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Conserved domains on  [gi|1622889542|ref|XP_014977224|]
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protein hinderin isoform X1 [Macaca mulatta]

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. ...
 175-494 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: 566.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 175 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 254
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 255 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSVARPQTYYQTKQRPKSAIQDSASESLIAFRNNSLKPVTL 334
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 335 HHPKDDLGKIPSET---TTCNYESPGRKPVDAVPTEKMPQEELHMKECPHLKPTP-TQCCGHRLA--ADHVHESHSTNTA 408
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPsSQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 409 PQHPKTHPESCSYCGLSWASLLHGGGALQPNET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 487
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 1622889542 488 QSRLDYN 494
Cdd:pfam15369 321 QSRLDYN 327
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 175-494 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: 566.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 175 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 254
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 255 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSVARPQTYYQTKQRPKSAIQDSASESLIAFRNNSLKPVTL 334
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 335 HHPKDDLGKIPSET---TTCNYESPGRKPVDAVPTEKMPQEELHMKECPHLKPTP-TQCCGHRLA--ADHVHESHSTNTA 408
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPsSQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 409 PQHPKTHPESCSYCGLSWASLLHGGGALQPNET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 487
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 1622889542 488 QSRLDYN 494
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 174-258 1.87e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.93  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 174 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 249
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135


                  ....*....
gi 1622889542 250 YLSEQQEKL 258
Cdd:PRK12704  136 LIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-283 8.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 181 KRRIANLIKELARVSEEK---EVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 257
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|....*.
gi 1622889542 258 LTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELA 399
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 169-273 9.19e-05

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: 44.88  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 169 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 247
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*.
gi 1622889542 248 QKYLSEQQEKLTmslselgAARMQEQ 273
Cdd:cd16269   268 QEALLEEGFKEQ-------AELLQEE 286
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 158-289 1.07e-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: 42.31  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 158 VDEQNSCRGEIKSASLKDLCLEDKRRIANLIKELARvsEEKEVTE-----ERLKAEQESFEKKIRQLEEQNELIIKEREA 232
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK--KEKELEKlnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDK 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622889542 233 LQLQYRECQELLSLYQKYlSEQQEKLTMSLSELgaarmqEQQVSSRKSTLQCSSVEL 289
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKK-IQKNKSLESQISEL------KKQNNQLKDNIEKKQQEI 241
 
Name Accession Description Interval E-value
KIAA1328 pfam15369
Uncharacterized protein KIAA1328; This function of this protein family remains uncharacterized. ...
 175-494 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: 566.75  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 175 DLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQ 254
Cdd:pfam15369   1 DLCPEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQQQYRECQELLSLYQKYLSEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 255 QEKLTMSLSELGAARMQEQQVSSRKSTLQCSSVELDGSYLSVARPQTYYQTKQRPKSAIQDSASESLIAFRNNSLKPVTL 334
Cdd:pfam15369  81 QEKLTMSLSELSAARMQEQQVSNKKSTLQPSSVELDGSYLSVAGPQTYYQTKRRPKSANQDSASESFYERRNNSLKPATL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 335 HHPKDDLGKIPSET---TTCNYESPGRKPVDAVPTEKMPQEELHMKECPHLKPTP-TQCCGHRLA--ADHVHESHSTNTA 408
Cdd:pfam15369 161 HNPKEDLDRLPSETglhRTCNYESSGRKQRDAHPTEKAPEEELKAKECPHLGPPPsSQCCGHRLSesSGSVHESHPTNMA 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 409 PQHPKTHPESCSYCGLSWASLLHGGGALQPNET-LKKQISEDRKQQLMLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 487
Cdd:pfam15369 241 PQYSKTHPESCSYCRLSWASGLHGRAALQPGETeLKKQLSEDRRQQLLLQKMELEIEKERLQHLLAQQETKLLLKQQQLH 320


                  ....*..
gi 1622889542 488 QSRLDYN 494
Cdd:pfam15369 321 QSRLDYN 327
PRK12704 PRK12704
phosphodiesterase; Provisional
 174-258 1.87e-06

