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Conserved domains on  [gi|19526986|ref|NP_598529|]
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argininosuccinate lyase [Mus musculus]

Protein Classification

argininosuccinate lyase( domain architecture ID 10102141)

argininosuccinate lyase catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-459 0e+00

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


:

Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 681.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  27 SISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPNDEDIHTANERRLKELIGEAAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 107 LHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 187 LLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTK 266
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 267 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMIAVLQVA 346
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 347 TGVISTLQIHRENMKQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNLLSLQELQTISPLFSGDV 424
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 19526986 425 SHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALL 459
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-459 0e+00

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 681.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  27 SISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPNDEDIHTANERRLKELIGEAAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 107 LHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 187 LLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTK 266
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 267 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMIAVLQVA 346
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 347 TGVISTLQIHRENMKQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNLLSLQELQTISPLFSGDV 424
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 19526986 425 SHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALL 459
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
PLN02646 PLN02646
argininosuccinate lyase
 1-463 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 677.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    1 MASESGKLWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFK 80
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   81 LHPNDEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTH 160
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  161 LQRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA 240
Cdd:PLN02646 171 LQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  241 EFLFWASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST 320
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  321 YNKDLQEDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAE 399
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19526986  400 TKGVALNLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALLQAQE 463
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 5-463 0e+00

Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439935 [Multi-domain]  Cd Length: 462  Bit Score: 676.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   5 SGKLWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPN 84
Cdd:COG0165   2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  85 DEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:COG0165  82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 165 QPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 244
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 245 WASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 324
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 325 LQEDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 403
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 404 ALNLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALLQAQE 463
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALR 461
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 8-459 0e+00

argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129918 [Multi-domain]  Cd Length: 455  Bit Score: 597.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986     8 LWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPNDED 87
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    88 IHTANERRLKELIGE-AAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:TIGR00838  81 IHMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   167 IRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   247 SLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   327 EDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19526986   406 NLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALL 459
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
Lyase_1 pfam00206
Lyase;
11-305 1.63e-131

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 382.49  E-value: 1.63e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    11 GRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQG-TFKLHPNDEDIH 89
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    90 TANERRLKELIGE-------AAGKLHTGRSRNDQVVTDLRLWMRQTCS-KLSALLRVLIGTMVDRAEAERDVLFPGYTHL 161
Cdd:pfam00206  81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALSeVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   162 QRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRE---LLRAELNF----GAITLNSMDATS 234
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19526986   235 ERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYST-GSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
 
Name Accession Description Interval E-value
Argininosuccinate_lyase cd01359
Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related ...
 27-459 0e+00

Argininosuccinate lyase (argininosuccinase, ASAL); This group contains ASAL and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASAL is a cytosolic enzyme which catalyzes the reversible breakdown of argininosuccinate to arginine and fumarate during arginine biosynthesis. In ureotelic species ASAL also catalyzes a reaction involved in the production of urea. Included in this group are the major soluble avian eye lens proteins from duck, delta 1 and delta 2 crystallin. Of these two isoforms only delta 2 has retained ASAL activity. These crystallins may have evolved by, gene recruitment of ASAL followed by gene duplication. In humans, mutations in ASAL result in the autosomal recessive disorder argininosuccinic aciduria.


Pssm-ID: 176463 [Multi-domain]  Cd Length: 435  Bit Score: 681.19  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  27 SISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPNDEDIHTANERRLKELIGEAAGK 106
Cdd:cd01359   1 SISFDRRLFEEDIAGSIAHAVMLAEQGILTEEEAAKILAGLAKIRAEIEAGAFELDPEDEDIHMAIERRLIERIGDVGGK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 107 LHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSER 186
Cdd:cd01359  81 LHTGRSRNDQVATDLRLYLRDALLELLELLLDLQRALLDRAEEHADTIMPGYTHLQRAQPITFGHYLLAYAEMLERDLER 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 187 LLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTK 266
Cdd:cd01359 161 LADAYKRVNVSPLGAGALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFVLEFLSAAALLMVHLSRLAEDLILWSTQ 240

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 267 EFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMIAVLQVA 346
Cdd:cd01359 241 EFGFVELPDAYSTGSSIMPQKKNPDVLELIRGKAGRVIGALAGLLTTLKGLPLAYNKDLQEDKEPLFDAVDTLIASLRLL 320

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 347 TGVISTLQIHRENMKQAL-SPDMLATDLAYYLVR-KGMPFRQAHEASGKAVFMAETKGVALNLLSLQELQTISPLFSGDV 424
Cdd:cd01359 321 TGVISTLTVNPERMREAAeAGFSTATDLADYLVReKGVPFREAHHIVGRAVRLAEEKGKDLSDLTLAELQAISPLFEEDV 400

                       410       420       430
                ....*....|....*....|....*....|....*
gi 19526986 425 SHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALL 459
Cdd:cd01359 401 REALDPENSVERRTSYGGTAPAEVREQIARARALL 435
PLN02646 PLN02646
argininosuccinate lyase
 1-463 0e+00

argininosuccinate lyase


Pssm-ID: 215348 [Multi-domain]  Cd Length: 474  Bit Score: 677.98  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    1 MASESGKLWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFK 80
Cdd:PLN02646  11 EAAKEKKLWGGRFEEGVTPAVEKFNESISFDKRLYKEDIMGSKAHASMLAKQGIITDEDRDSILDGLDEIEKEIEAGKFE 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   81 LHPNDEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTH 160
Cdd:PLN02646  91 WRPDREDVHMNNEARLTELIGEPAKKLHTARSRNDQVATDTRLWCRDAIDVIRKRIKTLQVALVELAEKNVDLVVPGYTH 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  161 LQRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVA 240
Cdd:PLN02646 171 LQRAQPVLLSHWLLSHVEQLERDAGRLVDCRPRVNFCPLGSCALAGTGLPIDRFMTAKDLGFTAPMRNSIDAVSDRDFVL 250

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  241 EFLFWASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPST 320
Cdd:PLN02646 251 EFLFANSITAIHLSRLGEEWVLWASEEFGFVTPSDAVSTGSSIMPQKKNPDPMELVRGKSARVIGDLVTVLALCKGLPTA 330

