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Conserved domains on  [gi|1722137665|ref|WP_146458106|]
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MULTISPECIES: HD-GYP domain-containing protein [Vibrio]

Protein Classification

HD-GYP domain-containing protein( domain architecture ID 11454351)

HD-GYP domain-containing protein functions as a cyclic nucleotide phosphodiesterase, such as Borreliella burgdorferi cyclic di-GMP phosphodiesterase PdeB that catalyzes the hydrolysis of cyclic diguanylate (c-di-GMP) to GMP

CATH:  1.10.3210.10
Gene Ontology:  GO:0004112|GO:0046872
PubMed:  11008484|9868367

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
153-469 2.30e-69

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


:

Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 224.47  E-value: 2.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 153 VGLVIVLLVTLTTMLTMIAVKDIFWLEHNPERLLDGTGKISVIKEFIYLAVVLGGYAITIMTLWSKLIKRILLSQEHALR 232
Cdd:COG2206     3 LLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLLAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 233 KVTSGEQGVRLPIFGYNELGSMASMTNIMLDSLETAQNEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKVLAQEL 312
Cdd:COG2206    83 ALLLAELLLLLAALESLLAELFEELRLGLLEELKKLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALAREL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 313 SksethstlLTPNYIELLYKSAPLHDVGKVGIPDNVLLKPGKLTDEEFEIMKGHPAIGAEALSiaekqlgSCSFLKVAKE 392
Cdd:COG2206   163 G--------LSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILK-------KLPGLSEVAE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722137665 393 ISLTHHEKWNGSGYPNQLSGEDIPLSGRLMALADVYDALISKRVYKPAFTHEQAKQIILEGNGTHFDPQVVQAFLAV 469
Cdd:COG2206   228 IVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKV 304
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
153-469 2.30e-69

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 224.47  E-value: 2.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 153 VGLVIVLLVTLTTMLTMIAVKDIFWLEHNPERLLDGTGKISVIKEFIYLAVVLGGYAITIMTLWSKLIKRILLSQEHALR 232
Cdd:COG2206     3 LLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLLAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 233 KVTSGEQGVRLPIFGYNELGSMASMTNIMLDSLETAQNEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKVLAQEL 312
Cdd:COG2206    83 ALLLAELLLLLAALESLLAELFEELRLGLLEELKKLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALAREL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 313 SksethstlLTPNYIELLYKSAPLHDVGKVGIPDNVLLKPGKLTDEEFEIMKGHPAIGAEALSiaekqlgSCSFLKVAKE 392
Cdd:COG2206   163 G--------LSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILK-------KLPGLSEVAE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722137665 393 ISLTHHEKWNGSGYPNQLSGEDIPLSGRLMALADVYDALISKRVYKPAFTHEQAKQIILEGNGTHFDPQVVQAFLAV 469
Cdd:COG2206   228 IVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKV 304
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
294-450 2.05e-22

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 93.17  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 294 TGAHILRTQEYVKVLAQELSKSETHstlltpnyIELLYKSAPLHDVGKVGIPDnvllkpgKLTDEEFEIMKGHPAIGAEA 373
Cdd:cd00077     3 RFEHSLRVAQLARRLAEELGLSEED--------IELLRLAALLHDIGKPGTPD-------AITEEESELEKDHAIVGAEI 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722137665 374 LSIAEKQLGSCSFLKVAKEISLTHHEKWNGSGYPNQLSGEDIPLSGRLMALADVYDALIS-KRVYKPAFTHEQAKQII 450
Cdd:cd00077    68 LRELLLEEVIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRdSREKRRRIAEEDLEELL 145
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
353-422 3.30e-17

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 75.71  E-value: 3.30e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 353 GKLTDEEFEIMKGHPAIGAEALSIAEKqlgscsFLKVAKEISLTHHEKWNGSGYPNQLSGEDIPLSGRLM 422
Cdd:pfam13487   1 GTLTPEEREIINRHPEHTARLLSTLPR------LPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
294-439 3.46e-14