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 50.93  E-value: 1.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 174 KDLCLEDKRRIANLIKELARVSEEKEV----TEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQK 249
Cdd:PRK12704   56 KEALLEAKEEIHKLRNEFEKELRERRNelqkLEKRLLQKEENLDRKLELLEKREEELEKKEKELEQKQQELEKKEEELEE 135


                  ....*....
gi 1622889542 250 YLSEQQEKL 258
Cdd:PRK12704  136 LIEEQLQEL 144
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 181-283 8.21e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.08  E-value: 8.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 181 KRRIANLIKELARVSEEK---EVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 257
Cdd:COG1196   294 LAELARLEQDIARLEERRrelEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAE 373

                          90       100
                  ....*....|....*....|....*.
gi 1622889542 258 LTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   374 LAEAEEELEELAEELLEALRAAAELA 399
GBP_C cd16269
Guanylate-binding protein, C-terminal domain; Guanylate-binding protein (GBP), C-terminal ...
 169-273 9.19e-05

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: 44.88  E-value: 9.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 169 KSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE-SFEKKIRQLEEQNEliiKEREALQLQYRECQELLSLY 247
Cdd:cd16269   191 QALTEKEKEIEAERAKAEAAEQERKLLEEQQRELEQKLEDQErSYEEHLRQLKEKME---EERENLLKEQERALESKLKE 267

                          90       100
                  ....*....|....*....|....*.
gi 1622889542 248 QKYLSEQQEKLTmslselgAARMQEQ 273
Cdd:cd16269   268 QEALLEEGFKEQ-------AELLQEE 286
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-283 2.30e-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: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 179 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKL 258
Cdd:COG1196   302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381

                          90       100
                  ....*....|....*....|....*
gi 1622889542 259 TMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   382 EELAEELLEALRAAAELAAQLEELE 406
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 122-265 5.96e-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: 41.83  E-value: 5.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 122 RSRHKLTSPKADVKLKTSRATDASISMESLKGT-GDSVDEQNSCRGEIKSAslkdlcledKRRIANLIKELARVSEEKEV 200
Cdd:COG1579    21 RLEHRLKELPAELAELEDELAALEARLEAAKTElEDLEKEIKRLELEIEEV---------EARIKKYEEQLGNVRNNKEY 91

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622889542 201 teERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSEL 265
Cdd:COG1579    92 --EALQKEIESLKRRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAEL 154
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
179-282 9.48e-04

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 42.74  E-value: 9.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 179 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFE---KKIRQLEEQNELIiKEREALQLQYRECQELLSLYQKYLSEQQ 255
Cdd:PRK03918  235 ELKEEIEELEKELESLEGSKRKLEEKIRELEERIEelkKEIEELEEKVKEL-KELKEKAEEYIKLSEFYEEYLDELREIE 313

                          90       100
                  ....*....|....*....|....*..
gi 1622889542 256 EKLTMSLSELGAARMQEQQVSSRKSTL 282
Cdd:PRK03918  314 KRLSRLEEEINGIEERIKELEEKEERL 340
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
181-283 9.94e-04

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 42.20  E-value: 9.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 181 KRRIANLIKELARVSEEKEVTEERL---KAEQESFEKKIRQLEEQNELIIKEREALQlqyrecQELLSLYQKY--LSEQQ 255
Cdd:COG4372    44 QEELEQLREELEQAREELEQLEEELeqaRSELEQLEEELEELNEQLQAAQAELAQAQ------EELESLQEEAeeLQEEL 117

                          90       100
                  ....*....|....*....|....*...
gi 1622889542 256 EKLtmsLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG4372   118 EEL---QKERQDLEQQRKQLEAQIAELQ 142
Mplasa_alph_rch TIGR04523
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ...
 158-289 1.07e-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: 42.31  E-value: 1.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 158 VDEQNSCRGEIKSASLKDLCLEDKRRIANLIKELARvsEEKEVTE-----ERLKAEQESFEKKIRQLEEQNELIIKEREA 232
Cdd:TIGR04523 114 NDKEQKNKLEVELNKLEKQKKENKKNIDKFLTEIKK--KEKELEKlnnkyNDLKKQKEELENELNLLEKEKLNIQKNIDK 191