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  321 YNKDLQEDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAE 399
Cdd:PLN02646 331 YNRDLQEDKEPLFDSVDTVSDMLEVATEFAQNITFNPERIKKSLPAGMLdATTLADYLVRKGVPFRETHHIVGAAVALAE 410

                        410       420       430       440       450       460
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19526986  400 TKGVALNLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALLQAQE 463
Cdd:PLN02646 411 SKGCELSDLTLEDLKSINPVFEEDVYEVLGVENSVEKFDSYGSTGSRSVLEQLEKWRTKLEITS 474
ArgH COG0165
Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part ...
 5-463 0e+00

Argininosuccinate lyase [Amino acid transport and metabolism]; Argininosuccinate lyase is part of the Pathway/BioSystem: Arginine biosynthesis


Pssm-ID: 439935 [Multi-domain]  Cd Length: 462  Bit Score: 676.82  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   5 SGKLWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPN 84
Cdd:COG0165   2 SMKLWGGRFSEGPDELVEEFNASISFDKRLAPYDIAGSIAHARMLAEQGIISAEEAAAILAGLDEIEAEIEAGAFEFDPE 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  85 DEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:COG0165  82 LEDIHMNIERRLIERIGDVGGKLHTGRSRNDQVATDFRLYLRDEILELIEALLALQEALLDLAEEHADTIMPGYTHLQRA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 165 QPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 244
Cdd:COG0165 162 QPVTFGHHLLAYAEMLLRDRERLADAYKRLNVSPLGAAALAGTTFPIDRERTAELLGFDGPTENSLDAVSDRDFALEFLS 241

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 245 WASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 324
Cdd:COG0165 242 AASLIMVHLSRLAEELILWSSSEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVIGNLTGLLTTMKGLPLAYNKD 321

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 325 LQEDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 403
Cdd:COG0165 322 LQEDKEPLFDAVDTLKLCLRLFAGMIATLKVNRERMREAAGAGfSTATDLADYLVRKGVPFREAHEIVGRLVRYAEEKGK 401

                       410       420       430       440       450       460
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 404 ALNLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALLQAQE 463
Cdd:COG0165 402 DLEDLTLEELQAFSPLIEEDVYEALDPEGSVAARDSYGGTAPEAVREQIARARARLAALR 461
PRK00855 PRK00855
argininosuccinate lyase; Provisional
 5-460 0e+00

argininosuccinate lyase; Provisional


Pssm-ID: 179143 [Multi-domain]  Cd Length: 459  Bit Score: 652.60  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    5 SGKLWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPN 84
Cdd:PRK00855   3 SNKLWGGRFSEGPDELVERFTASISFDKRLAEEDIAGSIAHARMLAKQGILSEEEAEKILAGLDEILEEIEAGKFEFSPE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   85 DEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRA 164
Cdd:PRK00855  83 LEDIHMAIEARLTERIGDVGGKLHTGRSRNDQVATDLRLYLRDEIDEIAELLLELQKALLDLAEEHADTIMPGYTHLQRA 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  165 QPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLF 244
Cdd:PRK00855 163 QPVTFGHHLLAYAEMLARDLERLRDARKRVNRSPLGSAALAGTTFPIDRERTAELLGFDGVTENSLDAVSDRDFALEFLS 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  245 WASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKD 324
Cdd:PRK00855 243 AASLLMVHLSRLAEELILWSSQEFGFVELPDAFSTGSSIMPQKKNPDVAELIRGKTGRVYGNLTGLLTVMKGLPLAYNRD 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  325 LQEDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPDM-LATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGV 403
Cdd:PRK00855 323 LQEDKEPLFDAVDTLKLSLEAMAGMLETLTVNKERMREAAGKGFsTATDLADYLVRKGVPFREAHEIVGKAVREAEERGV 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19526986  404 ALNLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALLQ 460
Cdd:PRK00855 403 DLADLSLEELQAFSPLITEDVYEVLTPEGSVAARNSIGGTAPEQVREQIARAKARLA 459
argH TIGR00838
argininosuccinate lyase; This model describes argininosuccinate lyase, but may include ...
 8-459 0e+00

argininosuccinate lyase; This model describes argininosuccinate lyase, but may include examples of avian delta crystallins, in which argininosuccinate lyase activity may or may not be present and the biological role is to provide the optically clear cellular protein of the eye lens. [Amino acid biosynthesis, Glutamate family]


Pssm-ID: 129918 [Multi-domain]  Cd Length: 455  Bit Score: 597.80  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986     8 LWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPNDED 87
Cdd:TIGR00838   1 LWGGRFTGGMDPRVAKFNASLSFDKELAEYDIEGSIAHTKMLKKAGILTEEEAAKIIEGLNELKEEGREGPFILDPDDED 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    88 IHTANERRLKELIGE-AAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:TIGR00838  81 IHMAIERELIDRVGEdLGGKLHTGRSRNDQVATDLRLYLRDHVLELAEALLDLQDALIELAEKHVETLMPGYTHLQRAQP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   167 IRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:TIGR00838 161 ITLAHHLLAYAEMLLRDYERLQDALKRVNVSPLGSGALAGTGFPIDREYLAELLGFDAVTENSLDAVSDRDFILELLFVA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   247 SLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:TIGR00838 241 ALIMVHLSRFAEDLILWSTGEFGFVELPDEFSSGSSIMPQKKNPDVAELIRGKTGRVQGNLTGMLMTLKALPLAYNRDLQ 320

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   327 EDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPD-MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:TIGR00838 321 EDKEPLFDALKTVELSLEMATGMLDTITVNKERMEEAASAGfSNATELADYLVRKGVPFREAHHIVGELVATAIERGKGL 400

