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Conserved domains on  [gi|219555720|ref|NP_001137237|]
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synaptonemal complex central element protein 1 [Mus musculus]

Protein Classification

SYCE1 domain-containing protein( domain architecture ID 10633620)

SYCE1 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
SYCE1 pfam15233
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal ...
49-200 6.83e-58

Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal complex central element protein 1, a component of the synaptonemal complex involved in meiosis, and synaptonemal complex central element protein 1-like, which may be involved in meiosis.


:

Pssm-ID: 464575 [Multi-domain]  Cd Length: 152  Bit Score: 183.86  E-value: 6.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   49 GSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRK 128
Cdd:pfam15233   1 GSLEPQIEDLINRINELQQAKKKSSEELGEAQALWEALQRELDSLNGEKVHLEEVLNKKQEALRILQLHCQEKESEAQRQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219555720  129 HSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMCVLDSSKEQLLKE 200
Cdd:pfam15233  81 HTLNEECKQRIEQYTFQIQEEKLKHRKQRMDFEEQLEDLMEQHKDLWEFHVPQRLAREIRALESSKEQLLKE 152
 
Name Accession Description Interval E-value
SYCE1 pfam15233
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal ...
49-200 6.83e-58

Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal complex central element protein 1, a component of the synaptonemal complex involved in meiosis, and synaptonemal complex central element protein 1-like, which may be involved in meiosis.


Pssm-ID: 464575 [Multi-domain]  Cd Length: 152  Bit Score: 183.86  E-value: 6.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   49 GSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRK 128
Cdd:pfam15233   1 GSLEPQIEDLINRINELQQAKKKSSEELGEAQALWEALQRELDSLNGEKVHLEEVLNKKQEALRILQLHCQEKESEAQRQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219555720  129 HSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMCVLDSSKEQLLKE 200
Cdd:pfam15233  81 HTLNEECKQRIEQYTFQIQEEKLKHRKQRMDFEEQLEDLMEQHKDLWEFHVPQRLAREIRALESSKEQLLKE 152
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-283 4.07e-10

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: 60.85  E-value: 4.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    33 QKIEDLMDMVKKL-QKVGSLEPRIEVLINRINEVQQAKKKASEELGE-----AQTVWDNLQKELDLLREEKVRLKDILNR 106
Cdd:TIGR02169  737 ERLEELEEDLSSLeQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLRE 816
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   107 KEETLRIMQLHCQEKESEAQRKHSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEH---LETLMSQHK------DTLEF 177
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaaLRDLESRLGdlkkerDELEA 896
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   178 HKPEhLTKEMCVLDSSKEQLLKEEKLMKVKLEDVRQRLCALGGPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLE 257
Cdd:TIGR02169  897 QLRE-LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
                          250       260
                   ....*....|....*....|....*.
gi 219555720   258 AAAQQHEQLQQRCHQLQQKRQRLKEE 283
Cdd:TIGR02169  976 LAIQEYEEVLKRLDELKEKRAKLEEE 1001
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
54-300 4.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  54 RIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRKHSMLQ 133
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720 134 ECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMcvLDSSKEQLLKEEKLMKVKLEDVRQ 213
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEE 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720 214 RLCALGGPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLEAAAQQHEQLQQRCHQLQQKRQRLKEELEKHGVQILA 293
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                 ....*..
gi 219555720 294 HSTQNEE 300
Cdd:COG1196  464 LLAELLE 470
PTZ00121 PTZ00121
MAEBL; Provisional
42-254 2.87e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   42 VKKLQKVGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKElDLLREEKVRLKDILNRKEETLRIMQLHCQEK 121
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  122 ESEAQRKHSMLQECKERISFLNSQIDK----EKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMCVLDSSKEQL 197
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219555720  198 LKEEKLMKVKLEDVRQRlcalggPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEE 254
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKE------AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
 
Name Accession Description Interval E-value
SYCE1 pfam15233
Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal ...
49-200 6.83e-58

Synaptonemal complex central element protein 1; This family of proteins includes synaptonemal complex central element protein 1, a component of the synaptonemal complex involved in meiosis, and synaptonemal complex central element protein 1-like, which may be involved in meiosis.


