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Conserved domains on  [gi|52632416|gb|AAH35297|]
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Replication factor C (activator 1) 1, 145kDa [Homo sapiens]

Protein Classification

AAA and RFC1 domain-containing protein; BRCT_RFC1 and RFC1 domain-containing protein( domain architecture ID 13027101)

protein containing domains BRCT_RFC1, AAA, and RFC1; protein containing domains COG5275, BRCT_RFC1, AAA, and RFC1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
RFC1 pfam08519
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ...
 915-1068 4.72e-78

Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor C, RFC1. RFC complexes hydrolyse ATP and load sliding clamps such as PCNA (proliferating cell nuclear antigen) onto double-stranded DNA. RFC1 is essential for RFC function in vivo.


:

Pssm-ID: 462507  Cd Length: 158  Bit Score: 253.27  E-value: 4.72e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    915 ICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMRGYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTV 994
Cdd:pfam08519    1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52632416    995 NMDYLSLLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWG----GKPSPFSKLDPKVKAAFTRAYNK 1068
Cdd:pfam08519   81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
PRK04195 super family cl35251
replication factor C large subunit; Provisional
 584-1003 1.79e-51

replication factor C large subunit; Provisional


The actual alignment was detected with superfamily member PRK04195:

Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 189.36  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   584 LLWVDKYKPTSLKTIIGQQgdqSCANKLLRWLRNWQKsssedkkhaakfgkfsgkddGSSFKAALLSGPPGVGKTTTASL 663
Cdd:PRK04195    2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLK--------------------GKPKKALLLYGPPGVGKTSLAHA 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   664 VCQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFysngaassvstKHALI-MDEVDGMAGNEDRGGIQELIGLIK 742
Cdd:PRK04195   59 LANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA-----------RRKLIlLDEVDGIHGNEDRGGARAILELIK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   743 HTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWC 822
Cdd:PRK04195  128 KAKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   823 ARSKALTYDQAKAdshRAKKDIKMGPFDVARKVFA---AGEETAHMSLVDKS-DLFFHdysiaplFVQEN----YIHVKP 894
Cdd:PRK04195  208 EGYGKLTLEDVKT---LGRRDREESIFDALDAVFKarnADQALEASYDVDEDpDDLIE-------WIDENipkeYDDPED 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   895 VAAGGDMkkhlmlLSRAadsicdgDLVDSQIRSKQNWSLLPaqaiYASvlpgELM------------RGYmTQFpTFPSW 962
Cdd:PRK04195  278 IARAYDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGF-TRY-QPPSY 334

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 52632416   963 LGKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLSLLR 1003
Cdd:PRK04195  335 WRLLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
BRCT_RFC1 cd17752
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ...
 402-480 6.25e-46

BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.


:

Pssm-ID: 349383 [Multi-domain]  Cd Length: 79  Bit Score: 159.30  E-value: 6.25e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52632416  402 GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIR 480
Cdd:cd17752    1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
PTZ00121 super family cl31754
MAEBL; Provisional
 14-404 1.30e-08

MAEBL; Provisional


The actual alignment was detected with superfamily member PTZ00121:

Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    14 KKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLP--- 90
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkka 1407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    91 --VSSKPGKISRQDPVTYISETDEEDDFMCKKA--ASKSKENGRSTNSHLGTSNMKKNEENTKTKNKplSPIKLTPTSVL 166
Cdd:PTZ00121 1408 deLKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKA 1485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   167 DYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEA-IAKQLQLDEDAELERQLHEDEEF--ARTLAMLDEEPKTKKARK 243
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKK 1565

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   244 DTEAGETFSSVQANLSKAEKHKyphKVKTAQVSDERKSYSPRKQSKYESSKESQQhSKSSADKIGEVSSPKasSKLAIMK 323
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEK--KKVEQLK 1639

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   324 RKEESSYKEIEPVASKRKENAIKLKGETKTPKKTKSspaKKESVSPEDSEKKRTNYQayrsyLNREGPKALGSKEIPKGA 403
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEA-----LKKEAEEAKKAEELKKKE 1711


                  .
gi 52632416   404 E 404
Cdd:PTZ00121 1712 A 1712
 
Name Accession Description Interval E-value
RFC1 pfam08519
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ...
 915-1068 4.72e-78

Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor C, RFC1. RFC complexes hydrolyse ATP and load sliding clamps such as PCNA (proliferating cell nuclear antigen) onto double-stranded DNA. RFC1 is essential for RFC function in vivo.


Pssm-ID: 462507  Cd Length: 158  Bit Score: 253.27  E-value: 4.72e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    915 ICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMRGYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTV 994
Cdd:pfam08519    1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52632416    995 NMDYLSLLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWG----GKPSPFSKLDPKVKAAFTRAYNK 1068
Cdd:pfam08519   81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
PRK04195 PRK04195
replication factor C large subunit; Provisional
 584-1003 1.79e-51

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 189.36  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   584 LLWVDKYKPTSLKTIIGQQgdqSCANKLLRWLRNWQKsssedkkhaakfgkfsgkddGSSFKAALLSGPPGVGKTTTASL 663
Cdd:PRK04195    2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLK--------------------GKPKKALLLYGPPGVGKTSLAHA 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   664 VCQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFysngaassvstKHALI-MDEVDGMAGNEDRGGIQELIGLIK 742
Cdd:PRK04195   59 LANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA-----------RRKLIlLDEVDGIHGNEDRGGARAILELIK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   743 HTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWC 822
Cdd:PRK04195  128 KAKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   823 ARSKALTYDQAKAdshRAKKDIKMGPFDVARKVFA---AGEETAHMSLVDKS-DLFFHdysiaplFVQEN----YIHVKP 894
Cdd:PRK04195  208 EGYGKLTLEDVKT---LGRRDREESIFDALDAVFKarnADQALEASYDVDEDpDDLIE-------WIDENipkeYDDPED 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   895 VAAGGDMkkhlmlLSRAadsicdgDLVDSQIRSKQNWSLLPaqaiYASvlpgELM------------RGYmTQFpTFPSW 962
Cdd:PRK04195  278 IARAYDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGF-TRY-QPPSY 334

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 52632416   963 LGKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLSLLR 1003
Cdd:PRK04195  335 WRLLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
BRCT_RFC1 cd17752
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ...
 402-480 6.25e-46

BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.


Pssm-ID: 349383 [Multi-domain]  Cd Length: 79  Bit Score: 159.30  E-value: 6.25e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52632416  402 GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIR 480
Cdd:cd17752    1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
398-479 9.73e-28

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 120.51  E-value: 9.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  398 EIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIIDEDGLLN 477
Cdd:COG0272  587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665


                 ..
gi 52632416  478 LI 479
Cdd:COG0272  666 LL 667
ligA PRK07956
NAD-dependent DNA ligase LigA; Validated
 392-479 1.85e-25

NAD-dependent DNA ligase LigA; Validated


Pssm-ID: 236137 [Multi-domain]  Cd Length: 665  Bit Score: 113.29  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   392 KALGSKEIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIID 471
Cdd:PRK07956  576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654


                  ....*...
gi 52632416   472 EDGLLNLI 479
Cdd:PRK07956  655 EEEFLRLL 662
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 648-776 5.54e-17

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 78.40  E-value: 5.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    648 LLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKsslkaIVAESLNNtsIKGFYSNgaASSVStKHALIMDEVDGMAG 727
Cdd:pfam00004    2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEA--AKKLA-PCVIFIDEIDALAG 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52632416    728 NEDRGGIQELIGLI------------KHTKIPIICMCNdrNHPKIRSLVHYCFDLRFQRPR 776
Cdd:pfam00004   72 SRGSGGDSESRRVVnqllteldgftsSNSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 404-479 5.34e-15

