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Conserved domains on  [gi|528490724|ref|XP_005167932|]
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SEC14 domain and spectrin repeat-containing protein 1 isoform X1 [Danio rerio]

Protein Classification

CRAL-TRIO domain-containing protein( domain architecture ID 10617211)

CRAL-TRIO domain-containing protein act as a lipid binding protein which may bind small lipophilic molecules such as retinal, inositol, and vitamin E

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
33-153 4.21e-14

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


:

Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 69.66  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   33 LCTEQTSMEELSTTLDYLLGIPSEKCKARGFTVIVDGRKSQ------WNIVKTVVLMLQNVIPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 528490724  107 KV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTDEFGGSLLYDH 153
Cdd:pfam13716  92 FLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC super family cl02488
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
383-607 1.07e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


The actual alignment was detected with superfamily member cd00176:

Pssm-ID: 413338 [Multi-domain]  Cd Length: 213  Bit Score: 50.14  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 383 AYEFHMTAQDLSQQLDGLLGMLCADVAPADGAAIQQTLK---HLEEKLKSVESALQTLREKGQALLDqmsnqtsfsygke 459
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKkheALEAELAAHEERVEALNELGEQLIE------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 460 vgvENKENIDHIHSVMEDMQLRKQRCEDMVDVRRLKMLQMVQLFKCEEDASQAVEWLGELLDALLKThiRLGDDSQETKV 539
Cdd:cd00176   69 ---EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEE 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528490724 540 LLEKHKKFV-DVAQSTYDYGRQLLQATVVLCQSLRCTTRSSGDTLPRLNRVWKQFTVTSDERQHRLEMA 607
Cdd:cd00176  144 LLKKHKELEeELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
COG4913 super family cl25907
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
242-438 7.38e-04

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


The actual alignment was detected with superfamily member COG4913:

Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  242 DELLAQPQVMKLLDSLREQYTK----YQEVCRQRSKRSQLEEIQTKVMQVV-NWLEGPGTDQLRTQWGIGDSIRASQALQ 316
Cdd:COG4913   215 EYMLEEPDTFEAADALVEHFDDleraHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAALRLWFAQRRLELLE 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  317 QKHEEIESQHSewfavyvELNQQIAALLSAGDEEDlMELKGLQQQLSDVCYRQASQLEFRQNVLQSAYEfhmTAQDLSQQ 396
Cdd:COG4913   295 AELEELRAELA-------RLEAELERLEARLDALR-EELDELEAQIRGNGGDRLEQLEREIERLERELE---ERERRRAR 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528490724  397 LDGLLGMLCADVA--PADGAAIQQTLKHLEEKLKSVESALQTLR 438
Cdd:COG4913   364 LEALLAALGLPLPasAEEFAALRAEAAALLEALEEELEALEEAL 407
 
Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
33-153 4.21e-14

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 69.66  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   33 LCTEQTSMEELSTTLDYLLGIPSEKCKARGFTVIVDGRKSQ------WNIVKTVVLMLQNVIPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 528490724  107 KV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTDEFGGSLLYDH 153
Cdd:pfam13716  92 FLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
383-607 1.07e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.14  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 383 AYEFHMTAQDLSQQLDGLLGMLCADVAPADGAAIQQTLK---HLEEKLKSVESALQTLREKGQALLDqmsnqtsfsygke 459
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKkheALEAELAAHEERVEALNELGEQLIE------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 460 vgvENKENIDHIHSVMEDMQLRKQRCEDMVDVRRLKMLQMVQLFKCEEDASQAVEWLGELLDALLKThiRLGDDSQETKV 539
Cdd:cd00176   69 ---EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEE 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528490724 540 LLEKHKKFV-DVAQSTYDYGRQLLQATVVLCQSLRCTTRSSGDTLPRLNRVWKQFTVTSDERQHRLEMA 607
Cdd:cd00176  144 LLKKHKELEeELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
10-149 3.89e-06