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622889542 233 LQLQYRECQELLSLYQKYlSEQQEKLTMSLSELgaarmqEQQVSSRKSTLQCSSVEL 289
Cdd:TIGR04523 192 IKNKLLKLELLLSNLKKK-IQKNKSLESQISEL------KKQNNQLKDNIEKKQQEI 241
DR0291 COG1579
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ...
 131-249 1.19e-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: 41.06  E-value: 1.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 131 KADVKLKTSRATDAsismESLKGTGDSVDEQNSCRGEIKSASLKDLCLEDK-----RRIANLIKELARVSEEKEVTEERL 205
Cdd:COG1579    65 ELEIEEVEARIKKY----EEQLGNVRNNKEYEALQKEIESLKRRISDLEDEilelmERIEELEEELAELEAELAELEAEL 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1622889542 206 KAEQESFEKKIRQLEEQNELIIKEREAL--QLQyrecQELLSLYQK 249
Cdd:COG1579   141 EEKKAELDEELAELEAELEELEAEREELaaKIP----PELLALYER 182
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 162-277 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: 42.36  E-value: 1.31e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  162 NSCRGEIKSASLKDLCLEDKRR-IANLIKELA--RVSEEKEVTE-----ERLKAEQESFEKKIRQLEEQNELIIKEREAL 233
Cdd:TIGR02169  815 REIEQKLNRLTLEKEYLEKEIQeLQEQRIDLKeqIKSIEKEIENlngkkEELEEELEELEAALRDLESRLGDLKKERDEL 894

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1622889542  234 QLQYRECQ----------ELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSS 277
Cdd:TIGR02169  895 EAQLRELErkieeleaqiEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPE 948
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 178-283 1.49e-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: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 178 LEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQ-NELIIKEREALQLQYRECQELLSLyQKYLSEQQE 256
Cdd:COG1196   392 LRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEeEEEEEALEEAAEEEAELEEEEEAL-LELLAELLE 470

                          90       100
                  ....*....|....*....|....*..
gi 1622889542 257 KLTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   471 EAALLEAALAELLEELAEAAARLLLLL 497
APG6_N pfam17675
Apg6 coiled-coil region; In yeast, 15 Apg proteins coordinate the formation of autophagosomes. ...
 173-246 1.58e-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: 39.12  E-value: 1.58e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622889542 173 LKDLCLEDKRrianLIKELARVseEKEvtEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQ-ELLSL 246
Cdd:pfam17675  50 LEKLEKEEEE----LLQELEEL--EKE--REELDAELEALEEELEALDEEEEEFWREYNALQLQLLEFQdERDSL 116
DUF724 pfam05266
Protein of unknown function (DUF724); This family contains several uncharacterized proteins ...
 176-232 1.74e-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: 39.95  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622889542 176 LCLEDKR-RIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREA 232
Cdd:pfam05266  98 LSLKDRQtKLLEELKKLEKKIAEEESEKRKLEEEIDELEKKILELERQLALAKEKKEA 155
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 178-246 2.10e-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: 38.75  E-value: 2.10e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622889542 178 LEDKRRIANLIKELARVSEEKEvteERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSL 246
Cdd:pfam20492  29 LEESEETAEELEEERRQAEEEA---ERLEQKRQEAEEEKERLEESAEMEAEEKEQLEAELAEAQEEIAR 94
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 140-283 2.13e-03

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


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 41.58  E-value: 2.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  140 RATDASISMESLKGTGDSVDEQNScRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEE---RLKAEQESFEKKI 216
Cdd:TIGR02168  790 QIEQLKEELKALREALDELRAELT-LLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEdieSLAAEIEELEELI 868

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622889542  217 RQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:TIGR02168  869 EELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLE 935
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
173-283 2.51e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 41.20  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 173 LKDLCLEDKRRIANLIKELARVSEEKEVTEERLKaEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELlslyqKYLS 252
Cdd:PRK03918  298 LSEFYEEYLDELREIEKRLSRLEEEINGIEERIK-ELEEKEERLEELKKKLKELEKRLEELEERHELYEEA-----KAKK 371

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1622889542 253 EQQEKLTMSLSELGAARMQE--QQVSSRKSTLQ 283
Cdd:PRK03918  372 EELERLKKRLTGLTPEKLEKelEELEKAKEEIE 404
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 179-283 3.18e-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: 3.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 179 EDKRRIANL---IKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQE-LLSLYQKYLSEQ 254
Cdd:COG1196   313 ELEERLEELeeeLAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEeLEELAEELLEAL 392