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 70.79  E-value: 5.34e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52632416    404 ENCLEGLIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMgrDSGQSKSDKAAALGTKIIDEDGLLNLI 479
Cdd:pfam00533    3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 643-772 3.03e-14

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 71.41  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  643 SFKAALLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSksslKAIVAESLNNTSIKGFYSNGAASSVSTkhaLIM 719
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLE----GLVVAELFGHFLVRLLFELAEKAKPGV---LFI 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 52632416  720 DEVDGMAGNEDRGGIQEL----IGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRF 772
Cdd:cd00009   91 DEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
BRCT smart00292
breast cancer carboxy-terminal domain;
404-479 2.61e-13

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 66.24  E-value: 2.61e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52632416     404 ENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAA--LGTKIIDEDGLLNLI 479
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAiaLGIPIVKEEWLLDCL 78
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 648-778 7.09e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 55.84  E-value: 7.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416     648 LLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFYSNGA-----ASSVSTKhALIM 719
Cdd:smart00382    6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalARKLKPD-VLIL 84

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52632416     720 DEVDGMAGNEDRGGIQE------LIGLIKHTKIPIICMCNDRNHPKIRSLVHyCFDLRFQRPRVE 778
Cdd:smart00382   85 DEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
PTZ00121 PTZ00121
MAEBL; Provisional
 14-404 1.30e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    14 KKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLP--- 90
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkka 1407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    91 --VSSKPGKISRQDPVTYISETDEEDDFMCKKA--ASKSKENGRSTNSHLGTSNMKKNEENTKTKNKplSPIKLTPTSVL 166
Cdd:PTZ00121 1408 deLKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKA 1485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   167 DYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEA-IAKQLQLDEDAELERQLHEDEEF--ARTLAMLDEEPKTKKARK 243
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKK 1565

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   244 DTEAGETFSSVQANLSKAEKHKyphKVKTAQVSDERKSYSPRKQSKYESSKESQQhSKSSADKIGEVSSPKasSKLAIMK 323
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEK--KKVEQLK 1639

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   324 RKEESSYKEIEPVASKRKENAIKLKGETKTPKKTKSspaKKESVSPEDSEKKRTNYQayrsyLNREGPKALGSKEIPKGA 403
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEA-----LKKEAEEAKKAEELKKKE 1711


                  .
gi 52632416   404 E 404
Cdd:PTZ00121 1712 A 1712
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 645-733 3.07e-06

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 51.07  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  645 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK------SSLKAIVAESLnntsikgfysnGAASSVstkhaLI 718
Cdd:COG0464  192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFDKAR-----------GLAPCV-----LF 255

                         90
                 ....*....|....*
gi 52632416  719 MDEVDGMAGNEDRGG 733
Cdd:COG0464  256 IDEADALAGKRGEVG 270
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 537-674 2.45e-05

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 48.41  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    537 SLAKTIKKETDVFWKSLDFKEQVAEETSGDSKARNLADD-------SSENKVENLLWVDKYKPTSlktiigqQGDQSCAN 609
Cdd:TIGR00602   18 SLISTITKWSLSRPTSSHRRKNSPSTDIHARKRGFLSLEqdtglelSSENLDGNEPWVEKYKPET-------QHELAVHK 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52632416    610 KLLRWLRNWQKSSS-EDKKHaakfgkfsgkddgssfKAALLSGPPGVGKTTTASLVCQELGYSYVE 674
Cdd:TIGR00602   91 KKIEEVETWLKAQVlENAPK----------------RILLITGPSGCGKSTTIKILSKELGIQVQE 140
 
Name Accession Description Interval E-value
RFC1 pfam08519
Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor ...
 915-1068 4.72e-78

Replication factor RFC1 C terminal domain; This is the C terminal domain of replication factor C, RFC1. RFC complexes hydrolyse ATP and load sliding clamps such as PCNA (proliferating cell nuclear antigen) onto double-stranded DNA. RFC1 is essential for RFC function in vivo.


Pssm-ID: 462507  Cd Length: 158  Bit Score: 253.27  E-value: 4.72e-78
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    915 ICDGDLVDSQIRSKQNWSLLPAQAIYASVLPGELMRGYMTQFPTFPSWLGKHSSTGKHDRIVQDLALHMSLRTYSSKRTV 994
Cdd:pfam08519    1 ISDGDLVDRMIRGEQQWSLLPTHAVFSSVRPASFMRGSMTGRINFPSWLGKNSKTGKNKRLLQELQYHMRLKTSGDKSEL 80

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52632416    995 NMDYLSLLRDALVQPLTSQGVDGVQDVVALMDTYYLMKEDFENIMEISSWG----GKPSPFSKLDPKVKAAFTRAYNK 1068
Cdd:pfam08519   81 RLDYLPLLRKRLTQPLLEEGKDGVDEVIDLMDEYYLTKEDWDNIVELSTWGvgpyGEEDPLKKIDTKVKAAFTRKYNK 158
PRK04195 PRK04195
replication factor C large subunit; Provisional
 584-1003 1.79e-51

replication factor C large subunit; Provisional


Pssm-ID: 235250 [Multi-domain]  Cd Length: 482  Bit Score: 189.36  E-value: 1.79e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   584 LLWVDKYKPTSLKTIIGQQgdqSCANKLLRWLRNWQKsssedkkhaakfgkfsgkddGSSFKAALLSGPPGVGKTTTASL 663
Cdd:PRK04195    2 MPWVEKYRPKTLSDVVGNE---KAKEQLREWIESWLK--------------------GKPKKALLLYGPPGVGKTSLAHA 58

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   664 VCQELGYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFysngaassvstKHALI-MDEVDGMAGNEDRGGIQELIGLIK 742
Cdd:PRK04195   59 LANDYGWEVIELNASDQRTADVIERVAGEAATSGSLFGA-----------RRKLIlLDEVDGIHGNEDRGGARAILELIK 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   743 HTKIPIICMCNDRNHPKIRSLVHYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWC 822
Cdd:PRK04195  128 KAKQPIILTANDPYDPSLRELRNACLMIEFKRLSTRSIVPVLKRICRKEGIECDDEALKEIAERSGGDLRSAINDLQAIA 207

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   823 ARSKALTYDQAKAdshRAKKDIKMGPFDVARKVFA---AGEETAHMSLVDKS-DLFFHdysiaplFVQEN----YIHVKP 894
Cdd:PRK04195  208 EGYGKLTLEDVKT---LGRRDREESIFDALDAVFKarnADQALEASYDVDEDpDDLIE-------WIDENipkeYDDPED 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   895 VAAGGDMkkhlmlLSRAadsicdgDLVDSQIRSKQNWSLLPaqaiYASvlpgELM------------RGYmTQFpTFPSW 962
Cdd:PRK04195  278 IARAYDA------LSRA-------DIFLGRVKRTQNYDLWR----YAS----DLMtagvalakekkkRGF-TRY-QPPSY 334

                         410       420       430       440
                  ....*....|....*....|....*....|....*....|.
gi 52632416   963 LGKHSSTGKHDRIVQDLALHMSLRTYSSKRTVNMDYLSLLR 1003
Cdd:PRK04195  335 WRLLSKTKEKRETRDSIAKKIAEKLHTSKRKVRREVLPFLS 375
BRCT_RFC1 cd17752
BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed ...
 402-480 6.25e-46

BRCT domain of replication factor C subunit 1 (RFC1) and similar proteins; RFC1, also termed activator 1 140 kDa subunit, or A1 140 kDa subunit, or activator 1 large subunit, or activator 1 subunit 1, or replication factor C 140 kDa subunit, or RF-C 140 kDa subunit, or RFC140, is the large subunit of replication factor C (RFC), which is a heteropentameric protein essential for DNA replication and repair. RFC1 can bind single- or double-stranded DNA. It could play a role in DNA transcription regulation as well as DNA replication and/or repair. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.