                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19526986   406 NLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALL 459
Cdd:TIGR00838 401 EELTLEELQKFSPEFDEDVYEALDPESSVEKRDAKGGTAPEEVLQAIAEAKARL 454
PRK04833 PRK04833
argininosuccinate lyase; Provisional
 8-448 2.06e-170

argininosuccinate lyase; Provisional


Pssm-ID: 179883 [Multi-domain]  Cd Length: 455  Bit Score: 486.80  E-value: 2.06e-170
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    8 LWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFK-LHPNDE 86
Cdd:PRK04833   3 LWGGRFTQAADQRFKQFNDSLRFDYRLAEQDIVGSVAWSKALVTVGVLTADEQQQLEEALNELLEEVRANPQQiLASDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   87 DIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:PRK04833  83 DIHSWVEGKLIDKVGDLGKKLHTGRSRNDQVATDLKLWCKDQVAELLTALRQLQSALVETAENNQDAVMPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  167 IRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:PRK04833 163 VTFAHWCLAYVEMLARDESRLQDALKRLDVSPLGSGALAGTAYEIDREQLAGWLGFASATRNSLDSVSDRDHVLELLSDA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  247 SLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:PRK04833 243 SISMVHLSRFAEDLIFFNSGEAGFVELSDRVTSGSSLMPQKKNPDALELIRGKCGRVQGALTGMLMTLKGLPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  327 EDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:PRK04833 323 EDKEGLFDALDTWLDCLHMAALVLDGIQVKRPRCQEAAQQGYAnATELADYLVAKGVPFREAHHIVGEAVVEAIRQGKPL 402

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|...
gi 19526986  406 NLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSV 448
Cdd:PRK04833 403 EDLPLAELQKFSSVIGDDVYPILSLQSCLDKRAAKGGVSPQQV 445
PRK12308 PRK12308
argininosuccinate lyase;
8-463 3.18e-151

argininosuccinate lyase;


Pssm-ID: 183425 [Multi-domain]  Cd Length: 614  Bit Score: 443.84  E-value: 3.18e-151
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    8 LWGGRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEE-WAQGTFKLHPNDE 86
Cdd:PRK12308   3 LWGGRFSQAADTRFKQFNDSLRFDYRLAEQDIVGSIAWSKALLSVGVLSEEEQQKLELALNELKLEvMEDPEQILLSDAE 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   87 DIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:PRK12308  83 DIHSWVEQQLIGKVGDLGKKLHTGRSRNDQVATDLKLWCRQQGQQLLLALDQLQQQMVNVAERHQGTVLPGYTHLQRAQP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  167 IRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWA 246
Cdd:PRK12308 163 VTFAHWCLAYVEMFERDYSRLEDALTRLDTCPLGSGALAGTAYPIDREALAHNLGFRRATRNSLDSVSDRDHVMELMSVA 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  247 SLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQ 326
Cdd:PRK12308 243 SISMLHLSRLAEDLIFYNSGESGFIELADTVTSGSSLMPQKKNPDALELIRGKTGRVYGALAGMMMTVKALPLAYNKDMQ 322

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  327 EDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALSPDML-ATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVAL 405
Cdd:PRK12308 323 EDKEGLFDALDTWNDCMEMAALCFDGIKVNGERTLEAAKQGYAnATELADYLVAKGIPFREAHHIVGVAVVGAIAKGCAL 402

                        410       420       430       440       450
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 19526986  406 NLLSLQELQTISPLFSGDVSHVWDYSHSVEQYSALGGTAKSSVEWQIRQVRALLQAQE 463
Cdd:PRK12308 403 EELSLEQLKEFSDVIEDDVYQILTIESCLEKRCALGGVSPEQVAYAVEQADKRLAARD 460
Lyase_I cd01334
Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; ...
 38-356 1.69e-133

Lyase class I family; a group of proteins which catalyze similar beta-elimination reactions; The Lyase class I family contains class II fumarase, aspartase, adenylosuccinate lyase (ASL), argininosuccinate lyase (ASAL), prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. It belongs to the Lyase_I superfamily. Proteins of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits.


Pssm-ID: 176461 [Multi-domain]  Cd Length: 325  Bit Score: 388.01  E-value: 1.69e-133
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  38 DVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQGTFKLHPNDEDIHTANERRLKELIGEA-AGKLHTGRSRNDQ 116
Cdd:cd01334   4 DLQVEKAHAKALAELGLLPKEAAEAILAALDEILEGIAADQVEQEGSGTHDVMAVEEVLAERAGELnGGYVHTGRSSNDI 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 117 VVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVQKRINV 196
Cdd:cd01334  84 VDTALRLALRDALDILLPALKALIDALAAKAEEHKDTVMPGRTHLQDAQPTTLGHELAAWAAELERDLERLEEALKRLNV 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 197 LPLGSGAIAGNPLGV--DRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFSFVQLS 274
Cdd:cd01334 164 LPLGGGAVGTGANAPpiDRERVAELLGFFGPAPNSTQAVSDRDFLVELLSALALLAVSLSKIANDLRLLSSGEFGEVELP 243

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 275 DAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEAVFEVSDTMIAVLQVATGVISTLQ 354
Cdd:cd01334 244 DAKQPGSSIMPQKVNPVILELVRGLAGRVIGNLAALLEALKGGPLEDNVDSPVEREALPDSFDLLDAALRLLTGVLEGLE 323


                ..
gi 19526986 355 IH 356
Cdd:cd01334 324 VN 325
Lyase_1 pfam00206
Lyase;
11-305 1.63e-131

Lyase;


Pssm-ID: 425524 [Multi-domain]  Cd Length: 312  Bit Score: 382.49  E-value: 1.63e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    11 GRFVGAVDPIMEKFNSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEEWAQG-TFKLHPNDEDIH 89
Cdd:pfam00206   1 GRFTVPADALMGIFTDRSRFNFRLGEEDIKGLAALKKAAAKANVILKEEAAAIIKALDEVAEEGKLDdQFPLKVWQEGSG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    90 TANERRLKELIGE-------AAGKLHTGRSRNDQVVTDLRLWMRQTCS-KLSALLRVLIGTMVDRAEAERDVLFPGYTHL 161
Cdd:pfam00206  81 TAVNMNLNEVIGEllgqlvhPNDHVHTGQSSNDQVPTALRLALKDALSeVLLPALRQLIDALKEKAKEFADIVKPGRTHL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   162 QRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRE---LLRAELNF----GAITLNSMDATS 234
Cdd:pfam00206 161 QDATPVTLGQELSGYAVALTRDRERLQQLLPRLLVLPLGGGTAVGTGLNADPEfaeLVAKELGFftglPVKAPNSFEATS 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19526986   235 ERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYST-GSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:pfam00206 241 DRDAVVELSGALALLATSLSKFAEDLRLLSSGPAGLVELSLAEGEpGSSIMPGKVNPDQLELLTGKAGRVMG 312
Lyase_I_like cd01594
Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and ...
 93-347 2.56e-59

Lyase class I_like superfamily: contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase, which catalyze similar beta-elimination reactions; Lyase class I_like superfamily of enzymes that catalyze beta-elimination reactions and are active as homotetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. This superfamily contains the lyase class I family, histidine ammonia-lyase and phenylalanine ammonia-lyase. The lyase class I family comprises proteins similar to class II fumarase, aspartase, adenylosuccinate lyase, argininosuccinate lyase, and 3-carboxy-cis, cis-muconate lactonizing enzyme which, for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. Histidine or phenylalanine ammonia-lyase catalyze a beta-elimination of ammonia from histidine and phenylalanine, respectively.


