|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
28-866 |
0e+00 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 700.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 28 YGY--GPGSLRELRAREFSRLAGTVYLDHAGATLFSQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHF 105
Cdd:PLN02724 12 YGYpdGPKPIDELRATEFARLKGVVYLDHAGATLYSESQLEAALADFSSNVYGNPHSQSDSSMRSSDTIESARQQVLEYF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 106 HTTAEDYTVIFTAGSTAALKLVAEAFPWvsqgpeSSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEdlwsAEERSA 185
Cdd:PLN02724 92 NAPPSDYACVFTSGATAALKLVGETFPW------SSESHFCYTLENHNSVLGIREYALEKGAAAIAVDIE----EAANQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 186 SASNPDCQLPH----------------------LFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAASYV 243
Cdd:PLN02724 162 TNSQGSVVVKSrglqrrntsklqkreddgeaynLFAFPSECNFSGAKFPLDLVKLIKDNQHSNFSKSGRWMVLLDAAKGC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 244 STSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLAGEDFYIPRQSVAQRFEDGTISFL 323
Cdd:PLN02724 242 GTSPPDLSRYPADFVVVSFYKIFGYPTGLGALLVRRDAAKLLKKKYFGGGTVAASIADIDFVKRRERVEQRFEDGTISFL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 324 DVIALKHGFDTLERLTggMENIKQHTFTLAQYTYVALSSLQYPNGAPVVRIYSDSEFS-SPEVQGPIINFNVLDDKGNII 402
Cdd:PLN02724 322 SIAALRHGFKLLNRLT--ISAIAMHTWALTHYVANSLRNLKHGNGAPVCVLYGNHTFKlEFHIQGPIVTFNLKRADGSWV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 403 GYSQVDKMASLYNIHLRTGCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQAFL 482
Cdd:PLN02724 400 GHREVEKLASLSGIQLRTGCFCNPGACAKYLGLSHKDLQANFEAGHVCWDDQDVIHGRPTGAVRVSFGYMSTFEDCQKFI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 483 RFIIdtrlhssgdwpvpqahadtgetgapsadsqadvipavmgRRSLSPqedaltgsrvwnnSSTVNAVPVAPPvcdvaR 562
Cdd:PLN02724 480 DFII---------------------------------------SSFVST-------------PKKRGNVTLRSK-----R 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 563 TQPTPSEKAAGVLEGalgpHVVTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFID 642
Cdd:PLN02724 503 TIPLPVLERKESFDS----HRLKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGEILTQKKVPEMCLITTFID 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 643 LRQRIMVIKAKGME-PIEVPLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHGK 721
Cdd:PLN02724 579 LESGKLVVRAPRCDhKLEIPLESDSQHEESGEVILCGNRAESMSYGTEINEWFTNALGRRCTLVRKSSSNTRVCRNRNPS 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 722 DQLPGTMAT-LSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFslkdlSLRFRANIIINGKRAFEEEKWDEISIGSL 800
Cdd:PLN02724 659 HSPCGDDESrLSFANEGQFLLISEASVEDLNRRLATGQEDAKIRLD-----PTRFRPNLVVSGGEAYAEDEWQSLSIGDA 733
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 801 RFQVLGPCHRCQMICIDQQTGQRNQ--HVFQKLSESRETK--VNFGMyLMHASLDLSSPCFLSVGSQVLP 866
Cdd:PLN02724 734 EFTVLGGCNRCQMINIDQETGLVNPsnEPLATLASYRRVKgkILFGI-LLRYEISDKRDQWIAVGSRVNP 802
|
|
| YcbX |
COG3217 |
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ... |
584-864 |
2.24e-53 |
|
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];
Pssm-ID: 442450 [Multi-domain] Cd Length: 240 Bit Score: 185.78 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 584 VTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRImVIKAKGMEPIEVPLE 663
Cdd:COG3217 4 VSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGGL-TLTAPGGESLTVDLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 664 EnsertqirqsrvcadrvstyDCGEKISSWLSTFFGRPCHLIKQSSNSQRNakkkhgkdqlpgtmATLSLVNEAQYLLIN 743
Cdd:COG3217 83 D--------------------DAGDAAAAWLSEYLGRPVRLVRLPPESRRG--------------PPVGFADGYPVLLIS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 744 TSSILELHRQLNTSDEngkeelfslkdlSLRFRANIIINGKRAFEEEKW--DEISIGSLRFQVLGPCHRCQMICIDQQTG 821
Cdd:COG3217 129 TASLADLNARLGAPVD------------MRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETG 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1519315834 822 QRNQHVFQKLSESR--ETKVNFGMYLMHAsldlsSPCFLSVGSQV 864
Cdd:COG3217 197 ERDPEPLRTLARYRgaDGHVDFGVNAIVL-----EGGTIRVGDEV 236
|
|
| MOSC_N |
pfam03476 |
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The ... |
584-701 |
6.52e-30 |
|
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The function of this domain is unknown, however it is predicted to adopt a beta barrel fold.
