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Conserved domains on  [gi|1720392887|ref|XP_030106282|]
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protein hinderin isoform X7 [Mus musculus]

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. ...
 173-495 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: 549.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1720392887 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 173-495 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: 549.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1720392887 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-275 1.51e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.40  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 172 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                          90       100
                  ....*....|....*....|....*...
gi 1720392887 248 YLSEQQEKLtLSLSELGAARAQEQQITK 275
Cdd:PRK12704  136 LIEEQLQEL-ERISGLTAEEAKEILLEK 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-277 9.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|..
gi 1720392887 256 LTLSLSELGAARAQEQQITKKK 277
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAA 395
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 167-273 2.11e-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: 43.72  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 167 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*...
gi 1720392887 246 QKYLSEQQEKLTlslselgaARAQEQQI 273
Cdd:cd16269   268 QEALLEEGFKEQ--------AELLQEEI 287
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-274 1.05e-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: 42.36  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  157 AEQNFCKRGMKSASLKDLCLEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720392887  234 QYRECQEllslYQKYLSEQQEKLTLSLSELGAAR-AQEQQIT 274
Cdd:TIGR02169  897 QLRELER----KIEELEAQIEKKRKRLSELKAKLeALEEELS 934
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 173-495 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: 549.03  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1720392887 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-275 1.51e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.40  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 172 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                          90       100
                  ....*....|....*....|....*...
gi 1720392887 248 YLSEQQEKLtLSLSELGAARAQEQQITK 275
Cdd:PRK12704  136 LIEEQLQEL-ERISGLTAEEAKEILLEK 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-277 9.14e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 45.70  E-value: 9.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|..
gi 1720392887 256 LTLSLSELGAARAQEQQITKKK 277
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAA 395
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 177-277 1.05e-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: 44.15  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 177 EDKRRIANLIKELARVSEEKEVteERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1579    70 EVEARIKKYEEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147

                          90       100
                  ....*....|....*....|.
gi 1720392887 257 TLSLSELgaaRAQEQQITKKK 277
Cdd:COG1579   148 DEELAEL---EAELEELEAER 165
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-276 2.04e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 2.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100
                  ....*....|....*....|
gi 1720392887 257 TLSLSELGAARAQEQQITKK 276
Cdd:COG1196   382 EELAEELLEALRAAAELAAQ 401
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 167-273 2.11e-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: 43.72  E-value: 2.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 167 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*...
gi 1720392887 246 QKYLSEQQEKLTlslselgaARAQEQQI 273
Cdd:cd16269   268 QEALLEEGFKEQ--------AELLQEEI 287
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-279 2.82e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.90  E-value: 2.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 171 LKDLCLEDKRRIANLIKELARVSEEKEVTEERLKtEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQ---- 246
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEeler 376

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720392887 247 -----------------KYLSEQQEKLTLSLSELGAARAQEQQITKKKNT 279
Cdd:PRK03918  377 lkkrltgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-275 4.04e-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: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 180 RRIANLIKELARVSEEkevtEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG1196   232 LKLRELEAELEELEAE----LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                          90
                  ....*....|....*.
gi 1720392887 260 LSELGAARAQEQQITK 275
Cdd:COG1196   308 EERRRELEERLEELEE 323
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 133-230 5.04e-04

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: 41.49  E-value: 5.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 133 KVKASRVTDASVSMESLKgagDSVAE---QNFCKRGMKSASLKDLCLEDKR-RIANLIKELARVSEEKEVTEERLKTEQE 208
Cdd:pfam05266  57 KVKKLQVDDSRSVFESLM---ESFAElekHGFDVKAPQSRINKLLSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEID 133

                          90       100
                  ....*....|....*....|..
gi 1720392887 209 SFEKKIRQLEEQNELIIKEREA 230
Cdd:pfam05266 134 ELEKKILELERQLALAKEKKEA 155
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
179-284 5.45e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 179 KRRIANLIKELARVSEEKEVTEERL---KTEQESFEKKIRQLEEQNELIIKEREALQlqyrecQELLSLYQKY--LSEQQ 253
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQ------EELESLQEEAeeLQEEL 117

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720392887 254 EKLtlsLSELGAARAQEQQITKKKNTPQCSL 284
Cdd:COG4372   118 EEL---QKERQDLEQQRKQLEAQIAELQSEI 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-272 8.50e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 42.62  E-value: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 179 KRRIANLIKELARVSEEKEVTEER---LKTEQESFEKKIRQLEEQNELIIKEREALQLQYRE--------CQELLSLYQK 247
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeaelaeaEEELEELAEE 387

                          90       100
                  ....*....|....*....|....*
gi 1720392887 248 YLSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEAL 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-274 1.05e-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: 42.36  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  157 AEQNFCKRGMKSASLKDLCLEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1720392887  234 QYRECQEllslYQKYLSEQQEKLTLSLSELGAAR-AQEQQIT 274
Cdd:TIGR02169  897 QLRELER----KIEELEAQIEKKRKRLSELKAKLeALEEELS 934
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 180-277 1.05e-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: 42.27  E-value: 1.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  180 RRIANLIKELArVSEEKEVTEERLKTEQESFEKKIRQL-----EEQNELIIKEREALQLQYRECQELLSLYQ------KY 248
Cdd:pfam02463  153 ERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIidleeLKLQELKLKEQAKKALEYYQLKEKLELEEeyllylDY 231

                           90       100
                   ....*....|....*....|....*....
gi 1720392887  249 LSEQQEKLTLsLSELGAARAQEQQITKKK 277
Cdd:pfam02463  232 LKLNEERIDL-LQELLRDEQEEIESSKQE 259
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-278 1.23e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.97  E-value: 1.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 163 KRGMKSASLKDLcLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFE---KKIRQLEEQneliIKEREALQLQYRECQ 239
Cdd:PRK03918  222 ELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEK----VKELKELKEKAEEYI 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1720392887 240 ELLSLYQKYLSEQQ--EKLTLSLSELGAA-RAQEQQITKKKN 278
Cdd:PRK03918  297 KLSEFYEEYLDELReiEKRLSRLEEEINGiEERIKELEEKEE 338
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-279 2.05e-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: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQ-NELIIKEREALQLQYRECQELLSLyQKYLSEQQE 254
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEEEAL-LELLAELLE 470

                          90       100
                  ....*....|....*....|....*
gi 1720392887 255 KLTLSLSELGAARAQEQQITKKKNT 279
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLL 495
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-324 2.05e-03

helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.


