVADTNNHQIKVMDLEARTVSVLPVCKSDsavvDGS--FPR 584
Cdd:cd14959 18 EGQFNSPSGFCLGEDEDIL-VADTNNHRIQVFDKEGEFKFQFGIPGKR----DGQlwYPN 72
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
218-504 |
8.28e-05 |
|
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: 44.88 E-value: 8.28e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 218 LPPSPLLFPGKVAVDHAtGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGrkdgmfsessfnsPQGVAI-ADNVIYVADT 296
Cdd:COG3386 2 LADAGFRLGEGPVWDPD-GRLYWVDIPGGRIHRYDPDGGAVEVFAEPSGR-------------PNGLAFdPDGRLLVADH 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 297 ENHLIRkIDLEAEKVTTVAgvgiqgtdteggEEGDKqPISSPwdvalgtsgsevqrNDiLWIAMAGThqIWAllldsGTL 376
Cdd:COG3386 68 GRGLVR-FDPADGEVTVLA------------DEYGK-PLNRP--------------ND-GVVDPDGR--LYF-----TDM 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 377 PKKSDlkKGTCIRFAGSGneenrnNAYPHKAGFAQPSGLALASEEpwSCLFVADSESSTVRTVSLR-DGAVkhlvgGERD 455
Cdd:COG3386 112 GEYLP--TGALYRVDPDG------SLRVLADGLTFPNGIAFSPDG--RTLYVADTGAGRIYRFDLDaDGTL-----GNRR 176
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 29789158 456 PmnLFAFGDVDGAginaklqhPLGVAWDEE-RqvLYVADSYNHKIKVVDP 504
Cdd:COG3386 177 V--FADLPDGPGG--------PDGLAVDADgN--LWVALWGGGGVVRFDP 214
|
|
| NHL_TRIM2_like |
cd14960 |
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; ... |
205-299 |
9.37e-05 |
|
NHL repeat domain of the tripartite motif-containing protein 2 (TRIM2) and related proteins; The E3 ubiquitin-protein ligase TRIM2 is responsible for ubiquinating the apoptosis-inducing Bcl-2-interacting mediator of cell death (Bim), when the latter is phosphorylated by p42/p44 MAPK. TRIM2 regulates the ubiquitination of neurofilament light subunit (NF-L), deficiencies in TRIM2 result in increased NF-L levels in axons and subsequent axonopathy. TRIM2 is also involved in regulating axon outgrowth during development; it contains RING and BBOX domains, the NHL repeat domain is located at its C-terminus. 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: 271330 [Multi-domain] Cd Length: 274 Bit Score: 45.03 E-value: 9.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 205 RDGKIGIKLFKESLPPSPLLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGpnpgrkdgmfSESSFNSPQGV 284
Cdd:cd14960 181 AEGEFLFKFGSNGEGNGQFNAPTGVAVD-SNGNIIVADWGNSRIQVFDSSGSFLSYINT----------SADPLYGPQGL 249
|
90
....*....|....*.
gi 29789158 285 AI-ADNVIYVADTENH 299
Cdd:cd14960 250 ALtSDGHVVVADSGNH 265
|
|
| YvrE |
COG3386 |
Sugar lactone lactonase YvrE [Carbohydrate transport and metabolism]; Sugar lactone lactonase ... |
479-568 |
1.18e-04 |
|
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: 44.50 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 479 GVAWDEErQVLYVADSYNHKIKVVDPKTKGCTTLAGTGdasdasssfaesafNEPGGLCIGESGRlLYVADTnNHQIKVM 558
Cdd:COG3386 12 GPVWDPD-GRLYWVDIPGGRIHRYDPDGGAVEVFAEPS--------------GRPNGLAFDPDGR-LLVADH-GRGLVRF 74
|
90
....*....|
gi 29789158 559 DLEARTVSVL 568
Cdd:COG3386 75 DPADGEVTVL 84
|
|
| NHL_TRIM32_like |
cd14961 |
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; ... |
161-303 |
2.43e-04 |
|
NHL repeat domain of the tripartite motif-containing protein 32 (TRIM32) and related proteins; The E3 ubiquitin-protein ligase TRIM32 (HT2A) is widely expressed and is responsible for ubiquinating a large variety of targets, including dysbindin (DTNBP1), NPHP7/Glis2, TAp73, and others. TRIM32 promotes disassociation of the plakoglobin-PI3K complex and reduces PI3K-Akt-FoxO signaling. Mutations in TRIM32 have been implemented in the two diverse diseases limb-girdle muscular dystrophy type 2H (LGMD2H) or sarcotubular myopathy (STM) and Bardet-Biedl syndrome type 11 (BBS11). 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: 271331 [Multi-domain] Cd Length: 273 Bit Score: 43.42 E-value: 2.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 161 CWPTLVILGPRGNLLFSligEGHRDKLFSYTSIALKYYKDRGQirdGKIGIKLFKESLPPSPLLFPGKVAVDHaTGRLVV 240