Pssm-ID: 349383 [Multi-domain]  Cd Length: 79  Bit Score: 159.30  E-value: 6.25e-46
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52632416  402 GAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDEDGLLNLIR 480
Cdd:cd17752    1 GAPNCLEGLTFVITGVLESLEREEAEDLIKRYGGKVTGSVSKKTSYLVVGRDAGPSKLEKAKELGTKIIDEDGLFDLIR 79
Lig COG0272
NAD-dependent DNA ligase [Replication, recombination and repair];
398-479 9.73e-28

NAD-dependent DNA ligase [Replication, recombination and repair];


Pssm-ID: 440042 [Multi-domain]  Cd Length: 668  Bit Score: 120.51  E-value: 9.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  398 EIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIIDEDGLLN 477
Cdd:COG0272  587 EAEAAADSPLAGKTFVLTGTLETMTRDEAKELIEALGGKVSGSVSKKTDYVVAGENAG-SKLDKAEELGVPILDEAEFLE 665


                 ..
gi 52632416  478 LI 479
Cdd:COG0272  666 LL 667
ligA PRK07956
NAD-dependent DNA ligase LigA; Validated
 392-479 1.85e-25

NAD-dependent DNA ligase LigA; Validated


Pssm-ID: 236137 [Multi-domain]  Cd Length: 665  Bit Score: 113.29  E-value: 1.85e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   392 KALGSKEIPKGAENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGqSKSDKAAALGTKIID 471
Cdd:PRK07956  576 LEAGVNMEYKGEEVDLAGKTVVLTGTLEQLSRDEAKEKLEALGAKVSGSVSKKTDLVVAGEAAG-SKLAKAQELGIEVLD 654


                  ....*...
gi 52632416   472 EDGLLNLI 479
Cdd:PRK07956  655 EEEFLRLL 662
BRCT_DNA_ligase_like cd17748
BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also ...
 407-478 5.76e-24

BRCT domain of bacterial NAD-dependent DNA ligase (LigA) and similar proteins; LigA, also called NAD(+)-dependent polydeoxyribonucleotide synthase, catalyzes the formation of phosphodiester linkages between 5'-phosphoryl and 3'-hydroxyl groups in double-stranded DNA using NAD as a coenzyme and as the energy source for the reaction. It is essential for DNA replication and repair of damaged DNA. The Trp-X-X-X-Cys/Ser signature motif of the BRCT family is not conserved in this family.


Pssm-ID: 349379 [Multi-domain]  Cd Length: 76  Bit Score: 96.40  E-value: 5.76e-24
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52632416  407 LEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSD----KAAALGTKIIDEDGLLNL 478
Cdd:cd17748    1 LAGKTFVFTGTLSSMSRDEAEELIEALGGKVQSSVSKKTDYLVVGDNAGSKLKKgeelKAKGLGIKIISEEEFLDL 76
AAA pfam00004
ATPase family associated with various cellular activities (AAA); AAA family proteins often ...
 648-776 5.54e-17

ATPase family associated with various cellular activities (AAA); AAA family proteins often perform chaperone-like functions that assist in the assembly, operation, or disassembly of protein complexes.


Pssm-ID: 459627 [Multi-domain]  Cd Length: 130  Bit Score: 78.40  E-value: 5.54e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    648 LLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKsslkaIVAESLNNtsIKGFYSNgaASSVStKHALIMDEVDGMAG 727
Cdd:pfam00004    2 LLYGPPGTGKTTLAKAVAKELGAPFIEISGSELVSK-----YVGESEKR--LRELFEA--AKKLA-PCVIFIDEIDALAG 71

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 52632416    728 NEDRGGIQELIGLI------------KHTKIPIICMCNdrNHPKIRSLVHYCFDLRFQRPR 776
Cdd:pfam00004   72 SRGSGGDSESRRVVnqllteldgftsSNSKVIVIAATN--RPDKLDPALLGRFDRIIEFPL 130
BRCT pfam00533
BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in ...
 404-479 5.34e-15

BRCA1 C Terminus (BRCT) domain; The BRCT domain is found predominantly in proteins involved in cell cycle checkpoint functions responsive to DNA damage. The BRCT domain of XRCC1 forms a homodimer in the crystal structure. This suggests that pairs of BRCT domains associate as homo- or heterodimers. BRCT domains are often found as tandem-repeat pairs. Structures of the BRCA1 BRCT domains revealed a basis for a widely utilized head-to-tail BRCT-BRCT oligomerization mode. This conserved tandem BRCT architecture facilitates formation of the canonical BRCT phospho-peptide interaction cleft at a groove between the BRCT domains. Disease associated missense and nonsense mutations in the BRCA1 BRCT domains disrupt peptide binding by directly occluding this peptide binding groove, or by disrupting key conserved BRCT core folding determinants.


Pssm-ID: 425736 [Multi-domain]  Cd Length: 75  Bit Score: 70.79  E-value: 5.34e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52632416    404 ENCLEGLIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMgrDSGQSKSDKAAALGTKIIDEDGLLNLI 479
Cdd:pfam00533    3 EKLFSGKTFVITG-LDGLERDELKELIEKLGGKVTDSLSKKTTHVIV--EARTKKYLKAKELGIPIVTEEWLLDCI 75
AAA cd00009
The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily ...
 643-772 3.03e-14

The AAA+ (ATPases Associated with a wide variety of cellular Activities) superfamily represents an ancient group of ATPases belonging to the ASCE (for additional strand, catalytic E) division of the P-loop NTPase fold. The ASCE division also includes ABC, RecA-like, VirD4-like, PilT-like, and SF1/2 helicases. Members of the AAA+ ATPases function as molecular chaperons, ATPase subunits of proteases, helicases, or nucleic-acid stimulated ATPases. The AAA+ proteins contain several distinct features in addition to the conserved alpha-beta-alpha core domain structure and the Walker A and B motifs of the P-loop NTPases.


Pssm-ID: 99707 [Multi-domain]  Cd Length: 151  Bit Score: 71.41  E-value: 3.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  643 SFKAALLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSksslKAIVAESLNNTSIKGFYSNGAASSVSTkhaLIM 719
Cdd:cd00009   18 PPKNLLLYGPPGTGKTTLARAIANELfrpGAPFLYLNASDLLE----GLVVAELFGHFLVRLLFELAEKAKPGV---LFI 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 52632416  720 DEVDGMAGNEDRGGIQEL----IGLIKHTKIPIICMCNDRNHPKIRSLVHYCFDLRF 772
Cdd:cd00009   91 DEIDSLSRGAQNALLRVLetlnDLRIDRENVRVIGATNRPLLGDLDRALYDRLDIRI 147
BRCT smart00292
breast cancer carboxy-terminal domain;
404-479 2.61e-13

breast cancer carboxy-terminal domain;


Pssm-ID: 214602 [Multi-domain]  Cd Length: 78  Bit Score: 66.24  E-value: 2.61e-13
                            10        20        30        40        50        60        70
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 52632416     404 ENCLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAA--LGTKIIDEDGLLNLI 479
Cdd:smart00292    1 PKLFKGKTFYITGSFDKEERDELKELIEALGGKVTSSLSSKTTTHVIVGSPEGGKLELLKAiaLGIPIVKEEWLLDCL 78
PLN03025 PLN03025
replication factor C subunit; Provisional
 586-818 4.58e-11

replication factor C subunit; Provisional


Pssm-ID: 178596 [Multi-domain]  Cd Length: 319  Bit Score: 65.52  E-value: 4.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   586 WVDKYKPTSLKTIIGQQGDQSCANKLLRwlrnwqksssedkkhaakfgkfsgkdDGSsFKAALLSGPPGVGKTTTA-SLV 664
Cdd:PLN03025    3 WVEKYRPTKLDDIVGNEDAVSRLQVIAR--------------------------DGN-MPNLILSGPPGTGKTTSIlALA 55

