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Conserved domains on  [gi|24659953|ref|NP_648106|]
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establishment of cohesion, isoform A [Drosophila melanogaster]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Acetyltransf_13 pfam13880
ESCO1/2 acetyl-transferase;
982-1050 1.41e-29

ESCO1/2 acetyl-transferase;


:

Pssm-ID: 464015  Cd Length: 69  Bit Score: 112.19  E-value: 1.41e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24659953    982 YPASCGVSRIWVSPLQRRSGIASKLLRVVQCHTVLGQEIARECIAFSTPTDDGRALARQFTGLDNFLTY 1050
Cdd:pfam13880    1 VPAKCGISRIWVSPSHRRKGIATRLLDAARSNFIYGYILEKDEIAFSQPTESGKAFARKYFGTDDFLVY 69
zf-C2H2_3 pfam13878
zinc-finger of acetyl-transferase ESCO;
839-878 3.42e-15

zinc-finger of acetyl-transferase ESCO;


:

Pssm-ID: 464013  Cd Length: 40  Bit Score: 70.34  E-value: 3.42e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 24659953    839 QYQIDAGQKAFGARQCQQCGLVYTVHEPEEELLHREYHNS 878
Cdd:pfam13878    1 QLILDLGQKSFGATQCKECGMVYNPGSPEDEKLHKKYHAR 40
PRK08581 super family cl35718
amidase domain-containing protein;
189-477 5.26e-04

amidase domain-containing protein;


The actual alignment was detected with superfamily member PRK08581:

Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.01  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   189 AAMLMKGQDSRSMLEKSKKKHNHSLKTTAQVHTTKPKKTSPAEESQSDDEKPSSSKNSRKNT-EVRETRSSQIISPKTRN 267
Cdd:PRK08581   27 ADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSnNIIDFIYKNLPQTNINQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   268 RRRPFTSADINCKTlkaaaHLHENMRSYDEEKTaavKLENSRSRSKSpvevfkSNDDAVKRNTGNTNNKTAKSSEVATAK 347
Cdd:PRK08581  107 LLTKNKYDDNYSLT-----TLIQNLFNLNSDIS---DYEQPRNSEKS------TNDSNKNSDSSIKNDTDTQSSKQDKAD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   348 RPESPGSSMKIDvevPESDEEASNHKPQKrqhPETSTPVAPSADaDSGSPQSKMRKVTLSSSIPTMAFYSHSGEAVTKSR 427
Cdd:PRK08581  173 NQKAPSSNNTKP---STSNKQPNSPKPTQ---PNQSNSQPASDD-TANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQK 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 24659953   428 RRPSISKNSlkqPTKISPTSRPLLGINKGVHHKIRKRHGFANRLPATDMD 477
Cdd:PRK08581  246 DYASQSKKD---KTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTR 292
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 945-1008 7.22e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


:

Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 7.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24659953  945 FIAVRKQQIVGFCLVQPLSQAHRFiqvdgtdyfseesypasCGVSRIWVSPLQRRSGIASKLLR 1008
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDT-----------------AYIGDLAVLPEYRGKGIGSALLE 48
 
Name Accession Description Interval E-value
Acetyltransf_13 pfam13880
ESCO1/2 acetyl-transferase;
982-1050 1.41e-29

ESCO1/2 acetyl-transferase;


Pssm-ID: 464015  Cd Length: 69  Bit Score: 112.19  E-value: 1.41e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24659953    982 YPASCGVSRIWVSPLQRRSGIASKLLRVVQCHTVLGQEIARECIAFSTPTDDGRALARQFTGLDNFLTY 1050
Cdd:pfam13880    1 VPAKCGISRIWVSPSHRRKGIATRLLDAARSNFIYGYILEKDEIAFSQPTESGKAFARKYFGTDDFLVY 69
zf-C2H2_3 pfam13878
zinc-finger of acetyl-transferase ESCO;
839-878 3.42e-15

zinc-finger of acetyl-transferase ESCO;