Pssm-ID: 176466 [Multi-domain]  Cd Length: 231  Bit Score: 194.36  E-value: 2.56e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  93 ERRLKELIGEAAGKLH------TGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQP 166
Cdd:cd01594  17 EEVLAGRAGELAGGLHgsalvhKGRSSNDIGTTALRLALRDALDDLLPLLKALIDALALKAEAHKGTVMPGRTHLQDAQP 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 167 IRWSHWILSHAVALTRDSERLLEVqkrinvlplgsgaiagnplgvdrellraelnfgaitlnsmdatserdFVAEFLFWA 246
Cdd:cd01594  97 VTLGYELRAWAQVLGRDLERLEEA-----------------------------------------------AVAEALDAL 129

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 247 SLCMTHLSRMAEDLILYGTKEFSFVQLSDA-YSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDL 325
Cdd:cd01594 130 ALAAAHLSKIAEDLRLLLSGEFGELGEPFLpGQPGSSIMPQKVNPVAAELVRGLAGLVIGNLVAVLTALKGGPERDNEDS 209

                       250       260
                ....*....|....*....|..
gi 19526986 326 QEDKEAVFEVSDTMIAVLQVAT 347
Cdd:cd01594 210 PSMREILADSLLLLIDALRLLL 231
PRK02186 PRK02186
argininosuccinate lyase; Provisional
 49-463 4.10e-52

argininosuccinate lyase; Provisional


Pssm-ID: 235010 [Multi-domain]  Cd Length: 887  Bit Score: 188.52  E-value: 4.10e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   49 LEKAGLLTKAEMQQILQGLDKVAEEWAQgTFKLHPNDEDIHTANERRLKELIGE-AAGKLHTGRSRNDQVVTDLRLWMRQ 127
Cdd:PRK02186 452 LGDTGIVAPERARPLLDAHRRLRDAGFA-PLLARPAPRGLYMLYEAYLIERLGEdVGGVLQTARSRNDINATTTKLHLRE 530

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  128 TCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGN 207
Cdd:PRK02186 531 ATSRAFDALWRLRRALVFKASANVDCALPIYSQYQPALPGSLGHYLLAVDGALARETHALFALFEHIDVCPLGAGAGGGT 610

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  208 PLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTGSSLMPQK 287
Cdd:PRK02186 611 TFPIDPEFVARLLGFEQPAPNSLDAVASRDGVLHFLSAMAAISTVLSRLAQDLQLWTTREFALVSLPDALTGGSSMLPQK 690

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  288 KNPDSLELIRSKAGRVFGRCAGLLMTLKGLPstYNKDLQEDKEAVFEVSDTMIAV---LQVATGVISTLQIHRENMKQAL 364
Cdd:PRK02186 691 KNPFLLEFVKGRAGVVAGALASASAALGKTP--FSNSFEAGSPMNGPIAQACAAIedaAAVLVLLIDGLEADQARMRAHL 768

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  365 -SPDMLATDLAYYLV-RKGMPFRQAHEASGKAVFMAETKGVAlnllSLQELQTISPLFSGDVSHVWDYSHsveQYSalGG 442
Cdd:PRK02186 769 eDGGVSATAVAESLVvRRSISFRSAHTQVGQAIRQSLDQGRS----SADALAALDPQFVSRAPLEWARSH---RFG--GG 839

                        410       420
                 ....*....|....*....|.
gi 19526986  443 TAKSSVEWQIRQVRALLQAQE 463
Cdd:PRK02186 840 PGAADLNAGLARACAALRDDE 860
PRK06705 PRK06705
argininosuccinate lyase; Provisional
 40-463 6.37e-42

argininosuccinate lyase; Provisional


Pssm-ID: 180664 [Multi-domain]  Cd Length: 502  Bit Score: 155.53  E-value: 6.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   40 QGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAEewaqgtfklHPNDEDIHTANERRL----KELIGEAA-----GKLHTG 110
Cdd:PRK06705  43 QVHKAHIVMLTEENLMKKEEAKFILHALKKVEE---------IPEEQLLYTEQHEDLfflvEHLISQEAksdfvSNMHIG 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  111 RSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEV 190
Cdd:PRK06705 114 RSRNDMGVTMYRMSLRRYVLRLMEHHLLLQESILQLAADHKETIMPAYTHTQPAQPTTFGHYTLAIYDTMQRDLERMKKT 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  191 QKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLILYGTKEFSF 270
Cdd:PRK06705 194 YKLLNQSPMGAAALSTTSFPIKRERVADLLGFTNVIENSYDAVAGADYLLEVSSLLMVMMTNTSRWIHDFLLLATKEYDG 273

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  271 VQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLKGLPSTYNKDLQEDKEA-VFEVSDTMIAVLQVATGV 349
Cdd:PRK06705 274 ITVARPYVQISSIMPQKRNPVSIEHARAITSSALGEAFTVFQMIHNTPFGDIVDTEDDLQPyLYKGIEKAIRVFCIMNAV 353

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  350 ISTLQIHRENMK-QALSPDMLATDLAYYLVRK-GMPFRQAHEASGKAVFMAETKGVALNLLSLQELQT-ISPLFSGDVSH 426
Cdd:PRK06705 354 IRTMKVEEDTLKrRSYKHAITITDFADVLTKNyGIPFRHAHHAASVIANMSLEQKKELHELCFKDVNIyLQEKFKIQLLE 433