Pssm-ID: 275316 [Multi-domain]  Cd Length: 745  Bit Score: 41.16  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 167 KSASLKDLCLEDKRRIANLIKELARvsEEKEVTE-----ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQEL 241
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKK--KEKELEKlnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 242 LSLYQKYlSEQQEKLTLSLSELgaaRAQEQQITKKKNTPQCSLMDLDGSFLSVArpQNYGQTK-ARPKSANQVSESFTEL 320
Cdd:TIGR04523 203 LSNLKKK-IQKNKSLESQISEL---KKQNNQLKDNIEKKQQEINEKTTEISNTQ--TQLNQLKdEQNKIKKQLSEKQKEL 276


                  ....
gi 1720392887 321 RNNS 324
Cdd:TIGR04523 277 EQNN 280
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
177-255 2.41e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.41e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720392887 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKkIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-275 2.71e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 41.05  E-value: 2.71e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  180 RRIANLIKELARvseeKEVTEERLKTEQESFEKKIRQLEEQNELiikEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG4913    338 DRLEQLEREIER----LERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                           90
                   ....*....|....*.
gi 1720392887  260 LSELGAARAQEQQITK 275
Cdd:COG4913    411 EAALRDLRRELRELEA 426
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 171-244 3.91e-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: 3.91e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720392887 171 LKDLCLEDKRrianLIKELARVseEKEvtEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQ-ELLSL 244
Cdd:pfam17675  50 LEKLEKEEEE----LLQELEEL--EKE--REELDAELEALEEELEALDEEEEEFWREYNALQLQLLEFQdERDSL 116
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-276 5.19e-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: 5.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          90       100
                  ....*....|....*....|.
gi 1720392887 256 LTLSLSELGAARAQEQQITKK 276
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLEL 464
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-275 5.69e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.90  E-value: 5.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  180 RRIANLIKELARVSEEKEVTEErLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG4913    668 REIAELEAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                           90
                   ....*....|....*.
gi 1720392887  260 LSELGAARAQEQQITK 275
Cdd:COG4913    747 LRALLEERFAAALGDA 762
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-273 6.32e-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: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQE---SFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          90       100
                  ....*....|....*....|.
gi 1720392887 253 QEKLTLSLSELGAARAQEQQI 273
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEA 377
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
177-274 6.33e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 177 EDKRRIANLIKELARVSEEKEvteeRLKTEQESFEKKIRQLEEQNEL--IIKEREALQLQYRECQELL-SLYQKY----- 248
Cdd:COG4717    85 EKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLeELEERLeelre 160

                          90       100
                  ....*....|....*....|....*.
gi 1720392887 249 LSEQQEKLTLSLSELGAARAQEQQIT 274
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQL 186
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
177-272 6.92e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 39.51  E-value: 6.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  177 EDKRRIANLIKELARVSEEKEVTE---ERLKTEQESFEKKIRQLEEQN--------ELIIKEREALQLQYRECQELLSLY 245
Cdd:COG4913    285 FAQRRLELLEAELEELRAELARLEaelERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARL 364

                           90       100
                   ....*....|....*....|....*..
gi 1720392887  246 QKYLSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAA 391
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-273 7.08e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.66  E-value: 7.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 171 LKDLCLEDKRRIANLIKELARvseeKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKyLS 250
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKR----TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-IE 241

                          90       100
                  ....*....|....*....|...
gi 1720392887 251 EQQEKLtlsLSELGAARAQEQQI 273
Cdd:PRK03918  242 ELEKEL---ESLEGSKRKLEEKI 261
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-278 7.59e-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: 39.65  E-value: 7.59e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  179 KRRIANLIKELARVSEEKEVTE----------ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKY 248
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELEskldelaeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                           90       100       110
                   ....*....|....*....|....*....|
gi 1720392887  249 LSEQQEKLTLSLSELGAARAQEQQITKKKN 278
Cdd:TIGR02168  388 VAQLELQIASLNNEIERLEARLERLEDRRE 417
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 169-272 7.85e-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: 39.65  E-value: 7.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887  169 ASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELlslyQKY 248
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL----EAQ 790

                           90       100
                   ....*....|....*....|....
gi 1720392887  249 LSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTL 814
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
177-272 8.05e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.12  E-value: 8.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720392887 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEE-QNELIIKEREALQLQyRECQELLSLYQKyLSEQQEK 255
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaQEELESLQEEAEELQ-EELEELQKERQD-LEQQRKQ 133

                          90
                  ....*....|....*..
gi 1720392887 256 LTLSLSELGAARAQEQQ 272
Cdd:COG4372   134 LEAQIAELQSEIAEREE 150
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 176-244 9.29e-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: 36.43  E-value: 9.29e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720392887 176 LEDKRRIANLIKELARVSEEKEvteERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSL 244
Cdd:pfam20492  29 LEESEETAEELEEERRQAEEEA---ERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIAR 94
 
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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