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Conserved domains on  [gi|18379168|ref|NP_565256|]
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Octicosapeptide/Phox/Bem1p family protein [Arabidopsis thaliana]

Protein Classification

PB1 domain-containing protein kinase; PB1 domain-containing protein; PB1 domain-containing protein kinase( domain architecture ID 12949837)

PB1 domain-containing protein kinase may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates; PB1 domain-containing protein kinase may catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine and/or tyrosine residues on protein substrates; PB1 domain-containing protein may mediate specific protein-protein interactions

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PB1_UP2 cd06410
Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific ...
78-179 1.17e-48

Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions.


:

Pssm-ID: 99731  Cd Length: 97  Bit Score: 165.86  E-value: 1.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168  78 MCSYGGHILPRPHDKSLCYMGGDTRIVVVDRNSSLPSLIARLSNTLLDGRSFTLKYQLPSEDLDSLISVTTDEDLDNMIE 157
Cdd:cd06410   1 LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVVVTLKYQLPDEDLDALISVSNDEDLKNMME 80
                        90       100
                ....*....|....*....|..
gi 18379168 158 EYDRTisasnSTKPSRLRLFLF 179
Cdd:cd06410  81 EYDRL-----SGGSARLRVFLF 97
PABP-1234 super family cl31127
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
536-662 6.56e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


The actual alignment was detected with superfamily member TIGR01628:

Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   536 QQPQQSFHQHAGRLDQQPYPVYYVTAPVPPrPYSMPVPQSpsvsdAAGSIPSNHPNSTMMPPPPNNHMRSVSSGKPEMGQ 615
Cdd:TIGR01628 369 AHLQDQFMQLQPRMRQLPMGSPMGGAMGQP-PYYGQGPQQ-----QFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNA 442
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18379168   616 AGvyttAPGVGGAQMVHQIPTNQQQFMGYSQIRHPPQSGSAGNPNYG 662
Cdd:TIGR01628 443 VR----APSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTAS 485
PRK10263 super family cl35903
DNA translocase FtsK; Provisional
357-624 1.80e-03

DNA translocase FtsK; Provisional


The actual alignment was detected with superfamily member PRK10263:

Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   357 PVTIALPAAPVTAATVSNEfQARVysdDERSDHGVQAGyrkPPTPRSQPQNLPPQQAHqlkSNSGGGHELPSPNSVSSDS 436
Cdd:PRK10263  336 PVEPVTQTPPVASVDVPPA-QPTV---AWQPVPGPQTG---EPVIAPAPEGYPQQSQY---AQPAVQYNEPLQQPVQPQQ 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   437 SMSNPMFHQRPSVYQEPIAQIPSGSTVVTGMINPSDPSTLLSQHQNQDPAYILHP--QFEQQSAQSQPQQQFIHtaaPPQ 514
Cdd:PRK10263  406 PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQStyQTEQTYQQPAAQEPLYQ---QPQ 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   515 YIHHhPSSGLPVPTYIQVYPSQQPQQSFHQHAGRLDQQPYPVYYVTAPVpPRPYSMPVPQSPSVS-DAAGSIPSNHPNST 593
Cdd:PRK10263  483 PVEQ-QPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPI-PEPVKEPEPIKSSLKaPSVAAVPPVEAAAA 560
                         250       260       270
                  ....*....|....*....|....*....|.
gi 18379168   594 MMPPPPNNHMRSVSSGKPEMGQAGVYTTAPG 624
Cdd:PRK10263  561 VSPLASGVKKATLATGAAATVAAPVFSLANS 591
 
Name Accession Description Interval E-value
PB1_UP2 cd06410
Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific ...
78-179 1.17e-48

Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions.


Pssm-ID: 99731  Cd Length: 97  Bit Score: 165.86  E-value: 1.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168  78 MCSYGGHILPRPHDKSLCYMGGDTRIVVVDRNSSLPSLIARLSNTLLDGRSFTLKYQLPSEDLDSLISVTTDEDLDNMIE 157
Cdd:cd06410   1 LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVVVTLKYQLPDEDLDALISVSNDEDLKNMME 80
                        90       100
                ....*....|....*....|..
gi 18379168 158 EYDRTisasnSTKPSRLRLFLF 179
Cdd:cd06410  81 EYDRL-----SGGSARLRVFLF 97
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
89-179 5.02e-19

