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Conserved domains on  [gi|2462560979|ref|XP_054174847|]
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protein hinderin isoform X2 [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. ...
 89-406 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: 552.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  89 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 168
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 248
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 249 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 320
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 321 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 399
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 2462560979 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. ...
 89-406 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: 552.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  89 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 168
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 248
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 249 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 320
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 321 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 399
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 2462560979 400 QSRLDYN 406
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 88-172 3.46e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  88 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 163
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135


                  ....*....
gi 2462560979 164 YLSEQQEKL 172
Cdd:PRK12704  136 LIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-197 1.20e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  95 KRRIANLIKELARVSEEK---EVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 171
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|....*.
gi 2462560979 172 LTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELA 399
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 83-187 2.91e-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: 42.95  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  83 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 161
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*.
gi 2462560979 162 QKYLSEQQEKLTmslselgAARMQEQ 187
Cdd:cd16269   268 QEALLEEGFKEQ-------AELLQEE 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-197 2.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979   54 RVTDASISMESLKGTGDSVDEQNScRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEE---RLKAEQESFEKKI 130
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELI 868

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462560979  131 RQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 89-406 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: 552.50  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  89 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 168
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 248
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 249 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 320
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979 321 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 399
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 2462560979 400 QSRLDYN 406
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 88-172 3.46e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 3.46e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  88 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 163
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135


                  ....*....
gi 2462560979 164 YLSEQQEKL 172
Cdd:PRK12704  136 LIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 95-197 1.20e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.31  E-value: 1.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  95 KRRIANLIKELARVSEEK---EVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 171
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|....*.
gi 2462560979 172 LTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELA 399
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 83-187 2.91e-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: 42.95  E-value: 2.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  83 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 161
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*.
gi 2462560979 162 QKYLSEQQEKLTmslselgAARMQEQ 187
Cdd:cd16269   268 QEALLEEGFKEQ-------AELLQEE 286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 93-197 3.12e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.77  E-value: 3.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  93 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 172
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100
                  ....*....|....*....|....*
gi 2462560979 173 TMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELE 406
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 36-179 1.23e-03

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: 40.68  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  36 RSRHKLMSPKADVKLKTSRVTDASISMESLKGT-GDSVDEQNSCRGEIKSAslkdlcledKRRIANLIKELARVSEEKEV 114
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTElEDLEKEIKRLELEIEEV---------EARIKKYEEQLGNVRNNKEY 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462560979 115 teERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSEL 179
Cdd:COG1579    92 --EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 92-197 2.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.08  E-value: 2.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  92 LEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 171
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471

                          90       100
                  ....*....|....*....|....*.
gi 2462560979 172 LTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   472 AALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 54-197 2.34e-03

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.20  E-value: 2.34e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979   54 RVTDASISMESLKGTGDSVDEQNScRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEE---RLKAEQESFEKKI 130
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELI 868

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462560979  131 RQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 90-146 3.70e-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: 38.79  E-value: 3.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462560979  90 LCLEDKR-RIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREA 146
Cdd:pfam05266  98 LSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEA 155
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
93-196 3.73e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 3.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  93 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFE---KKIRQLEEQNELIiKEREALQLQYRECQELLSLYQKYLSEQQ 169
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIE 313

                          90       100
                  ....*....|....*....|....*..
gi 2462560979 170 EKLTMSLSELGAARMQEQQVSSRKSTL 196
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERL 340
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 76-191 4.14e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 40.44  E-value: 4.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979   76 NSCRGEIKSASLKDLCLEDKRR-IANLIKELA--RVSEEKEVTE-----ERLKAEQESFEKKIRQLEEQNELIIKEREAL 147
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQeLQEQRIDLKeqIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 2462560979  148 QLQYRECQ----------ELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSS 191
Cdd:TIGR02169  895 EAQLRELErkieeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 45-163 4.42e-03

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: 39.14  E-value: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  45 KADVKLKTSRVTDAsismESLKGTGDSVDEQNSCRGEIKSASLKDLCLEDK-----RRIANLIKELARVSEEKEVTEERL 119
Cdd:COG1579    65 ELEIEEVEARIKKY----EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAEL 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2462560979 120 KAEQESFEKKIRQLEEQNELIIKEREALQLQYREcqELLSLYQK 163
Cdd:COG1579   141 EEKKAELDEELAELEAELEELEAEREELAAKIPP--ELLALYER 182
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 93-197 5.06e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.92  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  93 EDKRRIANL---IKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQE-LLSLYQKYLSEQ 168
Cdd:COG1196   313 ELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEAL 392

                          90       100
                  ....*....|....*....|....*....
gi 2462560979 169 QEKLTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEE 421
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 92-160 7.99e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.82  E-value: 7.99e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462560979  92 LEDKRRIANLIKELARVSEEKEvteERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSL 160
Cdd:pfam20492  29 LEESEETAEELEEERRQAEEEA---ERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIAR 94
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 81-197 8.52e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 8.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  81 EIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE---SFEKKIRQLEEQNELIIKEREALQLQYRECQEL 157
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEE 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2462560979 158 LSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 99-234 8.61e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 38.66  E-value: 8.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  99 ANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQneliikeREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSE 178
Cdd:COG3883   132 ADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA-------KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAE 204

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462560979 179 LGAArmQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASES 234
Cdd:COG3883   205 LAAA--EAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAGAA 258
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
72-197 8.94e-03

Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 38.98  E-value: 8.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  72 VDEQNSCRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELiIKEREALQLQY 151
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAEL 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2462560979 152 RECQELLSLYQKYLSEQQEK-LTMSLSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG4717   173 AELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQ 219
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 96-197 9.12e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.15  E-value: 9.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979  96 RRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMS 175
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100
                  ....*....|....*....|..
gi 2462560979 176 LSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG1196   315 EERLEELEEELAELEEELEELE 336
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
87-160 9.55e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 38.89  E-value: 9.55e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2462560979  87 LKDLCLEDKRRIANLIKELARVSEEKEVTEERLKaEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSL 160
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAK 370
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
96-197 9.65e-03

Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.13  E-value: 9.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462560979   96 RRIANLIKELARvseeKEVTEERLKAEQESFEKKIRQLEEQNELiikEREALQLQYRECQELLSLYQKYLSEQQEKLTMS 175
Cdd:COG4913    338 DRLEQLEREIER----LERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                           90       100
                   ....*....|....*....|..
gi 2462560979  176 LSELGAARMQEQQVSSRKSTLQ 197
Cdd:COG4913    411 EAALRDLRRELRELEAEIASLE 432
 
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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