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 69.25  E-value: 3.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665  294 TGAHILRTQEYVKVLAQELSKSEthstlltpnyIELLYKSAPLHDVGKVGIPDNVLLKpgkltdeeFEIMKGHPAIGAEa 373
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGLLD----------IELLLLAALLHDIGKPGTPDSFLVK--------TSVLEDHHFIGAE- 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722137665  374 lsIAEKQLGSCSFLKVAKEISLTHHEKWNGsgypnqLSGEDIPLSGRLMALADVYDALISKRVYKP 439
Cdd:smart00471  66 --ILLEEEEPRILEEILRTAILSHHERPDG------LRGEPITLEARIVKVADRLDALRADRRYRR 123
 
Name Accession Description Interval E-value
HDGYP COG2206
HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal ...
153-469 2.30e-69

HD-GYP domain, c-di-GMP phosphodiesterase class II (or its inactivated variant) [Signal transduction mechanisms];


Pssm-ID: 441808 [Multi-domain]  Cd Length: 316  Bit Score: 224.47  E-value: 2.30e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 153 VGLVIVLLVTLTTMLTMIAVKDIFWLEHNPERLLDGTGKISVIKEFIYLAVVLGGYAITIMTLWSKLIKRILLSQEHALR 232
Cdd:COG2206     3 LLLLLLLLLLLLLLLLALLLLLLLLLLLLLLLLLLLLLALLALLLLLLLLLALLALLLALLALLLLLLLLLLLLSLLLAV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 233 KVTSGEQGVRLPIFGYNELGSMASMTNIMLDSLETAQNEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKVLAQEL 312
Cdd:COG2206    83 ALLLAELLLLLAALESLLAELFEELRLGLLEELKKLVEELDELLPDALLALLAALDAKDPYTYGHSVRVAVLALALAREL 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 313 SksethstlLTPNYIELLYKSAPLHDVGKVGIPDNVLLKPGKLTDEEFEIMKGHPAIGAEALSiaekqlgSCSFLKVAKE 392
Cdd:COG2206   163 G--------LSEEELEDLGLAALLHDIGKIGIPDEILNKPGKLTDEEFEIIKKHPEYGYEILK-------KLPGLSEVAE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1722137665 393 ISLTHHEKWNGSGYPNQLSGEDIPLSGRLMALADVYDALISKRVYKPAFTHEQAKQIILEGNGTHFDPQVVQAFLAV 469
Cdd:COG2206   228 IVLQHHERLDGSGYPRGLKGEEIPLLARILAVADVYDALTSDRPYRKALSPEEALEELRKGAGTQFDPELVEAFIKV 304
RpfG COG3437
Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains ...
218-451 6.39e-27

Response regulator c-di-GMP phosphodiesterase, RpfG family, contains REC and HD-GYP domains [Signal transduction mechanisms];


Pssm-ID: 442663 [Multi-domain]  Cd Length: 224  Bit Score: 108.33  E-value: 6.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 218 KLIKRILLSQEHALRKVTSGEQGVRL-----P--IFgynelgsmasmTNIML---DSLETAQ--NEVKTTRDVAIVSLSA 285
Cdd:COG3437    20 ELLRQLLRTLGYDVVTAESGEEALELlleapPdlIL-----------LDVRMpgmDGFELLRllRADPSTRDIPVIFLTA 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 286 LAESRDN----ETGAH-----ILRTQEYVKVLAQELSKSETHSTLLtpNYIELLYKSAPLHDVGKVGIPDNVLLKPGKLT 356
Cdd:COG3437    89 LADPEDReralEAGADdyltkPFDPEELLARVRNALELRRLQRELD--DLVLYLKLAAPLHDIGKIGIPDAILLKPGKLT 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 357 DEEFEIMKGHPAIGAEALSiaekqlgSCSFLKVAKEIslthHEKWNGSGypnqlsgedipLSGRlmaladvyDALISKRv 436
Cdd:COG3437   167 PEEWEITHAHIGAEILSGS-------LLPLLQLAAEI----HERWDGSG-----------LSAR--------DALTSKK- 215
                         250
                  ....*....|....*
gi 1722137665 437 ykpaftHEQAKQIIL 451
Cdd:COG3437   216 ------LEEALEEIR 224
HDc cd00077
Metal dependent phosphohydrolases with conserved 'HD' motif
294-450 2.05e-22