Pssm-ID: 464013  Cd Length: 40  Bit Score: 70.34  E-value: 3.42e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 24659953    839 QYQIDAGQKAFGARQCQQCGLVYTVHEPEEELLHREYHNS 878
Cdd:pfam13878    1 QLILDLGQKSFGATQCKECGMVYNPGSPEDEKLHKKYHAR 40
PRK08581 PRK08581
amidase domain-containing protein;
189-477 5.26e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.01  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   189 AAMLMKGQDSRSMLEKSKKKHNHSLKTTAQVHTTKPKKTSPAEESQSDDEKPSSSKNSRKNT-EVRETRSSQIISPKTRN 267
Cdd:PRK08581   27 ADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSnNIIDFIYKNLPQTNINQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   268 RRRPFTSADINCKTlkaaaHLHENMRSYDEEKTaavKLENSRSRSKSpvevfkSNDDAVKRNTGNTNNKTAKSSEVATAK 347
Cdd:PRK08581  107 LLTKNKYDDNYSLT-----TLIQNLFNLNSDIS---DYEQPRNSEKS------TNDSNKNSDSSIKNDTDTQSSKQDKAD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   348 RPESPGSSMKIDvevPESDEEASNHKPQKrqhPETSTPVAPSADaDSGSPQSKMRKVTLSSSIPTMAFYSHSGEAVTKSR 427
Cdd:PRK08581  173 NQKAPSSNNTKP---STSNKQPNSPKPTQ---PNQSNSQPASDD-TANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQK 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 24659953   428 RRPSISKNSlkqPTKISPTSRPLLGINKGVHHKIRKRHGFANRLPATDMD 477
Cdd:PRK08581  246 DYASQSKKD---KTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTR 292
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 945-1008 7.22e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 7.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24659953  945 FIAVRKQQIVGFCLVQPLSQAHRFiqvdgtdyfseesypasCGVSRIWVSPLQRRSGIASKLLR 1008
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDT-----------------AYIGDLAVLPEYRGKGIGSALLE 48
 
Name Accession Description Interval E-value
Acetyltransf_13 pfam13880
ESCO1/2 acetyl-transferase;
982-1050 1.41e-29

ESCO1/2 acetyl-transferase;


Pssm-ID: 464015  Cd Length: 69  Bit Score: 112.19  E-value: 1.41e-29
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24659953    982 YPASCGVSRIWVSPLQRRSGIASKLLRVVQCHTVLGQEIARECIAFSTPTDDGRALARQFTGLDNFLTY 1050
Cdd:pfam13880    1 VPAKCGISRIWVSPSHRRKGIATRLLDAARSNFIYGYILEKDEIAFSQPTESGKAFARKYFGTDDFLVY 69
zf-C2H2_3 pfam13878
zinc-finger of acetyl-transferase ESCO;
839-878 3.42e-15

zinc-finger of acetyl-transferase ESCO;


Pssm-ID: 464013  Cd Length: 40  Bit Score: 70.34  E-value: 3.42e-15
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 24659953    839 QYQIDAGQKAFGARQCQQCGLVYTVHEPEEELLHREYHNS 878
Cdd:pfam13878    1 QLILDLGQKSFGATQCKECGMVYNPGSPEDEKLHKKYHAR 40
PRK08581 PRK08581
amidase domain-containing protein;
189-477 5.26e-04

amidase domain-containing protein;


Pssm-ID: 236304 [Multi-domain]  Cd Length: 619  Bit Score: 44.01  E-value: 5.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   189 AAMLMKGQDSRSMLEKSKKKHNHSLKTTAQVHTTKPKKTSPAEESQSDDEKPSSSKNSRKNT-EVRETRSSQIISPKTRN 267
Cdd:PRK08581   27 ADDPQKDSTAKTTSHDSKKSNDDETSKDTSSKDTDKADNNNTSNQDNNDKKFSTIDSSTSDSnNIIDFIYKNLPQTNINQ 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   268 RRRPFTSADINCKTlkaaaHLHENMRSYDEEKTaavKLENSRSRSKSpvevfkSNDDAVKRNTGNTNNKTAKSSEVATAK 347
Cdd:PRK08581  107 LLTKNKYDDNYSLT-----TLIQNLFNLNSDIS---DYEQPRNSEKS------TNDSNKNSDSSIKNDTDTQSSKQDKAD 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   348 RPESPGSSMKIDvevPESDEEASNHKPQKrqhPETSTPVAPSADaDSGSPQSKMRKVTLSSSIPTMAFYSHSGEAVTKSR 427
Cdd:PRK08581  173 NQKAPSSNNTKP---STSNKQPNSPKPTQ---PNQSNSQPASDD-TANQKSSSKDNQSMSDSALDSILDQYSEDAKKTQK 245