                          90       100
                  ....*....|....*....|....*....
gi 1622889542 255 QEKLTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   393 RAAAELAAQLEELEEAEEALLERLERLEE 421
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
158-283 4.21e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 4.21e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 158 VDEQNSCRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELiIKEREALQLQY 237
Cdd:COG4717    94 QEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERLEELEERLEELREL-EEELEELEAEL 172

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622889542 238 RECQELLSLYQKYLSEQQEK-LTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG4717   173 AELQEELEELLEQLSLATEEeLQDLAEELEELQQRLAELEEELEEAQ 219
COG4372 COG4372
Uncharacterized protein, contains DUF3084 domain [Function unknown];
179-283 4.41e-03

Uncharacterized protein, contains DUF3084 domain [Function unknown];


Pssm-ID: 443500 [Multi-domain]  Cd Length: 370  Bit Score: 39.89  E-value: 4.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 179 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEE-QNELIIKEREALQLQyRECQELLSLYQKyLSEQQEK 257
Cdd:COG4372    56 QAREELEQLEEELEQARSELEQLEEELEELNEQLQAAQAELAQaQEELESLQEEAEELQ-EELEELQKERQD-LEQQRKQ 133

                          90       100
                  ....*....|....*....|....*..
gi 1622889542 258 LTMSLSELGAA-RMQEQQVSSRKSTLQ 283
Cdd:COG4372   134 LEAQIAELQSEiAEREEELKELEEQLE 160
PRK03918 PRK03918
DNA double-strand break repair ATPase Rad50;
179-257 4.76e-03

DNA double-strand break repair ATPase Rad50;


Pssm-ID: 235175 [Multi-domain]  Cd Length: 880  Bit Score: 40.43  E-value: 4.76e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622889542 179 EDKRRIANLIKELARVSEEKEVTEERLKaEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEK 257
Cdd:PRK03918  204 EVLREINEISSELPELREELEKLEKEVK-ELEELKEEIEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEK 281
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 167-283 6.29e-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: 6.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 167 EIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEERLKAEQE---SFEKKIRQLEEQNELIIKEREALQLQYRECQEL 243
Cdd:COG1196   266 EAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEErrrELEERLEELEEELAELEEELEELEEELEELEEE 345

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1622889542 244 LSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   346 LEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELA 385
sbcc TIGR00618
exonuclease SbcC; All proteins in this family for which functions are known are part of an ...
 159-337 6.35e-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: 39.95  E-value: 6.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  159 DEQNSCRGEI----KSASLKDLCLEDKR-----RIANLIKELARVSEEkevteerLKAEQESFEKKIRQLEEQNELIIKE 229
Cdd:TIGR00618  187 AKKKSLHGKAelltLRSQLLTLCTPCMPdtyheRKQVLEKELKHLREA-------LQQTQQSHAYLTQKREAQEEQLKKQ 259

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  230 REALQLQyRECQELLSLyQKYLSEQQEKLTMS-----LSELGAARMQ-EQQVSSRKSTLQCSSVELDGSY---------- 293
Cdd:TIGR00618  260 QLLKQLR-ARIEELRAQ-EAVLEETQERINRArkaapLAAHIKAVTQiEQQAQRIHTELQSKMRSRAKLLmkraahvkqq 337

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1622889542  294 LSVARPQTYYQTKQRPKSAIQDSASESLiAFRNNSLKPVTLHHP 337
Cdd:TIGR00618  338 SSIEEQRRLLQTLHSQEIHIRDAHEVAT-SIREISCQQHTLTQH 380
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
159-280 6.40e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.75  E-value: 6.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 159 DEQNSCRGEIKSASlkdlclEDKRRIANLIKELARVSEEKEvteeRLKAEQESFEKKIRQLEEQNEL--IIKEREALQLQ 236
Cdd:COG4717    71 KELKELEEELKEAE------EKEEEYAELQEELEELEEELE----ELEAELEELREELEKLEKLLQLlpLYQELEALEAE 140

