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Conserved domains on  [gi|391353392|ref|NP_001254652|]
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centrosomal protein CCDC61 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
HD_CCDC61_N cd22284
N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; ...
 7-140 4.79e-74

N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; Coiled-coil domain-containing protein 61 (CCDC61), also known as variable flagellar number 3 (VFL3), is a centrosomal protein required for spindle assembly and precise chromosome alignments in mitosis. It is the human ortholog of proteins required for anchoring distinct sets of cytoskeletal fibers to centrioles in unicellular eukaryotes. CCDC61 monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These CCDC61 homodimers assembles into linear filaments. This model corresponds to the N-terminal head domain of CCDC61, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and PAXX.


:

Pssm-ID: 409001  Cd Length: 135  Bit Score: 230.18  E-value: 4.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392   7 LQVDYVFRGVEHAVRVMVS-GQVLELEVEDRMTADQWRGEFDAGFIEDLTHKTGNFKQFNIFCHMLESALTQSSESVTLD 85
Cdd:cd22284    2 ISAELTFRGVEYLVTLKVDeGESLSVEVEDKDTGERWRGSFTASYIEELTRKTGNFKKFSVFVKMLKSALLKTSESVSLD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 391353392  86 LLTYTDLESLRNRKMGGRPGSLAPrSAQLNSKRYLILIYSVEFDRIHYPLPLPYQ 140
Cdd:cd22284   82 LLTYQDLEELRNRKSGGSSRNSAS-SSDLNNKRYLILTYTVEFDRVHYPLPLPYV 135
Smc super family cl34174
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-277 3.65e-05

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


The actual alignment was detected with superfamily member COG1196:

Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392 153 RSLKEELGRLQGLDGQNTRDTRENEIWHLREQVSRLASEKRELEAQL----GRSREEALAGRAARQEAEALRGLVRGLEL 228
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 391353392 229 ELRQERGLGHRVAGRRgqdcRRLAKELEEAKASERSLRARLKTLTSELA 277
Cdd:COG1196  296 ELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
 
Name Accession Description Interval E-value
HD_CCDC61_N cd22284
N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; ...
 7-140 4.79e-74

N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; Coiled-coil domain-containing protein 61 (CCDC61), also known as variable flagellar number 3 (VFL3), is a centrosomal protein required for spindle assembly and precise chromosome alignments in mitosis. It is the human ortholog of proteins required for anchoring distinct sets of cytoskeletal fibers to centrioles in unicellular eukaryotes. CCDC61 monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These CCDC61 homodimers assembles into linear filaments. This model corresponds to the N-terminal head domain of CCDC61, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and PAXX.


Pssm-ID: 409001  Cd Length: 135  Bit Score: 230.18  E-value: 4.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392   7 LQVDYVFRGVEHAVRVMVS-GQVLELEVEDRMTADQWRGEFDAGFIEDLTHKTGNFKQFNIFCHMLESALTQSSESVTLD 85
Cdd:cd22284    2 ISAELTFRGVEYLVTLKVDeGESLSVEVEDKDTGERWRGSFTASYIEELTRKTGNFKKFSVFVKMLKSALLKTSESVSLD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 391353392  86 LLTYTDLESLRNRKMGGRPGSLAPrSAQLNSKRYLILIYSVEFDRIHYPLPLPYQ 140
Cdd:cd22284   82 LLTYQDLEELRNRKSGGSSRNSAS-SSDLNNKRYLILTYTVEFDRVHYPLPLPYV 135
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-277 3.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392 153 RSLKEELGRLQGLDGQNTRDTRENEIWHLREQVSRLASEKRELEAQL----GRSREEALAGRAARQEAEALRGLVRGLEL 228
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 391353392 229 ELRQERGLGHRVAGRRgqdcRRLAKELEEAKASERSLRARLKTLTSELA 277
Cdd:COG1196  296 ELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-277 5.30e-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: 46.20  E-value: 5.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392   174 RENEIWHLREQVSRLASEKRELEAQLGRSREEALA----GRAARQEAEALRGLVRGLELELRQERglghRVAGRRGQDCR 249
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEEleeeLEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIA 750

                           90       100
                   ....*....|....*....|....*...
gi 391353392   250 RLAKELEEAKASERSLRARLKTLTSELA 277
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELA 778
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 151-276 9.51e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.28  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392  151 IIRSLKEELGrLQGLDG-----------QNTRDTRENEIWHLREQVSRLASEKRELEAQ-----------LGRSREEALA 208
Cdd:pfam09787  26 LIASLKEGSG-VEGLDSstaltleleelRQERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaessreqLQELEEQLAT 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 391353392  209 GRAARQEAEA----LRGLVRGLELELRQERGLGHRVAGRRGQDCRRLAKEL---EEAKASERSLRARLKTLTSEL 276
Cdd:pfam09787 105 ERSARREAEAelerLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLtskSQSSSSQSELENRLHQLTETL 179
 