Pssm-ID: 281474 Cd Length: 118 Bit Score: 114.76 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 584 VTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQrIMVIKAKGMEPIEVPLE 663
Cdd:pfam03476 4 VSSLYVYPIKSCRGESLSRAELTAAGLAWDRRFMVVDSDGKFVTARREPRLVLIRTTLDEDG-GLTLTAPGMPDLSVPLA 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 1519315834 664 ENSerTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRP 701
Cdd:pfam03476 83 DNK--FDLRGVLVWGLSFSGRDCGDAAADWFSDFLGKP 118
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
50-482 |
2.26e-21 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 97.15 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAGATLFSQSQLESfTSDLMENTYGNPH--SQNISSKLThDTVEQVRYRIlAHFHTTAEDYTVIFTAGSTAALKLV 127
Cdd:cd06453 1 VYLDNAATSQKPQPVIDA-IVDYYRHYNANVHrgVHELSARAT-DAYEAAREKV-ARFINAPSPDEIIFTRNTTEAINLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 128 AEAFPWvSQGPessGSRFcyLTDS--HTSVVgmrnvtmainvistpvRPedlWS--AEERSAS----ASNPDCQLP---- 195
Cdd:cd06453 78 AYGLGR-ANKP---GDEI--VTSVmeHHSNI----------------VP---WQqlAERTGAKlkvvPVDDDGQLDleal 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 196 --------------HLfcypaqSNFSGVRYPlswIEEVksGRL-HPVSTPgkwfVLLDAASYVSTSPLDLSAHQADFVPI 260
Cdd:cd06453 133 eklltertklvavtHV------SNVLGTINP---VKEI--GEIaHEAGVP----VLVDGAQSAGHMPVDVQDLGCDFLAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 261 SFYKIFGfPTGLGALLVhnrAAPLLRKT--YFGGGTASAYLAGEDfYIPRQsVAQRFEDGTISFLDVIALKHGFDTLERL 338
Cdd:cd06453 198 SGHKMLG-PTGIGVLYG---KEELLEEMppYGGGGEMIEEVSFEE-TTYAD-LPHKFEAGTPNIAGAIGLGAAIDYLEKI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 339 tgGMENIKQHTFTLAQYTYVALSSLqypngaPVVRIYSDsefssPEVQGPIINFNVLDDKGNIIGYsqvdkmaslyniHL 418
Cdd:cd06453 272 --GMEAIAAHEHELTAYALERLSEI------PGVRVYGD-----AEDRAGVVSFNLEGIHPHDVAT------------IL 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519315834 419 RTgcfcntgacqrhLGIsneMVRkhfqAGHVCGdnMDLIDG-QPTGSVRISFGYMSTLDDVQAFL 482
Cdd:cd06453 327 DQ------------YGI---AVR----AGHHCA--QPLMRRlGVPGTVRASFGLYNTEEEIDALV 370
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
235-355 |
2.44e-04 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 44.84 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 235 VLLDAASYVSTSPLDLSAHQADFVPISFYKIFGfPTGLGAllVHNRAApLLRKT--YFGGG------TasaylagedFyi 306
Cdd:NF041166 419 VLVDGAQSVSHMPVDVQALDADFFVFSGHKVFG-PTGIGV--VYGKRD-LLEAMppWQGGGnmiadvT---------F-- 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1519315834 307 pRQSVAQ----RFEDGTISFLDVIALKHGFDTLERLtgGMENIKQHTFTLAQY 355
Cdd:NF041166 484 -EKTVYQpapnRFEAGTGNIADAVGLGAALDYVERI--GIENIARYEHDLLEY 533
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02724 |
PLN02724 |
Molybdenum cofactor sulfurase |
28-866 |
0e+00 |
|
Molybdenum cofactor sulfurase
Pssm-ID: 215384 [Multi-domain] Cd Length: 805 Bit Score: 700.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 28 YGY--GPGSLRELRAREFSRLAGTVYLDHAGATLFSQSQLESFTSDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHF 105
Cdd:PLN02724 12 YGYpdGPKPIDELRATEFARLKGVVYLDHAGATLYSESQLEAALADFSSNVYGNPHSQSDSSMRSSDTIESARQQVLEYF 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 106 HTTAEDYTVIFTAGSTAALKLVAEAFPWvsqgpeSSGSRFCYLTDSHTSVVGMRNVTMAINVISTPVRPEdlwsAEERSA 185
Cdd:PLN02724 92 NAPPSDYACVFTSGATAALKLVGETFPW------SSESHFCYTLENHNSVLGIREYALEKGAAAIAVDIE----EAANQP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 186 SASNPDCQLPH----------------------LFCYPAQSNFSGVRYPLSWIEEVKSGRLHPVSTPGKWFVLLDAASYV 243
Cdd:PLN02724 162 TNSQGSVVVKSrglqrrntsklqkreddgeaynLFAFPSECNFSGAKFPLDLVKLIKDNQHSNFSKSGRWMVLLDAAKGC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 244 STSPLDLSAHQADFVPISFYKIFGFPTGLGALLVHNRAAPLLRKTYFGGGTASAYLAGEDFYIPRQSVAQRFEDGTISFL 323
Cdd:PLN02724 242 GTSPPDLSRYPADFVVVSFYKIFGYPTGLGALLVRRDAAKLLKKKYFGGGTVAASIADIDFVKRRERVEQRFEDGTISFL 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 324 DVIALKHGFDTLERLTggMENIKQHTFTLAQYTYVALSSLQYPNGAPVVRIYSDSEFS-SPEVQGPIINFNVLDDKGNII 402
Cdd:PLN02724 322 SIAALRHGFKLLNRLT--ISAIAMHTWALTHYVANSLRNLKHGNGAPVCVLYGNHTFKlEFHIQGPIVTFNLKRADGSWV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 403 GYSQVDKMASLYNIHLRTGCFCNTGACQRHLGISNEMVRKHFQAGHVCGDNMDLIDGQPTGSVRISFGYMSTLDDVQAFL 482
Cdd:PLN02724 400 GHREVEKLASLSGIQLRTGCFCNPGACAKYLGLSHKDLQANFEAGHVCWDDQDVIHGRPTGAVRVSFGYMSTFEDCQKFI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 483 RFIIdtrlhssgdwpvpqahadtgetgapsadsqadvipavmgRRSLSPqedaltgsrvwnnSSTVNAVPVAPPvcdvaR 562
Cdd:PLN02724 480 DFII---------------------------------------SSFVST-------------PKKRGNVTLRSK-----R 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 563 TQPTPSEKAAGVLEGalgpHVVTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFID 642
Cdd:PLN02724 503 TIPLPVLERKESFDS----HRLKSITVYPIKSCAGFSVERWPLSETGLLYDREWMIQSLTGEILTQKKVPEMCLITTFID 578
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 643 LRQRIMVIKAKGME-PIEVPLEENSERTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRPCHLIKQSSNSQRNAKKKHGK 721
Cdd:PLN02724 579 LESGKLVVRAPRCDhKLEIPLESDSQHEESGEVILCGNRAESMSYGTEINEWFTNALGRRCTLVRKSSSNTRVCRNRNPS 658
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 722 DQLPGTMAT-LSLVNEAQYLLINTSSILELHRQLNTSDENGKEELFslkdlSLRFRANIIINGKRAFEEEKWDEISIGSL 800
Cdd:PLN02724 659 HSPCGDDESrLSFANEGQFLLISEASVEDLNRRLATGQEDAKIRLD-----PTRFRPNLVVSGGEAYAEDEWQSLSIGDA 733
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 801 RFQVLGPCHRCQMICIDQQTGQRNQ--HVFQKLSESRETK--VNFGMyLMHASLDLSSPCFLSVGSQVLP 866
Cdd:PLN02724 734 EFTVLGGCNRCQMINIDQETGLVNPsnEPLATLASYRRVKgkILFGI-LLRYEISDKRDQWIAVGSRVNP 802
|
|
| YcbX |
COG3217 |
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and ... |
584-864 |
2.24e-53 |
|
N-hydroxylaminopurine reductase subunit YcbX, contains MOSC domain [Nucleotide transport and metabolism, Defense mechanisms];
Pssm-ID: 442450 [Multi-domain] Cd Length: 240 Bit Score: 185.78 E-value: 2.24e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 584 VTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQRImVIKAKGMEPIEVPLE 663
Cdd:COG3217 4 VSRLYRYPVKSLAGEALESATLTAGGLPGDRRWALVDADGRFLTQRRHPRLALLRARLDEDGGL-TLTAPGGESLTVDLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 664 EnsertqirqsrvcadrvstyDCGEKISSWLSTFFGRPCHLIKQSSNSQRNakkkhgkdqlpgtmATLSLVNEAQYLLIN 743
Cdd:COG3217 83 D--------------------DAGDAAAAWLSEYLGRPVRLVRLPPESRRG--------------PPVGFADGYPVLLIS 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 744 TSSILELHRQLNTSDEngkeelfslkdlSLRFRANIIINGKRAFEEEKW--DEISIGSLRFQVLGPCHRCQMICIDQQTG 821
Cdd:COG3217 129 TASLADLNARLGAPVD------------MRRFRPNLVVDGLEPFAEDDWvgRRLRIGEVRLRVVKPCSRCVVTTVDPETG 196
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1519315834 822 QRNQHVFQKLSESR--ETKVNFGMYLMHAsldlsSPCFLSVGSQV 864
Cdd:COG3217 197 ERDPEPLRTLARYRgaDGHVDFGVNAIVL-----EGGTIRVGDEV 236
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
50-485 |
1.46e-44 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 166.08 E-value: 1.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAGATLFSQSQLEsFTSDLMENTYGNPH-SQNISSKLTHDTVEQVRYRILAHFHTtAEDYTVIFTAGSTAALKLVA 128
Cdd:COG0520 17 VYLDNAATGQKPRPVID-AIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGA-ASPDEIIFTRGTTEAINLVA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 129 EAFPWVSQGPEssgsrfCYLTDS--HTSVVGMRNVTMA--INVISTPVRPEDLWSAEErSASASNPDCQLphlFCYPAQS 204
Cdd:COG0520 95 YGLGRLKPGDE------ILITEMehHSNIVPWQELAERtgAEVRVIPLDEDGELDLEA-LEALLTPRTKL---VAVTHVS 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 205 NFSGVRYPLSWIeeVKSGRLHPVstpgkwFVLLDAASYVSTSPLDLSAHQADFVPISFYKIFGfPTGLGALLVHNRAAPL 284
Cdd:COG0520 165 NVTGTVNPVKEI--AALAHAHGA------LVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYG-PTGIGVLYGKRELLEA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 285 LRKTYFGGGTASayLAGEDFYIPrQSVAQRFEDGTISFLDVIALKHGFDTLERLtgGMENIKQHTFTLAQYTYVALSSLq 364