Pssm-ID: 464575 [Multi-domain]  Cd Length: 152  Bit Score: 183.86  E-value: 6.83e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   49 GSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRK 128
Cdd:pfam15233   1 GSLEPQIEDLINRINELQQAKKKSSEELGEAQALWEALQRELDSLNGEKVHLEEVLNKKQEALRILQLHCQEKESEAQRQ 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 219555720  129 HSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMCVLDSSKEQLLKE 200
Cdd:pfam15233  81 HTLNEECKQRIEQYTFQIQEEKLKHRKQRMDFEEQLEDLMEQHKDLWEFHVPQRLAREIRALESSKEQLLKE 152
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
33-283 4.07e-10

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: 60.85  E-value: 4.07e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    33 QKIEDLMDMVKKL-QKVGSLEPRIEVLINRINEVQQAKKKASEELGE-----AQTVWDNLQKELDLLREEKVRLKDILNR 106
Cdd:TIGR02169  737 ERLEELEEDLSSLeQEIENVKSELKELEARIEELEEDLHKLEEALNDlearlSHSRIPEIQAELSKLEEEVSRIEARLRE 816
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   107 KEETLRIMQLHCQEKESEAQRKHSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEH---LETLMSQHK------DTLEF 177
Cdd:TIGR02169  817 IEQKLNRLTLEKEYLEKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELeaaLRDLESRLGdlkkerDELEA 896
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   178 HKPEhLTKEMCVLDSSKEQLLKEEKLMKVKLEDVRQRLCALGGPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLE 257
Cdd:TIGR02169  897 QLRE-LERKIEELEAQIEKKRKRLSELKAKLEALEEELSEIEDPKGEDEEIPEEELSLEDVQAELQRVEEEIRALEPVNM 975
                          250       260
                   ....*....|....*....|....*.
gi 219555720   258 AAAQQHEQLQQRCHQLQQKRQRLKEE 283
Cdd:TIGR02169  976 LAIQEYEEVLKRLDELKEKRAKLEEE 1001
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
54-300 4.67e-08

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 54.56  E-value: 4.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  54 RIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRKHSMLQ 133
Cdd:COG1196  226 EAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIA 305
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720 134 ECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMcvLDSSKEQLLKEEKLMKVKLEDVRQ 213
Cdd:COG1196  306 RLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAE--LAEAEEALLEAEAELAEAEEELEE 383
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720 214 RLCALGGPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLEAAAQQHEQLQQRCHQLQQKRQRLKEELEKHGVQILA 293
Cdd:COG1196  384 LAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLE 463

                 ....*..
gi 219555720 294 HSTQNEE 300
Cdd:COG1196  464 LLAELLE 470
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
43-187 1.67e-06

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: 49.67  E-value: 1.67e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    43 KKLQKVGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKE 122
Cdd:TIGR02168  821 NLRERLESLERRIAATERRLEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELS 900
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219555720   123 SEAQRKHSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEM 187
Cdd:TIGR02168  901 EELRELESKRSELRRELEELREKLAQLELRLEGLEVRIDNLQERLSEEYSLTLEEAEALENKIED 965
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
46-291 2.27e-06

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: 49.28  E-value: 2.27e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    46 QKVGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEA 125
Cdd:TIGR02168  253 EELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELESKL 332
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   126 QRKHSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEmcvldsSKEQLLKEEKLMK 205
Cdd:TIGR02168  333 DELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQLEL------QIASLNNEIERLE 406
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   206 VKLEDVRQRLCALgGPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLEAAAQQHEQLQQRCHQLQQKRQRLKEELE 285
Cdd:TIGR02168  407 ARLERLEDRRERL-QQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485

                   ....*.
gi 219555720   286 KHGVQI 291
Cdd:TIGR02168  486 QLQARL 491
PTZ00121 PTZ00121
MAEBL; Provisional
42-254 2.87e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.98  E-value: 2.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   42 VKKLQKVGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKElDLLREEKVRLKDILNRKEETLRIMQLHCQEK 121
Cdd:PTZ00121 1563 KKKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAE-EAKKAEEAKIKAEELKKAEEEKKKVEQLKKK 1641
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  122 ESEAQRKHSMLQECKERISFLNSQIDK----EKAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMCVLDSSKEQL 197
Cdd:PTZ00121 1642 EAEEKKKAEELKKAEEENKIKAAEEAKkaeeDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEEL 1721
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 219555720  198 LKEEKLMKVKLEDVRQRlcalggPEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEE 254
Cdd:PTZ00121 1722 KKAEEENKIKAEEAKKE------AEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEE 1772
CCDC22 pfam05667
Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 ...
43-211 9.34e-06

Coiled-coil domain-containing protein 22; Human coiled-coil domain-containing protein 22 (CCDC22) is involved in regulation of NF-kappa-B signalling; the function may involve association with COMMD8 and a CUL1-dependent E3 ubiquitin ligase complex. It is part of the OMMD/CCDC22/CCDC93 (CCC) complex, which interacts with the multisubunit WASH complex required for endosomal deposition of F-actin and cargo trafficking in conjunction with the retromer. This entry also includes CCDC22 homologs from animals and plants.