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 47.29  E-value: 3.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724    10 LKKKLAFLSG--GKDRRSGLILTIPLCT---EQTSMEEL----STTLDYLLGIPSEKCKARGFTVIVD-----GRKSQWN 75
Cdd:smart00516   2 LELLKAYIPGgrGYDKDGRPVLIERAGRfdlKSVTLEELlrylVYVLEKILQEEKKTGGIEGFTVIFDlkglsMSNPDLS 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528490724    76 IVKTVVLMLQNVIPAEVSLVCVVKPDEFWDK--KVTHFcFWKEKDRLGFEVI-LVSANKLTRYIEPCQLTDEFGGSL 149
Cdd:smart00516  82 VLRKILKILQDHYPERLGKVYIINPPWFFRVlwKIIKP-FLDEKTREKIRFVgNDSKEELLEYIDKEQLPEELGGTL 157
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
242-438 7.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  242 DELLAQPQVMKLLDSLREQYTK----YQEVCRQRSKRSQLEEIQTKVMQVV-NWLEGPGTDQLRTQWGIGDSIRASQALQ 316
Cdd:COG4913   215 EYMLEEPDTFEAADALVEHFDDleraHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAALRLWFAQRRLELLE 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  317 QKHEEIESQHSewfavyvELNQQIAALLSAGDEEDlMELKGLQQQLSDVCYRQASQLEFRQNVLQSAYEfhmTAQDLSQQ 396
Cdd:COG4913   295 AELEELRAELA-------RLEAELERLEARLDALR-EELDELEAQIRGNGGDRLEQLEREIERLERELE---ERERRRAR 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528490724  397 LDGLLGMLCADVA--PADGAAIQQTLKHLEEKLKSVESALQTLR 438
Cdd:COG4913   364 LEALLAALGLPLPasAEEFAALRAEAAALLEALEEELEALEEAL 407
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
276-447 2.33e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 276 QLEEIQTKVMQVVNWLEGpgTDQLRTQWGIGDSIRASQALQQKHEEIES---QHSEWFAVYVELNQQIAALLSAGDEEDL 352
Cdd:cd00176    1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAelaAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 353 MELKGLQQQLSDVCyrqaSQLEFRQNVLQSAYEFHM---TAQDLSQQLDGLLGMLCADVAPADGAAIQ---QTLKHLEEK 426
Cdd:cd00176   79 ERLEELNQRWEELR----ELAEERRQRLEEALDLQQffrDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154
                        170       180
                 ....*....|....*....|.
gi 528490724 427 LKSVESALQTLREKGQALLDQ 447
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEE 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-490 3.72e-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: 40.81  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   254 LDSLREQYTKYQEVCRQrsKRSQLEEIQTKVMQVVNWLEGPGTDQLRTQWGIGDSIRASQALQQKHEEIESQHSEWFAVY 333
Cdd:TIGR02168  700 LAELRKELEELEEELEQ--LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   334 VELNQQIAAL--LSAGDEEDLM----ELKGLQQQLSDVCYRQASQLEFRQNVLQSAYEFHMTAQDLSQQLDGLLGMLcAD 407
Cdd:TIGR02168  778 AEAEAEIEELeaQIEQLKEELKalreALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-ES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   408 VAPA------DGAAIQQTLKHLEEKLKSVESALQTLREKGQALLDQMSNqtsfsYGKEVGvENKENIDHIHSVMEDMQLR 481
Cdd:TIGR02168  857 LAAEieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRE-----LESKRS-ELRRELEELREKLAQLELR 930