Cdd:COG0520 236 LPPFLGGGGMIE--WVSFDGTTY-ADLPRRFEAGTPNIAGAIGLGAAIDYLEAI--GMEAIEARERELTAYALEGLAAI- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 365 ypngaPVVRIYSDSEfssPEVQGPIINFNVlddKGniIGYSQVDKMASLYNIHLRTGCFCNTGACQRhLGIsnemvrkhf 444
Cdd:COG0520 310 -----PGVRILGPAD---PEDRSGIVSFNV---DG--VHPHDVAALLDDEGIAVRAGHHCAQPLMRR-LGV--------- 366
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1519315834 445 qaghvcgdnmdlidgqpTGSVRISFGYMSTLDDVQAFLRFI 485
Cdd:COG0520 367 -----------------PGTVRASFHLYNTEEEIDRLVEAL 390
|
|
| MOSC_N |
pfam03476 |
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The ... |
584-701 |
6.52e-30 |
|
MOSC N-terminal beta barrel domain; This domain is found to the N-terminus of pfam03473. The function of this domain is unknown, however it is predicted to adopt a beta barrel fold.
Pssm-ID: 281474 Cd Length: 118 Bit Score: 114.76 E-value: 6.52e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 584 VTNLYLYPIKSCAAFEVTRWPVGNQGLLYDRSWMVVNHNGVCLSQKQEPRLCLIQPFIDLRQrIMVIKAKGMEPIEVPLE 663
Cdd:pfam03476 4 VSSLYVYPIKSCRGESLSRAELTAAGLAWDRRFMVVDSDGKFVTARREPRLVLIRTTLDEDG-GLTLTAPGMPDLSVPLA 82
|
90 100 110
....*....|....*....|....*....|....*...
gi 1519315834 664 ENSerTQIRQSRVCADRVSTYDCGEKISSWLSTFFGRP 701
Cdd:pfam03476 83 DNK--FDLRGVLVWGLSFSGRDCGDAAADWFSDFLGKP 118
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
50-481 |
1.56e-27 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 115.42 E-value: 1.56e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAGATLFSQSQLESfTSDLMENTYGNPHS-QNISSKLTHDTVEQVRYRIlAHFHTTAEDYTVIFTAGSTAALKLVA 128
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDA-IQEYYTDYNGNVHRgVHTLGKEATQAYEEAREKV-AEFINAPSNDEIIFTSGTTEAINLVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 129 EAFPWvSQGPessGSRFCYLTDSHTSV-VGMRNVTMAINVISTPVRPEDLWS-AEERSASASNPDCQLphlFCYPAQSNF 206
Cdd:pfam00266 79 LSLGR-SLKP---GDEIVITEMEHHANlVPWQELAKRTGARVRVLPLDEDGLlDLDELEKLITPKTKL---VAITHVSNV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 207 SGVRYPlswIEEVKSgRLHPVstpgKWFVLLDAASYVSTSPLDLSAHQADFVPISFYKIFGfPTGLGALLVHNRAAPLLR 286
Cdd:pfam00266 152 TGTIQP---VPEIGK-LAHQY----GALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYG-PTGIGVLYGRRDLLEKMP 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 287 KTYFGGGT-ASAYLAGEDFYIPrqsvAQRFEDGTISFLDVIALKHGFDTLERLtgGMENIKQHTFTLAQYTYVALSSLqy 365
Cdd:pfam00266 223 PLLGGGGMiETVSLQESTFADA----PWKFEAGTPNIAGIIGLGAALEYLSEI--GLEAIEKHEHELAQYLYERLLSL-- 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 366 pngaPVVRIYsdsefsSPEVQGPIINFNVlddkgniIGYSQVDKMASL--YNIHLRTGCFCnTGACQRHLGIsnemvrkh 443
Cdd:pfam00266 295 ----PGIRLY------GPERRASIISFNF-------KGVHPHDVATLLdeSGIAVRSGHHC-AQPLMVRLGL-------- 348
|
410 420 430
....*....|....*....|....*....|....*...