Cdd:cd14961 145 CRPRFVAVSRLGAVAVT---EHLFANGTRSSSTRVKVFSSGGQ---LLGQIDSFGLNLVFPSLICASGVAFDS-EGNVIV 217
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 29789158 241 ADTGHHRILVIQKNGriqssiGGP--NPGRKDGMfsessfNSPQGVAI-ADNVIYVADTENHLIRK 303
Cdd:cd14961 218 ADTGSGAILCLGKPE------GFPilKPIVTQGL------SRPVGLAVtPDGSLVVLDSGNHCVKI 271
|
|
| NHL_brat_like |
cd14959 |
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; ... |
223-319 |
2.46e-04 |
|
NHL repeat domain of the Drosophila brain-tumor protein (brat) and similar proteins; Drosophila brain-tumor (brat) has been identified as a tumor suppressor that negatively regulates cell proliferation during development of the Drosophila larval brain. It appears to be recruited to the 3'-untranslated region of hunchback RNA and regulates its translation by forming a complex with Pumilio (Pum) and Nanos (Nos). The NHL domain of brat appears to be involved by interacting with the RNA-binding Puf repeats of Pumilio, a sequence-specific RNA binding protein. This family also contains the Caenorhabditis elegans homolog NCL-1. 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: 271329 [Multi-domain] Cd Length: 274 Bit Score: 43.41 E-value: 2.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 223 LLFPGKVAVDHATGRLVVADTGH--HRILVIQKNGRIQSSIGGPN-----------PGR---------------KDG--- 271
Cdd:cd14959 68 LWYPNKVAVCRVTGRYVVTDRGNprHRMQIFTKRGQFVRKFGARYlqhvrgltvdaAGHiivveskvmrvfifdESGnvl 147
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 29789158 272 -MFSESSF-NSPQGVAIADNVIYVADTENHLIRKIDLEAEKVTTVAGVGI 319
Cdd:cd14959 148 kWFDCSKYlEEPSDVAVNDNEIYICDNKGHCVVVFNYDGQFLRRIGGEGI 197
|
|
| NHL |
pfam01436 |
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
530-557 |
2.98e-04 |
|
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats.
Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 38.54 E-value: 2.98e-04
10 20
....*....|....*....|....*...
gi 29789158 530 FNEPGGLCIGESGRLlYVADTNNHQIKV 557
Cdd:pfam01436 1 FNRPHGVAVDSNGDI-YVADSENHRVQV 27
|
|
| NHL |
pfam01436 |
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is ... |
278-303 |
9.87e-04 |
|
NHL repeat; The NHL (NCL-1, HT2A and LIN-41) repeat is found in multiple tandem copies. It is about 40 residues long and resembles the WD repeat pfam00400. The repeats have a catalytic activity in Swiss:P10731, proteolysis has shown that the Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL) activity is localized to the repeats. Swiss:Q13049 interacts with the activation domain of Tat. This interaction is me diated by the NHL repeats.
Pssm-ID: 396153 [Multi-domain] Cd Length: 28 Bit Score: 37.00 E-value: 9.87e-04
10 20
....*....|....*....|....*..
gi 29789158 278 FNSPQGVAIA-DNVIYVADTENHLIRK 303
Cdd:pfam01436 1 FNRPHGVAVDsNGDIYVADSENHRVQV 27
|
|
| NHL_PAL_like |
cd14958 |
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
227-348 |
1.54e-03 |
|
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. 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: 271328 [Multi-domain] Cd Length: 300 Bit Score: 41.10 E-value: 1.54e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 227 GKVAVDHATGRLVVADTG---HHRILVIQKNGRIQSSIGgpnpgrkDGMFSessfnSPQGVAIA-DNVIYVADTENHLIR 302
Cdd:cd14958 33 GRVWDANSFDANVYVFKGpieEDTILVFDPDGGFLRSWG-------AGLFY-----MPHGLTIDpDGNIWVTDVGLHQVF 100
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 29789158 303 KIDLEAEKVTTvagvGIQGTDTEGGEegDKQPISSPWDVALGTSGS 348
Cdd:cd14958 101 KFDPEGKLLPL----LTLGERGEPGS--DQTHFCKPTDVAVAPDGD 140
|
|
| AhpC-TSA |
pfam00578 |
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ... |
74-174 |
1.79e-03 |
|
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).