                        410       420       430       440
                 ....*....|....*....|....*....|....*....|..
gi 19526986  427 V-WDYSHSVEQY----SALGGTAKSSVEWQIRQVRALLQAQE 463
Cdd:PRK06705 434 KeWEEIISPEAFiqkrNVYGGPSKKEMERMINNRKELFRKEE 475
PRK06389 PRK06389
argininosuccinate lyase; Provisional
 7-395 5.12e-36

argininosuccinate lyase; Provisional


Pssm-ID: 235791 [Multi-domain]  Cd Length: 434  Bit Score: 138.10  E-value: 5.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986    7 KLWGGrfvGAVDPIMEKF-----NSSISYDRHLWNVDVQGSKAYSRGLEKAGLLTKAEMQQILQGLDKVAeewaQGTFKL 81
Cdd:PRK06389   2 KIWSG---GAGEELENDFydnivKDDIDADKNLIKYEIINLLAYHVALAQRRLITEKAPKCVINALIDIY----KNGIEI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   82 HPNDEDIHTANERRLKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALL----RVLIGtmvdraeAERDVLFPG 157
Cdd:PRK06389  75 DLDLEDVHTAIENFVIRRCGDMFKNFRLFLSRNEQVHADLNLFIIDKIIEIEKILyeiiKVIPG-------FNLKGRLPG 147

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  158 YTHLQRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELNFGAITLNSMDATSERD 237
Cdd:PRK06389 148 YTHFRQAMPMTVNTYINYIKSILYHHINNLDSFLMDLREMPYGYGSGYGSPSSVKFNQMSELLGMEKNIKNPVYSSSLYI 227

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  238 FVAEFLFW--ASLCMThLSRMAEDLILYgtKEFSFVQLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLK 315
Cdd:PRK06389 228 KTIENISYliSSLAVD-LSRICQDIIIY--YENGIITIPDEFTTGSSLMPNKRNPDYLELFQGIAAESISVLSFIAQSEL 304

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  316 GLPSTYNKDLQEDKEAVFEVSDTMIAVLQVATGVISTLQIHRENMKqALSPDMLATDLAYYLVRKGMPFRQAHEASGKAV 395
Cdd:PRK06389 305 NKTTGYHRDFQIVKDSTISFINNFERILLGLPDLLYNIKFEITNEK-NIKNSVYATYNAWLAFKNGMDWKSAYAYIGNKI 383
Adenylsuccinate_lyase_like cd01595
Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis, ...
 93-389 3.20e-28

Adenylsuccinate lyase (ASL)_like; This group contains ASL, prokaryotic-type 3-carboxy-cis,cis-muconate cycloisomerase (pCMLE), and related proteins. These proteins are members of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and; the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). pCMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone, in the beta-ketoadipate pathway. ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176467 [Multi-domain]  Cd Length: 381  Bit Score: 115.29  E-value: 3.20e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  93 ERRLKELIGEAAGK-LHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSH 171
Cdd:cd01595  68 VYALAEKCGEDAGEyVHFGATSQDINDTALALQLRDALDIILPDLDALIDALAKLALEHKDTPMLGRTHGQHALPTTFGK 147

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 172 WILSHAVALTRDSERLLEVQKRINVL----PLGSGAIAG-NPLGVDRELLrAELNFGAITLNSMdaTSERDFVAEFLFWA 246
Cdd:cd01595 148 KFAVWAAELLRHLERLEEARERVLVGgisgAVGTHASLGpKGPEVEERVA-EKLGLKVPPITTQ--IEPRDRIAELLSAL 224

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 247 SLCMTHLSRMAEDLILYGTKEFSFVQL-SDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLkglpstyNKDL 325
Cdd:cd01595 225 ALIAGTLEKIATDIRLLQRTEIGEVEEpFEKGQVGSSTMPHKRNPIDSENIEGLARLVRALAAPALENL-------VQWH 297

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19526986 326 QED-------KEAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALS---PDMLATDLAYYLVRKGMPFRQAHE 389
Cdd:cd01595 298 ERDlsdssveRNILPDAFLLLDAALSRLQGLLEGLVVNPERMRRNLDltwGLILSEAVMMALAKKGLGRQEAYE 371
ASL_C2 pfam14698
Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of ...
 368-434 1.27e-27

Argininosuccinate lyase C-terminal; This domain is found at the C-terminus of argininosuccinate lyase.


Pssm-ID: 464268 [Multi-domain]  Cd Length: 68  Bit Score: 104.81  E-value: 1.27e-27
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19526986   368 MLATDLAYYLVRKGMPFRQAHEASGKAVFMAETKGVALNLLSLQELQTISPLFSGDVSHVWDYSHSV 434
Cdd:pfam14698   2 STATDLADYLVRKGVPFREAHEIVGRLVRLAEEKGKDLEDLTLEELQAISPLFEEDVYEALDPEASV 68
PurB COG0015
Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part ...
 44-390 3.11e-22

Adenylosuccinate lyase [Nucleotide transport and metabolism]; Adenylosuccinate lyase is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 439786 [Multi-domain]  Cd Length: 436  Bit Score: 98.62  E-value: 3.11e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  44 AYSRGLEKAGLLTKAEMQQIlqglDKVAEEwaqgtFKLHPN--DEDIHTAN------ERRLKELIGEAAGK-LHTGRSRN 114
Cdd:COG0015  30 ALAEAQAELGLIPAEAAAAI----RAAADD-----FEIDAEriKEIEKETRhdvkafVYALKEKVGAEAGEyIHFGATSQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 115 DqvVTD--LRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLEVQK 192
Cdd:COG0015 101 D--INDtaLALQLREALELLLPDLDALIAALAELAEEHKDTPMLGRTHGQHAEPTTFGKKLAVWAAELLRQLERLEEARE 178

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 193 RINVLPLGsGAiAGN-------PLGVDRELLrAELNFGAitlnSMDAT--SERDFVAEFLFWASLCMTHLSRMAEDLILY 263
Cdd:COG0015 179 RVLVGKIG-GA-VGTyaahgeaWPEVEERVA-EKLGLKP----NPVTTqiEPRDRHAELFSALALIAGSLEKIARDIRLL 251

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 264 GTKEFSFV-QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVFGRCAGLLMTLkglpstynkdLQEDkE------AV--FE 334
Cdd:COG0015 252 QRTEVGEVeEPFAKGQVGSSAMPHKRNPIDSENIEGLARLARALAAALLEAL----------ASWH-ErdlsdsSVerNI 320

                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19526986 335 VSDTMIAV---LQVATGVISTLQIHRENMKQALS---PDMLATDLAYYLVRKGMPFRQAHEA 390
Cdd:COG0015 321 LPDAFLLLdgaLERLLKLLEGLVVNPERMRANLDltgGLVLSEAVLMALVRRGLGREEAYEL 382
pCLME cd01597
prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains ...
 94-365 8.86e-22

prokaryotic 3-carboxy-cis,cis-muconate cycloisomerase (CMLE)_like; This subgroup contains pCLME and related proteins, and belongs to the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. CMLE catalyzes the cyclization of 3-carboxy-cis,cis-muconate (3CM) to 4-carboxy-muconolactone in the beta-ketoadipate pathway. This pathway is responsible for the catabolism of a variety of aromatic compounds into intermediates of the citric cycle in prokaryotic and eukaryotic micro-organisms.