gi 1519315834 444 fqaghvcgdnmdlidgqpTGSVRISFGYMSTLDDVQAF 481
Cdd:pfam00266 349 ------------------GGTVRASFYIYNTQEDVDRL 368
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
50-482 |
2.26e-21 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 97.15 E-value: 2.26e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAGATLFSQSQLESfTSDLMENTYGNPH--SQNISSKLThDTVEQVRYRIlAHFHTTAEDYTVIFTAGSTAALKLV 127
Cdd:cd06453 1 VYLDNAATSQKPQPVIDA-IVDYYRHYNANVHrgVHELSARAT-DAYEAAREKV-ARFINAPSPDEIIFTRNTTEAINLV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 128 AEAFPWvSQGPessGSRFcyLTDS--HTSVVgmrnvtmainvistpvRPedlWS--AEERSAS----ASNPDCQLP---- 195
Cdd:cd06453 78 AYGLGR-ANKP---GDEI--VTSVmeHHSNI----------------VP---WQqlAERTGAKlkvvPVDDDGQLDleal 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 196 --------------HLfcypaqSNFSGVRYPlswIEEVksGRL-HPVSTPgkwfVLLDAASYVSTSPLDLSAHQADFVPI 260
Cdd:cd06453 133 eklltertklvavtHV------SNVLGTINP---VKEI--GEIaHEAGVP----VLVDGAQSAGHMPVDVQDLGCDFLAF 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 261 SFYKIFGfPTGLGALLVhnrAAPLLRKT--YFGGGTASAYLAGEDfYIPRQsVAQRFEDGTISFLDVIALKHGFDTLERL 338
Cdd:cd06453 198 SGHKMLG-PTGIGVLYG---KEELLEEMppYGGGGEMIEEVSFEE-TTYAD-LPHKFEAGTPNIAGAIGLGAAIDYLEKI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 339 tgGMENIKQHTFTLAQYTYVALSSLqypngaPVVRIYSDsefssPEVQGPIINFNVLDDKGNIIGYsqvdkmaslyniHL 418
Cdd:cd06453 272 --GMEAIAAHEHELTAYALERLSEI------PGVRVYGD-----AEDRAGVVSFNLEGIHPHDVAT------------IL 326
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519315834 419 RTgcfcntgacqrhLGIsneMVRkhfqAGHVCGdnMDLIDG-QPTGSVRISFGYMSTLDDVQAFL 482
Cdd:cd06453 327 DQ------------YGI---AVR----AGHHCA--QPLMRRlGVPGTVRASFGLYNTEEEIDALV 370
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
50-488 |
3.11e-12 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 69.39 E-value: 3.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAgATlfsqSQLESFTSDLMENTY----GNPHS--QNISSKLThDTVEQVRYRIlAHFHTTAEDYTVIFTAGSTAA 123
Cdd:PLN02855 34 VYLDNA-AT----SQKPAAVLDALQDYYeeynSNVHRgiHALSAKAT-DAYELARKKV-AAFINASTSREIVFTRNATEA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 124 LKLVAeaFPW----VSQGPESSGSrfcyLTDSHTSVVGMRNVTMAINVISTPVR--PEDLWSAEERSASASnPDCQLPHL 197
Cdd:PLN02855 107 INLVA--YTWglanLKPGDEVILS----VAEHHSNIVPWQLVAQKTGAVLKFVGltPDEVLDVEQLKELLS-EKTKLVAT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 198 FcypAQSNFSGVRYPLSWIEEVKsgrlHPVSTPgkwfVLLDAASYVSTSPLDLSAHQADFVPISFYKIFGfPTGLGALlv 277
Cdd:PLN02855 180 H---HVSNVLGSILPVEDIVHWA----HAVGAK----VLVDACQSVPHMPVDVQTLGADFLVASSHKMCG-PTGIGFL-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 278 HNRAAPLLRKTYFGGGtasaylaGE---DFYIPRQSVAQ---RFEDGTISFLDVIALKHGFDTLERLtgGMENIKQHTFT 351
Cdd:PLN02855 246 WGKSDLLESMPPFLGG-------GEmisDVFLDHSTYAPppsRFEAGTPAIGEAIGLGAAIDYLSEI--GMDRIHEYEVE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 352 LAQYTYVALSSLqypngaPVVRIYSDSEfSSPEVQGPIINFNVLddkgniiGYSQVDKMASL---YNIHLRTGCFCnTGA 428