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   665 CQELGYSY----VELNASDTRSKSSLKaivaeslnnTSIKGFYSNGAASSVSTKHALIMDEVDGMAGnedrGGIQELIGL 740
Cdd:PLN03025   56 HELLGPNYkeavLELNASDDRGIDVVR---------NKIKMFAQKKVTLPPGRHKIVILDEADSMTS----GAQQALRRT 122

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   741 IK----HTKIPIICMCNDRNHPKIRSlvhYCFDLRFQRPRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLH 816
Cdd:PLN03025  123 MEiysnTTRFALACNTSSKIIEPIQS---RCAIVRFSRLSDQEILGRLMKVVEAEKVPYVPEGLEAIIFTADGDMRQALN 199


                  ..
gi 52632416   817 NL 818
Cdd:PLN03025  200 NL 201
HLD_clamp_RFC cd18140
helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein ...
 775-831 2.19e-10

helical lid domain of replication factor C subunit; Replication factor C (RFC) is five-protein clamp loader complex that forms a stable ATP-dependent complex with the sliding clamp, PCNA, which binds specifically to primed DNA. RFC subunits belong to the clamp loader clade of the AAA+ superfamily.


Pssm-ID: 350842 [Multi-domain]  Cd Length: 63  Bit Score: 57.15  E-value: 2.19e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 52632416  775 PRVEQIKGAMMSIAFKEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCARSKALTYD 831
Cdd:cd18140    1 LSKEQIVKRLREICKKEGVKIDEEALEAIAEKSEGDMRKAINDLQAAAAGGGVITEE 57
AAA smart00382
ATPases associated with a variety of cellular activities; AAA - ATPases associated with a ...
 648-778 7.09e-09

ATPases associated with a variety of cellular activities; AAA - ATPases associated with a variety of cellular activities. This profile/alignment only detects a fraction of this vast family. The poorly conserved N-terminal helix is missing from the alignment.


Pssm-ID: 214640 [Multi-domain]  Cd Length: 148  Bit Score: 55.84  E-value: 7.09e-09
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416     648 LLSGPPGVGKTTTASLVCQEL---GYSYVELNASDTRSKSSLKAIVAESLNNTSIKGFYSNGA-----ASSVSTKhALIM 719
Cdd:smart00382    6 LIVGPPGSGKTTLARALARELgppGGGVIYIDGEDILEEVLDQLLLIIVGGKKASGSGELRLRlalalARKLKPD-VLIL 84

                            90       100       110       120       130       140
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 52632416     720 DEVDGMAGNEDRGGIQE------LIGLIKHTKIPIICMCNDRNHPKIRSLVHyCFDLRFQRPRVE 778
Cdd:smart00382   85 DEITSLLDAEQEALLLLleelrlLLLLKSEKNLTVILTTNDEKDLGPALLRR-RFDRRIVLLLIL 148
BRCT cd00027
C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The ...
 410-473 8.04e-09

C-terminal domain of the breast cancer suppressor protein (BRCA1) and related domains; The BRCT (BRCA1 C-terminus) domain is found within many DNA damage repair and cell cycle checkpoint proteins. BRCT domains interact with each other forming homo/hetero BRCT multimers, but are also involved in BRCT-non-BRCT interactions and interactions within DNA strand breaks. BRCT tandem repeats bind to phosphopeptides; it has been shown that the repeats in human BRCA1 bind specifically to pS-X-X-F motifs, mediating the interaction between BRCA1 and the DNA helicase BACH1, or BRCA1 and CtIP, a transcriptional corepressor. It is assumed that BRCT repeats play similar roles in many signaling pathways associated with the response to DNA damage.


Pssm-ID: 349339 [Multi-domain]  Cd Length: 68  Bit Score: 53.13  E-value: 8.04e-09
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 52632416  410 LIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQSKSDKAAALGTKIIDED 473
Cdd:cd00027    1 LVICFSG-LDDEEREELKKLIEALGGKVSESLSSKVTHLIAKSPSGEKYYLAALAWGIPIVSPE 63
PTZ00121 PTZ00121
MAEBL; Provisional
 14-404 1.30e-08

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 59.77  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    14 KKLVSETVKKNEKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLP--- 90
Cdd:PTZ00121 1328 KKKADAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEKKKADEAKKKAEEDKkka 1407

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    91 --VSSKPGKISRQDPVTYISETDEEDDFMCKKA--ASKSKENGRSTNSHLGTSNMKKNEENTKTKNKplSPIKLTPTSVL 166
Cdd:PTZ00121 1408 deLKKAAAAKKKADEAKKKAEEKKKADEAKKKAeeAKKADEAKKKAEEAKKAEEAKKKAEEAKKADE--AKKKAEEAKKA 1485

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   167 DYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEA-IAKQLQLDEDAELERQLHEDEEF--ARTLAMLDEEPKTKKARK 243
Cdd:PTZ00121 1486 DEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAkKADEAKKAEEAKKADEAKKAEEKkkADELKKAEELKKAEEKKK 1565

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   244 DTEAGETFSSVQANLSKAEKHKyphKVKTAQVSDERKSYSPRKQSKYESSKESQQhSKSSADKIGEVSSPKasSKLAIMK 323
Cdd:PTZ00121 1566 AEEAKKAEEDKNMALRKAEEAK---KAEEARIEEVMKLYEEEKKMKAEEAKKAEE-AKIKAEELKKAEEEK--KKVEQLK 1639

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   324 RKEESSYKEIEPVASKRKENAIKLKGETKTPKKTKSspaKKESVSPEDSEKKRTNYQayrsyLNREGPKALGSKEIPKGA 403
Cdd:PTZ00121 1640 KKEAEEKKKAEELKKAEEENKIKAAEEAKKAEEDKK---KAEEAKKAEEDEKKAAEA-----LKKEAEEAKKAEELKKKE 1711


                  .
gi 52632416   404 E 404
Cdd:PTZ00121 1712 A 1712
PRK06195 PRK06195
DNA polymerase III subunit epsilon; Validated
 326-480 2.40e-08

DNA polymerase III subunit epsilon; Validated


Pssm-ID: 235735 [Multi-domain]  Cd Length: 309  Bit Score: 57.10  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   326 EESSYKEIEPVASKRKENAIKLKGETKTPKKTKSSPAKKESvsPEDSEKKRtnyqayrsylnregpkalgsKEIPKGAEN 405
Cdd:PRK06195  162 KELNSKDINEISKLLGVTLGYVNENGYKPSSRKGRILKRSN--RQAPRKKK--------------------KIIESFGFT 219

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   406 CLEGLIFVITGVLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMG--------RDSGQSKSDKAAAL-----GTKIIDE 472
Cdd:PRK06195  220 AFKEEVVVFTGGLASMTRDEAMILVRRLGGTVGSSVTKKTTYLVTNtkdiedlnREEMSNKLKKAIDLkkkgqNIKFLNE 299


                  ....*...
gi 52632416   473 DGLLNLIR 480
Cdd:PRK06195  300 EEFLQKCK 307
PRK13342 PRK13342
recombination factor protein RarA; Reviewed
 588-698 1.26e-07

recombination factor protein RarA; Reviewed


Pssm-ID: 237355 [Multi-domain]  Cd Length: 413  Bit Score: 55.48  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   588 DKYKPTSLKTIIGQQ---GdqscANKLLRwlrnwqksssedkkHAAKFGKFSgkddgsSFkaaLLSGPPGVGKTTTASLV 664
Cdd:PRK13342    4 ERMRPKTLDEVVGQEhllG----PGKPLR--------------RMIEAGRLS------SM---ILWGPPGTGKTTLARII 56