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 81.86  E-value: 5.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168     89 PHDKSLCYmGGDTRIVVVDRNSSLPSLIARLSNTL-LDGRSFTLKYQlpSEDLDsLISVTTDEDLDNMIEEYDRTISAsn 167
Cdd:smart00666   1 TVDVKLRY-GGETRRLSVPRDISFEDLRSKVAKRFgLDNQSFTLKYQ--DEDGD-LVSLTSDEDLEEAIEEYDSLGSK-- 74
                           90
                   ....*....|..
gi 18379168    168 stkpsRLRLFLF 179
Cdd:smart00666  75 -----KLRLHVF 81
PB1 pfam00564
PB1 domain;
89-179 9.95e-19

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 81.18  E-value: 9.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168    89 PHDKSLCYMGGDTRIVVVDRNSSLPSLIARLSNTLLDGrSFTLKYQLPSEDLDsLISVTTDEDLDNMIEEYDRTISAsns 168
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLD-DVDFKLKYPDEDGD-LVSLTSDEDLEEALEEARSLGSK--- 75
                          90
                  ....*....|.
gi 18379168   169 tkpsRLRLFLF 179
Cdd:pfam00564  76 ----SLRLHVF 82
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
536-662 6.56e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   536 QQPQQSFHQHAGRLDQQPYPVYYVTAPVPPrPYSMPVPQSpsvsdAAGSIPSNHPNSTMMPPPPNNHMRSVSSGKPEMGQ 615
Cdd:TIGR01628 369 AHLQDQFMQLQPRMRQLPMGSPMGGAMGQP-PYYGQGPQQ-----QFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNA 442
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18379168   616 AGvyttAPGVGGAQMVHQIPTNQQQFMGYSQIRHPPQSGSAGNPNYG 662
Cdd:TIGR01628 443 VR----APSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTAS 485
PRK10263 PRK10263
DNA translocase FtsK; Provisional
357-624 1.80e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   357 PVTIALPAAPVTAATVSNEfQARVysdDERSDHGVQAGyrkPPTPRSQPQNLPPQQAHqlkSNSGGGHELPSPNSVSSDS 436
Cdd:PRK10263  336 PVEPVTQTPPVASVDVPPA-QPTV---AWQPVPGPQTG---EPVIAPAPEGYPQQSQY---AQPAVQYNEPLQQPVQPQQ 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   437 SMSNPMFHQRPSVYQEPIAQIPSGSTVVTGMINPSDPSTLLSQHQNQDPAYILHP--QFEQQSAQSQPQQQFIHtaaPPQ 514
Cdd:PRK10263  406 PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQStyQTEQTYQQPAAQEPLYQ---QPQ 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   515 YIHHhPSSGLPVPTYIQVYPSQQPQQSFHQHAGRLDQQPYPVYYVTAPVpPRPYSMPVPQSPSVS-DAAGSIPSNHPNST 593
Cdd:PRK10263  483 PVEQ-QPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPI-PEPVKEPEPIKSSLKaPSVAAVPPVEAAAA 560
                         250       260       270
                  ....*....|....*....|....*....|.
gi 18379168   594 MMPPPPNNHMRSVSSGKPEMGQAGVYTTAPG 624
Cdd:PRK10263  561 VSPLASGVKKATLATGAAATVAAPVFSLANS 591
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
348-551 9.50e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 39.25  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   348 AAISSPPPMPVTIALPAAPVTAATVSNEFQAR-VYSDDErsdhgVQAGYR-KPPTPRSQPQNLPPQQAHQLKSNSGGGHE 425
Cdd:pfam09770 160 ASLWGVAPKKAAAPAPAPQPAAQPASLPAPSRkMMSLEE-----VEAAMRaQAKKPAQQPAPAPAQPPAAPPAQQAQQQQ 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   426 LPSPNSVSSDSSMSNPMFHQRPSVYQEPIAQI--PSGSTVVTGMINPSDPSTLLSQHQ---NQDPAYILH-PQFEQQSAQ 499
Cdd:pfam09770 235 QFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILqrPQSPQPDPAQPSIQPQAQQFHQQPppvPVQPTQILQnPNRLSAARV 314
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18379168   500 SQPQQQFIHTAAPPQYIHHHPSSGLPVPTYIQVYPSQQPQQSFHQHAGRLDQ 551
Cdd:pfam09770 315 GYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQLAQLSEEEKAAYLDE 366
 
Name Accession Description Interval E-value
PB1_UP2 cd06410
Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific ...
78-179 1.17e-48

Uncharacterized protein 2. The PB1 domain is a modular domain mediating specific protein-protein interaction which play a role in many critical cell processes such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domains, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as noncanonical PB1-interactions.