Pssm-ID: 176469 [Multi-domain]  Cd Length: 437  Bit Score: 97.31  E-value: 8.86e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  94 RRLKELIGEAAGK-LHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHW 172
Cdd:cd01597  79 KQLTAACGDAAGEyVHWGATTQDIIDTALVLQLRDALDLLERDLDALLDALARLAATHRDTPMVGRTHLQHALPITFGLK 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 173 ILSHAVALTRDSERLLEVQKRINVLPLGsGAiAGN--PLGVD----RELLRAELNFGAITLNSMdatSERDFVAEFLFWA 246
Cdd:cd01597 159 VAVWLSELLRHRERLDELRPRVLVVQFG-GA-AGTlaSLGDQglavQEALAAELGLGVPAIPWH---TARDRIAELASFL 233

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 247 SLCMTHLSRMAEDLILYGTKEFSFVQLSDAYSTG-SSLMPQKKNPDSLELIRSKAGRVFGRCAGLlmtLKGLPSTYNKDL 325
Cdd:cd01597 234 ALLTGTLGKIARDVYLLMQTEIGEVAEPFAKGRGgSSTMPHKRNPVGCELIVALARRVPGLAALL---LDAMVQEHERDA 310

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 19526986 326 QEDK---EAVFEVSDTMIAVLQVATGVISTLQIHRENMKQALS 365
Cdd:cd01597 311 GAWHaewIALPEIFLLASGALEQAEFLLSGLEVNEDRMRANLD 353
Adenylsuccinate_lyase_1 cd01360
Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins ...
 96-389 4.00e-16

Adenylsuccinate lyase (ASL)_subgroup 1; This subgroup contains bacterial and archeal proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP).


Pssm-ID: 176464 [Multi-domain]  Cd Length: 387  Bit Score: 79.90  E-value: 4.00e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  96 LKELIGEAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILS 175
Cdd:cd01360  74 IAEYCGEAGRYIHFGLTSSDVVDTALALQLREALDIILKDLKELLEVLKKKALEHKDTVMVGRTHGIHAEPTTFGLKFAL 153

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 176 HAVALTRDSERLLEVQKRINVLPLgSGAIaGN--PLGVDRELLRAELnfgaITLNSMDATSE---RDFVAEFLFWASLCM 250
Cdd:cd01360 154 WYAEFKRHLERLKEARERILVGKI-SGAV-GTyaNLGPEVEERVAEK----LGLKPEPISTQviqRDRHAEYLSTLALIA 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 251 THLSRMAEDL-------ILYGTKEFSFVQlsdaysTGSSLMPQKKNPDSLElirskagrvfgRCAGLLMTLKGL--PSTY 321
Cdd:cd01360 228 STLEKIATEIrhlqrteVLEVEEPFSKGQ------KGSSAMPHKRNPILSE-----------NICGLARVIRSNviPALE 290

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 322 NKDLQEDKE----AV--FEVSDTMIA---VLQVATGVISTLQIHRENMKQAL---------SPDMLAtdlayyLVRKGMP 383
Cdd:cd01360 291 NVALWHERDishsSVerVILPDATILldyILRRMTRVLENLVVYPENMRRNLnltkglifsQRVLLA------LVEKGMS 364


                ....*.
gi 19526986 384 FRQAHE 389
Cdd:cd01360 365 REEAYE 370
PRK13353 PRK13353
aspartate ammonia-lyase; Provisional
 110-305 5.04e-16

aspartate ammonia-lyase; Provisional


Pssm-ID: 183992 [Multi-domain]  Cd Length: 473  Bit Score: 80.03  E-value: 5.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  110 GRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLE 189
Cdd:PRK13353 138 AQSTNDVFPTAIRIAALNLLEGLLAAMGALQDVFEEKAAEFDHVIKMGRTQLQDAVPITLGQEFSAYARALKRDRKRIQQ 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  190 VQKRINVLPLGSGAIaGNPLGVDRE-LLRAELNFGAIT-------LNSMDATSERDFVAEFLFWASLCMTHLSRMAEDLI 261
Cdd:PRK13353 218 AREHLYEVNLGGTAV-GTGLNADPEyIERVVKHLAAITglplvgaEDLVDATQNTDAFVEVSGALKVCAVNLSKIANDLR 296

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 19526986  262 LYGTKE---FSFVQLSdAYSTGSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:PRK13353 297 LLSSGPrtgLGEINLP-AVQPGSSIMPGKVNPVMPEVVNQIAFQVIG 342
Aspartase cd01357
Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), ...
 110-290 1.62e-12

Aspartase; This subgroup contains Escherichia coli aspartase (L-aspartate ammonia-lyase), Bacillus aspartase and related proteins. It is a member of the Lyase class I family, which includes both aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid.