                          90       100       110
                  ....*....|....*....|....*....|....
gi 52632416   665 CQELGYSYVELNASDTrSKSSLKAIVAESLNNTS 698
Cdd:PRK13342   57 AGATDAPFEALSAVTS-GVKDLREVIEEARQRRS 89
44 PHA02544
clamp loader, small subunit; Provisional
 584-818 6.90e-07

clamp loader, small subunit; Provisional


Pssm-ID: 222866 [Multi-domain]  Cd Length: 316  Bit Score: 52.68  E-value: 6.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   584 LLWVDKYKPTSLKTIIGQQGDQscankllrwlrnwqksssedkkhaAKFGKFSgkDDGSSFKAALLSGPPGVGKTTTASL 663
Cdd:PHA02544    9 FMWEQKYRPSTIDECILPAADK------------------------ETFKSIV--KKGRIPNMLLHSPSPGTGKTTVAKA 62

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   664 VCQELGYSYVELNASDTRsksslkaivAESLNNtSIKGFysngaASSVSTK---HALIMDEVD--GMAGNED--RGGIQE 736
Cdd:PHA02544   63 LCNEVGAEVLFVNGSDCR---------IDFVRN-RLTRF-----ASTVSLTgggKVIIIDEFDrlGLADAQRhlRSFMEA 127

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   737 LiglikHTKIPIICMCNDRN--HPKIRSlvhYCFDLRFQRP-RVEQI--KGAM----MSIAFKEGLKIPPPAMNEIILGA 807
Cdd:PHA02544  128 Y-----SKNCSFIITANNKNgiIEPLRS---RCRVIDFGVPtKEEQIemMKQMivrcKGILEAEGVEVDMKVLAALVKKN 199

                         250
                  ....*....|.
gi 52632416   808 NQDIRQVLHNL 818
Cdd:PHA02544  200 FPDFRRTINEL 210
rfc PRK00440
replication factor C small subunit; Reviewed
 580-681 1.33e-06

replication factor C small subunit; Reviewed


Pssm-ID: 234763 [Multi-domain]  Cd Length: 319  Bit Score: 51.80  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   580 KVENLLWVDKYKPTSLKTIIGQQgdqscanKLLRWLRNWQKSssEDKKHAakfgkfsgkddgssfkaaLLSGPPGVGKTT 659
Cdd:PRK00440    1 AMMEEIWVEKYRPRTLDEIVGQE-------EIVERLKSYVKE--KNMPHL------------------LFAGPPGTGKTT 53

                          90       100
                  ....*....|....*....|....*..
gi 52632416   660 TASLVCQEL-GYSY----VELNASDTR 681
Cdd:PRK00440   54 AALALARELyGEDWrenfLELNASDER 80
PTZ00121 PTZ00121
MAEBL; Provisional
 14-405 1.57e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.84  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    14 KKLVSETVKKNEKTKSDEETLKA---KKGIKEIKVNSSRKEDDFKQKQPSKKKRIIYDSDS--ESEETLQVKNAKKPPEK 88
Cdd:PTZ00121 1496 KKKADEAKKAAEAKKKADEAKKAeeaKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEElkKAEEKKKAEEAKKAEED 1575

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    89 LPVSSKPGKISRQDPVTYISETDEEDDFMCKKAASKSKengRSTNSHLGTSNMKKNEENTKtknkplspikltptsvldy 168
Cdd:PTZ00121 1576 KNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKAEEAK---KAEEAKIKAEELKKAEEEKK------------------- 1633

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   169 fgtgSVQRSNKKMVASKRK--ELSQNTDESGLNDEAIAKQLQLDEDAELERQLHEDEEFARTLAMLDEEPKTKKAR--KD 244
Cdd:PTZ00121 1634 ----KVEQLKKKEAEEKKKaeELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEelKK 1709

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   245 TEAGETFSSVQANLSKAEKHKYPHKVKTAQVSDERKSYSPRKQSkyESSKESQQHSKSSADKIGEVSSPKASSKLAIMKR 324
Cdd:PTZ00121 1710 KEAEEKKKAEELKKAEEENKIKAEEAKKEAEEDKKKAEEAKKDE--EEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDE 1787

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   325 KEESSYKEIEpvaskRKENAIKLKGETKTPKKTKSSPAKKESVSPEDSEKKRTnyqAYRSYLNREGPKALGSKEIPKGAE 404
Cdd:PTZ00121 1788 EDEKRRMEVD-----KKIKDIFDNFANIIEGGKEGNLVINDSKEMEDSAIKEV---ADSKNMQLEEADAFEKHKFNKNNE 1859


                  .
gi 52632416   405 N 405
Cdd:PTZ00121 1860 N 1860
PTZ00121 PTZ00121
MAEBL; Provisional
 14-375 2.12e-06

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 52.45  E-value: 2.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    14 KKLVSETVKKNEKTKSDEETLK----AKKGIKEI--KVNSSRKEDDFKQKQPSKKKRIIYDSDSESE-ETLQVKNAKKPP 86
Cdd:PTZ00121 1301 KKKADEAKKKAEEAKKADEAKKkaeeAKKKADAAkkKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEaAEKKKEEAKKKA 1380

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    87 EKLpvSSKPGKISRQDPVTYISETDEEDDFMCKKAASKSKENGRSTnshlgtsnmKKNEENTKT---KNKPLSPIKLTPT 163
Cdd:PTZ00121 1381 DAA--KKKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAK---------KKAEEKKKAdeaKKKAEEAKKADEA 1449

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   164 SVLDYFGTGSVQRSNKKMVASKRKELSQNTDESGLNDEAIAKQLQLDEDAELERQLHEDEEFARTLAMLDEEPKTKKARK 243
Cdd:PTZ00121 1450 KKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKK 1529

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   244 DTEAGETFSSVQA-NLSKAEKHKYPHKVKTAQ---VSDERKSYSPRKQSKYESSKESQQHSKSSADKIGEVSSPKASSKL 319
Cdd:PTZ00121 1530 AEEAKKADEAKKAeEKKKADELKKAEELKKAEekkKAEEAKKAEEDKNMALRKAEEAKKAEEARIEEVMKLYEEEKKMKA 1609

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 52632416   320 AIMKRKEESSYKEIEpvasKRKENAIKLKGEtKTPKKTKSSPAKKESVSPEDSEKK 375
Cdd:PTZ00121 1610 EEAKKAEEAKIKAEE----LKKAEEEKKKVE-QLKKKEAEEKKKAEELKKAEEENK 1660
SpoVK COG0464
AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle ...
 645-733 3.07e-06

AAA+-type ATPase, SpoVK/Ycf46/Vps4 family [Cell wall/membrane/envelope biogenesis, Cell cycle control, cell division, chromosome partitioning, Signal transduction mechanisms];


Pssm-ID: 440232 [Multi-domain]  Cd Length: 397  Bit Score: 51.07  E-value: 3.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  645 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK------SSLKAIVAESLnntsikgfysnGAASSVstkhaLI 718
Cdd:COG0464  192 RGLLLYGPPGTGKTLLARALAGELGLPLIEVDLSDLVSKyvgeteKNLREVFDKAR-----------GLAPCV-----LF 255

                         90
                 ....*....|....*
gi 52632416  719 MDEVDGMAGNEDRGG 733
Cdd:COG0464  256 IDEADALAGKRGEVG 270
HolB COG0470
DNA polymerase III, delta prime subunit [Replication, recombination and repair];
646-824 3.94e-06

DNA polymerase III, delta prime subunit [Replication, recombination and repair];