Cdd:PLN02855 317 LGTYLYEKLSSV------PGVRIYGPKP-SEGVGRAALCAFNVE-------GIHPTDLSTFLdqqHGVAIRSGHHC-AQP 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 429 CQRHLGISnemvrkhfqaghvcgdnmdlidgqptGSVRISFGYMSTLDDVQAFLRFIIDT 488
Cdd:PLN02855 382 LHRYLGVN--------------------------ASARASLYFYNTKEEVDAFIHALKDT 415
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
41-480 |
2.42e-09 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 60.44 E-value: 2.42e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 41 REFSRLA-GTVYLDHAGATLFSQSQLESfTSDLMENTYGNPH-SQNISSKLTHDTVEQVRYRIlAHFHTTAEDYTVIFTA 118
Cdd:PRK10874 11 AQFPALQdAGVYLDSAATALKPQAVIEA-TQQFYSLSAGNVHrSQFAAAQRLTARYEAAREQV-AQLLNAPDAKNIVWTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 119 GSTAALKLVAEAF--PWVSQGPESSGSRfcylTDSHTSVVGMRNV---TMAiNVISTPVRPEDLwsaeersasasnPDC- 192
Cdd:PRK10874 89 GTTESINLVAQSYarPRLQPGDEIIVSE----AEHHANLVPWLMVaqqTGA-KVVKLPLGADRL------------PDVd 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 193 QLPHLFCYPAQ-------SNFSGVRYPLSWIEEV--KSGRLhpvstpgkwfVLLDAASYVSTSPLDLSAHQADFVPISFY 263
Cdd:PRK10874 152 LLPELITPRTRilalgqmSNVTGGCPDLARAITLahQAGMV----------VMVDGAQGAVHFPADVQALDIDFYAFSGH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 264 KIFGfPTGLGALlvHNRAApLLRKT--YFGGGTASAYLAGEDFyIPrQSVAQRFEDGTISFLDVIALKHGFDTLERLTgg 341
Cdd:PRK10874 222 KLYG-PTGIGVL--YGKSE-LLEAMspWQGGGKMLTEVSFDGF-TP-QSAPWRFEAGTPNVAGVIGLSAALEWLADID-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 342 MENIKQHTFTLAQYTYVALSSLqyPNgapvvriysdseFSSPEVQG-PIINFNVLDdkgniIGYSQVDKMASLYNIHLRT 420
Cdd:PRK10874 294 INQAESWSRSLATLAEDALAKL--PG------------FRSFRCQDsSLLAFDFAG-----VHHSDLVTLLAEYGIALRA 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 421 GCFCNTGACQRhLGISnemvrkhfqaghvcgdnmdlidgqptGSVRISFGYMSTLDDVQA 480
Cdd:PRK10874 355 GQHCAQPLLAA-LGVT--------------------------GTLRASFAPYNTQSDVDA 387
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
50-301 |
3.47e-06 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 50.04 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAGATLFSQSQLESFTSDLMENtYGNPHSQnissklTH-------DTVEQVRYRILAHFHTTAEDytVIFTAGSTA 122
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEH-FGNPHSR------THlygweseDAVEKARAQVAALIGADPKE--IIFTSGATE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 123 ----ALKLVAEAFP-----WVSQGPESSgsrfCYLTDSHTSVVGMRNVTMainvisTPVRPEDLWSAEErSASASNPDCQ 193
Cdd:PLN02651 72 snnlAIKGVMHFYKdkkkhVITTQTEHK----CVLDSCRHLQQEGFEVTY------LPVKSDGLVDLDE-LAAAIRPDTA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 194 LPHLFcypAQSNFSGVRYPLSWIEEVKSGRLHPVSTpgkwfvllDAASYVSTSPLDLSAHQADFVPISFYKIFGfPTGLG 273
Cdd:PLN02651 141 LVSVM---AVNNEIGVIQPVEEIGELCREKKVLFHT--------DAAQAVGKIPVDVDDLGVDLMSISGHKIYG-PKGVG 208
|
250 260
....*....|....*....|....*...
