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Conserved domains on  [gi|1907129524|ref|XP_036016989|]
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protein hinderin isoform X9 [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: 551.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1907129524 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: 551.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1907129524 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-275 1.70e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.01  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 172 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                          90       100
                  ....*....|....*....|....*...
gi 1907129524 248 YLSEQQEKLtLSLSELGAARAQEQQITK 275
Cdd:PRK12704  136 LIEEQLQEL-ERISGLTAEEAKEILLEK 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-277 9.30e-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: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|..
gi 1907129524 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 1.68e-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: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 167 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*...
gi 1907129524 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 1.31e-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: 41.98  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  157 AEQNFCKRGMKSASLKDLCLEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907129524  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: 551.35  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 173 DLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 253 QEKLTLSLSELGAARAQEQQITKKKNTPQCSLMDLDGSFLSVARPQNYGQTKARPKSANQ--VSESFTELRNNSLRPITL 330
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQdsASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 331 HHPKEDLERMSTKT---RTCTYESLGRRLINAAPIEKSLPVELKIKEYPNLPPTPSSQYCGHKCSESGAYVHENyHPTNM 407
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 408 APQCCKTHPESCSHCRIPWASQMHDRVILQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQL 487
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1907129524 488 HQSRLDYN 495
Cdd:pfam15369 320 HQSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-275 1.70e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 54.01  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 172 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                          90       100
                  ....*....|....*....|....*...
gi 1907129524 248 YLSEQQEKLtLSLSELGAARAQEQQITK 275
Cdd:PRK12704  136 LIEEQLQEL-ERISGLTAEEAKEILLEK 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-277 9.30e-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: 9.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|..
gi 1907129524 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 1.16e-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: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 177 EDKRRIANLIKELARVSEEKEVteERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1579    70 EVEARIKKYEEQLGNVRNNKEY--EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAEL 147

                          90       100
                  ....*....|....*....|.
gi 1907129524 257 TLSLSELgaaRAQEQQITKKK 277
Cdd:COG1579   148 DEELAEL---EAELEELEAER 165
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 167-273 1.68e-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: 1.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 167 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*...
gi 1907129524 246 QKYLSEQQEKLTlslselgaARAQEQQI 273
Cdd:cd16269   268 QEALLEEGFKEQ--------AELLQEEI 287
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-276 2.02e-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: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100
                  ....*....|....*....|
gi 1907129524 257 TLSLSELGAARAQEQQITKK 276
Cdd:COG1196   382 EELAEELLEALRAAAELAAQ 401
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-279 3.59e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 43.51  E-value: 3.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 171 LKDLCLEDKRRIANLIKELARVSEEKEVTEERLKtEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQ---- 246
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEeler 376

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907129524 247 -----------------KYLSEQQEKLTLSLSELGAARAQEQQITKKKNT 279
Cdd:PRK03918  377 lkkrltgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKELKK 426
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-275 4.11e-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: 4.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 180 RRIANLIKELARVSEEkevtEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG1196   232 LKLRELEAELEELEAE----LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARL 307

                          90
                  ....*....|....*.
gi 1907129524 260 LSELGAARAQEQQITK 275
Cdd:COG1196   308 EERRRELEERLEELEE 323
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 133-230 4.39e-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: 4.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 133 KVKASRVTDASVSMESLKgagDSVAE---QNFCKRGMKSASLKDLCLEDKR-RIANLIKELARVSEEKEVTEERLKTEQE 208
Cdd:pfam05266  57 KVKKLQVDDSRSVFESLM---ESFAElekHGFDVKAPQSRINKLLSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEID 133

                          90       100
                  ....*....|....*....|..
gi 1907129524 209 SFEKKIRQLEEQNELIIKEREA 230
Cdd:pfam05266 134 ELEKKILELERQLALAKEKKEA 155
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
179-284 6.02e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.58  E-value: 6.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 179 KRRIANLIKELARVSEEKEVTEERL---KTEQESFEKKIRQLEEQNELIIKEREALQlqyrecQELLSLYQKY--LSEQQ 253
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQ------EELESLQEEAeeLQEEL 117

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907129524 254 EKLtlsLSELGAARAQEQQITKKKNTPQCSL 284
Cdd:COG4372   118 EEL---QKERQDLEQQRKQLEAQIAELQSEI 145
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-272 8.65e-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: 8.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 179 KRRIANLIKELARVSEEKEVTEER---LKTEQESFEKKIRQLEEQNELIIKEREALQLQYRE--------CQELLSLYQK 247
Cdd:COG1196   308 EERRRELEERLEELEEELAELEEEleeLEEELEELEEELEEAEEELEEAEAELAEAEEALLEaeaelaeaEEELEELAEE 387

                          90       100
                  ....*....|....*....|....*
gi 1907129524 248 YLSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:COG1196   388 LLEALRAAAELAAQLEELEEAEEAL 412
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 180-277 1.24e-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: 41.88  E-value: 1.24e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  180 RRIANLIKELArVSEEKEVTEERLKTEQESFEKKIRQL-----EEQNELIIKEREALQLQYRECQELLSLYQ------KY 248
Cdd:pfam02463  153 ERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIidleeLKLQELKLKEQAKKALEYYQLKEKLELEEeyllylDY 231

                           90       100
                   ....*....|....*....|....*....
gi 1907129524  249 LSEQQEKLTLsLSELGAARAQEQQITKKK 277
Cdd:pfam02463  232 LKLNEERIDL-LQELLRDEQEEIESSKQE 259
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-274 1.31e-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: 41.98  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  157 AEQNFCKRGMKSASLKDLCLEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907129524  234 QYRECQEllslYQKYLSEQQEKLTLSLSELGAAR-AQEQQIT 274
Cdd:TIGR02169  897 QLRELER----KIEELEAQIEKKRKRLSELKAKLeALEEELS 934
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
163-278 1.70e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.59  E-value: 1.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 163 KRGMKSASLKDLcLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFE---KKIRQLEEQneliIKEREALQLQYRECQ 239
Cdd:PRK03918  222 ELEKLEKEVKEL-EELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEK----VKELKELKEKAEEYI 296

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907129524 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 2.10e-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: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQ-NELIIKEREALQLQYRECQELLSLyQKYLSEQQE 254
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEEEAL-LELLAELLE 470

                          90       100
                  ....*....|....*....|....*
gi 1907129524 255 KLTLSLSELGAARAQEQQITKKKNT 279
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLL 495
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
177-255 2.87e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.82  E-value: 2.87e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907129524 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKkIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-324 2.92e-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: 40.77  E-value: 2.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 167 KSASLKDLCLEDKRRIANLIKELARvsEEKEVTE-----ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQEL 241
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKK--KEKELEKlnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 242 LSLYQKYlSEQQEKLTLSLSELgaaRAQEQQITKKKNTPQCSLMDLDGSFLSVArpQNYGQTK-ARPKSANQVSESFTEL 320
Cdd:TIGR04523 203 LSNLKKK-IQKNKSLESQISEL---KKQNNQLKDNIEKKQQEINEKTTEISNTQ--TQLNQLKdEQNKIKKQLSEKQKEL 276


                  ....
gi 1907129524 321 RNNS 324
Cdd:TIGR04523 277 EQNN 280
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-275 3.03e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.67  E-value: 3.03e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  180 RRIANLIKELARvseeKEVTEERLKTEQESFEKKIRQLEEQNELiikEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG4913    338 DRLEQLEREIER----LERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                           90
                   ....*....|....*.
gi 1907129524  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 3.12e-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: 3.12e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907129524 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 5.20e-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: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   364 EEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEA 443

                          90       100
                  ....*....|....*....|.
gi 1907129524 256 LTLSLSELGAARAQEQQITKK 276
Cdd:COG1196   444 LEEAAEEEAELEEEEEALLEL 464
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
177-274 5.88e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 5.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 177 EDKRRIANLIKELARVSEEKEvteeRLKTEQESFEKKIRQLEEQNEL--IIKEREALQLQYRECQELL-SLYQKY----- 248
Cdd:COG4717    85 EKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLlpLYQELEALEAELAELPERLeELEERLeelre 160

                          90       100
                  ....*....|....*....|....*.
gi 1907129524 249 LSEQQEKLTLSLSELGAARAQEQQIT 274
Cdd:COG4717   161 LEEELEELEAELAELQEELEELLEQL 186
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-275 6.05e-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: 6.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  180 RRIANLIKELARVSEEKEVTEErLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTLS 259
Cdd:COG4913    668 REIAELEAELERLDASSDDLAA-LEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLE 746

                           90
                   ....*....|....*.
gi 1907129524  260 LSELGAARAQEQQITK 275
Cdd:COG4913    747 LRALLEERFAAALGDA 762
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 176-273 6.33e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 39.53  E-value: 6.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 176 LEDKRRIANLIKELARVSEEKEVTEERLKTEQE---SFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:COG1196   277 EELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356

                          90       100
                  ....*....|....*....|.
gi 1907129524 253 QEKLTLSLSELGAARAQEQQI 273
Cdd:COG1196   357 EAELAEAEEALLEAEAELAEA 377
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
177-272 7.75e-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: 7.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  177 EDKRRIANLIKELARVSEEKEVTE---ERLKTEQESFEKKIRQLEEQN--------ELIIKEREALQLQYRECQELLSLY 245
Cdd:COG4913    285 FAQRRLELLEAELEELRAELARLEaelERLEARLDALREELDELEAQIrgnggdrlEQLEREIERLERELEERERRRARL 364

                           90       100
                   ....*....|....*....|....*..
gi 1907129524  246 QKYLSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:COG4913    365 EALLAALGLPLPASAEEFAALRAEAAA 391
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 179-278 7.81e-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: 39.27  E-value: 7.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  179 KRRIANLIKELARVSEEKEVTE----------ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKY 248
Cdd:TIGR02168  308 RERLANLERQLEELEAQLEELEskldelaeelAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSK 387

                           90       100       110
                   ....*....|....*....|....*....|
gi 1907129524  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 7.94e-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: 39.27  E-value: 7.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  169 ASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELlslyQKY 248
Cdd:TIGR02168  715 EQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL----EAQ 790

                           90       100
                   ....*....|....*....|....
gi 1907129524  249 LSEQQEKLTLSLSELGAARAQEQQ 272
Cdd:TIGR02168  791 IEQLKEELKALREALDELRAELTL 814
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 167-259 8.13e-03

exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129705 [Multi-domain]  Cd Length: 1042  Bit Score: 39.18  E-value: 8.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524  167 KSASLKDLCLEDKR-----RIANLIKELARVSEEkevteerLKTEQESFEKKIRQLEEQNELIIKEREALQLQyRECQEL 241
Cdd:TIGR00618  201 LRSQLLTLCTPCMPdtyheRKQVLEKELKHLREA-------LQQTQQSHAYLTQKREAQEEQLKKQQLLKQLR-ARIEEL 272

                           90
                   ....*....|....*...
gi 1907129524  242 LSLyQKYLSEQQEKLTLS 259
Cdd:TIGR00618  273 RAQ-EAVLEETQERINRA 289
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-273 9.33e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 9.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 171 LKDLCLEDKRRIANLIKELARvseeKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKyLS 250
Cdd:PRK03918  167 LGEVIKEIKRRIERLEKFIKR----TENIEELIKEKEKELEEVLREINEISSELPELREELEKLEKEVKELEELKEE-IE 241

                          90       100
                  ....*....|....*....|...
gi 1907129524 251 EQQEKLtlsLSELGAARAQEQQI 273
Cdd:PRK03918  242 ELEKEL---ESLEGSKRKLEEKI 261
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
177-272 9.38e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 38.73  E-value: 9.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907129524 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEE-QNELIIKEREALQLQyRECQELLSLYQKyLSEQQEK 255
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaQEELESLQEEAEELQ-EELEELQKERQD-LEQQRKQ 133

                          90
                  ....*....|....*..
gi 1907129524 256 LTLSLSELGAARAQEQQ 272
Cdd:COG4372   134 LEAQIAELQSEIAEREE 150
 
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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