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622889542 237 YRECQELL-SLYQKY--LSEQQEKLTMSLSELGAARMQEQQVSSRKS 280
Cdd:COG4717   141 LAELPERLeELEERLeeLRELEEELEELEAELAELQEELEELLEQLS 187
PRK12705 PRK12705
hypothetical protein; Provisional
 180-258 6.66e-03

hypothetical protein; Provisional


Pssm-ID: 237178 [Multi-domain]  Cd Length: 508  Bit Score: 39.69  E-value: 6.66e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 180 DKRRIANLIKELARVSEEKEVTEERLKAEQESF---EKKIRQLEEQNELIIKEREALQlQYRECQELLSLYQKYLSEQQE 256
Cdd:PRK12705   82 EEERLVQKEEQLDARAEKLDNLENQLEEREKALsarELELEELEKQLDNELYRVAGLT-PEQARKLLLKLLDAELEEEKA 160


                  ..
gi 1622889542 257 KL 258
Cdd:PRK12705  161 QR 162
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 182-283 7.03e-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: 7.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 182 RRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELLSLYQKYLSEQQEKLTMS 261
Cdd:COG1196   235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRREL 314

                          90       100
                  ....*....|....*....|..
gi 1622889542 262 LSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG1196   315 EERLEELEEELAELEEELEELE 336
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
160-283 8.87e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 39.37  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 160 EQNSCRGEIKSASLKDLCLEDKRRIANLIKELARVSEEKEVTEER---LKAEQESFEKKIRQLEEQNELIIKEREALQlq 236
Cdd:COG4717   103 ELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAELPERleeLEERLEELRELEEELEELEAELAELQEELE-- 180

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622889542 237 yRECQELLSLYQKYLSEQQEKLTMSLSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG4717   181 -ELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELE 226
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
182-283 8.90e-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: 8.90e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  182 RRIANLIKELARvseeKEVTEERLKAEQESFEKKIRQLEEQNELiikEREALQLQYRECQELLSLYQKYLSEQQEKLTMS 261
Cdd:COG4913    338 DRLEQLEREIER----LERELEERERRRARLEALLAALGLPLPA---SAEEFAALRAEAAALLEALEEELEALEEALAEA 410

                           90       100
                   ....*....|....*....|..
gi 1622889542  262 LSELGAARMQEQQVSSRKSTLQ 283
Cdd:COG4913    411 EAALRDLRRELRELEAEIASLE 432
OmpH pfam03938
Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH ...
 179-269 9.12e-03

Outer membrane protein (OmpH-like); This family includes outer membrane proteins such as OmpH among others. Skp (OmpH) has been characterized as a molecular chaperone that interacts with unfolded proteins as they emerge in the periplasm from the Sec translocation machinery.


Pssm-ID: 461098 [Multi-domain]  Cd Length: 140  Bit Score: 37.17  E-value: 9.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542 179 EDKRRIANLIKELARVSEEKEVTEERLKAEQESFEKKIRQLEE-----QNELIIKEREALQLQYRECQELLSLYQKYLSE 253
Cdd:pfam03938  16 EGKAAQAQLEKKFKKRQAELEAKQKELQKLYEELQKDGALLEEereekEQELQKKEQELQQLQQKAQQELQKKQQELLQP 95

                          90
                  ....*....|....*.
gi 1622889542 254 QQEKLTMSLSELGAAR 269
Cdd:pfam03938  96 IQDKINKAIKEVAKEK 111
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 114-283 9.92e-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: 9.92e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  114 GISTEGNVRSRHKLTSPK-------ADVKLKTSRATDASISMESLKGTGDSVDEQnscrgeikSASLKDLCLEDKRRIAN 186
Cdd:TIGR02168  659 GVITGGSAKTNSSILERRreieeleEKIEELEEKIAELEKALAELRKELEELEEE--------LEQLRKELEELSRQISA 730

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622889542  187 LIKELARVSEEKEVTEERLKAEQESFEKKIRQLEEQNELIIKEREALQLQYRECQELlslyQKYLSEQQEKLTMSLSELG 266
Cdd:TIGR02168  731 LRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEEL----EAQIEQLKEELKALREALD 806

                          170
                   ....*....|....*..
gi 1622889542  267 AARMQEQQVSSRKSTLQ 283
Cdd:TIGR02168  807 ELRAELTLLNEEAANLR 823
 
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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