gi 1519315834 274 ALLVHNRAAPLLRKTYFGGGTASAYLAG 301
Cdd:PLN02651 209 ALYVRRRPRVRLEPLMSGGGQERGRRSG 236
|
|
| MOSC |
pfam03473 |
MOSC domain; The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich ... |
730-847 |
5.64e-06 |
|
MOSC domain; The MOSC (MOCO sulfurase C-terminal) domain is a superfamily of beta-strand-rich domains identified in the molybdenum cofactor sulfurase and several other proteins from both prokaryotes and eukaryotes. These MOSC domains contain an absolutely conserved cysteine and occur either as stand-alone forms such as Swiss:P32157, or fused to other domains such as NifS-like catalytic domain in Molybdenum cofactor sulfurase. The MOSC domain is predicted to be a sulfur-carrier domain that receives sulfur abstracted by the pyridoxal phosphate-dependent NifS-like enzymes, on its conserved cysteine, and delivers it for the formation of diverse sulfur-metal clusters.
Pssm-ID: 460936 Cd Length: 116 Bit Score: 46.03 E-value: 5.64e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 730 TLSLVNEAQYLLINTSSILELHRQLNTSD-ENGkeelfslkdlslRFRANIIINGkrafeeEKWDEISIGSlRFQVLGPC 808
Cdd:pfam03473 3 KHHGGDDKAVLLYSRESYDAWNAELGRGPlDPG------------RFRENLVVSG------GTWKEVCIGD-RFRIGGAC 63
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1519315834 809 HRCQMICiDQQTGQRNQHVFQ--KLSESRETKVNFGMYLMH 847
Cdd:pfam03473 64 LRLEVTQ-PREPCKTLAKRFGerRVDKRFKGSGRFGWYLRV 103
|
|
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
50-132 |
8.57e-05 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 45.81 E-value: 8.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 50 VYLDHAGATLFSQSQLESFTsDLMENTYGNPHSQNISSKLTHDTVEQVRYRILAHFHTTAEDytVIFTAGST----AALK 125
Cdd:COG1104 4 IYLDNAATTPVDPEVLEAML-PYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEE--IIFTSGGTeannLAIK 80
|
....*..
gi 1519315834 126 LVAEAFP 132
Cdd:COG1104 81 GAARAYR 87
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
235-355 |
2.44e-04 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 44.84 E-value: 2.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519315834 235 VLLDAASYVSTSPLDLSAHQADFVPISFYKIFGfPTGLGAllVHNRAApLLRKT--YFGGG------TasaylagedFyi 306
Cdd:NF041166 419 VLVDGAQSVSHMPVDVQALDADFFVFSGHKVFG-PTGIGV--VYGKRD-LLEAMppWQGGGnmiadvT---------F-- 483
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1519315834 307 pRQSVAQ----RFEDGTISFLDVIALKHGFDTLERLtgGMENIKQHTFTLAQY 355
Cdd:NF041166 484 -EKTVYQpapnRFEAGTGNIADAVGLGAALDYVERI--GIENIARYEHDLLEY 533
|
|
| |