                   ....*....
gi 528490724   482 KQRCEDMVD 490
Cdd:TIGR02168  931 LEGLEVRID 939
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
297-533 5.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  297 DQLRTQWGIG-DSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALlsagdeedlmelkglQQQLSDvcYRQASQLEF 375
Cdd:COG4913   596 RRIRSRYVLGfDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---------------QERREA--LQRLAEYSW 658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  376 RQNVLQSAyefHMTAQDLSQQLDGLlgmlcaDVAPADgaaiqqtLKHLEEKLKSVESALQTLREKGQALLDQMSnqtsfs 455
Cdd:COG4913   659 DEIDVASA---EREIAELEAELERL------DASSDD-------LAALEEQLEELEAELEELEEELDELKGEIG------ 716
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528490724  456 ygkevgvENKENIDHIHSVMEDMQLRKQRCEDMVDVRRLKML-QMVQLFKCEEDASQAVEWLGELLDALLKTHIRLGDD 533
Cdd:COG4913   717 -------RLEKELEQAEEELDELQDRLEAAEDLARLELRALLeERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
 
Name Accession Description Interval E-value
CRAL_TRIO_2 pfam13716
Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain ...
33-153 4.21e-14

Divergent CRAL/TRIO domain; This family includes divergent members of the CRAL-TRIO domain family. This family includes ECM25 that contains a divergent CRAL-TRIO domain identified by Gallego and colleagues.


Pssm-ID: 463965 [Multi-domain]  Cd Length: 140  Bit Score: 69.66  E-value: 4.21e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   33 LCTEQTSMEELSTTLDYLLGIPSEKCKARGFTVIVDGRKSQ------WNIVKTVVLMLQNVIPAEVSLVCVVKPDEFWDK 106
Cdd:pfam13716  12 LPSRPASLDDLDRLLFYLLKTLSEKLKGKPFVVVVDHTGVTsenfpsLSFLKKAYDLLPRAFKKNLKAVYVVHPSTFLRT 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 528490724  107 KV-THFCFWKEKDRLGFEVILVSANKLTRYIEPCQLTDEFGGSLLYDH 153
Cdd:pfam13716  92 FLkTLGSLLGSKKLRKKVHYVSSLSELWEGIDREQLPTELPGVLSYDE 139
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
383-607 1.07e-06

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 50.14  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 383 AYEFHMTAQDLSQQLDGLLGMLCADVAPADGAAIQQTLK---HLEEKLKSVESALQTLREKGQALLDqmsnqtsfsygke 459
Cdd:cd00176    2 LQQFLRDADELEAWLSEKEELLSSTDYGDDLESVEALLKkheALEAELAAHEERVEALNELGEQLIE------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 460 vgvENKENIDHIHSVMEDMQLRKQRCEDMVDVRRLKMLQMVQLFKCEEDASQAVEWLGELLDALLKThiRLGDDSQETKV 539
Cdd:cd00176   69 ---EGHPDAEEIQERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASE--DLGKDLESVEE 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528490724 540 LLEKHKKFV-DVAQSTYDYGRQLLQATVVLCQSLRCTTRSSGDTLPRLNRVWKQFTVTSDERQHRLEMA 607
Cdd:cd00176  144 LLKKHKELEeELEAHEPRLKSLNELAEELLEEGHPDADEEIEEKLEELNERWEELLELAEERQKKLEEA 212
SEC14 smart00516
Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain ...
10-149 3.89e-06

Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p); Domain in homologues of a S. cerevisiae phosphatidylinositol transfer protein (Sec14p) and in RhoGAPs, RhoGEFs and the RasGAP, neurofibromin (NF1). Lipid-binding domain. The SEC14 domain of Dbl is known to associate with G protein beta/gamma subunits.