Metal dependent phosphohydrolases with conserved 'HD' motif


Pssm-ID: 238032 [Multi-domain]  Cd Length: 145  Bit Score: 93.17  E-value: 2.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 294 TGAHILRTQEYVKVLAQELSKSETHstlltpnyIELLYKSAPLHDVGKVGIPDnvllkpgKLTDEEFEIMKGHPAIGAEA 373
Cdd:cd00077     3 RFEHSLRVAQLARRLAEELGLSEED--------IELLRLAALLHDIGKPGTPD-------AITEEESELEKDHAIVGAEI 67
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1722137665 374 LSIAEKQLGSCSFLKVAKEISLTHHEKWNGSGYPNQLSGEDIPLSGRLMALADVYDALIS-KRVYKPAFTHEQAKQII 450
Cdd:cd00077    68 LRELLLEEVIKLIDELILAVDASHHERLDGLGYPDGLKGEEITLEARIVKLADRLDALRRdSREKRRRIAEEDLEELL 145
HD_5 pfam13487
HD domain; HD domains are metal dependent phosphohydrolases.
353-422 3.30e-17

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 433249 [Multi-domain]  Cd Length: 64  Bit Score: 75.71  E-value: 3.30e-17
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 353 GKLTDEEFEIMKGHPAIGAEALSIAEKqlgscsFLKVAKEISLTHHEKWNGSGYPNQLSGEDIPLSGRLM 422
Cdd:pfam13487   1 GTLTPEEREIINRHPEHTARLLSTLPR------LPKEVAEIIAQHHERLDGSGYPRGLKGEEIPLGARIL 64
HD pfam01966
HD domain; HD domains are metal dependent phosphohydrolases.
294-431 2.60e-14

HD domain; HD domains are metal dependent phosphohydrolases.


Pssm-ID: 460398 [Multi-domain]  Cd Length: 110  Bit Score: 69.19  E-value: 2.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 294 TGAHILRTQEYVKVLAQELSKSEthstlltpnyIELLYKSAPLHDVGKVGIPDNvllkpgkltDEEFEIMKGHPAIGAEA 373
Cdd:pfam01966   1 RLEHSLRVALLARELAEELGELD----------RELLLLAALLHDIGKGPFGDE---------KPEFEIFLGHAVVGAEI 61
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1722137665 374 LSIAEKQLGSCSFLKVAKEisltHHEKWNGSGYPnqlsgEDIPLSGRLMALADVYDAL 431
Cdd:pfam01966  62 LRELEKRLGLEDVLKLILE----HHESWEGAGYP-----EEISLEARIVKLADRLDAL 110
HDc smart00471
Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic ...
294-439 3.46e-14

Metal dependent phosphohydrolases with conserved 'HD' motif; Includes eukaryotic cyclic nucleotide phosphodiesterases (PDEc). This profile/HMM does not detect HD homologues in bacterial glycine aminoacyl-tRNA synthetases (beta subunit).


Pssm-ID: 214679 [Multi-domain]  Cd Length: 124  Bit Score: 69.25  E-value: 3.46e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665  294 TGAHILRTQEYVKVLAQELSKSEthstlltpnyIELLYKSAPLHDVGKVGIPDNVLLKpgkltdeeFEIMKGHPAIGAEa 373
Cdd:smart00471   5 VFEHSLRVAQLAAALAEELGLLD----------IELLLLAALLHDIGKPGTPDSFLVK--------TSVLEDHHFIGAE- 65
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1722137665  374 lsIAEKQLGSCSFLKVAKEISLTHHEKWNGsgypnqLSGEDIPLSGRLMALADVYDALISKRVYKP 439
Cdd:smart00471  66 --ILLEEEEPRILEEILRTAILSHHERPDG------LRGEPITLEARIVKVADRLDALRADRRYRR 123
NtrY COG5000
Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism ...
191-348 7.35e-04