Pssm-ID: 440238 [Multi-domain]  Cd Length: 289  Bit Score: 49.97  E-value: 3.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  646 AALLSGPPGVGKTTTA-----SLVCQELGYS------------------YVELNA---SDTRSKSSLKAIVaESLNNTSI 699
Cdd:COG0470   20 ALLLHGPPGIGKTTLAlalarDLLCENPEGGkacgqchsrlmaagnhpdLLELNPeekSDQIGIDQIRELG-EFLSLTPL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  700 KGFYSngaassvstkhALIMDEVDGMAGNEDRGGIQELIGLIKHTkiPIICMCNDRNH--PKIRSLvhyCFDLRFQRPRV 777
Cdd:COG0470   99 EGGRK-----------VVIIDEADAMNEAAANALLKTLEEPPKNT--PFILIANDPSRllPTIRSR---CQVIRFRPPSE 162

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 52632416  778 EQIKGAMmsiafkEGLKIPPPAMNEIILGANQDIRQVLHNLSMWCAR 824
Cdd:COG0470  163 EEALAWL------REEGVDEDALEAILRLAGGDPRAAINLLQALAGR 203
BRCT_PARP1 cd17747
BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2. ...
 407-473 7.77e-06

BRCT domain of poly [ADP-ribose] polymerase 1 (PARP-1) and similar proteins; PARP-1 (EC 2.4.2.30), also termed ADP-ribosyltransferase diphtheria toxin-like 1 (ARTD1), or NAD(+) ADP-ribosyltransferase 1 (ADPRT 1), or poly[ADP-ribose] synthase 1, is involved in the base excision repair (BER) pathway, by catalyzing the poly(ADP-ribosyl)ation of a limited number of acceptor proteins involved in chromatin architecture and in DNA metabolism.


Pssm-ID: 349378 [Multi-domain]  Cd Length: 76  Bit Score: 44.83  E-value: 7.77e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  407 LEGLIFVITGVLeSIERDEAKSLIERYGGKVTGNVSKKTNYLV---MGRDSGQSKSDKAAALGTKIIDED 473
Cdd:cd17747    1 LTGMKFALIGKL-SKSKDELKKLIEKLGGKVASKVTKKVTLCIstkAEVEKMSKKMKEAKEAGVPVVSED 69
RecA-like_protease cd19481
proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of ...
 645-753 1.92e-05

proteases similar to RecA; RecA-like NTPases. This family includes the NTP binding domain of F1 and V1 H(+)ATPases, DnaB and related helicases as well as bacterial RecA and related eukaryotic and archaeal recombinases. This group also includes bacterial conjugation proteins and related DNA transfer proteins involved in type II and type IV secretion.


Pssm-ID: 410889 [Multi-domain]  Cd Length: 158  Bit Score: 46.12  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  645 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSKSS------LKAI--VAESLnntsikgfysngaASSVstkha 716
Cdd:cd19481   27 KGILLYGPPGTGKTLLAKALAGELGLPLIVVKLSSLLSKYVgeseknLRKIfeRARRL-------------APCI----- 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 52632416  717 LIMDEVDGMAGNEDRGG------------IQELIGLIKHTKIPIICMCN 753
Cdd:cd19481   89 LFIDEIDAIGRKRDSSGesgelrrvlnqlLTELDGVNSRSKVLVIAATN 137
BRCT_TopBP1_rpt2_like cd17731
second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; ...
 407-456 1.95e-05

second BRCT domain of DNA topoisomerase 2-binding protein 1 (TopBP1) and similar proteins; TopBP1, also termed DNA topoisomerase II-beta-binding protein 1, or DNA topoisomerase II-binding protein 1, functions in DNA replication and damage response. It binds double-stranded DNA breaks and nicks as well as single-stranded DNA. TopBP1 contains six copies of BRCT domain. The family corresponds to the second BRCT domain.


Pssm-ID: 349363 [Multi-domain]  Cd Length: 77  Bit Score: 43.68  E-value: 1.95e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 52632416  407 LEGLIFVITGvLESIERDEAKSLIERYGGKVTGNVSKKTNYLVMGRDSGQ 456
Cdd:cd17731    3 FKGLVICVTG-FDSEERKEIQQLVEQNGGSYSPDLSKNCTHLIAGSPSGQ 51
RarA COG2256
Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, ...
 592-692 2.00e-05

Replication-associated recombination protein RarA (DNA-dependent ATPase) [Replication, recombination and repair];


Pssm-ID: 441857 [Multi-domain]  Cd Length: 439  Bit Score: 48.51  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  592 PTSLKTIIGQQgdqscanKLL---RWLRNWQKSssedkkhaakfGKFSgkddgsSFkaaLLSGPPGVGKTTTASLVCQEL 668
Cdd:COG2256   21 PRTLDEVVGQE-------HLLgpgKPLRRAIEA-----------GRLS------SM---ILWGPPGTGKTTLARLIANAT 73

                         90       100
                 ....*....|....*....|....
gi 52632416  669 GYSYVELNASDTrSKSSLKAIVAE 692
Cdd:COG2256   74 DAEFVALSAVTS-GVKDIREVIEE 96
rad24 TIGR00602
checkpoint protein rad24; All proteins in this family for which functions are known are ...
 537-674 2.45e-05

checkpoint protein rad24; All proteins in this family for which functions are known are involved in DNA damage tolerance (likely cell cycle checkpoints).This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129690 [Multi-domain]  Cd Length: 637  Bit Score: 48.41  E-value: 2.45e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    537 SLAKTIKKETDVFWKSLDFKEQVAEETSGDSKARNLADD-------SSENKVENLLWVDKYKPTSlktiigqQGDQSCAN 609
Cdd:TIGR00602   18 SLISTITKWSLSRPTSSHRRKNSPSTDIHARKRGFLSLEqdtglelSSENLDGNEPWVEKYKPET-------QHELAVHK 90

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 52632416    610 KLLRWLRNWQKSSS-EDKKHaakfgkfsgkddgssfKAALLSGPPGVGKTTTASLVCQELGYSYVE 674
Cdd:TIGR00602   91 KKIEEVETWLKAQVlENAPK----------------RILLITGPSGCGKSTTIKILSKELGIQVQE 140
PTZ00121 PTZ00121
MAEBL; Provisional
 18-404 2.95e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.60  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    18 SETVKKNEKTKSDEETLKA---KKGIKEIKVNSSRKEDDFKQKQPSKKkriiYDSDSESEETLQVKNAKKPPEKlpvsSK 94
Cdd:PTZ00121 1172 AEDAKKAEAARKAEEVRKAeelRKAEDARKAEAARKAEEERKAEEARK----AEDAKKAEAVKKAEEAKKDAEE----AK 1243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    95 PGKISRQDPVTYISETDEEDDFMCKKAASKSKEnGRSTNSHLGTSNMKKNEENTKTKNKPLS---PIKLTPTSVLDYFGT 171
Cdd:PTZ00121 1244 KAEEERNNEEIRKFEEARMAHFARRQAAIKAEE-ARKADELKKAEEKKKADEAKKAEEKKKAdeaKKKAEEAKKADEAKK 1322

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   172 GSVQRSNKKMVASKRKELSQNTDESG-LNDEAIAKQLQLDEDAELERQLHEDEEF--ARTLAMLDEEPKT-----KKARK 243
Cdd:PTZ00121 1323 KAEEAKKKADAAKKKAEEAKKAAEAAkAEAEAAADEAEAAEEKAEAAEKKKEEAKkkADAAKKKAEEKKKadeakKKAEE 1402

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   244 DTEAGETFSSVQANLSKAEKHKYPHKVKTAQVSDERKSYSPRKQSKYESSKESQQHSKSSADKIGEVSSPKASSKLAIMK 323
Cdd:PTZ00121 1403 DKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKAEEA 1482

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   324 RKEESSYKEIEPvASKRKENAIKLKGETKTPKKTKSSPAKKESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGA 403
Cdd:PTZ00121 1483 KKADEAKKKAEE-AKKKADEAKKAAEAKKKADEAKKAEEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAE 1561


                  .
gi 52632416   404 E 404
Cdd:PTZ00121 1562 E 1562
PTZ00121 PTZ00121
MAEBL; Provisional
 25-404 3.74e-05