Pssm-ID: 461708 [Multi-domain]  Cd Length: 600  Bit Score: 47.33  E-value: 9.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   43 KKLQKVGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKE 122
Cdd:pfam05667 304 EKLQFTNEAPAATSSPPTKVETEEELQQQREEELEELQEQLEDLESSIQELEKEIKKLESSIKQVEEELEELKEQNEELE 383
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  123 SEAQRK---HSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDtlefHKPEHLTKEmcvldSSKEQLLK 199
Cdd:pfam05667 384 KQYKVKkktLDLLPDAEENIAKLQALVDASAQRLVELAGQWEKHRVPLIEEYRA----LKEAKSNKE-----DESQRKLE 454
                         170
                  ....*....|..
gi 219555720  200 EEKLMKVKLEDV 211
Cdd:pfam05667 455 EIKELREKIKEV 466
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
75-288 9.34e-05

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: 44.28  E-value: 9.34e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    75 ELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRKHSMLQECKERISFLNSQIDKEKAKLR 154
Cdd:TIGR02168  233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLA 312
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   155 KLRLDFEEhletlmsqhkdtlefhkpehLTKEMCVLDSSKEQLLKEEKLMKVKLEDVRQRLCALGGP-EGSSSLIEGLFL 233
Cdd:TIGR02168  313 NLERQLEE--------------------LEAQLEELESKLDELAEELAELEEKLEELKEELESLEAElEELEAELEELES 372
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 219555720   234 RSHEAAAAMQMFKDENKKAEEFLEAAAQQHEQLQQRCHQLQQKRQRLKEELEKHG 288
Cdd:TIGR02168  373 RLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELL 427
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
78-286 4.06e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.21  E-value: 4.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   78 EAQTVWDNLQKELDLLREEKVRLKDILnRKEETLRIMQLHCQEKEsEAQRKHSMLQECKERISFLNSQ--IDKEKAKLRK 155
Cdd:COG4913   222 DTFEAADALVEHFDDLERAHEALEDAR-EQIELLEPIRELAERYA-AARERLAELEYLRAALRLWFAQrrLELLEAELEE 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  156 LRLDFEEhLETLMSQHKDTLEFHKPEHLTKEMCVLDSS---KEQLLKEEKLMKVKLEDVRQRLCALggpegsSSLIEGLF 232
Cdd:COG4913   300 LRAELAR-LEAELERLEARLDALREELDELEAQIRGNGgdrLEQLEREIERLERELEERERRRARL------EALLAALG 372
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 219555720  233 LrshEAAAAMQMFKDENKKAEEFLEAAAQQHEQLQQRCHQLQQKRQRLKEELEK 286
Cdd:COG4913   373 L---PLPASAEEFAALRAEAAALLEALEEELEALEEALAEAEAALRDLRRELRE 423
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
45-280 9.32e-04

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: 41.20  E-value: 9.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    45 LQKVGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEkvrlkdiLNRKEETLRIMQLHCQEKESE 124
Cdd:TIGR02168  767 EERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEE-------AANLRERLESLERRIAATERR 839
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   125 AQRKHSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMS--QHKDTLEFHKpEHLTKEMCVLDSSKEQLLKEEK 202
Cdd:TIGR02168  840 LEDLEEQIEELSEDIESLAAEIEELEELIEELESELEALLNERASleEALALLRSEL-EELSEELRELESKRSELRRELE 918
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 219555720   203 LMKVKLEDVRQRLcalggpEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLEaaaqqhEQLQQRCHQLQQKRQRL 280
Cdd:TIGR02168  919 ELREKLAQLELRL------EGLEVRIDNLQERLSEEYSLTLEEAEALENKIEDDE------EEARRRLKRLENKIKEL 984
PRK12704 PRK12704
phosphodiesterase; Provisional
65-169 1.61e-03