Name Accession Description Interval E-value
HD_CCDC61_N cd22284
N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; ...
 7-140 4.79e-74

N-terminal head domain found in coiled-coil domain-containing protein 61 and similar proteins; Coiled-coil domain-containing protein 61 (CCDC61), also known as variable flagellar number 3 (VFL3), is a centrosomal protein required for spindle assembly and precise chromosome alignments in mitosis. It is the human ortholog of proteins required for anchoring distinct sets of cytoskeletal fibers to centrioles in unicellular eukaryotes. CCDC61 monomers are comprised of an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal region. These monomers homodimerize through two homodimerization domains, the N-terminal globular head domains and long extended alpha-helical coiled-coil regions. These CCDC61 homodimers assembles into linear filaments. This model corresponds to the N-terminal head domain of CCDC61, which is structurally related to other XRCC4-superfamily members, XRCC4, XLF, SAS6, and PAXX.


Pssm-ID: 409001  Cd Length: 135  Bit Score: 230.18  E-value: 4.79e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392   7 LQVDYVFRGVEHAVRVMVS-GQVLELEVEDRMTADQWRGEFDAGFIEDLTHKTGNFKQFNIFCHMLESALTQSSESVTLD 85
Cdd:cd22284    2 ISAELTFRGVEYLVTLKVDeGESLSVEVEDKDTGERWRGSFTASYIEELTRKTGNFKKFSVFVKMLKSALLKTSESVSLD 81

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 391353392  86 LLTYTDLESLRNRKMGGRPGSLAPrSAQLNSKRYLILIYSVEFDRIHYPLPLPYQ 140
Cdd:cd22284   82 LLTYQDLEELRNRKSGGSSRNSAS-SSDLNNKRYLILTYTVEFDRVHYPLPLPYV 135
HD_XRCC4-like_N cd22210
N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily ...
 15-139 3.57e-14

N-terminal head domain found in the XRCC4 superfamily of proteins; The XRCC4 superfamily includes five families: XRCC4, XLF, PAXX, SAS6 and CCDC61. XRCC4 (X-ray repair cross-complementing protein 4), XLF (XRCC4-like factor) and PAXX (paralog of XRCC4 and XLF) play crucial roles in the non-homologous end-joining (NHEJ) DNA repair pathway. SAS6 (spindle assembly abnormal protein 6) and CCDC61 (coiled-coil domain-containing protein 61) have a centrosomal/centriolar function. Members of this superfamily have an N-terminal globular head domain, a centrally located coiled-coil, and a C-terminal low-complexity region. They form homodimers through two homodimerization domains: an N-terminal globular head domain and a parallel coiled-coil domain. In addition, some members such as XRCC4 and XLF form symmetric heterodimers that interact through their globular head domains at the opposite end of the homodimer interface, and may form XLF-XRCC4 filaments. This model corresponds to the N-terminal head domain of XRCC4 superfamily proteins.


Pssm-ID: 408999  Cd Length: 115  Bit Score: 68.72  E-value: 3.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392  15 GVEHAVRVMVSG---QVLELEVEDrmTADQWRGEFDAGFIEDLTHKTGNFKQFNIFCHMLESALTQS---SESVTLDLLT 88
Cdd:cd22210   11 LEELTFKVETEVaneRGLRLHVSD--DAFLWTGEVSESDISQLKNDQGILVDFASFPGKLRSALEKCilaSDRFTFVLTI 88

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 391353392  89 YTDleslrnrkmggrpgslaprsaqlnsKRYLILIYSVEFDRIHYPLPLPY 139
Cdd:cd22210   89 RGD-------------------------EAYLKLVEILDEQLPHITFALRK 114
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 153-277 3.65e-05

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 46.47  E-value: 3.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392 153 RSLKEELGRLQGLDGQNTRDTRENEIWHLREQVSRLASEKRELEAQL----GRSREEALAGRAARQEAEALRGLVRGLEL 228
Cdd:COG1196  216 RELKEELKELEAELLLLKLRELEAELEELEAELEELEAELEELEAELaeleAELEELRLELEELELELEEAQAEEYELLA 295

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 391353392 229 ELRQERGLGHRVAGRRgqdcRRLAKELEEAKASERSLRARLKTLTSELA 277
Cdd:COG1196  296 ELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELE 340
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 174-277 5.30e-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: 46.20  E-value: 5.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392   174 RENEIWHLREQVSRLASEKRELEAQLGRSREEALA----GRAARQEAEALRGLVRGLELELRQERglghRVAGRRGQDCR 249
Cdd:TIGR02168  675 RRREIEELEEKIEELEEKIAELEKALAELRKELEEleeeLEQLRKELEELSRQISALRKDLARLE----AEVEQLEERIA 750

                           90       100
                   ....*....|....*....|....*...
gi 391353392   250 RLAKELEEAKASERSLRARLKTLTSELA 277
Cdd:TIGR02168  751 QLSKELTELEAEIEELEERLEEAEEELA 778
SMC_prok_A TIGR02169
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ...
 148-275 3.71e-04