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 48.21  E-value: 3.74e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    25 EKTKSDEETLKAKKGIKEIKVNSSRKEDDFKQKQPSKKKRiiyDSDSESEETLQVKNAKKPPE-KLPVSSKPGKISRQDP 103
Cdd:PTZ00121 1085 EDNRADEATEEAFGKAEEAKKTETGKAEEARKAEEAKKKA---EDARKAEEARKAEDARKAEEaRKAEDAKRVEIARKAE 1161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   104 VTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKTKNKPLSPIKLTPTSVLDYFGTGSVQRSNKKMVA 183
Cdd:PTZ00121 1162 DARKAEEARKAEDAKKAEAARKAEEVRKAEELRKAEDARKAEAARKAEEERKAEEARKAEDAKKAEAVKKAEEAKKDAEE 1241

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   184 SKRKELSQNTDESGLNDEAIAKQL---QLDEDAELERQLHE---------DEEFARTLAMLDEEPKTKKARKDTEAGETF 251
Cdd:PTZ00121 1242 AKKAEEERNNEEIRKFEEARMAHFarrQAAIKAEEARKADElkkaeekkkADEAKKAEEKKKADEAKKKAEEAKKADEAK 1321

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   252 SSVQANLSKAE--KHKYPHKVKTAQVSDERKSYSPRKQSKYESSKESQQHSKSSADKIGEVSSPKASS--KLAIMKRKEE 327
Cdd:PTZ00121 1322 KKAEEAKKKADaaKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKADAAKKKAEEkkKADEAKKKAE 1401

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   328 SSYKEIEPV----ASKRKENAIKLKGETKtpKKTKSSPAKKESVSPEDSEKKRTNYQAYRSYLNREGPKALGSKEIPKGA 403
Cdd:PTZ00121 1402 EDKKKADELkkaaAAKKKADEAKKKAEEK--KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKKA 1479


                  .
gi 52632416   404 E 404
Cdd:PTZ00121 1480 E 1480
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 174-398 1.08e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 46.61  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   174 VQRSNKKMvASKRKELSQNTDESGLNDEAIAKQLQLDEDAELERQLHEDEEFArtlamldEEPKTKKARKDTEAGEtfss 253
Cdd:PTZ00449  489 IKKSKKKL-APIEEEDSDKHDEPPEGPEASGLPPKAPGDKEGEEGEHEDSKES-------DEPKEGGKPGETKEGE---- 556

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   254 VQANLSKAEKHKyPHKVK--TAQVSDERKSYSPRKQSKYESSKESQQHSKSSADKigevsSPK--ASSKLAIMKRKEESS 329
Cdd:PTZ00449  557 VGKKPGPAKEHK-PSKIPtlSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPK-----SPKlpELLDIPKSPKRPESP 630

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 52632416   330 YKEIEPVASKRKENAIKLKGeTKTPKKTKSSPAKKESVSPEDSEKkrtnyqAYRSYLNregpKALGSKE 398
Cdd:PTZ00449  631 KSPKRPPPPQRPSSPERPEG-PKIIKSPKPPKSPKPPFDPKFKEK------FYDDYLD----AAAKSKE 688
CDC6 COG1474
Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];
647-792 1.74e-04

Cdc6-related protein, AAA superfamily ATPase [Replication, recombination and repair];


Pssm-ID: 441083 [Multi-domain]  Cd Length: 389  Bit Score: 45.22  E-value: 1.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  647 ALLSGPPGVGKTTTASLVCQELGY---------SYVELNASDTRSKSS-LKAIVAESLNNTSIkgfysngAASSVSTKHA 716
Cdd:COG1474   54 VLIYGPTGTGKTAVAKYVLEELEEeaeergvdvRVVYVNCRQASTRYRvLSRILEELGSGEDI-------PSTGLSTDEL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416  717 ----------------LIMDEVDGMAGNEDRGGIQELIGL---IKHTKIPIICMCND---RNH--PKIRSlVHYCFDLRF 772
Cdd:COG1474  127 fdrlyealderdgvlvVVLDEIDYLVDDEGDDLLYQLLRAneeLEGARVGVIGISNDlefLENldPRVKS-SLGEEEIVF 205

                        170       180
                 ....*....|....*....|...
gi 52632416  773 QRPRVEQIKGAMM---SIAFKEG 792
Cdd:COG1474  206 PPYDADELRDILEdraELAFYDG 228
Rad17 pfam03215
Rad17 P-loop domain;
578-684 3.08e-04

Rad17 P-loop domain;


Pssm-ID: 367398 [Multi-domain]  Cd Length: 186  Bit Score: 43.02  E-value: 3.08e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    578 ENKVENLLWVDKYKPTSlktiigqQGDQSCANKLLRWLRNWQKSSS-EDKKHaakfgkfsgkddgssfKAALLSGPPGVG 656
Cdd:pfam03215    1 INDDGGEQWYEKYKPNC-------LEQLAVHKRKIKDVQEWLDAMFlENAKH----------------RILLISGPSGCG 57

                           90       100
                   ....*....|....*....|....*....
gi 52632416    657 KTTTASLVCQELGYSYVE-LNASDTRSKS 684
Cdd:pfam03215   58 KSTVIKELSKELGPKYREwSNPTSFRSPP 86
Fap7 COG1936
Broad-specificity NMP kinase [Nucleotide transport and metabolism];
648-676 1.49e-03

Broad-specificity NMP kinase [Nucleotide transport and metabolism];


Pssm-ID: 441539 [Multi-domain]  Cd Length: 173  Bit Score: 40.57  E-value: 1.49e-03
                         10        20
                 ....*....|....*....|....*....
gi 52632416  648 LLSGPPGVGKTTTASLVCQELGYSYVELN 676
Cdd:COG1936    4 AITGTPGTGKTTVAKLLAERLGLEVIHLN 32
CMPK cd02020
Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine ...
 649-673 2.12e-03

Cytidine monophosphate kinase (CMPK) catalyzes the reversible phosphorylation of cytidine monophosphate (CMP) to produce cytidine diphosphate (CDP), using ATP as the preferred phosphoryl donor.


Pssm-ID: 238978 [Multi-domain]  Cd Length: 147  Bit Score: 39.78  E-value: 2.12e-03
                         10        20
                 ....*....|....*....|....*
gi 52632416  649 LSGPPGVGKTTTASLVCQELGYSYV 673
Cdd:cd02020    4 IDGPAGSGKSTVAKLLAKKLGLPYL 28
RuvB_N pfam05496
Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the ...
 648-669 2.13e-03

Holliday junction DNA helicase RuvB P-loop domain; The RuvB protein makes up part of the RuvABC revolvasome which catalyzes the resolution of Holliday junctions that arise during genetic recombination and DNA repair. Branch migration is catalyzed by the RuvB protein that is targeted to the Holliday junction by the structure specific RuvA protein. This family contains the N-terminal region of the protein.