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 24659953   428 RRPSISKNSlkqPTKISPTSRPLLGINKGVHHKIRKRHGFANRLPATDMD 477
Cdd:PRK08581  246 DYASQSKKD---KTETSNTKNPQLPTQDELKHKSKPAQSFENDVNQSNTR 292
PTZ00112 PTZ00112
origin recognition complex 1 protein; Provisional
 159-389 9.54e-04

origin recognition complex 1 protein; Provisional


Pssm-ID: 240274 [Multi-domain]  Cd Length: 1164  Bit Score: 43.44  E-value: 9.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   159 IRRSPRTFSAQKDPDAFSSPESFQTRLSKVAAMLMKGQDSRSMLEKSKKKHNHSLKTTAQVHTTKPKKtspaeesqsdDE 238
Cdd:PTZ00112  204 MRRSPRNTSTIKNNTNDKNKEKNKEKDKNIKKDRDGDKQTKRNSEKSKVQNSHFDVRILRSYTKENKK----------DE 273

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24659953   239 KPSSSKNSRKNTEVRETRSSQIISPKTRNRRRPFTSADincktLKAAAHLHENMRSYDEEK-TAAVKLENSRSRSKSPVE 317
Cdd:PTZ00112  274 KNVVSGIRSSVLLKRKSQCLRKDSYVYSNHQKKAKTGD-----PKNIIHRNNGSSNSNNDDtSSSNHLGSNRISNRNPSS 348

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24659953   318 VFKSNDDaVKRNTGNTNNKTAKSSEVATAKRPESPGSSM-KIDVEVPESDEEASNHKPQKRQHPE-TSTPVAPS 389
Cdd:PTZ00112  349 PYKKQTT-TKHTNNTKNNKYNKTKTTQKFNHPLRHHATInKRSSMLPMSEQKGRGASEKSEYIKEfTMEEVAKL 421
NAT_SF cd04301
N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer ...
 945-1008 7.22e-03

N-Acyltransferase superfamily: Various enzymes that characteristically catalyze the transfer of an acyl group to a substrate; NAT (N-Acyltransferase) is a large superfamily of enzymes that mostly catalyze the transfer of an acyl group to a substrate and are implicated in a variety of functions, ranging from bacterial antibiotic resistance to circadian rhythms in mammals. Members include GCN5-related N-Acetyltransferases (GNAT) such as Aminoglycoside N-acetyltransferases, Histone N-acetyltransferase (HAT) enzymes, and Serotonin N-acetyltransferase, which catalyze the transfer of an acetyl group to a substrate. The kinetic mechanism of most GNATs involves the ordered formation of a ternary complex: the reaction begins with Acetyl Coenzyme A (AcCoA) binding, followed by binding of substrate, then direct transfer of the acetyl group from AcCoA to the substrate, followed by product and subsequent CoA release. Other family members include Arginine/ornithine N-succinyltransferase, Myristoyl-CoA: protein N-myristoyltransferase, and Acyl-homoserinelactone synthase which have a similar catalytic mechanism but differ in types of acyl groups transferred. Leucyl/phenylalanyl-tRNA-protein transferase and FemXAB nonribosomal peptidyltransferases which catalyze similar peptidyltransferase reactions are also included.


Pssm-ID: 173926 [Multi-domain]  Cd Length: 65  Bit Score: 36.10  E-value: 7.22e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24659953  945 FIAVRKQQIVGFCLVQPLSQAHRFiqvdgtdyfseesypasCGVSRIWVSPLQRRSGIASKLLR 1008
Cdd:cd04301    2 LVAEDDGEIVGFASLSPDGSGGDT-----------------AYIGDLAVLPEYRGKGIGSALLE 48
 
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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