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


Pssm-ID: 274009 [Multi-domain]  Cd Length: 1164  Bit Score: 43.52  E-value: 3.71e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392   148 LQGIIRSLKEELGRLQGLDGQNTRDTRENEIWHLREQVSRLASEKRELEAQLGRSREEALAGRAARQEAEALRglvrgLE 227
Cdd:TIGR02169  770 LEEDLHKLEEALNDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEYLEKEIQELQEQR-----ID 844

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 391353392   228 LELrQERGLGHRVAGRRGQdCRRLAKELEEAKASERSLRARLKTLTSE 275
Cdd:TIGR02169  845 LKE-QIKSIEKEIENLNGK-KEELEEELEELEAALRDLESRLGDLKKE 890
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 152-278 3.78e-04

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 43.39  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392 152 IRSLKEELGRLQgldgqNTRDTRENEIWHLREQVSRLASEKRELEAQLGRSREEALAGRAARQEAEA-LRGLVRGLELEL 230
Cdd:COG1196  234 LRELEAELEELE-----AELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAeLARLEQDIARLE 308

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 391353392 231 RQERGLGHRVAgRRGQDCRRLAKELEEAKASERSLRARLKTLTSELAL 278
Cdd:COG1196  309 ERRRELEERLE-ELEEELAELEEELEELEEELEELEEELEEAEEELEE 355
COG4913 COG4913
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
152-283 5.45e-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: 5.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392  152 IRSLKEELGRLQGLDGQNTRDTRENEIWHLREQVSRLASEKRELEAQLGRSREEALAGRAARQEA-----EALRGLVRGL 226
Cdd:COG4913   271 LAELEYLRAALRLWFAQRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGNggdrlEQLEREIERL 350

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392  227 ELELRQE-----------RGLG-------------HRVAGRRGQDCRRLAKELE----EAKASERSLRARLKTLTSELAL 278
Cdd:COG4913   351 ERELEERerrrarleallAALGlplpasaeefaalRAEAAALLEALEEELEALEealaEAEAALRDLRRELRELEAEIAS 430


                  ....*
gi 391353392  279 YKRGR 283
Cdd:COG4913   431 LERRK 435
Golgin_A5 pfam09787
Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining ...
 151-276 9.51e-04

Golgin subfamily A member 5; Members of this family of proteins are involved in maintaining Golgi structure. They stimulate the formation of Golgi stacks and ribbons, and are involved in intra-Golgi retrograde transport. Two main interactions have been characterized: one with RAB1A that has been activated by GTP-binding and another with isoform CASP of CUTL1.


Pssm-ID: 462900 [Multi-domain]  Cd Length: 305  Bit Score: 41.28  E-value: 9.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392  151 IIRSLKEELGrLQGLDG-----------QNTRDTRENEIWHLREQVSRLASEKRELEAQ-----------LGRSREEALA 208
Cdd:pfam09787  26 LIASLKEGSG-VEGLDSstaltleleelRQERDLLREEIQKLRGQIQQLRTELQELEAQqqeeaessreqLQELEEQLAT 104

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 391353392  209 GRAARQEAEA----LRGLVRGLELELRQERGLGHRVAGRRGQDCRRLAKEL---EEAKASERSLRARLKTLTSEL 276
Cdd:pfam09787 105 ERSARREAEAelerLQEELRYLEEELRRSKATLQSRIKDREAEIEKLRNQLtskSQSSSSQSELENRLHQLTETL 179
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 148-277 1.27e-03

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


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 41.46  E-value: 1.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392 148 LQGIIRSLKEELGRL-QGLDGQNTRDTR-ENEIWHLREQVSRLASEKRELEAQLGRSREEALAGRAARQEAEALRGLVRG 225
Cdd:COG1196  286 AQAEEYELLAELARLeQDIARLEERRRElEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEE 365

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 391353392 226 LELELRQERGLGHRVAGRRGQDCRRLAKELEEAKASERSLRARLKTLTSELA 277
Cdd:COG1196  366 ALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLE 417
COG2433 COG2433
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
156-286 7.85e-03

Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];


Pssm-ID: 441980 [Multi-domain]  Cd Length: 644  Bit Score: 39.07  E-value: 7.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 391353392 156 KEELGRLQGLDGQNTRDTRENEIWHLREQVSRLASEKRELEAQLGRSREealagRAARQEAEaLRGLVRGLELELRQERG 235
Cdd:COG2433  393 EEPEAEREKEHEERELTEEEEEIRRLEEQVERLEAEVEELEAELEEKDE-----RIERLERE-LSEARSEERREIRKDRE 466

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 391353392 236 LghrvaGRRGQDCRRLAKELEEAKASERSLRARLKTLTSELALYKRGRRTP 286
Cdd:COG2433  467 I-----SRLDREIERLERELEEERERIEELKRKLERLKELWKLEHSGELVP 512
 
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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