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Conserved domains on  [gi|1222019860|ref|NP_001340847|]
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protein hinderin isoform 3 [Homo sapiens]

Protein Classification

KIAA1328 domain-containing protein( domain architecture ID 10634053)

KIAA1328 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 93-406 0e+00

Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. This family of proteins is found in eukaryotes.


:

Pssm-ID: 464679  Cd Length: 327  Bit Score: 536.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  93 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKERE----EYRECQELLSLYQKYLSEQ 168
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREalqqQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 248
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 249 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 320
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 321 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 399
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 1222019860 400 QSRLDYN 406
Cdd:pfam15369 321 QSRLDYN 327
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 93-406 0e+00

Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. This family of proteins is found in eukaryotes.


Pssm-ID: 464679  Cd Length: 327  Bit Score: 536.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  93 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKERE----EYRECQELLSLYQKYLSEQ 168
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREalqqQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 248
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 249 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 320
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 321 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 399
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 1222019860 400 QSRLDYN 406
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 92-172 1.52e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  92 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREEY----RECQELLSLYQK 163
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELeqkqQELEKKEEELEE 135


                  ....*....
gi 1222019860 164 YLSEQQEKL 172
Cdd:PRK12704  136 LIEEQLQEL 144
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 49-163 1.58e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  49 KADVKLKTSRVTDAsismESLKGTGDSVDEQNSCRGEIKSASLKDLCLEDK-----RRIANLIKELARVSEEKEVTEERL 123
Cdd:COG1579    65 ELEIEEVEARIKKY----EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAEL 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222019860 124 KAEQESFEKKIRQLEEQNELIIKEREEYREC--QELLSLYQK 163
Cdd:COG1579   141 EEKKAELDEELAELEAELEELEAEREELAAKipPELLALYER 182
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 87-193 2.08e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  87 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREEYREcqELLSLYQKYL 165
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLK--EQERALESKL 265

                          90       100
                  ....*....|....*....|....*...
gi 1222019860 166 SEQQEKLTMSLSElgAARMQEQQVSSRK 193
Cdd:cd16269   266 KEQEALLEEGFKE--QAELLQEEIRSLK 291
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 93-406 0e+00

Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. This family of proteins is found in eukaryotes.


Pssm-ID: 464679  Cd Length: 327  Bit Score: 536.71  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  93 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKERE----EYRECQELLSLYQKYLSEQ 168
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREalqqQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 248
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 249 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 320
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 321 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 399
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 1222019860 400 QSRLDYN 406
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 92-172 1.52e-04

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 44.38  E-value: 1.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  92 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREEY----RECQELLSLYQK 163
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELeqkqQELEKKEEELEE 135


                  ....*....
gi 1222019860 164 YLSEQQEKL 172
Cdd:PRK12704  136 LIEEQLQEL 144
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 49-163 1.58e-04

Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];


Pssm-ID: 441187 [Multi-domain]  Cd Length: 236  Bit Score: 43.37  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  49 KADVKLKTSRVTDAsismESLKGTGDSVDEQNSCRGEIKSASLKDLCLEDK-----RRIANLIKELARVSEEKEVTEERL 123
Cdd:COG1579    65 ELEIEEVEARIKKY----EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAEL 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1222019860 124 KAEQESFEKKIRQLEEQNELIIKEREEYREC--QELLSLYQK 163
Cdd:COG1579   141 EEKKAELDEELAELEAELEELEAEREELAAKipPELLALYER 182
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 87-193 2.08e-04

Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal domain. Guanylate-binding proteins (GBPs) are synthesized after activation of the cell by interferons. The biochemical properties of GBPs are clearly different from those of Ras-like and heterotrimeric GTP-binding proteins. They bind guanine nucleotides with low affinity (micromolar range), are stable in their absence, and have a high turnover GTPase. In addition to binding GDP/GTP, they have the unique ability to bind GMP with equal affinity and hydrolyze GTP not only to GDP, but also to GMP. This C-terminal domain has been shown to mediate inhibition of endothelial cell proliferation by inflammatory cytokines.