Pssm-ID: 99731  Cd Length: 97  Bit Score: 165.86  E-value: 1.17e-48
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168  78 MCSYGGHILPRPHDKSLCYMGGDTRIVVVDRNSSLPSLIARLSNTLLDGRSFTLKYQLPSEDLDSLISVTTDEDLDNMIE 157
Cdd:cd06410   1 LCSYGGRILPRPPDGQLRYVGGETRIVSVDRSISFKELVSKLSELFGAGVVVTLKYQLPDEDLDALISVSNDEDLKNMME 80
                        90       100
                ....*....|....*....|..
gi 18379168 158 EYDRTisasnSTKPSRLRLFLF 179
Cdd:cd06410  81 EYDRL-----SGGSARLRVFLF 97
PB1 smart00666
PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. ...
89-179 5.02e-19

PB1 domain; Phox and Bem1p domain, present in many eukaryotic cytoplasmic signalling proteins. The domain adopts a beta-grasp fold, similar to that found in ubiquitin and Ras-binding domains. A motif, variously termed OPR, PC and AID, represents the most conserved region of the majority of PB1 domains, and is necessary for PB1 domain function. This function is the formation of PB1 domain heterodimers, although not all PB1 domain pairs associate.


Pssm-ID: 214770  Cd Length: 81  Bit Score: 81.86  E-value: 5.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168     89 PHDKSLCYmGGDTRIVVVDRNSSLPSLIARLSNTL-LDGRSFTLKYQlpSEDLDsLISVTTDEDLDNMIEEYDRTISAsn 167
Cdd:smart00666   1 TVDVKLRY-GGETRRLSVPRDISFEDLRSKVAKRFgLDNQSFTLKYQ--DEDGD-LVSLTSDEDLEEAIEEYDSLGSK-- 74
                           90
                   ....*....|..
gi 18379168    168 stkpsRLRLFLF 179
Cdd:smart00666  75 -----KLRLHVF 81
PB1 pfam00564
PB1 domain;
89-179 9.95e-19

PB1 domain;


Pssm-ID: 395447  Cd Length: 84  Bit Score: 81.18  E-value: 9.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168    89 PHDKSLCYMGGDTRIVVVDRNSSLPSLIARLSNTLLDGrSFTLKYQLPSEDLDsLISVTTDEDLDNMIEEYDRTISAsns 168
Cdd:pfam00564   1 TVRLKLRYGGGIRRFLSVSRGISFEELRALVEQRFGLD-DVDFKLKYPDEDGD-LVSLTSDEDLEEALEEARSLGSK--- 75
                          90
                  ....*....|.
gi 18379168   169 tkpsRLRLFLF 179
Cdd:pfam00564  76 ----SLRLHVF 82
PB1 cd05992
The PB1 domain is a modular domain mediating specific protein-protein interactions which play ...
94-179 3.33e-17

The PB1 domain is a modular domain mediating specific protein-protein interactions which play a role in many critical cell processes, such as osteoclastogenesis, angiogenesis, early cardiovascular development, and cell polarity. A canonical PB1-PB1 interaction, which involves heterodimerization of two PB1 domain, is required for the formation of macromolecular signaling complexes ensuring specificity and fidelity during cellular signaling. The interaction between two PB1 domain depends on the type of PB1. There are three types of PB1 domains: type I which contains an OPCA motif, acidic aminoacid cluster, type II which contains a basic cluster, and type I/II which contains both an OPCA motif and a basic cluster. Interactions of PB1 domains with other protein domains have been described as a noncanonical PB1-interactions. The PB1 domain module is conserved in amoebas, fungi, animals, and plants.


Pssm-ID: 99716 [Multi-domain]  Cd Length: 81  Bit Score: 76.55  E-value: 3.33e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168  94 LCYMGGDTRIVVVDRNSSLPSLIARLSnTLLDGRSFTLKYQLPSEDLDsLISVTTDEDLDNMIEEYDRtisasnsTKPSR 173
Cdd:cd05992   5 VKYGGEIRRFVVVSRSISFEDLRSKIA-EKFGLDAVSFKLKYPDEDGD-LVTISSDEDLEEAIEEARR-------SGSKK 75

                ....*.
gi 18379168 174 LRLFLF 179
Cdd:cd05992  76 LRLFVF 81
PABP-1234 TIGR01628
polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins ...
536-662 6.56e-04

polyadenylate binding protein, human types 1, 2, 3, 4 family; These eukaryotic proteins recognize the poly-A of mRNA and consists of four tandem RNA recognition domains at the N-terminus (rrm: pfam00076) followed by a PABP-specific domain (pfam00658) at the C-terminus. The protein is involved in the transport of mRNA's from the nucleus to the cytoplasm. There are four paralogs in Homo sapiens which are expressed in testis, platelets, broadly expressed and of unknown tissue range.