Pssm-ID: 214706 [Multi-domain]  Cd Length: 158  Bit Score: 47.29  E-value: 3.89e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724    10 LKKKLAFLSG--GKDRRSGLILTIPLCT---EQTSMEEL----STTLDYLLGIPSEKCKARGFTVIVD-----GRKSQWN 75
Cdd:smart00516   2 LELLKAYIPGgrGYDKDGRPVLIERAGRfdlKSVTLEELlrylVYVLEKILQEEKKTGGIEGFTVIFDlkglsMSNPDLS 81
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 528490724    76 IVKTVVLMLQNVIPAEVSLVCVVKPDEFWDK--KVTHFcFWKEKDRLGFEVI-LVSANKLTRYIEPCQLTDEFGGSL 149
Cdd:smart00516  82 VLRKILKILQDHYPERLGKVYIINPPWFFRVlwKIIKP-FLDEKTREKIRFVgNDSKEELLEYIDKEQLPEELGGTL 157
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
242-438 7.38e-04

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 42.98  E-value: 7.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  242 DELLAQPQVMKLLDSLREQYTK----YQEVCRQRSKRSQLEEIQTKVMQVV-NWLEGPGTDQLRTQWGIGDSIRASQALQ 316
Cdd:COG4913   215 EYMLEEPDTFEAADALVEHFDDleraHEALEDAREQIELLEPIRELAERYAaARERLAELEYLRAALRLWFAQRRLELLE 294
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  317 QKHEEIESQHSewfavyvELNQQIAALLSAGDEEDlMELKGLQQQLSDVCYRQASQLEFRQNVLQSAYEfhmTAQDLSQQ 396
Cdd:COG4913   295 AELEELRAELA-------RLEAELERLEARLDALR-EELDELEAQIRGNGGDRLEQLEREIERLERELE---ERERRRAR 363
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 528490724  397 LDGLLGMLCADVA--PADGAAIQQTLKHLEEKLKSVESALQTLR 438
Cdd:COG4913   364 LEALLAALGLPLPasAEEFAALRAEAAALLEALEEELEALEEAL 407
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
501-642 8.08e-04

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 41.28  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 501 QLFKCEEDASQAVEWLGELLDALLKTHirLGDDSQETKVLLEKHKKFVDVAQSTYDYGRQLLQATVVLCQSLRCTTRSSG 580
Cdd:cd00176    1 KLQQFLRDADELEAWLSEKEELLSSTD--YGDDLESVEALLKKHEALEAELAAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 528490724 581 DTLPRLNRVWKQFTVTSDERQHRLEMASAFHTAAEKIVRESPELAELLVDVEAYEEVETLGK 642
Cdd:cd00176   79 ERLEELNQRWEELRELAEERRQRLEEALDLQQFFRDADDLEQWLEEKEAALASEDLGKDLES 140
SPEC cd00176
Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members ...
276-447 2.33e-03

Spectrin repeats, found in several proteins involved in cytoskeletal structure; family members include spectrin, alpha-actinin and dystrophin; the spectrin repeat forms a three helix bundle with the second helix interrupted by proline in some sequences; the repeats are independent folding units; tandem repeats are found in differing numbers and arrange in an antiparallel manner to form dimers; the repeats are defined by a characteristic tryptophan (W) residue in helix A and a leucine (L) at the carboxyl end of helix C and separated by a linker of 5 residues; two copies of the repeat are present here