Pssm-ID: 293879 [Multi-domain]  Cd Length: 291  Bit Score: 43.33  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  87 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREEYREcqELLSLYQKYL 165
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLK--EQERALESKL 265

                          90       100
                  ....*....|....*....|....*...
gi 1222019860 166 SEQQEKLTMSLSElgAARMQEQQVSSRK 193
Cdd:cd16269   266 KEQEALLEEGFKE--QAELLQEEIRSLK 291
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
99-197 8.88e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 41.81  E-value: 8.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  99 KRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREEYRECQELLSLYQKYLSEQQEKLTMSLSE 178
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQAQEELESLQEEAEELQEELEELQKE 123

                          90
                  ....*....|....*....
gi 1222019860 179 LGAARMQEQQVSSRKSTLQ 197
Cdd:COG4372   124 RQDLEQQRKQLEAQIAELQ 142
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-197 1.47e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  99 KRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREEYRECQELLSLYQKYLSEQQEKLTMSLSE 178
Cdd:COG1196   294 LAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90
                  ....*....|....*....
gi 1222019860 179 LGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   374 LAEAEEELEELAEELLEAL 392
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 91-172 3.49e-03

Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. Autophagy is a bulk degradation process induced by starvation in eukaryotic cells. Apg6/Vps30p has two distinct functions in the autophagic process, either associated with the membrane or in a retrieval step of the carboxypeptidase Y sorting pathway.


Pssm-ID: 465452 [Multi-domain]  Cd Length: 127  Bit Score: 37.96  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  91 LKDLCLEDKRRIANLIKELARVSEEKEVTE---ERLKAEQESFEKKIRQLEEQ-NELIIKEREEYREcqelLSLYQKYLS 166
Cdd:pfam17675  32 LKKLEKETPEELEELEKELEKLEKEEEELLqelEELEKEREELDAELEALEEElEALDEEEEEFWRE----YNALQLQLL 107


                  ....*.
gi 1222019860 167 EQQEKL 172
Cdd:pfam17675 108 EFQDER 113
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 99-197 6.51e-03

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  99 KRRIANLIKELARVSEEKEVTEERLKAEQEsfekkirQLEEQNELIIKEREEYRECQELLSLYQKYLSEQQEKLTMSLSE 178
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEELEELEE-------ELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEE 380

                          90
                  ....*....|....*....
gi 1222019860 179 LGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   381 LEELAEELLEALRAAAELA 399
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 94-150 6.64e-03

Protein of unknown function (DUF724); This family contains several uncharacterized proteins found in Arabidopsis thaliana and other plants. This region is often found associated with Agenet domains and may contain coiled-coil.


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 38.02  E-value: 6.64e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1222019860  94 LCLEDKR-RIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREE 150
Cdd:pfam05266  98 LSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEA 155
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 100-197 8.19e-03

RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The SMC (structural maintenance of chromosomes) superfamily proteins have ATP-binding domains at the N- and C-termini, and two extended coiled-coil domains separated by a hinge in the middle. The eukaryotic SMC proteins form two kind of heterodimers: the SMC1/SMC3 and the SMC2/SMC4 types. These heterodimers constitute an essential part of higher order complexes, which are involved in chromatin and DNA dynamics. This family also includes the RecF and RecN proteins that are involved in DNA metabolism and recombination.


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.18  E-value: 8.19e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860  100 RRIANLIKELArVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREEYRECQELLSLYQKYLSEQQEKLTMSLSEL 179
Cdd:pfam02463  153 ERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIIDLEELKLQELKLKEQAKKALEYYQLKEKLELEEEYLLYLDY 231

                           90
                   ....*....|....*...
gi 1222019860  180 GAARMQEQQVSSRKSTLQ 197
Cdd:pfam02463  232 LKLNEERIDLLQELLRDE 249
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 101-197 8.88e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 38.59  E-value: 8.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1222019860 101 RIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREEYRECQELLSLYQKYLSE---QQEKLTMSLS 177
Cdd:COG4942    21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAElekEIAELRAELE 100

                          90       100
                  ....*....|....*....|...
gi 1222019860 178 ELG---AARMQEQQVSSRKSTLQ 197
Cdd:COG4942   101 AQKeelAELLRALYRLGRQPPLA 123
 
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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