Pssm-ID: 130689 [Multi-domain]  Cd Length: 562  Bit Score: 42.87  E-value: 6.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   536 QQPQQSFHQHAGRLDQQPYPVYYVTAPVPPrPYSMPVPQSpsvsdAAGSIPSNHPNSTMMPPPPNNHMRSVSSGKPEMGQ 615
Cdd:TIGR01628 369 AHLQDQFMQLQPRMRQLPMGSPMGGAMGQP-PYYGQGPQQ-----QFNGQPLGWPRMSMMPTPMGPGGPLRPNGLAPMNA 442
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 18379168   616 AGvyttAPGVGGAQMVHQIPTNQQQFMGYSQIRHPPQSGSAGNPNYG 662
Cdd:TIGR01628 443 VR----APSRNAQNAAQKPPMQPVMYPPNYQSLPLSQDLPQPQSTAS 485
PRK10263 PRK10263
DNA translocase FtsK; Provisional
357-624 1.80e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 1.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   357 PVTIALPAAPVTAATVSNEfQARVysdDERSDHGVQAGyrkPPTPRSQPQNLPPQQAHqlkSNSGGGHELPSPNSVSSDS 436
Cdd:PRK10263  336 PVEPVTQTPPVASVDVPPA-QPTV---AWQPVPGPQTG---EPVIAPAPEGYPQQSQY---AQPAVQYNEPLQQPVQPQQ 405
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   437 SMSNPMFHQRPSVYQEPIAQIPSGSTVVTGMINPSDPSTLLSQHQNQDPAYILHP--QFEQQSAQSQPQQQFIHtaaPPQ 514
Cdd:PRK10263  406 PYYAPAAEQPAQQPYYAPAPEQPAQQPYYAPAPEQPVAGNAWQAEEQQSTFAPQStyQTEQTYQQPAAQEPLYQ---QPQ 482
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   515 YIHHhPSSGLPVPTYIQVYPSQQPQQSFHQHAGRLDQQPYPVYYVTAPVpPRPYSMPVPQSPSVS-DAAGSIPSNHPNST 593
Cdd:PRK10263  483 PVEQ-QPVVEPEPVVEETKPARPPLYYFEEVEEKRAREREQLAAWYQPI-PEPVKEPEPIKSSLKaPSVAAVPPVEAAAA 560
                         250       260       270
                  ....*....|....*....|....*....|.
gi 18379168   594 MMPPPPNNHMRSVSSGKPEMGQAGVYTTAPG 624
Cdd:PRK10263  561 VSPLASGVKKATLATGAAATVAAPVFSLANS 591
PAT1 pfam09770
Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate ...
348-551 9.50e-03

Topoisomerase II-associated protein PAT1; Members of this family are necessary for accurate chromosome transmission during cell division.


Pssm-ID: 401645 [Multi-domain]  Cd Length: 846  Bit Score: 39.25  E-value: 9.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   348 AAISSPPPMPVTIALPAAPVTAATVSNEFQAR-VYSDDErsdhgVQAGYR-KPPTPRSQPQNLPPQQAHQLKSNSGGGHE 425
Cdd:pfam09770 160 ASLWGVAPKKAAAPAPAPQPAAQPASLPAPSRkMMSLEE-----VEAAMRaQAKKPAQQPAPAPAQPPAAPPAQQAQQQQ 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18379168   426 LPSPNSVSSDSSMSNPMFHQRPSVYQEPIAQI--PSGSTVVTGMINPSDPSTLLSQHQ---NQDPAYILH-PQFEQQSAQ 499
Cdd:pfam09770 235 QFPPQIQQQQQPQQQPQQPQQHPGQGHPVTILqrPQSPQPDPAQPSIQPQAQQFHQQPppvPVQPTQILQnPNRLSAARV 314
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18379168   500 SQPQQQFIHTAAPPQYIHHHPSSGLPVPTYIQVYPSQQPQQSFHQHAGRLDQ 551
Cdd:pfam09770 315 GYPQNPQPGVQPAPAHQAHRQQGSFGRQAPIITHPQQLAQLSEEEKAAYLDE 366
 
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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