Pssm-ID: 176462 [Multi-domain]  Cd Length: 450  Bit Score: 69.09  E-value: 1.62e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 110 GRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALTRDSERLLE 189
Cdd:cd01357 133 SQSTNDVYPTALRLALILLLRKLLDALAALQEAFQAKAREFADVLKMGRTQLQDAVPMTLGQEFGAYATALKRDRARIYK 212

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 190 VQKRINVLPLGSGAIaGNPLGVD---RELLRAELNfgAIT-------LNSMDATSERD-FVAeflFWASL--CMTHLSRM 256
Cdd:cd01357 213 ARERLREVNLGGTAI-GTGINAPpgyIELVVEKLS--EITglplkraENLIDATQNTDaFVE---VSGALkrLAVKLSKI 286

                       170       180       190       200
                ....*....|....*....|....*....|....*....|..
gi 19526986 257 AEDLILY------GTKEFSF--VQlsdaysTGSSLMPQKKNP 290
Cdd:cd01357 287 ANDLRLLssgpraGLGEINLpaVQ------PGSSIMPGKVNP 322
PRK14515 PRK14515
aspartate ammonia-lyase; Provisional
 49-305 7.81e-12

aspartate ammonia-lyase; Provisional


Pssm-ID: 237743 [Multi-domain]  Cd Length: 479  Bit Score: 66.95  E-value: 7.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   49 LEKAGLLTKAEMQQILQGLD----KVAEEWAQGTFKLHPNDEDIH---------TANE---RRLKELIGEAAGKLH---- 108
Cdd:PRK14515  58 VKKAAALANTDVGRLELNKGgaiaEAAQEILDGKWHDHFIVDPIQggagtsmnmNANEviaNRALELLGMEKGDYHyisp 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  109 -----TGRSRNDQVVTDLRLwmrQTCSKLSALLRVLiGTMVD----RAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVA 179
Cdd:PRK14515 138 nshvnMAQSTNDAFPTAIHI---ATLNALEGLLQTM-GYMHDvfelKAEQFDHVIKMGRTHLQDAVPIRLGQEFKAYSRV 213

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  180 LTRDSERLLEVQKRINVLPLGSGAIaGNPLGVDRELLRAEL----NFGAITLNS----MDATSERDFVAEFLFWASLCMT 251
Cdd:PRK14515 214 LERDMKRIQQSRQHLYEVNMGATAV-GTGLNADPEYIEAVVkhlaAISELPLVGaedlVDATQNTDAYTEVSAALKVCMM 292

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19526986  252 HLSRMAEDLILYGTKE---FSFVQLSdAYSTGSSLMPQKKNPDSLELIRSKAGRVFG 305
Cdd:PRK14515 293 NMSKIANDLRLMASGPrvgLAEIMLP-ARQPGSSIMPGKVNPVMPEVINQIAFQVIG 348
PRK05975 PRK05975
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 94-300 9.73e-12

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 168324 [Multi-domain]  Cd Length: 351  Bit Score: 66.23  E-value: 9.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   94 RRLKELIG-EAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTM--VDRAEAERDVLfpGYTHLQRAQPIRWS 170
Cdd:PRK05975  88 RQLRAAVGeEAAAHVHFGATSQDVIDTSLMLRLKAASEILAARLGALIARLdaLEATFGQNALM--GHTRMQAAIPITVA 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  171 HWILSHAVALTRDSERLLEVQKRINVLPLGSGAIAGNPLGVDRELLRAELnfgAITLNSMDAT---SERDFVAEFLFWAS 247
Cdd:PRK05975 166 DRLASWRAPLLRHRDRLEALRADVFPLQFGGAAGTLEKLGGKAAAVRARL---AKRLGLEDAPqwhSQRDFIADFAHLLS 242

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19526986  248 LCMTHLSRMAEDLILygtkefsFVQLSDAYST----GSSLMPQKKNPDSLELIRSKA 300
Cdd:PRK05975 243 LVTGSLGKFGQDIAL-------MAQAGDEISLsgggGSSAMPHKQNPVAAETLVTLA 292
PRK09053 PRK09053
3-carboxy-cis,cis-muconate cycloisomerase; Provisional
 102-364 1.44e-11

3-carboxy-cis,cis-muconate cycloisomerase; Provisional


Pssm-ID: 181627 [Multi-domain]  Cd Length: 452  Bit Score: 66.19  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  102 EAAGKLHTGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIRWSHWILSHAVALT 181
Cdd:PRK09053  97 EAARYVHWGATSQDIIDTGLVLQLRDALDLLEPDLDRLCDALATLAARHRATPMVGRTWLQQALPVTLGLKFAGWLDALL 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  182 RDSERLLEVQKRINVLPLG--SGAIA---GNPLGVdRELLRAELNfgaITLNSMDATSERDFVAEFLFWASLCMTHLSRM 256
Cdd:PRK09053 177 RHRQRLAALRPRALVLQFGgaAGTLAslgEQALPV-AQALAAELQ---LALPALPWHTQRDRIAEFASALGLLAGTLGKI 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  257 AEDLILYGTKEFSFV-QLSDAYSTGSSLMPQKKNPDSLELIRSKAGRVfgrcAGLLMTL-KGLPSTYNKDL---QEDKEA 331
Cdd:PRK09053 253 ARDVSLLMQTEVGEVfEPAAAGKGGSSTMPHKRNPVGCAAVLTAATRA----PGLVATLfAAMPQEHERALggwHAEWDT 328

                        250       260       270
                 ....*....|....*....|....*....|...
gi 19526986  332 VFEVSDTMIAVLQVATGVISTLQIHRENMKQAL 364
Cdd:PRK09053 329 LPELACLAAGALAQMAQIVEGLEVDAARMRANL 361
aspA PRK12273
aspartate ammonia-lyase; Provisional
 91-290 7.57e-11

aspartate ammonia-lyase; Provisional


Pssm-ID: 237031 [Multi-domain]  Cd Length: 472  Bit Score: 63.99  E-value: 7.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986   91 ANE----RRLkELIGEAAG---KLH------TGRSRNDQVVTDLRLWMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPG 157
Cdd:PRK12273 109 ANEvianRAL-ELLGHEKGeyqYVHpndhvnMSQSTNDAYPTAIRIALLLSLRKLLDALEQLQEAFEAKAKEFADILKMG 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  158 YTHLQRAQPIRWSHWILSHAVALTRDSERLLEVQKRINVLPLGSGAIaGNPLGVD---RELLRAELNfgAIT-------L 227
Cdd:PRK12273 188 RTQLQDAVPMTLGQEFGAYAVALAEDRKRLYRAAELLREVNLGATAI-GTGLNAPpgyIELVVEKLA--EITglplvpaE 264

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19526986  228 NSMDATSERD-FVAeflFWASL--CMTHLSRMAEDLILY------GTKEFSF--VQlsdaysTGSSLMPQKKNP 290
Cdd:PRK12273 265 DLIEATQDTGaFVE---VSGALkrLAVKLSKICNDLRLLssgpraGLNEINLpaVQ------AGSSIMPGKVNP 329
Aspartase_like cd01596
aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains ...
 91-290 2.09e-07

aspartase (L-aspartate ammonia-lyase) and fumarase class II enzymes; This group contains aspartase (L-aspartate ammonia-lyase), fumarase class II enzymes, and related proteins. It is a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. Aspartase catalyzes the reversible deamination of aspartic acid. Fumarase catalyzes the reversible hydration/dehydration of fumarate to L-malate during the Krebs cycle.


