NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|530413895|ref|XP_005258375|]
View 

protein hinderin isoform X4 [Homo sapiens]

Protein Classification

KIAA1328 domain-containing protein( domain architecture ID 10634053)

KIAA1328 domain-containing protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
48-365 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: 542.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895   48 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 127
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  128 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 207
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  208 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 279
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  280 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 358
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320

                  ....*..
gi 530413895  359 QSRLDYN 365
Cdd:pfam15369 321 QSRLDYN 327
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
48-365 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: 542.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895   48 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 127
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  128 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 207
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  208 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 279
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  280 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 358
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320

                  ....*..
gi 530413895  359 QSRLDYN 365
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
47-131 3.84e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  47 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 122
Cdd:PRK12704  56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                 ....*....
gi 530413895 123 YLSEQQEKL 131
Cdd:PRK12704 136 LIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
54-156 1.50e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  54 KRRIANLIKELARVSEEK---EVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 130
Cdd:COG1196  294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         90       100
                 ....*....|....*....|....*.
gi 530413895 131 LTMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELA 399
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
42-146 5.04e-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: 42.18  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  42 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 120
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267
                         90       100
                 ....*....|....*....|....*.
gi 530413895 121 QKYLSEQQEKLTmslselgAARMQEQ 146
Cdd:cd16269  268 QEALLEEGFKEQ-------AELLQEE 286
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
13-156 3.05e-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: 40.43  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895    13 RVTDASISMESLKGTGDSVDEQNScRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEE---RLKAEQESFEKKI 89
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELI 868
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413895    90 RQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
48-365 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: 542.10  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895   48 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 127
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  128 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSIARPQTYYQTKQRPKSAVQDSASESLIAFRNNSLKPVTL 207
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  208 HHPKDDLDKIPSET---TTCNCESPGRKP--AVPTEKMPQEELHMKECPHLKPTPS-QCCGHRLA--ADRVHDSHPTNMT 279
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQrdAHPTEKAPEEELKAKECPHLGPPPSsQCCGHRLSesSGSVHESHPTNMA 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  280 PQHPKTHPESCSYCRLSWASLVHGGGALQPIET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 358
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320

                  ....*..
gi 530413895  359 QSRLDYN 365
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
47-131 3.84e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 49.78  E-value: 3.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  47 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 122
Cdd:PRK12704  56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                 ....*....
gi 530413895 123 YLSEQQEKL 131
Cdd:PRK12704 136 LIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
54-156 1.50e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.93  E-value: 1.50e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  54 KRRIANLIKELARVSEEK---EVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 130
Cdd:COG1196  294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373
                         90       100
                 ....*....|....*....|....*.
gi 530413895 131 LTMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:COG1196  374 LAEAEEELEELAEELLEALRAAAELA 399
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
52-156 3.76e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  52 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 131
Cdd:COG1196  302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
                         90       100
                 ....*....|....*....|....*
gi 530413895 132 TMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:COG1196  382 EELAEELLEALRAAAELAAQLEELE 406
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
42-146 5.04e-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: 42.18  E-value: 5.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  42 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 120
Cdd:cd16269  191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267
                         90       100
                 ....*....|....*....|....*.
gi 530413895 121 QKYLSEQQEKLTmslselgAARMQEQ 146
Cdd:cd16269  268 QEALLEEGFKEQ-------AELLQEE 286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
51-156 2.49e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 40.69  E-value: 2.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  51 LEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 130
Cdd:COG1196  392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEE 471
                         90       100
                 ....*....|....*....|....*.
gi 530413895 131 LTMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:COG1196  472 AALLEAALAELLEELAEAAARLLLLL 497
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
13-156 3.05e-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: 40.43  E-value: 3.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895    13 RVTDASISMESLKGTGDSVDEQNScRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEE---RLKAEQESFEKKI 89
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELI 868
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530413895    90 RQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
52-138 3.61e-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: 3.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  52 EDKRRIANLIKELARVSEEKEVteERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 131
Cdd:COG1579   70 EVEARIKKYEEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147

                 ....*..
gi 530413895 132 TMSLSEL 138
Cdd:COG1579  148 DEELAEL 154
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
49-105 4.02e-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: 4.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530413895   49 LCLEDKR-RIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREA 105
Cdd:pfam05266  98 LSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEA 155
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
35-150 5.58e-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: 39.67  E-value: 5.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895    35 NSCRGEIKSASLKDLCLEDKRR-IANLIKELA--RVSEEKEVTE-----ERLKAEQESFEKKIRQLEEQNELIIKEREAL 106
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQeLQEQRIDLKeqIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDEL 894
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 530413895   107 QLQYRECQ----------ELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSS 150
Cdd:TIGR02169  895 EAQLRELErkieeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
52-155 5.77e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 5.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  52 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFE---KKIRQLEEQNELIiKEREALQLQYRECQELLSLYQKYLSEQQ 128
Cdd:PRK03918 235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIE 313
                         90       100
                 ....*....|....*....|....*..
gi 530413895 129 EKLTMSLSELGAARMQEQQVSSRKSTL 155
Cdd:PRK03918 314 KRLSRLEEEINGIEERIKELEEKEERL 340
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
52-156 5.81e-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: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895  52 EDKRRIANL---IKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQE-LLSLYQKYLSEQ 127
Cdd:COG1196  313 ELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEAL 392
                         90       100
                 ....*....|....*....|....*....
gi 530413895 128 QEKLTMSLSELGAARMQEQQVSSRKSTLQ 156
Cdd:COG1196  393 RAAAELAAQLEELEEAEEALLERLERLEE 421
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
4-122 8.42e-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: 37.98  E-value: 8.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530413895   4 KADVKLKTSRVTDAsismESLKGTGDSVDEQNSCRGEIKSASLKDLCLEDK-----RRIANLIKELARVSEEKEVTEERL 78
Cdd:COG1579   65 ELEIEEVEARIKKY----EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAEL 140
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 530413895  79 KAEQESFEKKIRQLEEQNELIIKEREALQLQYREcqELLSLYQK 122
Cdd:COG1579  141 EEKKAELDEELAELEAELEELEAEREELAAKIPP--ELLALYER 182
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH