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Conserved domains on  [gi|1958743550|ref|XP_038952956|]
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protein hinderin isoform X6 [Rattus norvegicus]

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. ...
 173-496 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: 523.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 173 DLCVEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 253 QEKLTMSLSELGAARAQEQQITKKKITHQSSLVNLDGSYLSVAKPQTC-QTRARPKSENQDSASESHTALRNNSLKPVTL 331
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYyQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 332 HHPKQDLERMSTET---RTCTYESPGRRLINAAPVEEALPEELKIKDYPNLLPTPSSQYCGHKYSESEAYVHENyHPTNM 408
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 409 ASQCCKTHPESCSHCRMSWASLMHDGVTLQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQQLLAQQETKLLLKQQQL 488
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1958743550 489 HQSRLDYN 496
Cdd:pfam15369 320 HQSRLDYN 327
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 173-496 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: 523.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 173 DLCVEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 253 QEKLTMSLSELGAARAQEQQITKKKITHQSSLVNLDGSYLSVAKPQTC-QTRARPKSENQDSASESHTALRNNSLKPVTL 331
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYyQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 332 HHPKQDLERMSTET---RTCTYESPGRRLINAAPVEEALPEELKIKDYPNLLPTPSSQYCGHKYSESEAYVHENyHPTNM 408
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 409 ASQCCKTHPESCSHCRMSWASLMHDGVTLQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQQLLAQQETKLLLKQQQL 488
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1958743550 489 HQSRLDYN 496
Cdd:pfam15369 320 HQSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-283 3.52e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 172 KDLCVEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958743550 248 YLSEQQEKLTmSLSELGAARAQEQQI--TKKKITHQSS 283
Cdd:PRK12704  136 LIEEQLQELE-RISGLTAEEAKEILLekVEEEARHEAA 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-288 3.98e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958743550 256 LTMSLSELGAARAQEQQITKKKITHQSSLVNLD 288
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELE 406
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-273 9.12e-04

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: 9.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550  157 AEQSFCKRGLKSASLKDLCVEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958743550  234 QYRECQ----------ELLSLYQKYLSEQQEKLTMSLSELGAARAQEQQI 273
Cdd:TIGR02169  897 QLRELErkieeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 167-273 9.25e-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: 41.41  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 167 KSASLKDLCVEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*...
gi 1958743550 246 QKYLSEQQEKLTmslselgaARAQEQQI 273
Cdd:cd16269   268 QEALLEEGFKEQ--------AELLQEEI 287
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 173-496 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: 523.23  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 173 DLCVEDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 252
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 253 QEKLTMSLSELGAARAQEQQITKKKITHQSSLVNLDGSYLSVAKPQTC-QTRARPKSENQDSASESHTALRNNSLKPVTL 331
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYyQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 332 HHPKQDLERMSTET---RTCTYESPGRRLINAAPVEEALPEELKIKDYPNLLPTPSSQYCGHKYSESEAYVHENyHPTNM 408
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPSSQCCGHRLSESSGSVHES-HPTNM 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 409 ASQCCKTHPESCSHCRMSWASLMHDGVTLQPRETDIEKQLSEDRRQQLMLQKMELEIEKERLQQLLAQQETKLLLKQQQL 488
Cdd:pfam15369 240 APQYSKTHPESCSYCRLSWASGLHGRAALQPGETELKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQL 319


                  ....*...
gi 1958743550 489 HQSRLDYN 496
Cdd:pfam15369 320 HQSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 172-283 3.52e-07

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 52.86  E-value: 3.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 172 KDLCVEDKRRIANLIKELARVSEEKEV----TEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 247
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1958743550 248 YLSEQQEKLTmSLSELGAARAQEQQI--TKKKITHQSS 283
Cdd:PRK12704  136 LIEEQLQELE-RISGLTAEEAKEILLekVEEEARHEAA 172
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-288 3.98e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 179 KRRIANLIKELARVSEEK---EVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1958743550 256 LTMSLSELGAARAQEQQITKKKITHQSSLVNLD 288
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELAAQLEELE 406
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-287 5.66e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.00  E-value: 5.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 256
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1958743550 257 TMSLSELGAARAQEQQITKKKITHQSSLVNL 287
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELEEAEEAL 412
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 157-273 9.12e-04

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: 9.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550  157 AEQSFCKRGLKSASLKDLCVEDKRRIANL---IKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQL 233
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLkeqIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEA 896

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958743550  234 QYRECQ----------ELLSLYQKYLSEQQEKLTMSLSELGAARAQEQQI 273
Cdd:TIGR02169  897 QLRELErkieeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEI 946
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 167-273 9.25e-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: 41.41  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 167 KSASLKDLCVEDKRRIANLIKELARVSEEKEVTEERLKTEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 245
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*...
gi 1958743550 246 QKYLSEQQEKLTmslselgaARAQEQQI 273
Cdd:cd16269   268 QEALLEEGFKEQ--------AELLQEEI 287
COG4026 COG4026
Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General ...
 165-263 1.15e-03

Uncharacterized conserved protein, contains TOPRIM domain, potential nuclease [General function prediction only];


Pssm-ID: 443204 [Multi-domain]  Cd Length: 287  Bit Score: 41.25  E-value: 1.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 165 GLKSASLKDLCVEDKRRIANLIKELARVSEEKE--VTE-ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYrecQEL 241
Cdd:COG4026   120 GLKSLQNIPEYNELREELLELKEKIDEIAKEKEklTKEnEELESELEELREEYKKLREENSILEEEFDNIKSEY---SDL 196

                          90       100
                  ....*....|....*....|..
gi 1958743550 242 LSLYQKYLSEQQEKlTMSLSEL 263
Cdd:COG4026   197 KSRFEELLKKRLLE-VFSLEEL 217
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 180-287 1.18e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.85  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 180 RRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMS 259
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100
                  ....*....|....*....|....*...
gi 1958743550 260 LSELGAARAQEQQITKKKITHQSSLVNL 287
Cdd:COG1196   315 EERLEELEEELAELEEELEELEEELEEL 342
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
177-277 1.77e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFE---KKIRQLEEQNELiIKEREALQLQYRECQELLSLYQKYLSEQQ 253
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEKVKE-LKELKEKAEEYIKLSEFYEEYLDELREIE 313

                          90       100
                  ....*....|....*....|....
gi 1958743550 254 EKLTMSLSELGAARAQEQQITKKK 277
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKE 337
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 167-287 2.27e-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: 2.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 167 KSASLKDLCVEDKRRIANLIKELARvsEEKEVTE-----ERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQEL 241
Cdd:TIGR04523 125 ELNKLEKQKKENKKNIDKFLTEIKK--KEKELEKlnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDKIKNKLLKLELL 202

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1958743550 242 LSLYQKYlSEQQEKLTMSLSELgaaRAQEQQITKKKITHQSSLVNL 287
Cdd:TIGR04523 203 LSNLKKK-IQKNKSLESQISEL---KKQNNQLKDNIEKKQQEINEK 244
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
171-277 2.81e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 2.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 171 LKDLCVEDKRRIANLIKELARVSEEKEVTEERLKtEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQ---- 246
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEAKAKKEeler 376

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958743550 247 -----------------KYLSEQQEKLTMSLSELGAARAQEQQITKKK 277
Cdd:PRK03918  377 lkkrltgltpeklekelEELEKAKEEIEEEISKITARIGELKKEIKEL 424
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 177-275 2.83e-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: 2.83e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 177 EDKRRIANLIKELARVSEEKEVTEER---LKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQ 253
Cdd:COG1196   222 LKELEAELLLLKLRELEAELEELEAEleeLEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLE 301

                          90       100
                  ....*....|....*....|..
gi 1958743550 254 EKLTMSLSELGAARAQEQQITK 275
Cdd:COG1196   302 QDIARLEERRRELEERLEELEE 323
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 177-269 6.28e-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: 38.37  E-value: 6.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550 177 EDKRRIANLIKELARVSEEKEVT-----EERLKTEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSE 251
Cdd:COG1579    70 EVEARIKKYEEQLGNVRNNKEYEalqkeIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDE 149

                          90
                  ....*....|....*...
gi 1958743550 252 QQEKLTMSLSELGAARAQ 269
Cdd:COG1579   150 ELAELEAELEELEAEREE 167
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 170-230 6.68e-03

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


Pssm-ID: 428400 [Multi-domain]  Cd Length: 188  Bit Score: 38.02  E-value: 6.68e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958743550 170 SLKDlcveDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKKIRQLEEQNELIIKEREA 230
Cdd:pfam05266  99 SLKD----RQTKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEA 155
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
180-275 6.93e-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: 6.93e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550  180 RRIANLIKELARvseeKEVTEERLKTEQESFEKKIRQLEEQNELiikEREALQLQYRECQELLSLYQKYLSEQQEKLTMS 259
Cdd:COG4913    338 DRLEQLEREIER----LERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                           90
                   ....*....|....*.
gi 1958743550  260 LSELGAARAQEQQITK 275
Cdd:COG4913    411 EAALRDLRRELRELEA 426
SMC_N pfam02463
RecF/RecN/SMC N terminal domain; This domain is found at the N terminus of SMC proteins. The ...
 180-278 7.90e-03

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


Pssm-ID: 426784 [Multi-domain]  Cd Length: 1161  Bit Score: 39.18  E-value: 7.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958743550  180 RRIANLIKELArVSEEKEVTEERLKTEQESFEKKIRQL-----EEQNELIIKEREALQLQYRECQELLSLYQ------KY 248
Cdd:pfam02463  153 ERRLEIEEEAA-GSRLKRKKKEALKKLIEETENLAELIidleeLKLQELKLKEQAKKALEYYQLKEKLELEEeyllylDY 231

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958743550  249 LSEQQEKLTmSLSELGAARAQEQQITKKKI 278
Cdd:pfam02463  232 LKLNEERID-LLQELLRDEQEEIESSKQEI 260
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
177-255 8.21e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 39.28  E-value: 8.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958743550 177 EDKRRIANLIKELARVSEEKEVTEERLKTEQESFEKkIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 255
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLEKEVKELEELKEE-IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
 
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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