phosphodiesterase; Provisional


Pssm-ID: 237177 [Multi-domain]  Cd Length: 520  Bit Score: 40.15  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  65 VQQAKKKAS----EELGEAQTVWDNLQKELDllREEKVRLKDiLNRKEETLRIMQLHCQEKESEAQRKHSMLQECKERIS 140
Cdd:PRK12704  44 LEEAKKEAEaikkEALLEAKEEIHKLRNEFE--KELRERRNE-LQKLEKRLLQKEENLDRKLELLEKREEELEKKEKELE 120
                         90       100
                 ....*....|....*....|....*....
gi 219555720 141 FLNSQIDKEKAKLRKLRLDFEEHLETLMS 169
Cdd:PRK12704 121 QKQQELEKKEEELEELIEEQLQELERISG 149
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
33-172 2.06e-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: 2.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   33 QKIEDLMDMVKKLQK----VGSLEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREekvRLKDILNRKE 108
Cdd:COG4913   668 REIAELEAELERLDAssddLAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQD---RLEAAEDLAR 744
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 219555720  109 ETLRImqlhcqekESEAQRKHSMLQECKERISF-LNSQIDKEKAKLRKLrldfEEHLETLMSQHK 172
Cdd:COG4913   745 LELRA--------LLEERFAAALGDAVERELREnLEERIDALRARLNRA----EEELERAMRAFN 797
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
62-291 3.21e-03

chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 39.28  E-value: 3.21e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720    62 INEVQQAKKKASEELGEA-------QTVWDNLQKELDLLREEK---VRLKDILNRKEE---TLRIMQLHCQEKESEA-QR 127
Cdd:TIGR02169  165 VAEFDRKKEKALEELEEVeenierlDLIIDEKRQQLERLRRERekaERYQALLKEKREyegYELLKEKEALERQKEAiER 244
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   128 KHSMLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETL------------------MSQHKDTLEFHKP--EHLTKEM 187
Cdd:TIGR02169  245 QLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvkekigeleaeIASLERSIAEKERelEDAEERL 324
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   188 CVLDSSKEQLLKEEKLMKVKLEDVRQRLCALGGP-EGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLEAAAQQHEQL 266
Cdd:TIGR02169  325 AKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEyAELKEELEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINEL 404
                          250       260
                   ....*....|....*....|....*
gi 219555720   267 QQRCHQLQQKRQRLKEELEKHGVQI 291
Cdd:TIGR02169  405 KRELDRLQEELQRLSEELADLNAAI 429
PTZ00121 PTZ00121
MAEBL; Provisional
69-301 8.71e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 38.20  E-value: 8.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720   69 KKKASEELGEAQTV--WDNLQKELDLLREEKVRlKDILNRKEETLRIMQLHCQE--KESEAQRKHSMLQECKERISFLNS 144
Cdd:PTZ00121 1532 EAKKADEAKKAEEKkkADELKKAEELKKAEEKK-KAEEAKKAEEDKNMALRKAEeaKKAEEARIEEVMKLYEEEKKMKAE 1610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  145 QIDKE---KAKLRKLRLDFEEHLETLMSQHKDTLEFHKPEHLTKEMCVLDSSKEQLLKEEKLMKVKLEDVRQRlcalggp 221
Cdd:PTZ00121 1611 EAKKAeeaKIKAEELKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA------- 1683
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  222 egssslieglflrsheaaaamqmfKDENKKAEEFL---EAAAQQHEQLQQRCHQLQQKRQRLKEELEKHGVQILAHSTQN 298
Cdd:PTZ00121 1684 ------------------------EEDEKKAAEALkkeAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAEEAKKEA 1739

                  ...
gi 219555720  299 EED 301
Cdd:PTZ00121 1740 EED 1742
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
51-269 8.90e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 37.99  E-value: 8.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720  51 LEPRIEVLINRINEVQQAKKKASEELGEAQTVWDNLQKELDLLREEKVRLKDILNRKEETLRIMQLHCQEKESEAQRKHS 130
Cdd:COG1196  321 LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAA 400
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 219555720 131 MLQECKERISFLNSQIDKEKAKLRKLRLDFEEHLETLMSQHKDTLEfhkpehltkemcvLDSSKEQLLKEEKLMKVKLED 210
Cdd:COG1196  401 QLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEE-------------AAEEEAELEEEEEALLELLAE 467
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 219555720 211 VRQRLcalggpEGSSSLIEGLFLRSHEAAAAMQMFKDENKKAEEFLEAAAQQHEQLQQR 269
Cdd:COG1196  468 LLEEA------ALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLR 520
 
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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