Pssm-ID: 425763 [Multi-domain] Cd Length: 124 Bit Score: 38.74 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 74 KDLCGKVVVLDFF-TYCCINCIHVLPDLHALERRFsDKDGLLIVGVHSAKfpnekvLDNIKSAVLRYNITHPVVNDADAS 152
Cdd:pfam00578 21 SDYRGKWVVLFFYpADWTPVCTTELPALADLYEEF-KKLGVEVLGVSVDS------PESHKAFAEKYGLPFPLLSDPDGE 93
|
90 100
....*....|....*....|....*...
gi 29789158 153 L------WQELEVSCWPTLVILGPRGNL 174
Cdd:pfam00578 94 VaraygvLNEEEGGALRATFVIDPDGKV 121
|
|
| NHL |
cd05819 |
NHL repeat unit of beta-propeller proteins; The NHL(NCL-1, HT2A and LIN-41)-repeat is found in ... |
166-251 |
2.24e-03 |
|
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: 40.38 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 166 VILGPRGNLLFSLIGEGHRDKLFSY-TSIAL---------KYYKDRGQI--RDGKIGIKLFKESLPPSPLLFPGKVAVDh 233
Cdd:cd05819 173 QVFDPDGNFLTTFGSTGTGPGQFNYpTGIAVdsdgniyvaDSGNNRVQVfdPDGAGFGGNGNFLGSDGQFNRPSGLAVD- 251
|
90
....*....|....*...
gi 29789158 234 ATGRLVVADTGHHRILVI 251
Cdd:cd05819 252 SDGNLYVADTGNNRIQVF 269
|
|
| NHL_PAL_like |
cd14958 |
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
476-563 |
2.69e-03 |
|
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. 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: 271328 [Multi-domain] Cd Length: 300 Bit Score: 40.32 E-value: 2.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 476 HPLGVAWDEERQVlYVADSY-NHKIKVVDPKTK-----GcttlagtgdasdaSSSFAESAFNEPGGLCIGESGRLlYVAD 549
Cdd:cd14958 129 KPTDVAVAPDGDI-FVADGYcNSRIVKFSPDGKllkswG-------------EPGSGPGQFNLPHSIALDEDGRV-YVAD 193
|
90
....*....|....
gi 29789158 550 TNNHQIKVMDLEAR 563
Cdd:cd14958 194 RENGRIQVFDADGK 207
|
|
| TlpA_like_ScsD_MtbDsbE |
cd03011 |
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE ... |
78-173 |
3.40e-03 |
|
TlpA-like family, suppressor for copper sensitivity D protein (ScsD) and actinobacterial DsbE homolog subfamily; composed of ScsD, the DsbE homolog of Mycobacterium tuberculosis (MtbDsbE) and similar proteins, all containing a redox-active CXXC motif. The Salmonella typhimurium ScsD is a thioredoxin-like protein which confers copper tolerance to copper-sensitive mutants of E. coli. MtbDsbE has been characterized as an oxidase in vitro, catalyzing the disulfide bond formation of substrates like hirudin. The reduced form of MtbDsbE is more stable than its oxidized form, consistent with an oxidase function. This is in contrast to the function of DsbE from gram-negative bacteria which is a specific reductase of apocytochrome c.
Pssm-ID: 239309 [Multi-domain] Cd Length: 123 Bit Score: 38.05 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 78 GKVVVLDFFTYCCINCIHVLPDLHALERRFSdkdgllIVGVHSAKFPNEKVldniKSAVLRYNITHPVVNDADASLWQEL 157
Cdd:cd03011 20 GKPVLVYFWATWCPVCRFTSPTVNQLAADYP------VVSVALRSGDDGAV----ARFMQKKGYGFPVINDPDGVISARW 89
|
90
....*....|....*.
gi 29789158 158 EVSCWPTLVILGPRGN 173
Cdd:cd03011 90 GVSVTPAIVIVDPGGI 105
|
|
| NHL_PAL_like |
cd14958 |
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the ... |
205-350 |
4.28e-03 |
|
Peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PAL, EC 4.3.2.5); PAL catalyzes the N-dealkylation of peptidyl-alpha-hydroxyglycine, which results in an alpha-amidated peptide and glyoxylate. Amidation of the C-terminus is required for the activity of many peptide hormones and neuropeptides. The catalytic residues of PAL are located on several NHL-repeats. 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: 271328 [Multi-domain] Cd Length: 300 Bit Score: 39.94 E-value: 4.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 29789158 205 RDGKIgIKLF-KESLPPSPLLFPGKVAVDhATGRLVVADTGHHRILVIQKNGRIQSSIGGPNPGRkdgmfsessfnsPQG 283
Cdd:cd14958 157 PDGKL-LKSWgEPGSGPGQFNLPHSIALD-EDGRVYVADRENGRIQVFDADGKFLTEWTNPELGR------------PYA 222
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 29789158 284 VAI-ADNVIYVADTENHLIRKIDLEAEKVTTVAGVGIqgtDTEGGEEGDKQPISSPWDVALGtSGSEV 350
Cdd:cd14958 223 LAIdPDGLLYVVDGPPRLNRSLPVRGFVIRIGKGLIL---GRFGPGGKAPGQFQNPHDIAVD-SGGDI 286
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