Pssm-ID: 398900 [Multi-domain]  Cd Length: 159  Bit Score: 40.18  E-value: 2.13e-03
                           10        20
                   ....*....|....*....|..
gi 52632416    648 LLSGPPGVGKTTTASLVCQELG 669
Cdd:pfam05496   37 LLYGPPGLGKTTLANIIANEMG 58
COG1223 COG1223
Predicted ATPase, AAA+ superfamily [General function prediction only];
648-678 2.54e-03

Predicted ATPase, AAA+ superfamily [General function prediction only];


Pssm-ID: 440836 [Multi-domain]  Cd Length: 246  Bit Score: 41.02  E-value: 2.54e-03
                         10        20        30
                 ....*....|....*....|....*....|.
gi 52632416  648 LLSGPPGVGKTTTASLVCQELGYSYVELNAS 678
Cdd:COG1223   39 LFYGPPGTGKTMLAEALAGELKLPLLTVRLD 69
ruvB TIGR00635
Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions ...
 648-669 2.99e-03

Holliday junction DNA helicase, RuvB subunit; All proteins in this family for which functions are known are 5'-3' DNA helicases that, as part of a complex with RuvA homologs serve as a 5'-3' Holliday junction helicase. RuvA specifically binds Holliday junctions as a sandwich of two tetramers and maintains the configuration of the junction. It forms a complex with two hexameric rings of RuvB, the subunit that contains helicase activity. The complex drives ATP-dependent branch migration of the Holliday junction recombination intermediate. The endonuclease RuvC resolves junctions. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 129721 [Multi-domain]  Cd Length: 305  Bit Score: 41.13  E-value: 2.99e-03
                           10        20
                   ....*....|....*....|..
gi 52632416    648 LLSGPPGVGKTTTASLVCQELG 669
Cdd:TIGR00635   34 LLYGPPGLGKTTLAHIIANEMG 55
RuvB COG2255
Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, ...
 648-669 3.89e-03

Holliday junction resolvasome RuvABC, ATP-dependent DNA helicase subunit RuvB [Replication, recombination and repair];


Pssm-ID: 441856 [Multi-domain]  Cd Length: 337  Bit Score: 40.83  E-value: 3.89e-03
                         10        20
                 ....*....|....*....|..
gi 52632416  648 LLSGPPGVGKTTTASLVCQELG 669
Cdd:COG2255   58 LLYGPPGLGKTTLAHIIANEMG 79
RPT1 COG1222
ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein ...
 645-683 4.03e-03

ATP-dependent 26S proteasome regulatory subunit [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440835 [Multi-domain]  Cd Length: 326  Bit Score: 40.76  E-value: 4.03e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 52632416  645 KAALLSGPPGVGKTTTASLVCQELGYSYVELNASDTRSK 683
Cdd:COG1222  113 KGVLLYGPPGTGKTLLAKAVAGELGAPFIRVRGSELVSK 151
PTZ00121 PTZ00121
MAEBL; Provisional
 18-317 4.17e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.67  E-value: 4.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    18 SETVKKNEKtKSDEETLKAKKGIKEIKVNSSRKEDDFK------QKQPSKKKRIIYDSDSESEETLQVKNAKKPPEKLPV 91
Cdd:PTZ00121 1583 AEEAKKAEE-ARIEEVMKLYEEEKKMKAEEAKKAEEAKikaeelKKAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKI 1661

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    92 SSKPGKISRQDPVTYISETDEEDDFMCKKAASKSKENGRSTNSHlgtsNMKKNEENTKTKNKPLSPIKltptsvldyfgt 171
Cdd:PTZ00121 1662 KAAEEAKKAEEDKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAE----ELKKKEAEEKKKAEELKKAE------------ 1725

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   172 gSVQRSNKKMVASKRKELSQNTDESGLNDEAIAKQLQLDEDAELERQLHEDEEFARTLAMLDEEPKTKKARKDTEAGETF 251
Cdd:PTZ00121 1726 -EENKIKAEEAKKEAEEDKKKAEEAKKDEEEKKKIAHLKKEEEKKAEEIRKEKEAVIEEELDEEDEKRRMEVDKKIKDIF 1804

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 52632416   252 SSVqANLSKAEKHKYPHKVKTAQVSD-ERKSYSPRKQSKYESSKESQQHSKSSADKIGEVSSPKASS 317
Cdd:PTZ00121 1805 DNF-ANIIEGGKEGNLVINDSKEMEDsAIKEVADSKNMQLEEADAFEKHKFNKNNENGEDGNKEADF 1870
ruvB PRK00080
Holliday junction branch migration DNA helicase RuvB;
648-669 4.94e-03

Holliday junction branch migration DNA helicase RuvB;


Pssm-ID: 234619 [Multi-domain]  Cd Length: 328  Bit Score: 40.50  E-value: 4.94e-03
                          10        20
                  ....*....|....*....|..
gi 52632416   648 LLSGPPGVGKTTTASLVCQELG 669
Cdd:PRK00080   55 LLYGPPGLGKTTLANIIANEMG 76
PTZ00121 PTZ00121
MAEBL; Provisional
 18-596 5.20e-03

MAEBL; Provisional


Pssm-ID: 173412 [Multi-domain]  Cd Length: 2084  Bit Score: 41.28  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    18 SETVKKNEKTKSDEETLKAKKGIKE--IKVNSSRKEDDFKQKQPSKKKriiyDSDSESEETLQVKNAKKPPEKLPVSSKP 95
Cdd:PTZ00121 1245 AEEERNNEEIRKFEEARMAHFARRQaaIKAEEARKADELKKAEEKKKA----DEAKKAEEKKKADEAKKKAEEAKKADEA 1320

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416    96 GKISRQ-----DPVTYISETDEEDDFMCKKAASKSKENGRSTNSHLGTSNMKKNEENTKTknkplspikltptsvlDYFG 170
Cdd:PTZ00121 1321 KKKAEEakkkaDAAKKKAEEAKKAAEAAKAEAEAAADEAEAAEEKAEAAEKKKEEAKKKA----------------DAAK 1384

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   171 TGSVQRSNKKMVASKRKELSQNTDESGLNDEAIAKQLQLDEDAELERQLHEDEEFArtlamlDEEPKTKKARKDTEAGEt 250
Cdd:PTZ00121 1385 KKAEEKKKADEAKKKAEEDKKKADELKKAAAAKKKADEAKKKAEEKKKADEAKKKA------EEAKKADEAKKKAEEAK- 1457

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   251 fssvqanlsKAEKHKypHKVKTAQVSDERKSYSPRKQSKYESSKESQQHSKssadKIGEVSSPKASSKLAIMKRKEESSY 330
Cdd:PTZ00121 1458 ---------KAEEAK--KKAEEAKKADEAKKKAEEAKKADEAKKKAEEAKK----KADEAKKAAEAKKKADEAKKAEEAK 1522

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   331 KEIEpvaSKRKENAIKLKGETKTPKKTKSSPAKKESVSPEDSEKKRTNyQAYRSYLNREgpKALGSKEIPKGAENCLEGL 410
Cdd:PTZ00121 1523 KADE---AKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAE-EAKKAEEDKN--MALRKAEEAKKAEEARIEE 1596

                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   411 IFVITGVLESIERDEAKSLIERYGG----KVTGNVSKKTNYLVMGRDSGQSKSD--KAAALGTKIIDEDgllnLIRTMPG 484
Cdd:PTZ00121 1597 VMKLYEEEKKMKAEEAKKAEEAKIKaeelKKAEEEKKKVEQLKKKEAEEKKKAEelKKAEEENKIKAAE----EAKKAEE 1672

                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 52632416   485 KKSKYEIAVETEMKKESKLERTPQKNVQGKRKISPSKKESESKKSRPTSKRDSLAKTIKKEtdvfwkslDFKEQVAEETS 564
Cdd:PTZ00121 1673 DKKKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELKKKEAEEKKKAEELKKAEEENKIKAE--------EAKKEAEEDKK 1744

                         570       580       590
                  ....*....|....*....|....*....|..
gi 52632416   565 GDSKARnlADDSSENKVENLLWVDKYKPTSLK 596
Cdd:PTZ00121 1745 KAEEAK--KDEEEKKKIAHLKKEEEKKAEEIR 1774
AAA_17 pfam13207
AAA domain;
650-679 5.98e-03

AAA domain;


Pssm-ID: 463810 [Multi-domain]  Cd Length: 136  Bit Score: 38.37  E-value: 5.98e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 52632416    650 SGPPGVGKTTTASLVCQELGYSYVelNASD 679
Cdd:pfam13207    1 TGVPGSGKTTQLKKLAEKLGFPHI--SAGD 28
 
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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