Pssm-ID: 176468 [Multi-domain]  Cd Length: 450  Bit Score: 53.20  E-value: 2.09e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  91 ANE---RRLKELIGEAAGK---LHtgrsrNDQVV-----TD------LRLWMRQTCSKLSALLRVLIGTMVDRAEAERDV 153
Cdd:cd01596 102 VNEviaNRALELLGGKKGKypvHP-----NDDVNnsqssNDdfppaaHIAAALALLERLLPALEQLQDALDAKAEEFADI 176

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 154 LFPGYTHLQRAQPIR----WSHWilshAVALTRDSERLLEVQKRINVLPLGSGAIaGNPLGVDR---ELLRAELNfgAIT 226
Cdd:cd01596 177 VKIGRTHLQDAVPLTlgqeFSGY----AAQLARDIARIEAALERLRELNLGGTAV-GTGLNAPPgyaEKVAAELA--ELT 249

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 227 L-------NSMDATSERD-FVAeflFWASL--CMTHLSRMAEDLILY------GTKEFSF--VQLsdaystGSSLMPQKK 288
Cdd:cd01596 250 GlpfvtapNLFEATAAHDaLVE---VSGALktLAVSLSKIANDLRLLssgpraGLGEINLpaNQP------GSSIMPGKV 320


                ..
gi 19526986 289 NP 290
Cdd:cd01596 321 NP 322
Adenylsuccinate_lyase_2 cd03302
Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins ...
 58-389 2.51e-06

Adenylsuccinate lyase (ASL)_subgroup 2; This subgroup contains mainly eukaryotic proteins similar to ASL, a member of the Lyase class I family. Members of this family for the most part catalyze similar beta-elimination reactions in which a C-N or C-O bond is cleaved with the release of fumarate as one of the products. These proteins are active as tetramers. The four active sites of the homotetrameric enzyme are each formed by residues from three different subunits. ASL catalyzes two steps in the de novo purine biosynthesis: the conversion of 5-aminoimidazole-(N-succinylocarboxamide) ribotide (SAICAR) into 5-aminoimidazole-4-carboxamide ribotide (AICAR) and, the conversion of adenylsuccinate (SAMP) into adenosine monophosphate (AMP). ASL deficiency has been linked to several pathologies including psychomotor retardation with autistic features, epilepsy and muscle wasting.


Pssm-ID: 176471 [Multi-domain]  Cd Length: 436  Bit Score: 49.62  E-value: 2.51e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  58 AEMQQILqGLDKVAEEWAQgtFKLHPNDEDIHTA--NERRLK-----------ELIGEAAGKLHTG-RSRNDQVVTDLrL 123
Cdd:cd03302  31 AEAEKEL-GLDISDEQIEE--MKANVENIDFEIAaaEEKKLRhdvmahvhafgLLCPAAAGIIHLGaTSCFVTDNTDL-I 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 124 WMRQTCSKLSALLRVLIGTMVDRAEAERDVLFPGYTHLQRAQPI----RWSHWILSHAVALTRDSERLLEVQKRINVLPL 199
Cdd:cd03302 107 QIRDALDLILPKLAAVIDRLAEFALEYKDLPTLGFTHYQPAQLTtvgkRACLWIQDLLMDLRNLERLRDDLRFRGVKGTT 186

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 200 GSGA-----IAGNPLGVDR--ELLRAELNFgAITLNSMDATSERDFVAEFLFWASLCMTHLSRMAEDL-ILYGTKE---- 267
Cdd:cd03302 187 GTQAsfldlFEGDHDKVEAldELVTKKAGF-KKVYPVTGQTYSRKVDIDVLNALSSLGATAHKIATDIrLLANLKEveep 265

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986 268 FSFVQlsdaysTGSSLMPQKKNPdslelIRSKagrvfgRCAGLLMTLKGLPS----TYNKDLQE---DKEAV-------- 332
Cdd:cd03302 266 FEKGQ------IGSSAMPYKRNP-----MRSE------RCCSLARHLMNLASnaaqTASTQWFErtlDDSANrriaipea 328

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 19526986 333 FEVSDTMIAVLQ-VATG-VISTLQIHReNMKQALsPDMLATDLAYYLVRKGMPFRQAHE 389
Cdd:cd03302 329 FLAADAILITLQnISEGlVVYPKVIER-HIRQEL-PFMATENIIMAAVKAGGDRQDAHE 385
PRK08937 PRK08937
adenylosuccinate lyase; Provisional
 280-389 1.95e-05

adenylosuccinate lyase; Provisional


Pssm-ID: 236352 [Multi-domain]  Cd Length: 216  Bit Score: 45.79  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19526986  280 GSSLMPQKKNPDSLELIRSKAGRVFGRcagLLMTLKGLPSTYNKDLQEDKE---AVFEVSDTMIAVLQVATGVISTLQIH 356
Cdd:PRK08937  58 GSSAMPHKRNPIGSERITGLARVLRSY---LVTALENVPLWHERDLSHSSAeriALPDAFLALDYILNRFVNILENLVVF 134

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 19526986  357 RENMKQAL---SPDMLATDLAYYLVRKGMPFRQAHE 389
Cdd:PRK08937 135 PENIERNLdktLGFIATERVLLELVEKGMGREEAHE 170
fumC PRK00485
fumarate hydratase; Reviewed
 136-200 2.90e-03

fumarate hydratase; Reviewed


Pssm-ID: 234779 [Multi-domain]  Cd Length: 464  Bit Score: 40.07  E-value: 2.90e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19526986  136 LRVLIGTMVDRAEAERDVLFPGYTHLQRAQPIR----WSHWilshAVALTRDSERLLEVQKRINVLPLG 200
Cdd:PRK00485 164 LEHLRDTLAAKAEEFADIVKIGRTHLQDATPLTlgqeFSGY----AAQLEHGIERIEAALPHLYELALG 228
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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