Signal transduction histidine kinase NtrY involved in nitrogen fixation and metabolism regulation [Signal transduction mechanisms];


Pssm-ID: 444024 [Multi-domain]  Cd Length: 422  Bit Score: 41.87  E-value: 7.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 191 KISVIKEFIYLAVVLGGYAITIMTLWSKLIKRILLSQEHALRKVTSGEQGVRLPIFGYNELGSMASMTNIMLDSLETAQN 270
Cdd:COG5000     4 QILFLLLLLLIALLLLLLALWLALLLARRLTRPLRRLAEATRAVAAGDLSVRLPVTGDDEIGELARAFNRMTDQLKEQRE 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 271 EVKTTR----------DVAIVSLSA--------------LAESRDNETG---AHILRTQEYVKVLAQELSKSETHSTLLT 323
Cdd:COG5000    84 ELEERRryletilenlPAGVIVLDAdgritlanpaaerlLGIPLEELIGkplEELLPELDLAELLREALERGWQEEIELT 163
                         170       180
                  ....*....|....*....|....*.
gi 1722137665 324 PNYIE-LLYKSAPLHDVGKVGIPDNV 348
Cdd:COG5000   164 RDGRRtLLVRASPLRDDGYVIVFDDI 189
NarQ COG3850
Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction ...
192-312 1.71e-03

Signal transduction histidine kinase NarQ, nitrate/nitrite-specific [Signal transduction mechanisms];


Pssm-ID: 443059 [Multi-domain]  Cd Length: 448  Bit Score: 41.02  E-value: 1.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 192 ISVIKEFIYLAVVLGGYAITIMTLW--SKLIKRILLSQEHALRKVTSGEQGVRLPIFGYNELGSMASMTNIMLDSLETAQ 269
Cdd:COG3850   112 AAAINRKLALLRLLLALLLALLLAYllRRRIVRPLRRLTQAAERIARGDFDARVPVSGRDELGTLARAFNRMADELQELY 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1722137665 270 NEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKVLAQEL 312
Cdd:COG3850   192 AELEEEEELEAELELLALLDELLLLAALLLLLALLLALLLAAL 234
HAMP COG2770
HAMP domain [Signal transduction mechanisms];
8-312 3.15e-03

HAMP domain [Signal transduction mechanisms];


Pssm-ID: 442051 [Multi-domain]  Cd Length: 631  Bit Score: 40.10  E-value: 3.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665   8 QSLTTQLYAIAGVLFGTYGSRVCPMLDTLTTLEIFTQVSVVFALVWFVRHYLLARHALVKQGRFAQLDTLLFFAASVPFA 87
Cdd:COG2770    14 LLLLLLLLAGALLVLALISLRLLLALLLLLLLLLALLLLLLLLLLLLLAALVLLALLLAAALLLLLLLLSLVALAALLLA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665  88 LYYNLSYDFTIDSNLKVLFGMTLFGFFTGSILQLKAKLAQMDKMEHSGQFDFQLIGERSSLVKQMVGLVIVLLVTLTTML 167
Cdd:COG2770    94 LLLLLLLALLLLLAALLLLLLLAALALLLLLLLLLAALLALLLALALLALLLGLAAARLLLAALLALAAALALALGAGEL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1722137665 168 TMIAVKDIFWLEHNPERLLDGTGKISVI------KEFIYLAVVLGGYAITIMTLWSKLIKRILLSQ----EHALRKVTSG 237
Cdd:COG2770   174 LLLADLAAAIAALLAALLLLLLGGLLLVvlleaaLAALLLLLLLALLALLLALLLALLLARRITRPlrrlAEAARRIAAG 253
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1722137665 238 EQGVRLPIFGYNELGSMASMTNIMLDSLETAQNEVKTTRDVAIVSLSALAESRDNETGAHILRTQEYVKVLAQEL 312
Cdd:COG2770   254 DLDVRIPVSRKDEIGELARAFNRMADSLRESIEEAEEEEELAEAELARLLEALLELLLALLLLLLALLLLAAAAL 328
 
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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