Pssm-ID: 238103 [Multi-domain]  Cd Length: 213  Bit Score: 40.12  E-value: 2.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 276 QLEEIQTKVMQVVNWLEGpgTDQLRTQWGIGDSIRASQALQQKHEEIES---QHSEWFAVYVELNQQIAALLSAGDEEDL 352
Cdd:cd00176    1 KLQQFLRDADELEAWLSE--KEELLSSTDYGDDLESVEALLKKHEALEAelaAHEERVEALNELGEQLIEEGHPDAEEIQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 353 MELKGLQQQLSDVCyrqaSQLEFRQNVLQSAYEFHM---TAQDLSQQLDGLLGMLCADVAPADGAAIQ---QTLKHLEEK 426
Cdd:cd00176   79 ERLEELNQRWEELR----ELAEERRQRLEEALDLQQffrDADDLEQWLEEKEAALASEDLGKDLESVEellKKHKELEEE 154
                        170       180
                 ....*....|....*....|.
gi 528490724 427 LKSVESALQTLREKGQALLDQ 447
Cdd:cd00176  155 LEAHEPRLKSLNELAEELLEE 175
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
254-490 3.72e-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: 40.81  E-value: 3.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   254 LDSLREQYTKYQEVCRQrsKRSQLEEIQTKVMQVVNWLEGPGTDQLRTQWGIGDSIRASQALQQKHEEIESQHSEWFAVY 333
Cdd:TIGR02168  700 LAELRKELEELEEELEQ--LRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEEL 777
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   334 VELNQQIAAL--LSAGDEEDLM----ELKGLQQQLSDVCYRQASQLEFRQNVLQSAYEFHMTAQDLSQQLDGLLGMLcAD 407
Cdd:TIGR02168  778 AEAEAEIEELeaQIEQLKEELKalreALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDI-ES 856
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724   408 VAPA------DGAAIQQTLKHLEEKLKSVESALQTLREKGQALLDQMSNqtsfsYGKEVGvENKENIDHIHSVMEDMQLR 481
Cdd:TIGR02168  857 LAAEieeleeLIEELESELEALLNERASLEEALALLRSELEELSEELRE-----LESKRS-ELRRELEELREKLAQLELR 930

                   ....*....
gi 528490724   482 KQRCEDMVD 490
Cdd:TIGR02168  931 LEGLEVRID 939
YhaN COG4717
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
253-455 3.85e-03

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


Pssm-ID: 443752 [Multi-domain]  Cd Length: 641  Bit Score: 40.52  E-value: 3.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 253 LLDSLREQYTKYQEVCRQRSKRSQLEEIQTKvmqvvNWLEGPGTDQLRTQWGIGDSIRASQALQQKHEEIESQHSEwfAV 332
Cdd:COG4717  292 LLAREKASLGKEAEELQALPALEELEEEELE-----ELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEE--LQ 364
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724 333 YVELNQQIAALLSAGDEEDLMELKGLQQQlsdvcYRQASQLEFRQNVLQsayefhmtaqdlsQQLDGLLGMLCADVAPAD 412
Cdd:COG4717  365 LEELEQEIAALLAEAGVEDEEELRAALEQ-----AEEYQELKEELEELE-------------EQLEELLGELEELLEALD 426
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 528490724 413 GAAIQQTLKHLEEKLKSVESALQTLREKGQAL---LDQMSNQTSFS 455
Cdd:COG4717  427 EEELEEELEELEEELEELEEELEELREELAELeaeLEQLEEDGELA 472
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
297-533 5.32e-03

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


Pssm-ID: 443941 [Multi-domain]  Cd Length: 1089  Bit Score: 40.28  E-value: 5.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  297 DQLRTQWGIG-DSIRASQALQQKHEEIESQHSEWFAVYVELNQQIAALlsagdeedlmelkglQQQLSDvcYRQASQLEF 375
Cdd:COG4913   596 RRIRSRYVLGfDNRAKLAALEAELAELEEELAEAEERLEALEAELDAL---------------QERREA--LQRLAEYSW 658
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 528490724  376 RQNVLQSAyefHMTAQDLSQQLDGLlgmlcaDVAPADgaaiqqtLKHLEEKLKSVESALQTLREKGQALLDQMSnqtsfs 455
Cdd:COG4913   659 DEIDVASA---EREIAELEAELERL------DASSDD-------LAALEEQLEELEAELEELEEELDELKGEIG------ 716
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 528490724  456 ygkevgvENKENIDHIHSVMEDMQLRKQRCEDMVDVRRLKML-QMVQLFKCEEDASQAVEWLGELLDALLKTHIRLGDD 533
Cdd:COG4913   717 -------RLEKELEQAEEELDELQDRLEAAEDLARLELRALLeERFAAALGDAVERELRENLEERIDALRARLNRAEEE 788
 
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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